|
Name |
Accession |
Description |
Interval |
E-value |
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
14-369 |
0e+00 |
|
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: 630.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 14 QGTSGIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAG--GRILIGDTDVTHLPPYKRG 91
Cdd:TIGR03258 1 GACGGIRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGltGRIAIADRDLTHAPPHKRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 92 LAMVVQNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:TIGR03258 81 LALLFQNYALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 172 LDEPLSALDAQIRHNMVEEIACLHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLG 251
Cdd:TIGR03258 161 LDEPLSALDANIRANMREEIAALHEELPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 252 RANILSAIALGITEAPGLVDVSCGGAVIRAFSRGSHHGYNKLLCIRPQHLSLTPRSAYSNRFNATLQSVHWQGDLTHLLC 331
Cdd:TIGR03258 241 AANILPAIALGITEAPGLVDVSCGGAVIFAFGDGRHDGRDKLACIRPEHLALTPRPAGEGRFHATIASVEWHGAALHLLC 320
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 566074967 332 DV-AGETVRMV---LTHVNPLPRVGDKLALWFEPDDAVLIEV 369
Cdd:TIGR03258 321 DLdAACDEPMLvtmLRGRGPAPERGAKLALDCEADDAVLIEP 362
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
16-368 |
3.32e-158 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 448.01 E-value: 3.32e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 16 TSGIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMV 95
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 96 VQNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 176 LSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLGRANI 255
Cdd:COG3842 163 LSALDAKLREEMREELRRLQREL-GITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 256 LSAIALGITEApglvDVSCGGAVIRAFS-RGSHHGYNKLLCIRPQHLSLTPRSAySNRFNATLQSVHWQGDLTHLLCDVA 334
Cdd:COG3842 242 LPGTVLGDEGG----GVRTGGRTLEVPAdAGLAAGGPVTVAIRPEDIRLSPEGP-ENGLPGTVEDVVFLGSHVRYRVRLG 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 566074967 335 -GETVRMVLT-HVNPLPRVGDKLALWFEPDDAVLIE 368
Cdd:COG3842 317 dGQELVVRVPnRAALPLEPGDRVGLSWDPEDVVVLP 352
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
17-366 |
1.63e-140 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 402.91 E-value: 1.63e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 17 SGIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVV 96
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 97 QNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:COG3839 82 QSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 177 SALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLG--RAN 254
Cdd:COG3839 162 SNLDAKLRVEMRAEIKRLHRRL-GTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGspPMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 255 ILSAIALGiteapglVDVSCGGAVIRAFSRGSHHGYNKL-LCIRPQHLSLTPRSAysNRFNATLQSVHWQGDLTHLLCDV 333
Cdd:COG3839 241 LLPGTVEG-------GGVRLGGVRLPLPAALAAAAGGEVtLGIRPEHLRLADEGD--GGLEATVEVVEPLGSETLVHVRL 311
|
330 340 350
....*....|....*....|....*....|...
gi 566074967 334 AGETVRMVLTHVNPLpRVGDKLALWFEPDDAVL 366
Cdd:COG3839 312 GGQELVARVPGDTRL-RPGDTVRLAFDPERLHL 343
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
18-357 |
4.97e-117 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 343.28 E-value: 4.97e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 18 GIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDV-THLPPYKRGLAMVV 96
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 97 QNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 177 SALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLGRANIL 256
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDEL-GGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 257 SAIAL-GITEAPGlvdvsCGGAVIRAFSRGSHHGYnkllcIRPQHLSLTPRSAYSNRFNATLQSVHWQGDLTHLLC---D 332
Cdd:COG1118 241 RGRVIgGQLEADG-----LTLPVAEPLPDGPAVAG-----VRPHDIEVSREPEGENTFPATVARVSELGPEVRVELkleD 310
|
330 340
....*....|....*....|....*...
gi 566074967 333 VAGETVRMVLTH---VNPLPRVGDKLAL 357
Cdd:COG1118 311 GEGQPLEAEVTKeawAELGLAPGDPVYL 338
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
19-251 |
4.67e-114 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 331.12 E-value: 4.67e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQN 98
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 99 YALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 566074967 179 LDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLG 251
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKEL-GITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
19-232 |
2.53e-107 |
|
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: 313.30 E-value: 2.53e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQN 98
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 99 YALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 566074967 179 LDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03259 161 LDAKLREELREELKELQREL-GITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
12-301 |
1.44e-104 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 312.27 E-value: 1.44e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 12 ASQGTSGIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRG 91
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 92 LAMVVQNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 172 LDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLG 251
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKL-GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 566074967 252 RANILSAIALGITeAPGLVDVSCGGAVIRAFSRGSHHGYNKL-LCIRPQHL 301
Cdd:PRK09452 247 EINIFDATVIERL-DEQRVRANVEGRECNIYVNFAVEPGQKLhVLLRPEDL 296
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
49-367 |
1.77e-99 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 297.87 E-value: 1.77e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 49 LIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQNYALFPHLKVEDNVAFGLRAQKQPKALINER 128
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 129 VTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTH 208
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQL-GITFVFVTH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 209 DQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLGRANILSAIALGITEApGLVDVSCGGAVIRAFSRGSHH 288
Cdd:TIGR01187 160 DQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSE-QVVLAGVEGRRCDIYTDVPVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 289 GYNKL-LCIRPQHLSL--TPRSAYSNRFNATLQSVHWQGD--LTHLLCDVAGE---TVRMVLTHVNPLPRVGDKLALWFE 360
Cdd:TIGR01187 239 KDQPLhVVLRPEKIVIeeEDEANSSNAIIGHVIDITYLGMtlEVHVRLETGQKvlvSEFFNEDDPHMSPSIGDRVGLTWH 318
|
....*..
gi 566074967 361 PDDAVLI 367
Cdd:TIGR01187 319 PGSEVVL 325
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
33-360 |
1.96e-96 |
|
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: 290.79 E-value: 1.96e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQNYALFPHLKVEDNVA 112
Cdd:TIGR03265 19 ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQSYALFPNLTVADNIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 113 FGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIA 192
Cdd:TIGR03265 99 YGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 193 CLHRELPELTILyVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLGRANILSAIALGITEAP-GLVD 271
Cdd:TIGR03265 179 QLQRRLGVTTIM-VTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPGTRGGGSRARvGGLT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 272 VSCGGAVIRAFSRGShhgynklLCIRPQHLSLTPRSAYSNRFNATLQSVHWQGDLTHLLCDVAGETVRMVLTHVNP--LP 349
Cdd:TIGR03265 258 LACAPGLAQPGASVR-------LAVRPEDIRVSPAGNAANLLLARVEDMEFLGAFYRLRLRLEGLPGQALVADVSAseVE 330
|
330
....*....|...
gi 566074967 350 RVGDKLA--LWFE 360
Cdd:TIGR03265 331 RLGIRAGqpIWIE 343
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
19-226 |
1.98e-95 |
|
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: 283.38 E-value: 1.98e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQN 98
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 99 YALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 566074967 179 LDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRL-GTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
34-344 |
2.57e-93 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 282.73 E-value: 2.57e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQNYALFPHLKVEDNVAF 113
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 114 GLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIAC 193
Cdd:NF040840 96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 194 LHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLGRANILSAIAlgiTEAPGLVDVS 273
Cdd:NF040840 176 WHREF-GFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGVA---EKGGEGTILD 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 566074967 274 CGGAVIRAFSRGSHHGYnklLCIRPQH--LSLTP-RSAYSNRFNATLQSVHWQGDLTHLLCDVaGETVRMVLTH 344
Cdd:NF040840 252 TGNIKIELPEEKKGKVR---IGIRPEDitISTEKvKTSARNEFKGKVEEIEDLGPLVKLTLDV-GIILVAFITR 321
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
19-361 |
2.88e-90 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 275.06 E-value: 2.88e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQN 98
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 99 YALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 179 LDAQIRHNMVEEIaclhRELPE---LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLGRANI 255
Cdd:PRK11432 167 LDANLRRSMREKI----RELQQqfnITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 256 LSAialgiTEAPGLVDVScGGAVIR--AFSRGSHHGyNKLLCIRPQHLSLTPRSAYSNRfnATLQSVHWQGDLTHLLCDV 333
Cdd:PRK11432 243 FPA-----TLSGDYVDIY-GYRLPRpaAFAFNLPDG-ECTVGVRPEAITLSEQGEESQR--CTIKHVAYMGPQYEVTVDW 313
|
330 340 350
....*....|....*....|....*....|.
gi 566074967 334 AGETvrmVLTHVNPL---PRVGDKLALWFEP 361
Cdd:PRK11432 314 HGQE---LLLQVNATqlqPDLGEHYYLEIHP 341
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-255 |
5.98e-90 |
|
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: 269.98 E-value: 5.98e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYhGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQN 98
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 99 YALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566074967 179 LDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLGRANI 255
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEF-GVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
13-226 |
7.62e-90 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 270.81 E-value: 7.62e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 13 SQGTSGIVLDSLRVAYH----GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPy 88
Cdd:COG1116 2 SAAAPALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 89 krGLAMVVQNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPR 168
Cdd:COG1116 81 --DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 169 VLLLDEPLSALDAQIRHNMVEEIACLHRELPeLTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETG-KTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
17-363 |
2.48e-89 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 272.87 E-value: 2.48e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 17 SGIVLDSLRVAYHGNV-VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMV 95
Cdd:PRK11650 2 AGLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 96 VQNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIaVR-PRVLLLDE 174
Cdd:PRK11650 82 FQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAI-VRePAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 175 PLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLGRA- 253
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRL-KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPa 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 254 -NILsaiALGITEAPGLVDVSCGGAVIRAFSRGSHHGYNKLLCIRPQHLSLTPRSAysnRFNATLQSVHWQGDLTHLLCD 332
Cdd:PRK11650 240 mNLL---DGRVSADGAAFELAGGIALPLGGGYRQYAGRKLTLGIRPEHIALSSAEG---GVPLTVDTVELLGADNLAHGR 313
|
330 340 350
....*....|....*....|....*....|.
gi 566074967 333 VAGETVRMVLTHvNPLPRVGDKLALWFEPDD 363
Cdd:PRK11650 314 WGGQPLVVRLPH-QERPAAGSTLWLHLPANQ 343
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
18-251 |
6.49e-88 |
|
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: 264.97 E-value: 6.49e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 18 GIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQ 97
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 98 NYALFPHLKVEDNVAFGLRAQKQ----PKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 174 EPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLG 251
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDEL-HVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
19-256 |
7.65e-87 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 262.43 E-value: 7.65e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQN 98
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 99 YALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 179 LDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLGRANIL 256
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEV-HVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
19-223 |
7.16e-85 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 256.63 E-value: 7.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGN----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPykrGLAM 94
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 95 VVQNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 566074967 175 PLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIM 223
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRET-GKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
23-369 |
1.54e-84 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 261.31 E-value: 1.54e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 23 SLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQNYALF 102
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 103 PHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQ 182
Cdd:PRK11607 104 PHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 183 IRHNMVEEIACLhRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLGRANILSAI--- 259
Cdd:PRK11607 184 LRDRMQLEVVDI-LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGVlke 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 260 ----ALgITEAPGLV---DVSCGGAVIrafsrgshHGYNKLLCIRPQHLSLTPRSAySNRFN-ATLQSVH--WQGDLT-- 327
Cdd:PRK11607 263 rqedGL-VIDSPGLVhplKVDADASVV--------DNVPVHVALRPEKIMLCEEPP-ADGCNfAVGEVIHiaYLGDLSiy 332
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 566074967 328 HLLCDvAGETVRMVLTHVN----PLPRVGDKLALWFEPDDAVLIEV 369
Cdd:PRK11607 333 HVRLK-SGQMISAQLQNAHryrkGLPTWGDEVRLCWEADSCVVLTV 377
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-294 |
2.43e-83 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 255.79 E-value: 2.43e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYK--RGLAMV 95
Cdd:COG1125 2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 96 VQNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGM--SDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:COG1125 82 IQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 174 EPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLGRA 253
Cdd:COG1125 162 EPFGALDPITREQLQDELLRLQREL-GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGAD 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 566074967 254 NILSaiALGITEAPGLVD-----VSCGGAVIRAFSRGSHHGYNKLL 294
Cdd:COG1125 241 RGLR--RLSLLRVEDLMLpepptVSPDASLREALSLMLERGVDWLL 284
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
27-362 |
7.83e-78 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 243.78 E-value: 7.83e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 27 AYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQNYALFPHLK 106
Cdd:PRK11000 12 AYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSYALYPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 107 VEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHN 186
Cdd:PRK11000 92 VAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 187 MVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLG--RANILSAIALGIT 264
Cdd:PRK11000 172 MRIEISRLHKRL-GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGspKMNFLPVKVTATA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 265 EAPGLVDVSCGGAV-IRAFSRGSHHGYNKLLCIRPQHlsLTPRSAYSNRFNATLQSVHWQGDLTHLLCDVagETVRMVLT 343
Cdd:PRK11000 251 IEQVQVELPNRQQVwLPVEGRGVQVGANMSLGIRPEH--LLPSDIADVTLEGEVQVVEQLGNETQIHIQI--PAIRQNLV 326
|
330 340
....*....|....*....|..
gi 566074967 344 HVNP---LPRVGDKLALWFEPD 362
Cdd:PRK11000 327 YRQNdvvLVEEGATFAIGLPPE 348
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
19-252 |
1.99e-77 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 238.12 E-value: 1.99e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGnvvlKPL--SLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVV 96
Cdd:COG3840 2 LRLDDLTYRYGD----FPLrfDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 97 QNYALFPHLKVEDNVAFGLR-------AQKQpkalineRVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIaVRPR- 168
Cdd:COG3840 78 QENNLFPHLTVAQNIGLGLRpglkltaEQRA-------QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCL-VRKRp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 169 VLLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAE 248
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCRER-GLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAA 228
|
....
gi 566074967 249 FLGR 252
Cdd:COG3840 229 YLGI 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
19-252 |
7.13e-77 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 236.81 E-value: 7.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYK--RGLAMV 95
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 96 VQNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSD--YAARYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 566074967 174 EPLSALDAQIRHNMVEEIACLHRELPElTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLGR 252
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGK-TIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
33-262 |
5.36e-76 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 238.44 E-value: 5.36e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQNYALFPHLKVEDNVA 112
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 113 FGL----RAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMV 188
Cdd:PRK10851 97 FGLtvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 566074967 189 EEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLGRANILSAIALG 262
Cdd:PRK10851 177 RWLRQLHEEL-KFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNRLQGTIRG 249
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
19-252 |
1.04e-75 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 233.73 E-value: 1.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVT----HLPPYKRGLAM 94
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 95 VVQNYALFPHLKVEDNVAFGLR-AQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIkVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 174 EPLSALDAQirhnMVEEIACLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLG 251
Cdd:COG1126 162 EPTSALDPE----LVGEVLDVMRDLAKegMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLS 237
|
.
gi 566074967 252 R 252
Cdd:COG1126 238 K 238
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
19-241 |
4.25e-72 |
|
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: 224.47 E-value: 4.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLP-----PYKRGLA 93
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekelyELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 94 MVVQNYALFPHLKVEDNVAFGLRAQ-KQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 566074967 173 DEPLSALDAQIRHNMVEEIACLHRELPeLTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELRDELG-LTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
19-241 |
1.99e-71 |
|
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: 222.59 E-value: 1.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYH-GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVT--HLPPYKRGLAMV 95
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkkNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 96 VQN--YALFpHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:COG1122 81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 174 EPLSALDAQIRHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKE--GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
38-249 |
4.34e-71 |
|
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: 222.90 E-value: 4.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP------YKRGLAMVVQNYALFPHLKVEDNV 111
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelrelRRKKISMVFQSFALLPHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 112 AFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEI 191
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDEL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 192 ACLHRELPElTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEF 249
Cdd:cd03294 204 LRLQAELQK-TIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-241 |
1.26e-70 |
|
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: 229.40 E-value: 1.26e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 7 AVHAPASQGTSGIVLDSLRVAYHGN-----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTD 81
Cdd:COG1123 249 RAAPAAAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 82 VTHLP-----PYKRGLAMVVQN--YALFPHLKVEDNVAFGLRAQKQ-PKALINERVTQALKTVGMS-DYAARYPHQLSGG 152
Cdd:COG1123 329 LTKLSrrslrELRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYPHELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 153 QQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQREL-GLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
....*....
gi 566074967 233 ETRALYQHP 241
Cdd:COG1123 488 PTEEVFANP 496
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
38-325 |
4.88e-69 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 220.74 E-value: 4.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDV------THLPPYKRGLAMVVQNYALFPHLKVEDNV 111
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargIFLPPHRRRIGYVFQEARLFPHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 112 AFGLRAQKQPKALIN-ERVTQALktvGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEE 190
Cdd:COG4148 99 LYGRKRAPRAERRISfDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 191 IACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLGRANILSAIALGITEAPGLV 270
Cdd:COG4148 176 LERLRDEL-DIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVAAHDPDYGLT 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 566074967 271 DVSCGGAVIRAFSRGSHHGYNKLLCIRPQH--LSLTPRSAYS--NRFNATLQSVHWQGD 325
Cdd:COG4148 255 RLALGGGRLWVPRLDLPPGTRVRVRIRARDvsLALEPPEGSSilNILPGRVVEIEPADG 313
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
19-226 |
8.48e-68 |
|
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: 212.77 E-value: 8.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTH----LPPYKRGLAM 94
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkknINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 95 VVQNYALFPHLKVEDNVAFGLR-AQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 566074967 174 EPLSALDAQirhnMVEEIACLHRELPE--LTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:cd03262 161 EPTSALDPE----LVGEVLDVMKDLAEegMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-251 |
4.57e-67 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 211.97 E-value: 4.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAY----HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP--YKRGL 92
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkaFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 93 AMVVQNY--ALFPHLKVEDNVAFGLRAQKQPKalINERVTQALKTVGM-SDYAARYPHQLSGGQQQRVAIARAIAVRPRV 169
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLPD--REERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 170 LLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEF 249
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREER-GLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTREL 238
|
..
gi 566074967 250 LG 251
Cdd:COG1124 239 LA 240
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
30-255 |
6.48e-66 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 212.79 E-value: 6.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 30 GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP------YKRGLAMVVQNYALFP 103
Cdd:TIGR01186 5 GKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 104 HLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:TIGR01186 85 HMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 184 RHNMVEEIACLHRELPElTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLGRANI 255
Cdd:TIGR01186 165 RDSMQDELKKLQATLQK-TIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDL 235
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
21-232 |
1.36e-65 |
|
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: 207.36 E-value: 1.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 21 LDSLRVAYHG----NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLP-----PYKRG 91
Cdd:cd03257 4 VKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 92 LAMVVQNY--ALFPHLKVEDNVAFGLRAQKQP--KALINERVTQALKTVGMS-DYAARYPHQLSGGQQQRVAIARAIAVR 166
Cdd:cd03257 84 IQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 167 PRVLLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQEEL-GLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
19-237 |
7.23e-65 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 206.07 E-value: 7.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP-YKRGLAMVVQ 97
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAeVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 98 NYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 178 ALDAQIRHNMVEEIaclhRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:COG1131 161 GLDPEARRELWELL----RELAAegKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-242 |
1.28e-64 |
|
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: 205.43 E-value: 1.28e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYK-----RGLA 93
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 94 MVVQNYALFPHLKVEDNVAFGLRAQKQ-PKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 173 DEPLSALDAQIRHNMVEEIACLHRELPeLTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPP 242
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELG-LTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
19-228 |
2.36e-64 |
|
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: 203.88 E-value: 2.36e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGN----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRG--- 91
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 92 ---LAMVVQNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPR 168
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 169 VLLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALtLADKIGIMKDGSL 228
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEA-GTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
19-230 |
3.77e-64 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 203.74 E-value: 3.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYH-GNV---VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRG--- 91
Cdd:COG1136 5 LELRNLTKSYGtGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 92 ---LAMVVQNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPR 168
Cdd:COG1136 85 rrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 169 VLLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQtEALTLADKIGIMKDGSLIA 230
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNREL-GTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-223 |
3.79e-64 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 205.10 E-value: 3.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 17 SGIVLDSLRVAYHGNV----VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHlPPYKRGL 92
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 93 amVVQNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:COG4525 81 --VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 566074967 173 DEPLSALDAQIRHNMVEEIACLHRElPELTILYVTHDQTEALTLADKIGIM 223
Cdd:COG4525 159 DEPFGALDALTREQMQELLLDVWQR-TGKGVFLITHSVEEALFLATRLVVM 208
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-287 |
4.28e-64 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 207.24 E-value: 4.28e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGN----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP-----YK 89
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelraAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 90 RGLAMVVQNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRV 169
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 170 LLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEF 249
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINREL-GLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 566074967 250 LGRaniLSAIALGITEAPGLVDVSCGGAVIRAFSRGSH 287
Cdd:COG1135 241 LPT---VLNDELPEELLARLREAAGGGRLVRLTFVGES 275
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
19-256 |
1.26e-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: 203.35 E-value: 1.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRG--LAMVV 96
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELArrIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 97 QNYALFPHLKVEDNVAFG----LRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:COG1120 82 QEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 173 DEPLSALDaqIRH--NMVEEIACLHRELPeLTILYVTHDQTEALTLADKIGIMKDGSLIAHGET---------RALYQHP 241
Cdd:COG1120 162 DEPTSHLD--LAHqlEVLELLRRLARERG-RTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPeevltpellEEVYGVE 238
|
250
....*....|....*
gi 566074967 242 PNRFAAEFLGRANIL 256
Cdd:COG1120 239 ARVIEDPVTGRPLVL 253
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
28-226 |
2.80e-63 |
|
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: 199.72 E-value: 2.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 28 YHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVT----HLPPYKRGLAMVVQNYALFP 103
Cdd:cd03229 10 YGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGMVFQDFALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 104 HLKVEDNVAFGlraqkqpkalinervtqalktvgmsdyaaryphqLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:cd03229 90 HLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 566074967 184 RHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:cd03229 136 RREVRALLKSLQAQL-GITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
43-232 |
9.37e-63 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 199.83 E-value: 9.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 43 PGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDT------DVTHLPPYKRGLAMVVQNYALFPHLKVEDNVAFGLR 116
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 117 AQKQPKALIneRVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIACLHR 196
Cdd:cd03297 102 RKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 566074967 197 ELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03297 180 NL-NIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
20-226 |
1.05e-62 |
|
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: 199.62 E-value: 1.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 20 VLDSLRVAYHG--NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGL--AMV 95
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 96 VQN--YALFpHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:cd03225 81 FQNpdDQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 566074967 174 EPLSALDAQIRHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAE--GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-253 |
1.53e-62 |
|
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: 208.22 E-value: 1.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHG--NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAG---GRILIGDTDVTHLPPYKRG-- 91
Cdd:COG1123 5 LEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 92 LAMVVQN--YALFPhLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRV 169
Cdd:COG1123 85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 170 LLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEF 249
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRER-GTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVPR 242
|
....
gi 566074967 250 LGRA 253
Cdd:COG1123 243 LGAA 246
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
30-210 |
1.43e-60 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 194.50 E-value: 1.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 30 GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHL-----PPYKRGLAMVVQNYALFPH 104
Cdd:COG2884 14 GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrreiPYLRRRIGVVFQDFRLLPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 105 LKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQir 184
Cdd:COG2884 94 RTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPE-- 171
|
170 180
....*....|....*....|....*...
gi 566074967 185 hnMVEEIACLHRELPEL--TILYVTHDQ 210
Cdd:COG2884 172 --TSWEIMELLEEINRRgtTVLIATHDL 197
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
19-237 |
1.44e-60 |
|
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: 194.71 E-value: 1.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFV-----QPAGGRILIGDTDVTHLPP----YK 89
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVdvleLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 90 RGLAMVVQNYALFPhLKVEDNVAFGLRAQ-KQPKALINERVTQALKTVGMSDYAAR--YPHQLSGGQQQRVAIARAIAVR 166
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHgIKLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 566074967 167 PRVLLLDEPLSALDAQIRHNMVEEIACLHRelpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKK---EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
19-241 |
1.71e-60 |
|
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: 194.72 E-value: 1.71e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGN----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYK----- 89
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 90 RGLAMVVQNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRV 169
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 170 LLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINREL-GLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
19-239 |
4.89e-59 |
|
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: 191.22 E-value: 4.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP-YKRGLAMVVQ 97
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 98 NYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 178 ALDAQIRHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQ 239
Cdd:COG4555 162 GLDVMARRLLREILRALKKE--GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-234 |
4.92e-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: 4.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLppyKRGLAMVVQN 98
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA---RRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 99 YAL---FPhLKVEDNVAFGLRAQ----KQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:COG1121 84 AEVdwdFP-ITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 566074967 172 LDEPLSALDAQIRHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGsLIAHGET 234
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRRE--GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPP 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
18-214 |
4.93e-59 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 190.00 E-value: 4.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 18 GIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQP---AGGRILIGDTDVTHLPPYKRGLAM 94
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 95 VVQNYALFPHLKVEDNVAFGL-----RAQKQpkalinERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRV 169
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALpptigRAQRR------ARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 566074967 170 LLLDEPLSALDA----QIRHNMVEEIAclHRELPelTILyVTHDQTEAL 214
Cdd:COG4136 155 LLLDEPFSKLDAalraQFREFVFEQIR--QRGIP--ALL-VTHDEEDAP 198
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
28-263 |
5.58e-57 |
|
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: 186.48 E-value: 5.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 28 YHGN--VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDV---THLPPYKRGLAMVVQNyalf 102
Cdd:TIGR04520 10 YPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeENLWEIRKKVGMVFQN---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 103 PH-----LKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:TIGR04520 86 PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 178 ALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALtLADKIGIMKDGSLIAHGetralyqhPPnrfaAEFLGRANILS 257
Cdd:TIGR04520 166 MLDPKGRKEVLETIRKLNKEE-GITVISITHDMEEAV-LADRVIVMNKGKIVAEG--------TP----REIFSQVELLK 231
|
....*.
gi 566074967 258 AIALGI 263
Cdd:TIGR04520 232 EIGLDV 237
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
17-252 |
4.18e-56 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 183.80 E-value: 4.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 17 SGIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPY--KRGL-- 92
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqQKGLir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 93 ------AMVVQNYALFPHLKVEDNVAFG-LRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAV 165
Cdd:PRK11264 82 qlrqhvGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 166 RPRVLLLDEPLSALDAQirhnMVEEIACLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPN 243
Cdd:PRK11264 162 RPEVILFDEPTSALDPE----LVGEVLNTIRQLAQekRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
....*....
gi 566074967 244 RFAAEFLGR 252
Cdd:PRK11264 238 PRTRQFLEK 246
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
19-237 |
4.19e-56 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 183.72 E-value: 4.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNV-VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP-----YKRGL 92
Cdd:COG3638 3 LELRNLSKRYPGGTpALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralrrLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 93 AMVVQNYALFPHLKVEDNVAFGLRAQK-QPKALIN-------ERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIA 164
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGRLGRTsTWRSLLGlfppedrERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 566074967 165 VRPRVLLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:COG3638 163 QEPKLILADEPVASLDPKTARQVMDLLRRIARED-GITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
31-250 |
1.36e-55 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 182.21 E-value: 1.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 31 NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGL----AMVVQNYALFPHLK 106
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQFYLFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 107 VEDNVAFG-LRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRH 185
Cdd:PRK09493 94 ALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRH 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 566074967 186 nmveEIACLHRELPE--LTILYVTHDqteaLTLADKIG---IMKDGSLIAH-GETRALYQHPPNRFAAEFL 250
Cdd:PRK09493 174 ----EVLKVMQDLAEegMTMVIVTHE----IGFAEKVAsrlIFIDKGRIAEdGDPQVLIKNPPSQRLQEFL 236
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
38-241 |
1.53e-55 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 184.94 E-value: 1.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLP-----PYKRGLAMVVQN-YA-LFPHLKVEDN 110
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgrelrPLRRRMQMVFQDpYAsLNPRMTVGDI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAFGLRAQKQ-PKALINERVTQALKTVGMS-DYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD----AQIR 184
Cdd:COG4608 118 IAEPLRIHGLaSKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQVL 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 566074967 185 hNMVEEiacLHRELpELTILYVTHDqteaLT----LADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:COG4608 198 -NLLED---LQDEL-GLTYLFISHD----LSvvrhISDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
24-252 |
3.08e-55 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 181.34 E-value: 3.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 24 LRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRA------------VAGFVQPAGGRILIGDTDVTHLppyKRG 91
Cdd:TIGR00972 7 LNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSlnrmndlvpgvrIEGKVLFDGQDIYDKKIDVVEL---RRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 92 LAMVVQNYALFPhLKVEDNVAFGLRAQK-QPKALINERVTQALKTVGM----SDYAARYPHQLSGGQQQRVAIARAIAVR 166
Cdd:TIGR00972 84 VGMVFQKPNPFP-MSIYDNIAYGPRLHGiKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARALAVE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 167 PRVLLLDEPLSALDAqIRHNMVEEiacLHRELPE-LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRF 245
Cdd:TIGR00972 163 PEVLLLDEPTSALDP-IATGKIEE---LIQELKKkYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKR 238
|
....*...
gi 566074967 246 AAEFL-GR 252
Cdd:TIGR00972 239 TEDYIsGR 246
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-241 |
6.48e-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: 181.50 E-value: 6.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGN-----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTH-----LPPY 88
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkkkLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 89 KRGLAMVVQN--YALFpHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMS-DYAARYPHQLSGGQQQRVAIARAIAV 165
Cdd:TIGR04521 81 RKKVGLVFQFpeHQLF-EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 166 RPRVLLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEK-GLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-241 |
1.03e-54 |
|
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: 182.56 E-value: 1.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 24 LRVAYH---GNV-VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQP---AGGRILIGDTDVTHLPP------YKR 90
Cdd:COG0444 7 LKVYFPtrrGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkelrkiRGR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 91 GLAMVVQN-Y-ALFPHLKVEDNVAFGLRA-QKQPKALINERVTQALKTVGMSD---YAARYPHQLSGGQQQRVAIARAIA 164
Cdd:COG0444 87 EIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVMIARALA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566074967 165 VRPRVLLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:COG0444 167 LEPKLLIADEPTTALDVTIQAQILNLLKDLQREL-GLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENP 242
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
34-177 |
2.21e-54 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 175.91 E-value: 2.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTH--LPPYKRGLAMVVQNYALFPHLKVEDNV 111
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 112 AFGLRAQKQPKALINERVTQALKTVGMSDYAAR----YPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
37-232 |
5.87e-54 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 176.91 E-value: 5.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 37 LSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQNYALFPHLKVEDNVAFGLR 116
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 117 AQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIaVRPR-VLLLDEPLSALDAQIRHNMVEEIACLH 195
Cdd:cd03298 97 PGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVL-VRDKpVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 566074967 196 RElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03298 176 AE-TKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
21-232 |
7.68e-54 |
|
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: 177.63 E-value: 7.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 21 LDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKR---GLAMVVQ 97
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 98 NYALFPHLKVEDNVAFGLRAQKQPKAL----------INERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRP 167
Cdd:cd03219 83 IPRLFPELTVLENVMVAAQARTGSGLLlararreereARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566074967 168 RVLLLDEPLSALDAQIRHNMVEEIaclhRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELI----RELRErgITVLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
19-228 |
9.54e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 176.16 E-value: 9.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP--YKRGLAMVV 96
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpeWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 97 QNYALFPHlKVEDNVAFGLRAQKQPkaLINERVTQALKTVGMSDYAARYP-HQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERK--FDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 566074967 176 LSALDAQIRHnMVEEIacLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSL 228
Cdd:COG4619 158 TSALDPENTR-RVEEL--LREYLAEegRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
38-234 |
7.61e-53 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 174.28 E-value: 7.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQNYALFPHLKVEDNVAFGLRA 117
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 118 QKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIaVRPR-VLLLDEPLSALDAQIRHNMVEEIACLHR 196
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCL-VRPNpILLLDEPFSALDPLLREEMLALVKQLCS 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 566074967 197 ElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGET 234
Cdd:TIGR01277 177 E-RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-252 |
8.58e-53 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 175.61 E-value: 8.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 10 APASQGTSGIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRA-------VAGF-VQpagGRILIGDTD 81
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGArVE---GEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 82 VthlppYKRGL---------AMVVQNYALFPHlKVEDNVAFGLRAQ-KQPKALINERVTQALKTVG--------MSDYAA 143
Cdd:COG1117 80 I-----YDPDVdvvelrrrvGMVFQKPNPFPK-SIYDNVAYGLRLHgIKSKSELDEIVEESLRKAAlwdevkdrLKKSAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 144 RyphqLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD----AQIrhnmvEEiacLHREL-PELTILYVTHDQTEALTLAD 218
Cdd:COG1117 154 G----LSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistAKI-----EE---LILELkKDYTIVIVTHNMQQAARVSD 221
|
250 260 270
....*....|....*....|....*....|....*
gi 566074967 219 KIGIMKDGSLIAHGETRALYQHPPNRFAAEFL-GR 252
Cdd:COG1117 222 YTAFFYLGELVEFGPTEQIFTNPKDKRTEDYItGR 256
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
21-232 |
8.90e-53 |
|
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: 173.01 E-value: 8.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 21 LDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVqnya 100
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 101 lfphlkvednvafglraqkqpkalinerVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:cd03214 78 ----------------------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 566074967 181 AQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03214 130 IAHQIELLELLRRLARER-GKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
21-232 |
1.53e-52 |
|
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: 173.49 E-value: 1.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 21 LDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPpykRGLAMVVQNYA 100
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---KRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 101 L---FPhLKVEDNVAFGL----RAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:cd03235 79 IdrdFP-ISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 566074967 174 EPLSALDAQIRHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIgIMKDGSLIAHG 232
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRRE--GMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
21-232 |
2.67e-52 |
|
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: 174.07 E-value: 2.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 21 LDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKR---GLAMVVQ 97
Cdd:COG0411 7 VRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlGIARTFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 98 NYALFPHLKVEDNVAFGLRAQKQPKAL---------------INERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARA 162
Cdd:COG0411 87 NPRLFPELTVLENVLVAAHARLGRGLLaallrlprarreereARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 163 IAVRPRVLLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPEETEELAELIRRLRDER-GITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
34-287 |
1.24e-51 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 174.99 E-value: 1.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP-----YKRGLAMVVQNYALFPHLKVE 108
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrkARRQIGMIFQHFNLLSSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 109 DNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMV 188
Cdd:PRK11153 101 DNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSIL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 189 EEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFlgranILSAIALGITEApg 268
Cdd:PRK11153 181 ELLKDINREL-GLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF-----IQSTLHLDLPED-- 252
|
250 260
....*....|....*....|....*
gi 566074967 269 LVD------VSCGGAVIRAFSRGSH 287
Cdd:PRK11153 253 YLArlqaepTTGSGPLLRLEFTGES 277
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
19-240 |
1.45e-51 |
|
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: 171.98 E-value: 1.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP-----YKRGL 92
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 93 AMVVQNYALFPHLKVEDNVAFGLRAQKQP-KALIN-------ERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIA 164
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRSTwRSLFGlfpkeekQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 165 VRPRVLLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQH 240
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREE-GITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
14-226 |
3.68e-51 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 171.40 E-value: 3.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 14 QGTSgIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRgla 93
Cdd:PRK11247 9 QGTP-LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 94 MVVQNYALFPHLKVEDNVAFGLRAQKQPKALinervtQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 566074967 174 EPLSALDAQIRHNMVEEIACLHRElPELTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQ-HGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
21-247 |
4.10e-51 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 171.04 E-value: 4.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 21 LDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHlPPYKRGLamVVQNYA 100
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 101 LFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 181 AQIRHNMVEEIACLHRELPElTILYVTHDQTEALTLADKIgimkdgSLIAHGETRALYQHPPN---RFAA 247
Cdd:PRK11248 161 AFTREQMQTLLLKLWQETGK-QVLLITHDIEEAVFMATEL------VLLSPGPGRVVERLPLNfarRFVA 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
38-237 |
4.12e-50 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 167.84 E-value: 4.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQNYALFPHLKVEDNVAFGL-- 115
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 116 -----RAQKQpkalineRVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNM--- 187
Cdd:PRK10771 99 glklnAAQRE-------KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMltl 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 566074967 188 VEEIaCLHRelpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:PRK10771 172 VSQV-CQER---QLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
30-279 |
5.63e-50 |
|
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: 171.06 E-value: 5.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 30 GNVVLKpLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDV------THLPPYKRGLAMVVQNYALFP 103
Cdd:TIGR02142 10 GDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkgIFLPPEKRRIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 104 HLKVEDNVAFGLRAQKQPKALIN-ERVTQALktvGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQ 182
Cdd:TIGR02142 89 HLSVRGNLRYGMKRARPSERRISfERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 183 IRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALyQHPPNRFAAEFLGRANILSAIALG 262
Cdd:TIGR02142 166 RKYEILPYLERLHAEF-GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV-WASPDLPWLAREDQGSLIEGVVAE 243
|
250
....*....|....*..
gi 566074967 263 ITEAPGLVDVSCGGAVI 279
Cdd:TIGR02142 244 HDQHYGLTALRLGGGHL 260
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
34-241 |
1.41e-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: 174.10 E-value: 1.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVqPAGGRILIGDTDVTHLP-----PYKRGLAMVVQN-YA-LFPHLK 106
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrralrPLRRRMQVVFQDpFGsLSPRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 107 VEDNVAFGLRAQ--KQPKALINERVTQALKTVGMS-DYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:COG4172 381 VGQIIAEGLRVHgpGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 184 RHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:COG4172 461 QAQILDLLRDLQREH-GLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
18-250 |
1.84e-49 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 166.34 E-value: 1.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 18 GIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDT--DVTHLPPYKRGLA-- 93
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAIRLlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 94 ----MVVQNYALFPHLKVEDN-VAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPR 168
Cdd:COG4161 82 qkvgMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 169 VLLLDEPLSALDAQIRHNMVEEIaclhRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGeTRALYQHPPNRFA 246
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEII----RELSQtgITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQPQTEAF 236
|
....
gi 566074967 247 AEFL 250
Cdd:COG4161 237 AHYL 240
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
19-228 |
2.29e-49 |
|
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: 163.72 E-value: 2.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP-YKRGLAMVVQ 97
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEeVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 98 NYALFPHLKVEDNVafglraqkqpkalinervtqalktvgmsdyaaryphQLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 566074967 178 ALDAQIRHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGSL 228
Cdd:cd03230 125 GLDPESRREFWELLRELKKE--GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-237 |
2.76e-49 |
|
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: 165.30 E-value: 2.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 21 LDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKR---GLAMVVQ 97
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 98 NYALFPHLKVEDN--VAFGLRAQKQPKALInERVTQ---ALKTvgMSDYAARyphQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:cd03224 83 GRRIFPELTVEENllLGAYARRRAKRKARL-ERVYElfpRLKE--RRKQLAG---TLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 566074967 173 DEPLSALDAQIRHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDE--GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
34-226 |
1.09e-48 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 164.18 E-value: 1.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKrglaMVV-QNYALFPHLKVEDNVA 112
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR----MVVfQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 113 FGLRA--QKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEE 190
Cdd:TIGR01184 77 LAVDRvlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 566074967 191 IACLHRElPELTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:TIGR01184 157 LMQIWEE-HRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
34-240 |
4.71e-48 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 164.03 E-value: 4.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPY--KRGLAMVVQNY-ALFPHLKVEDN 110
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWdvRRQVGMVFQNPdNQFVGATVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEE 190
Cdd:PRK13635 103 VAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLET 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 566074967 191 IACLHRELpELTILYVTHDQTEALTlADKIGIMKDGSLIAHGETRALYQH 240
Cdd:PRK13635 183 VRQLKEQK-GITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
21-251 |
8.75e-48 |
|
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: 161.69 E-value: 8.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 21 LDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKR---GLAMVVQ 97
Cdd:COG0410 6 VENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 98 NYALFPHLKVEDN---VAFGLRAQKQPKALInERVTQ---ALKtvgmsDYAARYPHQLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:COG0410 86 GRRIFPSLTVEENlllGAYARRDRAEVRADL-ERVYElfpRLK-----ERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 172 LDEPLSALDAQIRHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPpnRFAAEFLG 251
Cdd:COG0410 160 LDEPSLGLAPLIVEEIFEIIRRLNRE--GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP--EVREAYLG 235
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-240 |
1.18e-47 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 169.55 E-value: 1.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 10 APASQGTSGIVLDSLRVAYH-GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP- 87
Cdd:COG4988 328 PLPAAGPPSIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPa 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 88 -YKRGLAMVVQNYALFpHLKVEDNVAFGlraqkQPKAlINERVTQALKTVGMSDYAARYPH-----------QLSGGQQQ 155
Cdd:COG4988 408 sWRRQIAWVPQNPYLF-AGTIRENLRLG-----RPDA-SDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQ 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 156 RVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIACLHRelpELTILYVTHDqTEALTLADKIGIMKDGSLIAHGETR 235
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK---GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHE 556
|
....*
gi 566074967 236 ALYQH 240
Cdd:COG4988 557 ELLAK 561
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
27-226 |
3.13e-47 |
|
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: 159.72 E-value: 3.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 27 AYHGNV-VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHL-----PPYKRGLAMVVQNYA 100
Cdd:TIGR02673 10 AYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLrgrqlPLLRRRIGVVFQDFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 101 LFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:TIGR02673 90 LLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 566074967 181 AQirhnMVEEIACLHRELPE--LTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:TIGR02673 170 PD----LSERILDLLKRLNKrgTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
19-213 |
3.51e-47 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 159.18 E-value: 3.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP-YKRGLAMVVQ 97
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 98 NYALFPHLKVEDNVAFGLRAQKQPKAliNERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 566074967 178 ALDAQIRHnMVEEIACLHRELpELTILYVTHDQTEA 213
Cdd:COG4133 161 ALDAAGVA-LLAELIAAHLAR-GGAVLLTTHQPLEL 194
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-237 |
6.25e-47 |
|
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: 159.21 E-value: 6.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHG--NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDV-THLPPYKRGLAMV 95
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 96 VQNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 176 LSALDAQIRHNMVEeiaCLHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:cd03263 161 TSGLDPASRRAIWD---LILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
19-240 |
7.37e-47 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 159.77 E-value: 7.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTH-----LPPYKRGL 92
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrgkkLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 93 AMVVQNYALFPHLKVEDNVAFG-LRAQKQPKALIN-------ERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIA 164
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGrLGYKPTWRSLLGrfseedkERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 165 VRPRVLLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQH 240
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKED-GITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
34-255 |
2.18e-46 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 162.90 E-value: 2.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP------YKRGLAMVVQNYALFPHLKV 107
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 108 EDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNM 187
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 188 VEEIACLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLGRANI 255
Cdd:PRK10070 204 QDELVKLQAK-HQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDI 270
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-232 |
2.28e-46 |
|
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: 168.09 E-value: 2.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 6 TAVHAPASQGTsgIVLDSLRVAYHGNV--VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVT 83
Cdd:COG2274 463 SKLSLPRLKGD--IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLR 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 84 HLPP--YKRGLAMVVQNYALFpHLKVEDNVAFGlraqkQPKALInERVTQALKTVGMSDYAARYPH-----------QLS 150
Cdd:COG2274 541 QIDPasLRRQIGVVLQDVFLF-SGTIRENITLG-----DPDATD-EEIIEAARLAGLHDFIEALPMgydtvvgeggsNLS 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 151 GGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMveeIACLHRELPELTILYVTHDqTEALTLADKIGIMKDGSLIA 230
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAII---LENLRRLLKGRTVIIIAHR-LSTIRLADRIIVLDKGRIVE 689
|
..
gi 566074967 231 HG 232
Cdd:COG2274 690 DG 691
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
24-226 |
2.53e-46 |
|
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: 155.48 E-value: 2.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 24 LRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP--YKRGLAMVvqnyal 101
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeeLRRRIGYV------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 102 fphlkvednvafglraqkqpkalinervtqalktvgmsdyaarypHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDA 181
Cdd:cd00267 79 ---------------------------------------------PQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 566074967 182 QIRHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:cd00267 114 ASRERLLELLRELAEE--GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
24-232 |
2.71e-46 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 158.74 E-value: 2.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 24 LRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYK--RGLAMVVQNYAL 101
Cdd:COG4559 7 LSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 102 -FPhLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIA-------VRPRVLLLD 173
Cdd:COG4559 87 aFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 174 EPLSALDaqIRH-NMVEEIAclhRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:COG4559 166 EPTSALD--LAHqHAVLRLA---RQLARrgGGVVAVLHDLNLAAQYADRILLLHQGRLVAQG 222
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-209 |
3.15e-46 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 158.43 E-value: 3.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 3 MKTTAVHApasqgtsgIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDV 82
Cdd:COG4598 1 MTDTAPPA--------LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 83 tHLPPYKRG----------------LAMVVQNYALFPHLKVEDNVAFG-LRAQKQPKALINERVTQALKTVGMSDYAARY 145
Cdd:COG4598 73 -RLKPDRDGelvpadrrqlqrirtrLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAY 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 146 PHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQirhnMVEEIACLHRELPE--LTILYVTHD 209
Cdd:COG4598 152 PAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPE----LVGEVLKVMRDLAEegRTMLVVTHE 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
17-241 |
7.47e-46 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 156.73 E-value: 7.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 17 SGIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKR---GLA 93
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 94 MVVQNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 174 EPLSALD--AqirhnmVEEIACLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:COG1137 162 EPFAGVDpiA------VADIQKIIRHLKErgIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-232 |
4.85e-45 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 162.64 E-value: 4.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 4 KTTAVHAPASQGtsGIVLDSLRVAYHGNV-VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDV 82
Cdd:COG1132 327 PPGAVPLPPVRG--EIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 83 THLPP--YKRGLAMVVQNYALFpHLKVEDNVAFGlraqkQPKALiNERVTQALKTVGMSDYAARYPH-----------QL 149
Cdd:COG1132 405 RDLTLesLRRQIGVVPQDTFLF-SGTIRENIRYG-----RPDAT-DEEVEEAAKAAQAHEFIEALPDgydtvvgergvNL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 150 SGGQQQRVAIARAIAVRPRVLLLDEPLSALD----AQIRHNmveeiacLHRELPELTILYVTHdQTEALTLADKIGIMKD 225
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDteteALIQEA-------LERLMKGRTTIVIAH-RLSTIRNADRILVLDD 549
|
....*..
gi 566074967 226 GSLIAHG 232
Cdd:COG1132 550 GRIVEQG 556
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-246 |
1.24e-44 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 154.02 E-value: 1.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDT--DVTHLPPYKRGLA--- 93
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKAIRElrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 94 ---MVVQNYALFPHLKVEDN-VAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRV 169
Cdd:PRK11124 83 nvgMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 566074967 170 LLLDEPLSALDAQIRHNMVEEIaclhRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFA 246
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSII----RELAEtgITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQPQTEAFK 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-226 |
1.52e-44 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 151.00 E-value: 1.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGN--VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP--YKRGLAM 94
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLesLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 95 VVQNYALFpHLKVEDNVafglraqkqpkalinervtqalktvgmsdyaaryphqLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 566074967 175 PLSALDAQIRHNMVEEIaclHRELPELTILYVTHDqTEALTLADKIGIMKDG 226
Cdd:cd03228 123 ATSALDPETEALILEAL---RALAKGKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
28-241 |
2.84e-44 |
|
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: 152.70 E-value: 2.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 28 YHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKR---GLAMVVQNYALFPH 104
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYLPQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 105 LKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIr 184
Cdd:cd03218 90 LTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 566074967 185 hnmVEEIACLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:cd03218 169 ---VQDIQKIIKILKDrgIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-232 |
4.54e-44 |
|
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: 161.57 E-value: 4.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 4 KTTAVHAPASQGtsGIVLDSLRVAYHGNV--VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTD 81
Cdd:TIGR03375 451 GTRFLHRPRLQG--EIEFRNVSFAYPGQEtpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVD 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 82 VTHLPPY--KRGLAMVVQNYALFpHLKVEDNVAFGLRAqkqpkaLINERVTQALKTVGMSDYAARYPH-----------Q 148
Cdd:TIGR03375 529 IRQIDPAdlRRNIGYVPQDPRLF-YGTLRDNIALGAPY------ADDEEILRAAELAGVTEFVRRHPDgldmqigergrS 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 149 LSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEiacLHRELPELTILYVTHdQTEALTLADKIGIMKDGSL 228
Cdd:TIGR03375 602 LSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDR---LKRWLAGKTLVLVTH-RTSLLDLVDRIIVMDNGRI 677
|
....
gi 566074967 229 IAHG 232
Cdd:TIGR03375 678 VADG 681
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-238 |
8.31e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 152.96 E-value: 8.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGN---VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVT--HLPPYKRGLA 93
Cdd:PRK13650 5 IEVKNLTFKYKEDqekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 94 MVVQNY-ALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:PRK13650 85 MVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 173 DEPLSALDAQIRHNMVEEIACLhRELPELTILYVTHDQTEaLTLADKIGIMKDGSLIAHGETRALY 238
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGI-RDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
21-237 |
1.71e-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: 150.37 E-value: 1.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 21 LDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKR---GLAMVVQ 97
Cdd:TIGR03410 3 VSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 98 NYALFPHLKVEDNVAFGLRAQKQPKALINERVTQ---ALKtvgmsDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:TIGR03410 83 GREIFPRLTVEENLLTGLAALPRRSRKIPDEIYElfpVLK-----EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 175 PLSAldaqIRHNMVEEIACLHRELPE---LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:TIGR03410 158 PTEG----IQPSIIKDIGRVIRRLRAeggMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
28-220 |
2.14e-43 |
|
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: 149.30 E-value: 2.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 28 YHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP------YKRGLAMVVQNYAL 101
Cdd:TIGR03608 8 FGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSkkaskfRREKLGYLFQNFAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 102 FPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDA 181
Cdd:TIGR03608 88 IENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 566074967 182 QIRHnmveEIACLHRELPE--LTILYVTHDqTEALTLADKI 220
Cdd:TIGR03608 168 KNRD----EVLDLLLELNDegKTIIIVTHD-PEVAKQADRV 203
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-232 |
5.26e-43 |
|
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: 148.89 E-value: 5.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAY--HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPY--KRGLAM 94
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 95 VVQNYALFpHLKVEDNVAFGLRAQKqpkaliNERVTQALKTVGMSDYAARYPH-----------QLSGGQQQRVAIARAI 163
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 566074967 164 AVRPRVLLLDEPLSALDAQIRHNMVEEiacLHRELPELTILYVTHdQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKER---LRQLLGDKTLIIITH-RPSLLDLVDRIIVMDSGRIVADG 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
24-232 |
1.07e-42 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 149.15 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 24 LRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYK--RGLAMVVQNYAL 101
Cdd:PRK13548 8 LSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 102 -FPhLKVEDNVAFGL----RAQKQPKALinerVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIA------VRPRVL 170
Cdd:PRK13548 88 sFP-FTVEEVVAMGRaphgLSRAEDDAL----VAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 566074967 171 LLDEPLSALDaqIRHNmvEEIACLHRELPE---LTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:PRK13548 163 LLDEPTSALD--LAHQ--HHVLRLARQLAHergLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
32-239 |
2.68e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 149.04 E-value: 2.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVT----HLPPYKRGLAMVVQ--NYALFPHl 105
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSDIRKKVGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 106 KVEDNVAFGLRAQKQPKALINERVTQALKTVGMS--DYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 184 RHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQ 239
Cdd:PRK13637 180 RDEILNKIKELHKEY-NMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
29-209 |
3.18e-42 |
|
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: 146.78 E-value: 3.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 29 HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHL-----PPYKRGLAMVVQNYALFP 103
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgraiPYLRRKIGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 104 HLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:cd03292 92 DRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDT 171
|
170 180
....*....|....*....|....*.
gi 566074967 184 RHNMVEEIACLHreLPELTILYVTHD 209
Cdd:cd03292 172 TWEIMNLLKKIN--KAGTTVVVATHA 195
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-242 |
5.49e-42 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 154.15 E-value: 5.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 9 HAPASQGTSGIVLDSLRVAYHGNV--VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLP 86
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 87 P--YKRGLAMVVQNYALFpHLKVEDNVAFGlraqkQPKAlINERVTQALKTVGMSDYAARYPH-----------QLSGGQ 153
Cdd:COG4987 404 EddLRRRIAVVPQRPHLF-DTTLRENLRLA-----RPDA-TDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 154 QQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEiacLHRELPELTILYVTHDQTeALTLADKIGIMKDGSLIAHGE 233
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD---LLEALAGRTVLLITHRLA-GLERMDRILVLEDGRIVEQGT 552
|
....*....
gi 566074967 234 TRALYQHPP 242
Cdd:COG4987 553 HEELLAQNG 561
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-241 |
8.43e-42 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 153.30 E-value: 8.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 21 LDSLRVAYHGN----VVLKPLSLTIEPGEVLALIGPSGSGKT----TVLRAVAGFVQPAGGRILIGDTDVTHLPPYK--- 89
Cdd:COG4172 9 VEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 90 -RG--LAMVVQN--YALFPHLKVEDNVAFGLRA-QKQPKALINERVTQALKTVGMSDYAAR---YPHQLSGGQQQRVAIA 160
Cdd:COG4172 89 iRGnrIAMIFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 161 RAIAVRPRVLLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDqteaLTL----ADKIGIMKDGSLIAHGETRA 236
Cdd:COG4172 169 MALANEPDLLIADEPTTALDVTVQAQILDLLKDLQREL-GMALLLITHD----LGVvrrfADRVAVMRQGEIVEQGPTAE 243
|
....*
gi 566074967 237 LYQHP 241
Cdd:COG4172 244 LFAAP 248
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
33-228 |
8.57e-42 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 145.63 E-value: 8.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPpYKRGLAM-------VVQNYALFPHL 105
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLS-YSQKIILrreligyIFQSFNLIPHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 106 KVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRH 185
Cdd:NF038007 99 SIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNAR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 566074967 186 NMVEEIACLHRElpELTILYVTHDQtEALTLADKIGIMKDGSL 228
Cdd:NF038007 179 AVLQQLKYINQK--GTTIIMVTHSD-EASTYGNRIINMKDGKL 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
19-234 |
9.05e-42 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 146.77 E-value: 9.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP--YKRGLAMVV 96
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSreLAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 97 QNYALFPHLKVEDNVAFGlR---AQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:COG4604 82 QENHINSRLTVRELVAFG-RfpySKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 566074967 174 EPLSALDaqIRHnMVEEIACLHRELPEL--TILYVTHDQTEALTLADKIGIMKDGSLIAHGET 234
Cdd:COG4604 161 EPLNNLD--MKH-SVQMMKLLRRLADELgkTVVIVLHDINFASCYADHIVAMKDGRVVAQGTP 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
34-241 |
1.59e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 147.09 E-value: 1.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVT------HLPPYKRGLAMVVQnyalFPHLK- 106
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQ----FPEHQl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 107 ----VEDNVAFGLRAQKQPKALINERVTQALKTVGMS-DYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDA 181
Cdd:PRK13634 99 feetVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 182 QIRHNMVEEIACLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:PRK13634 179 KGRKEMMEMFYKLHKE-KGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
19-236 |
5.42e-41 |
|
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: 144.11 E-value: 5.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGN----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPpyKRGLA- 93
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD--EDARAr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 94 -------MVVQNYALFPHLKVEDNVAFG--LRAQKQPKAlineRVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIA 164
Cdd:COG4181 87 lrarhvgFVFQSFQLLPTLTALENVMLPleLAGRRDARA----RARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 165 VRPRVLLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALtLADKIGIMKDGSLIAHGETRA 236
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRER-GTTLVLVTHDPALAA-RCDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
28-229 |
7.96e-41 |
|
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: 142.78 E-value: 7.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 28 YHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGlAMVVQN--YALFphl 105
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSI-GYVMQDvdYQLF--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 106 kvEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDaqiRH 185
Cdd:cd03226 86 --TDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD---YK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 566074967 186 NMvEEIACLHRELPEL--TILYVTHDQTEALTLADKIGIMKDGSLI 229
Cdd:cd03226 161 NM-ERVGELIRELAAQgkAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
19-237 |
1.45e-40 |
|
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: 142.51 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLP-PYKRGLAMVVQ 97
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPrEVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 98 NYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 178 ALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEF-GMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
32-232 |
3.99e-40 |
|
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: 141.35 E-value: 3.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLP-PYKRGLAMVVQNYALFPHLKVEDN 110
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRLGFVSDSTGLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEE 190
Cdd:cd03266 99 LEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 566074967 191 IaclhRELPEL--TILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03266 179 I----RQLRALgkCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
24-244 |
4.62e-40 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 142.22 E-value: 4.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 24 LRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRA------------VAGFVQPAGGRILIGDTDVTHLppyKRG 91
Cdd:PRK14239 11 LSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSinrmndlnpevtITGSIVYNGHNIYSPRTDTVDL---RKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 92 LAMVVQNYALFPhLKVEDNVAFGLR-AQKQPKALINERVTQALKTVGMSDYAARYPHQ----LSGGQQQRVAIARAIAVR 166
Cdd:PRK14239 88 IGMVFQQPNPFP-MSIYENVVYGLRlKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 167 PRVLLLDEPLSALDAqIRHNMVEEIacLHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNR 244
Cdd:PRK14239 167 PKIILLDEPTSALDP-ISAGKIEET--LLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHK 241
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
33-241 |
6.79e-40 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 141.90 E-value: 6.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHlPPYK---RGLAMVVQ--NYALFPHLKV 107
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY-GDYKyrcKHIRMIFQdpNTSLNPRLNI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 108 EDNVAFGLR------AQKQpkaliNERVTQALKTVGMS-DYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:COG4167 107 GQILEEPLRlntdltAEER-----EERIFATLRLVGLLpEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 566074967 181 AQIRHNMVEeiacLHRELPE---LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:COG4167 182 MSVRSQIIN----LMLELQEklgISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
27-237 |
1.51e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 146.32 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 27 AYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP---YKRGLAMVVQNYALFP 103
Cdd:COG1129 13 SFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaQAAGIAIIHQELNLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 104 HLKVEDNVAFGLRAQKQP---KALINERVTQALKTVGMS-DyaaryPHQ----LSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:COG1129 93 NLSVAENIFLGREPRRGGlidWRAMRRRARELLARLGLDiD-----PDTpvgdLSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566074967 176 LSALDAQirhnmveEIACLH---RELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:COG1129 168 TASLTER-------EVERLFriiRRLKAqgVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-250 |
1.90e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 140.75 E-value: 1.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 23 SLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRA------------VAGFVQPAGGRILIGDTDVTHLppyKR 90
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneearVEGEVRLFGRNIYSPDVDPIEV---RR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 91 GLAMVVQNYALFPHLKVEDNVAFGLRAQK--QPKALINERVTQALKTVGM----SDYAARYPHQLSGGQQQRVAIARAIA 164
Cdd:PRK14267 86 EVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 165 VRPRVLLLDEPLSALDAqIRHNMVEEIacLHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNR 244
Cdd:PRK14267 166 MKPKILLMDEPTANIDP-VGTAKIEEL--LFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHE 242
|
....*.
gi 566074967 245 FAAEFL 250
Cdd:PRK14267 243 LTEKYV 248
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
30-241 |
2.88e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 140.60 E-value: 2.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 30 GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIG----DTDVTHLPPYKRGLAMVVQNY--ALF- 102
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepiKYDKKSLLEVRKTVGIVFQNPddQLFa 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 103 PhlKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQ 182
Cdd:PRK13639 94 P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 566074967 183 irhnMVEEIACLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:PRK13639 172 ----GASQIMKLLYDLNKegITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
31-233 |
4.34e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 140.13 E-value: 4.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 31 NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVT--HLPPYKRGLAMVVQNY-ALFPHLKV 107
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkeNLKEIRKKIGIIFQNPdNQFIGATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 108 EDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNM 187
Cdd:PRK13632 102 EDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 566074967 188 VEEIACLHRELPElTILYVTHDQTEALtLADKIGIMKDGSLIAHGE 233
Cdd:PRK13632 182 KKIMVDLRKTRKK-TLISITHDMDEAI-LADKVIVFSEGKLIAQGK 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
19-232 |
4.35e-39 |
|
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: 138.48 E-value: 4.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGeVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRG-LAMVVQ 97
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 98 NYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 178 ALDAQIRH---NMVEEIAclhrelPELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03264 160 GLDPEERIrfrNLLSELG------EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-237 |
1.41e-38 |
|
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: 138.29 E-value: 1.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPA-GGRILI-----GDTDVTHLppyKRGL 92
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLfgerrGGEDVWEL---RKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 93 AMV---VQNYaLFPHLKVEDNVAFGLRAQ----KQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAV 165
Cdd:COG1119 81 GLVspaLQLR-FPRDETVLDVVLSGFFDSiglyREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 166 RPRVLLLDEPLSALDAQIRHNMVEEIACLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAE-GAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
30-232 |
7.21e-38 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 138.85 E-value: 7.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 30 GNVVLKpLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDT---DV---THLPPYKRGLAMVVQNYALFP 103
Cdd:PRK11144 11 GDLCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAekgICLPPEKRRIGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 104 HLKVEDNVAFGLRAQKQPKAlinERVTQALktvGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:PRK11144 90 HYKVRGNLRYGMAKSMVAQF---DKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 566074967 184 RHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:PRK11144 164 KRELLPYLERLAREI-NIPILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
37-244 |
1.93e-37 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 135.66 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 37 LSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDV-----THLPPYKRGLAMVVQNYALFPHLKVEDNV 111
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 112 AFGLRAQKQ-PKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEE 190
Cdd:PRK11831 106 AYPLREHTQlPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 566074967 191 IACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNR 244
Cdd:PRK11831 186 ISELNSAL-GVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR 238
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
32-238 |
3.15e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 135.60 E-value: 3.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVT---HLPPYKRGLAMVVQNyalfPHLK-- 106
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeeNLWDIRNKAGMVFQN----PDNQiv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 107 ---VEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:PRK13633 100 atiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 566074967 184 RHNMVEEIACLHRELpELTILYVTHDQTEALTlADKIGIMKDGSLIAHGETRALY 238
Cdd:PRK13633 180 RREVVNTIKELNKKY-GITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
28-232 |
8.63e-37 |
|
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: 132.34 E-value: 8.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 28 YHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQNYALFPHLKV 107
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPGFYPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 108 EDNVAFGLRAQKQPKalinERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNM 187
Cdd:cd03268 90 RENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKEL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 566074967 188 VEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03268 166 RELILSLRDQ--GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-231 |
1.36e-36 |
|
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: 130.24 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPY---KRGLAMV 95
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdarRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 96 vqnyalfphlkvednvafglraqkqpkalinervtqalktvgmsdyaarypHQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:cd03216 81 ---------------------------------------------------YQLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 176 LSALDAQIRHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAH 231
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ--GVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
30-237 |
2.34e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 132.94 E-value: 2.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 30 GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPY----KRGLAMVVQNYALFPhL 105
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvrsKVGLVFQDPDDQVFS-S 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 106 KVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRH 185
Cdd:PRK13647 96 TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 566074967 186 NMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:PRK13647 176 TLMEILDRLHNQ--GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-232 |
2.79e-36 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 131.58 E-value: 2.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYH-GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTH--LPPYKRGLAMV 95
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 96 VQNYALFpHLKVEDNVAFGlraqkQPKAlINERVTQALKTVGMSDYAARYPHQ-----------LSGGQQQRVAIARAIA 164
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYG-----RPDA-TDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 165 VRPRVLLLDEPLSALDAQIRHNMVEEIA--CLHRelpelTILYVTHDQTEALTlADKIGIMKDGSLIAHG 232
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRdvSKGR-----TTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-240 |
5.71e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 131.80 E-value: 5.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGN--VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVT--HLPPYKRGLAM 94
Cdd:PRK13648 8 IVFKNVSFQYQSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITddNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 95 VVQN-YALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:PRK13648 88 VFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566074967 174 EPLSALDAQIRHNMVEEIACLHRElPELTILYVTHDQTEALTlADKIGIMKDGSLIAHGETRALYQH 240
Cdd:PRK13648 168 EATSMLDPDARQNLLDLVRKVKSE-HNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
17-220 |
2.29e-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: 135.49 E-value: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 17 SGIVLDSLRVAYHG-NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP--YKRGLA 93
Cdd:TIGR02857 320 SSLEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAdsWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 94 MVVQNYALFPHlKVEDNVAFGLRAQKQpkalinERVTQALKTVGMSDYAARYP-----------HQLSGGQQQRVAIARA 162
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLARPDASD------AEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 163 IAVRPRVLLLDEPLSALDAQIRHNMVEEIACLHRelpELTILYVTHDqTEALTLADKI 220
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ---GRTVLLVTHR-LALAALADRI 526
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
24-232 |
4.36e-35 |
|
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: 127.78 E-value: 4.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 24 LRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLP-------PYKRGLamvv 96
Cdd:cd03269 6 VTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEERGL---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 97 qnyalFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:cd03269 82 -----YPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 177 SALDAQIRHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARA--GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
11-234 |
6.22e-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: 134.49 E-value: 6.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 11 PASQGTsgIVLDSLRVAYHG--NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPY 88
Cdd:COG4618 325 PRPKGR--LSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 89 KRG-----LAmvvQNYALFPHlKVEDNVA-FGlraqkQPKAlinERVTQALKTVGMSDYAARYP-----------HQLSG 151
Cdd:COG4618 403 ELGrhigyLP---QDVELFDG-TIAENIArFG-----DADP---EKVVAAAKLAGVHEMILRLPdgydtrigeggARLSG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 152 GQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRhnmveeiACLHRELPEL-----TILYVTHDQTeALTLADKIGIMKDG 226
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDDEGE-------AALAAAIRALkargaTVVVITHRPS-LLAAVDKLLVLRDG 542
|
....*...
gi 566074967 227 SLIAHGET 234
Cdd:COG4618 543 RVQAFGPR 550
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-266 |
1.11e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 129.07 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYK-------RG 91
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeeRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 92 lamvvqnyaLFPHLKVEDNVAF-----GLraqkqPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVR 166
Cdd:COG4152 82 ---------LYPKMKVGEQLVYlarlkGL-----SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 167 PRVLLLDEPLSALD---AQIrhnMVEEIaclhRELPE--LTILYVTH--DQTEAltLADKIGIMKDGSLIAHGETRALY- 238
Cdd:COG4152 148 PELLILDEPFSGLDpvnVEL---LKDVI----RELAAkgTTVIFSSHqmELVEE--LCDRIVIINKGRKVLSGSVDEIRr 218
|
250 260
....*....|....*....|....*...
gi 566074967 239 QHPPNRFAAEFLGRANILSAIAlGITEA 266
Cdd:COG4152 219 QFGRNTLRLEADGDAGWLRALP-GVTVV 245
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
33-241 |
1.58e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 128.38 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQP---AGGRILIGDTDVTHLPPY--KRGLAMVVQNY-ALFPHLK 106
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWdiREKVGIVFQNPdNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 107 VEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHN 186
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 566074967 187 MVEEIACLHRElPELTILYVTHDQTEAlTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:PRK13640 182 ILKLIRKLKKK-NNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
38-241 |
2.03e-34 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 127.41 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYK---RGLAMVVQNYALF------------ 102
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarMGVVRTFQHVRLFremtvienllva 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 103 PHLKVEDNVAFGL-------RAQKQpkALinERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:PRK11300 105 QHQQLKTGLFSGLlktpafrRAESE--AL--DRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 176 LSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEH-NVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
38-241 |
3.05e-34 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 128.93 E-value: 3.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLA-----MVVQN-YA-LFPHLKVEDN 110
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqkiqIVFQNpYGsLNPRKKVGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAFGLraqkqpkaLIN---------ERVTQALKTVGM-SDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK11308 115 LEEPL--------LINtslsaaerrEKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 566074967 181 AQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:PRK11308 187 VSVQAQVLNLMMDLQQEL-GLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-238 |
4.25e-34 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 125.81 E-value: 4.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAY--HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTH--LPPYKRGLAM 94
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDytLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 95 VVQNYALFpHLKVEDNVAFGLRAQKQpkalinERVTQALKTVGMSDYAARYPH-----------QLSGGQQQRVAIARAI 163
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGRPGATR------EEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566074967 164 AVRPRVLLLDEPLSALDaqirhNMVEEI--ACLHRELPELTILYVTHDQTeALTLADKIGIMKDGSLIAHGETRALY 238
Cdd:cd03251 154 LKDPPILILDEATSALD-----TESERLvqAALERLMKNRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELL 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
37-234 |
5.75e-34 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 131.46 E-value: 5.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 37 LSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGR--ILIGD--TDVTHLPPYKRG-----LAMVVQNYALFPHLKV 107
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDewVDMTKPGPDGRGrakryIGILHQEYDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 108 EDNV--AFGLraqKQPKALINERVTQALKTVGMSDYAA-----RYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:TIGR03269 383 LDNLteAIGL---ELPDELARMKAVITLKMVGFDEEKAeeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 566074967 181 AQIRHNMVEEIACLHRELPElTILYVTHDQTEALTLADKIGIMKDGSLIAHGET 234
Cdd:TIGR03269 460 PITKVDVTHSILKAREEMEQ-TFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-208 |
2.09e-33 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 130.31 E-value: 2.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 17 SGIVLDSLRVA-YHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRIligdtdvtHLPPYKRglamv 95
Cdd:COG4178 361 GALALEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGAR----- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 96 vqnyALF----PHLKVEDnvafgLRAQ----KQPKALINERVTQALKTVGMSDYAARY------PHQLSGGQQQRVAIAR 161
Cdd:COG4178 428 ----VLFlpqrPYLPLGT-----LREAllypATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFAR 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 566074967 162 AIAVRPRVLLLDEPLSALDAQIRHNMveeIACLHRELPELTILYVTH 208
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAAL---YQLLREELPGTTVISVGH 542
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
24-250 |
2.19e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 124.70 E-value: 2.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 24 LRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVT---------------HLPPY 88
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadknQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 89 KRGLAMVVQNYALFPHLKVEDNVafgLRAQKQ----PKALINERVTQALKTVGMSDYA-ARYPHQLSGGQQQRVAIARAI 163
Cdd:PRK10619 91 RTRLTMVFQHFNLWSHMTVLENV---MEAPIQvlglSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 164 AVRPRVLLLDEPLSALDAQirhnMVEEIACLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPE----LVGEVLRIMQQLAEegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
....*....
gi 566074967 242 PNRFAAEFL 250
Cdd:PRK10619 244 QSPRLQQFL 252
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
34-238 |
3.71e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 124.82 E-value: 3.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVT--HLPPYKRGLAMVVQNY-ALFPHLKVEDN 110
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEE 190
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 566074967 191 IACLhRELPELTILYVTHDQTEALTlADKIGIMKDGSLIAHGETRALY 238
Cdd:PRK13642 183 IHEI-KEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
33-241 |
4.53e-33 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 130.23 E-value: 4.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP--YKRGLAMVVQNYALFPHlKVEDN 110
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHhyLHRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAFGLRaqKQPKalinERVTQALKTVGMSDYAARYPH-----------QLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:TIGR00958 575 IAYGLT--DTPD----EEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 180 DAQIRHNMVEEiaclhRELPELTILYVTHdQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:TIGR00958 649 DAECEQLLQES-----RSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-241 |
6.39e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 123.94 E-value: 6.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIG--DT-DVTHLPPYKRGLAM 94
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgiDTgDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 95 VVQN-YALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 174 EPLSALDAQIRHNMVEEIACLHRElpELTILYVTHDqTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEK--GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
33-239 |
6.39e-33 |
|
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: 122.65 E-value: 6.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP--YKRGLAMVVQNYALFPhLKVEDN 110
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLrwLRSQIGLVSQEPVLFD-GTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAFGLRAQKQpkalinERVTQALKTVGMSDYAARYPH-----------QLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:cd03249 97 IRYGKPDATD------EEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 180 DAQirhnmVEEI--ACLHRELPELTILYVTHDQTeALTLADKIGIMKDGSLIAHGETRALYQ 239
Cdd:cd03249 171 DAE-----SEKLvqEALDRAMKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELMA 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
27-218 |
8.21e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 121.19 E-value: 8.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 27 AYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTdvthlppykRGLAMVVQNYAL---FP 103
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------ARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 104 hLKVEDNVAFGLRAQKQP----KALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:NF040873 72 -LTVRDLVAMGRWARRGLwrrlTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 566074967 180 DAQIRHNMVEEIACLHRElpELTILYVTHDQtEALTLAD 218
Cdd:NF040873 151 DAESRERIIALLAEEHAR--GATVVVVTHDL-ELVRRAD 186
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
10-239 |
1.75e-32 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 127.89 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 10 APASQGTSGIVLDSLRVAYHGN---VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLP 86
Cdd:TIGR02204 329 TLPVPLRGEIEFEQVNFAYPARpdqPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLD 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 87 P--YKRGLAMVVQNYALFPHlKVEDNVAFGlraqkQPKAlINERVTQALKTVGMSDYAARYPH-----------QLSGGQ 153
Cdd:TIGR02204 409 PaeLRARMALVPQDPVLFAA-SVMENIRYG-----RPDA-TDEEVEAAARAAHAHEFISALPEgydtylgergvTLSGGQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 154 QQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIACLhreLPELTILYVTHDQTEALTlADKIGIMKDGSLIAHGE 233
Cdd:TIGR02204 482 RQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETL---MKGRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGT 557
|
....*.
gi 566074967 234 TRALYQ 239
Cdd:TIGR02204 558 HAELIA 563
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-237 |
1.82e-32 |
|
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: 121.82 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGN--VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP--YKRGLAM 94
Cdd:cd03252 1 ITFEHVRFRYKPDgpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPawLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 95 VVQNYALFpHLKVEDNVAFGlraqkqPKALINERVTQALKTVGMSDYAARYPH-----------QLSGGQQQRVAIARAI 163
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALA------DPGMSMERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 566074967 164 AVRPRVLLLDEPLSALDAQIRHNMVEEiacLHRELPELTILYVTHdQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRN---MHDICAGRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-252 |
1.93e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 122.08 E-value: 1.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQ------PAGGRILIGDTDVTHLPPYK--RGLAMVVQNYALFPH 104
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKlrKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 105 LKVEDNVAFGLRAQK-QPKALINERVTQALKTVGM----SDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:PRK14246 105 LSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 566074967 180 DAQIRHNMVEEIACLHRelpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEF-LGR 252
Cdd:PRK14246 185 DIVNSQAIEKLITELKN---EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYvIGR 255
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-250 |
2.33e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 121.94 E-value: 2.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQ-----PAGGRILIGDTDVTHLP--PYKRG 91
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDviELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 92 LAMVVQNYALFPHLKVEDNVAFGLRAQK--QPKALINERVTQALKTVGMSDY--------AARyphqLSGGQQQRVAIAR 161
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLWDEvkdrldapAGK----LSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 162 AIAVRPRVLLLDEPLSALDAQirhnMVEEIACLHREL-PELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQH 240
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPE----NTAKIESLFLELkKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
250
....*....|
gi 566074967 241 PPNRFAAEFL 250
Cdd:PRK14247 236 PRHELTEKYV 245
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
33-228 |
4.92e-32 |
|
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: 120.27 E-value: 4.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIgdtDVTHLPPYK-----RGLAMVVQNYALFPHlKV 107
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL---DGKPISQYEhkylhSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 108 EDNVAFGLraqkQPKALinERVTQALKTVGMSDYAARYPH-----------QLSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:cd03248 105 QDNIAYGL----QSCSF--ECVKEAAQKAHAHSFISELASgydtevgekgsQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 566074967 177 SALDAQIRHnmveEIACLHRELPELTILYVTHDQTEALTLADKIGIMKDGSL 228
Cdd:cd03248 179 SALDAESEQ----QVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-232 |
5.27e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 120.61 E-value: 5.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 21 LDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVV---Q 97
Cdd:COG4674 13 VEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIGrkfQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 98 NYALFPHLKVEDNVAFGLRAQKQPKALI--------NERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRV 169
Cdd:COG4674 93 KPTVFEELTVFENLELALKGDRGVFASLfarltaeeRDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 170 LLLDEPLSALDAQIRHNMVE---EIACLHrelpelTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:COG4674 173 LLLDEPVAGMTDAETERTAEllkSLAGKH------SVVVVEHDMEFVRQIARKVTVLHQGSVLAEG 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
30-209 |
6.04e-32 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 119.98 E-value: 6.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 30 GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHL-----PPYKRGLAMVVQNYALFPH 104
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 105 LKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIR 184
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180
....*....|....*....|....*..
gi 566074967 185 hnmvEEIACLHRELPE--LTILYVTHD 209
Cdd:PRK10908 174 ----EGILRLFEEFNRvgVTVLMATHD 196
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
19-232 |
8.37e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 120.50 E-value: 8.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP--YKRGLAMVV 96
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrqLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 97 QNYALFPHLKVEDNVAFG----------LRAQKQpkalinERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVR 166
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGrspwlslwgrLSAEDN------ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 167 PRVLLLDEPLSALDaqIRHNMveEIACLHRELPEL--TILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:PRK11231 157 TPVVLLDEPTTYLD--INHQV--ELMRLMRELNTQgkTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
28-241 |
8.57e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 121.06 E-value: 8.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 28 YHGNV-VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVT--HLPPYKRGLAMVVQNY--ALF 102
Cdd:PRK13652 13 YSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFVGLVFQNPddQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 103 PHlKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQ 182
Cdd:PRK13652 93 SP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 183 irhnMVEEIACLHRELPE---LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:PRK13652 172 ----GVKELIDFLNDLPEtygMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-226 |
9.37e-32 |
|
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: 117.70 E-value: 9.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGN--VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP--YKRGLAM 94
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPneLGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 95 VVQNYALFPHlKVEDNVafglraqkqpkalinervtqalktvgmsdyaaryphqLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 566074967 175 PLSALDAQIRHNMVEEIACLhrELPELTILYVTHdQTEALTLADKIGIMKDG 226
Cdd:cd03246 123 PNSHLDVEGERALNQAIAAL--KAAGATRIVIAH-RPETLASADRILVLEDG 171
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
30-220 |
1.11e-31 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 119.05 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 30 GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP--YKRGLAMVVQNYALFPHlKV 107
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiYRQQVSYCAQTPTLFGD-TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 108 EDNVAF--GLRAQK-QPKALINErvtqaLKTVGMSDYAARYP-HQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:PRK10247 98 YDNLIFpwQIRNQQpDPAIFLDD-----LERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 566074967 184 RHNmVEEIacLHRELPE--LTILYVTHDQTEaLTLADKI 220
Cdd:PRK10247 173 KHN-VNEI--IHRYVREqnIAVLWVTHDKDE-INHADKV 207
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-229 |
1.18e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 120.19 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 31 NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRG--LAMVVQNYAL--FPHLK 106
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAkyIGRVFQDPMMgtAPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 107 VEDNVA----------FGLRAQKQPKALINERVTQ-------ALKT-VGmsdyaaryphQLSGGQQQRVAIARAIAVRPR 168
Cdd:COG1101 99 IEENLAlayrrgkrrgLRRGLTKKRRELFRELLATlglglenRLDTkVG----------LLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 566074967 169 VLLLDEPLSALD---AQIRHNMVEEIACLHRelpeLTILYVTHDQTEALTLADKIGIMKDGSLI 229
Cdd:COG1101 169 LLLLDEHTAALDpktAALVLELTEKIVEENN----LTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
32-238 |
1.89e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 120.27 E-value: 1.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTH------LPPYKRGLAMVVQnyalFPHL 105
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 106 KV-EDNVA----FGLRAQKQPKALINERVTQALKTVGMS-DYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:PRK13646 97 QLfEDTVEreiiFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 566074967 180 DAQIRHNMVEEIACLHRELPElTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALY 238
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENK-TIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
38-241 |
2.43e-31 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 120.97 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKR-----GLAMVVQN--YALFPHLKVEDN 110
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAFGLRA--QKQPKALINERVTQALKTVGM-SDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNM 187
Cdd:PRK15079 121 IAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 566074967 188 VEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:PRK15079 201 VNLLQQLQREM-GLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-251 |
2.90e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 119.43 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 23 SLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRA-------VAGFVQPA----GGRILIGDTDVTHlppYKRG 91
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRYSGdvllGGRSIFNYRDVLE---FRRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 92 LAMVVQNYALFPhLKVEDNVAFGLRA-----QKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVR 166
Cdd:PRK14271 103 VGMLFQRPNPFP-MSIMDNVLAGVRAhklvpRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 167 PRVLLLDEPLSALDAQIRHNMVEEIACLhreLPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFA 246
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSL---ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
....*
gi 566074967 247 AEFLG 251
Cdd:PRK14271 259 ARYVA 263
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-241 |
3.00e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 124.57 E-value: 3.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 26 VAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVqPAGGRILIGDTDVTHLPP--YKRGLAMVVQNYALFp 103
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPesWRKHLSWVGQNPQLP- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 104 HLKVEDNVAFGlraqkQPKAlINERVTQALKTVGMSDYAARYPH-----------QLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:PRK11174 436 HGTLRDNVLLG-----NPDA-SDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 566074967 173 DEPLSALDAQiRHNMVeeIACLHRELPELTILYVTHdQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:PRK11174 510 DEPTASLDAH-SEQLV--MQALNAASRRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
33-244 |
5.65e-31 |
|
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: 118.37 E-value: 5.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP-----YKRGLAMVVQNY--ALFPHL 105
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRkqrraFRRDVQLVFQDSpsAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 106 KVEDNVAFGLRAQKQPKALINERVTQA-LKTVGM-SDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDaqi 183
Cdd:TIGR02769 106 TVRQIIGEPLRHLTSLDESEQKARIAElLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD--- 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 184 RHNMVEEIACLhRELPE---LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRAL--YQHPPNR 244
Cdd:TIGR02769 183 MVLQAVILELL-RKLQQafgTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLlsFKHPAGR 247
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-252 |
5.73e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 118.35 E-value: 5.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 22 DSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRA-------VAGFvqPAGGRILIGDTDV--THLPP--YKR 90
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGF--RVEGKVTFHGKNLyaPDVDPveVRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 91 GLAMVVQNYALFPHlKVEDNVAFGLRAQKQpKALINERVTQALKTVGMSDYAARYPHQ----LSGGQQQRVAIARAIAVR 166
Cdd:PRK14243 92 RIGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 167 PRVLLLDEPLSALDAqIRHNMVEEiacLHRELPE-LTILYVTHDQTEALTLADKIGIM---------KDGSLIAHGETRA 236
Cdd:PRK14243 170 PEVILMDEPCSALDP-ISTLRIEE---LMHELKEqYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEK 245
|
250
....*....|....*..
gi 566074967 237 LYQHPPNRFAAEFL-GR 252
Cdd:PRK14243 246 IFNSPQQQATRDYVsGR 262
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
33-228 |
9.92e-31 |
|
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: 115.22 E-value: 9.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPY---KRGLAMVV---QNYALFPHLK 106
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdaiRAGIAYVPedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 107 VEDNVAFglraqkqpkalinervtqalktvgmsdyaaryPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDaqirhn 186
Cdd:cd03215 95 VAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD------ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 566074967 187 mVEEIACLHRELPEL-----TILYVTHDQTEALTLADKIGIMKDGSL 228
Cdd:cd03215 137 -VGAKAEIYRLIRELadagkAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-232 |
1.52e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 116.53 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPY---KRGLAMV 95
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 96 VQNYALFPHLKVEDNVAFGLRAQKQ-PKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIRDDlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 175 PLSALDAQIRHNMVEEIAclHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIE--HLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHG 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
33-240 |
5.64e-30 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 120.59 E-value: 5.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTH--LPPYKRGLAMVVQNYALFPHlKVEDN 110
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADytLASLRRQVALVSQDVVLFND-TIANN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAFGLRAQkqpkaLINERVTQALKTVGMSDYAARYP---HQ--------LSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:TIGR02203 426 IAYGRTEQ-----ADRAEIERALAAAYAQDFVDKLPlglDTpigengvlLSGGQRQRLAIARALLKDAPILILDEATSAL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 566074967 180 DAQiRHNMVEeiACLHRELPELTILYVTHDQTeALTLADKIGIMKDGSLIAHGETRALYQH 240
Cdd:TIGR02203 501 DNE-SERLVQ--AALERLMQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
33-232 |
6.80e-30 |
|
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: 113.41 E-value: 6.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAG--GRILIGDTDVtHLPPYKRGLAMVVQNYALFPHLKVEDN 110
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPL-DKRSFRKIIGYVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAFglraqkqpkalinervTQALKtvgmsdyaaryphQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVE- 189
Cdd:cd03213 103 LMF----------------AAKLR-------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSl 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 566074967 190 --EIACLHRelpelTILYVTHD-QTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03213 154 lrRLADTGR-----TIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
38-235 |
1.22e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.98 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP---YKRGLAMVVQNYALFPHLKVEDNVAFG 114
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPrdaIALGIGMVHQHFMLVPNLTVAENIVLG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 115 L---RAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQirhnmveEI 191
Cdd:COG3845 105 LeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQ-------EA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 566074967 192 ACLHRELPEL-----TILYVTHDQTEALTLADKIGIMKDGSLIAHGETR 235
Cdd:COG3845 178 DELFEILRRLaaegkSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-238 |
1.54e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.94 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 20 VLDSLRVAYH---GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTH----LPPYKRGL 92
Cdd:PRK13636 5 ILKVEELNYNysdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrkgLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 93 AMVVQ--NYALFPhLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVL 170
Cdd:PRK13636 85 GMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 171 LLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALY 238
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKEL-GLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-250 |
2.08e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 114.36 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 18 GIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRA------------VAGFVQPAGGRILIGDTDVTHL 85
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKClnrmnelesevrVEGRVEFFNQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 86 ppyKRGLAMVVQNYALFPhLKVEDNVAFGLRAQK-QPKALINERVTQALKTVGMSDYAARYPHQ----LSGGQQQRVAIA 160
Cdd:PRK14258 87 ---RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 161 RAIAVRPRVLLLDEPLSALDAqIRHNMVEEIACLHRELPELTILYVTHDQTEALTLADKIGIMKD-----GSLIAHGETR 235
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDP-IASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTK 241
|
250
....*....|....*
gi 566074967 236 ALYQHPPNRFAAEFL 250
Cdd:PRK14258 242 KIFNSPHDSRTREYV 256
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-182 |
2.18e-29 |
|
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: 112.45 E-value: 2.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 21 LDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP-YKRGLAMVVQNY 99
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDePHENILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 100 ALFPHLKVEDNVAFgLRAQKQPKALineRVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:TIGR01189 83 GLKPELSALENLHF-WAAIHGGAQR---TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
...
gi 566074967 180 DAQ 182
Cdd:TIGR01189 159 DKA 161
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
34-234 |
2.49e-29 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 114.12 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRG--LAMVVQN--YALFPHLKVED 109
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqrIRMIFQDpsTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 110 NVAFGLRAQKQPKALINE-RVTQALKTVGM-SDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNM 187
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREkQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 566074967 188 VEeiacLHRELPE---LTILYVTHDQTEALTLADKIGIMKDGSLIAHGET 234
Cdd:PRK15112 189 IN----LMLELQEkqgISYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
37-244 |
3.37e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 118.80 E-value: 3.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 37 LSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYK-----RGLAMVVQN-YA-LFPHLKVED 109
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 110 NVAFGLRAQK--QPKAlINERVTQALKTVGM-SDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHN 186
Cdd:PRK10261 423 SIMEPLRVHGllPGKA-AAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQ 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 566074967 187 MVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALY---QHPPNR 244
Cdd:PRK10261 502 IINLLLDLQRDF-GIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFenpQHPYTR 561
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-250 |
3.47e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 118.27 E-value: 3.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 25 RVAYHgnVVLKPLSLTIEPGEVLALIGPSGSGKTT----VLRAVAgfvqpAGGRILIGDTDVTHLP-----PYKRGLAMV 95
Cdd:PRK15134 295 TVDHN--VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNrrqllPVRHRIQVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 96 VQ--NYALFPHLKVEDNVAFGLRA-QKQPKALINE-RVTQALKTVGMS-DYAARYPHQLSGGQQQRVAIARAIAVRPRVL 170
Cdd:PRK15134 368 FQdpNSSLNPRLNVLQIIEEGLRVhQPTLSAAQREqQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 171 LLDEPLSALDAQIRhnmvEEIACLHRELPE---LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAA 247
Cdd:PRK15134 448 ILDEPTSSLDKTVQ----AQILALLKSLQQkhqLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTR 523
|
...
gi 566074967 248 EFL 250
Cdd:PRK15134 524 QLL 526
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
33-230 |
7.23e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 117.90 E-value: 7.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP------YKRGLAMVVQNYALFPHLK 106
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalaqlRREHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 107 VEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAqirHN 186
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS---HS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 566074967 187 MVEEIACLHrELPEL--TILYVTHDQTEAlTLADKIGIMKDGSLIA 230
Cdd:PRK10535 180 GEEVMAILH-QLRDRghTVIIVTHDPQVA-AQAERVIEIRDGEIVR 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
32-227 |
1.98e-28 |
|
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: 110.60 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILI----GDTDVTHLPPY------KRGLAMVVQnyal 101
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPReilalrRRTIGYVSQ---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 102 fpHLKV------EDNVAFGLRAQKQPKALINERVTQALKTVGM-SDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:COG4778 101 --FLRViprvsaLDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 175 PLSALDAQIRHNMVEEIAclhrelpEL-----TILYVTHDQTEALTLADKIGIMKDGS 227
Cdd:COG4778 179 PTASLDAANRAVVVELIE-------EAkargtAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
29-232 |
2.82e-28 |
|
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: 110.01 E-value: 2.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 29 HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLP--PYKRGLAMVVQNYALFPHlK 106
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkSLRSMIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 107 VEDNVAFG-LRAQKqpkalinERVTQALKTVGMSDYAARYP-----------HQLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:cd03254 93 IMENIRLGrPNATD-------EEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 175 PLSALDAQirhnmVEEI--ACLHRELPELTILYVTHDQTealTL--ADKIGIMKDGSLIAHG 232
Cdd:cd03254 166 ATSNIDTE-----TEKLiqEALEKLMKGRTSIIIAHRLS---TIknADKILVLDDGKIIEEG 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
37-240 |
3.12e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 111.37 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 37 LSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTH------LPPYKRGLAMVVQnyalFPHLK---- 106
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIKQIRKKVGLVFQ----FPESQlfee 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 107 -VEDNVAFGLR----AQKQPKALINERvtqaLKTVGMS-DYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK13649 102 tVLKDVAFGPQnfgvSQEEAEALAREK----LALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 181 AQIRHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQH 240
Cdd:PRK13649 178 PKGRKELMTLFKKLHQS--GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
33-231 |
3.26e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 110.29 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRG------LAMVVQNYALFPHLK 106
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqkLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 107 VEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHN 186
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 566074967 187 MVEEIACLHRElPELTILYVTHDqteaLTLADKIGI---MKDGSLIAH 231
Cdd:PRK11629 184 IFQLLGELNRL-QGTAFLVVTHD----LQLAKRMSRqleMRDGRLTAE 226
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
24-232 |
3.46e-28 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 110.16 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 24 LRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGF--VQPAGGRILIGDTDVTHLPPYKR---GLAMVVQN 98
Cdd:COG0396 6 LHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERaraGIFLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 99 YALFPHLKVED--NVAFGLRAQKQPKALI-NERVTQALKTVGMS-DYAARYPHQ-LSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:COG0396 86 PVEIPGVSVSNflRTALNARRGEELSAREfLKLLKEKMKELGLDeDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 566074967 174 EPLSALDA---QIrhnMVEEIACLHRelPELTILYVTHdQTEALTL--ADKIGIMKDGSLIAHG 232
Cdd:COG0396 166 ETDSGLDIdalRI---VAEGVNKLRS--PDRGILIITH-YQRILDYikPDFVHVLVDGRIVKSG 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-271 |
3.58e-28 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 111.13 E-value: 3.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 16 TSGIVLDSLRVAY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHlpPYKRGL-A 93
Cdd:PRK15056 4 QAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ--ALQKNLvA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 94 MVVQNYAL---FPHLkVEDNVAFGLRAQ----KQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVR 166
Cdd:PRK15056 82 YVPQSEEVdwsFPVL-VEDVVMMGRYGHmgwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 167 PRVLLLDEPLSALDAQIRhnmvEEIACLHRELPE--LTILYVTHDQTEALTLADKIgIMKDGSLIAHGETRalyqhppNR 244
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTE----ARIISLLRELRDegKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTE-------TT 228
|
250 260
....*....|....*....|....*....
gi 566074967 245 FAAEFLGRA--NILSAIALGITEAPGLVD 271
Cdd:PRK15056 229 FTAENLELAfsGVLRHVALNGSEESIITD 257
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
37-271 |
9.53e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 110.21 E-value: 9.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 37 LSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVT------HLPPYKRGLAMVVQ--NYALFPHLKVE 108
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQfpESQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 109 DnVAFGLRAQKQPKALINERVTQALKTVGMS-DYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNM 187
Cdd:PRK13643 105 D-VAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEM 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 188 VEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQhppnrfaaeflgRANILSAIALGITEAP 267
Cdd:PRK13643 184 MQLFESIHQS--GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ------------EVDFLKAHELGVPKAT 249
|
....
gi 566074967 268 GLVD 271
Cdd:PRK13643 250 HFAD 253
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
16-240 |
1.34e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 110.28 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 16 TSGIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRI-LIGDTDVTHLPPYKRGLAM 94
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIsLCGEPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 95 VVQNYALFPHLKVEDNVA-----FGLRAQKqpkalINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRV 169
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLvfgryFGLSAAA-----ARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 566074967 170 LLLDEPLSALDAQIRHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQH 240
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLAR--GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
34-235 |
1.98e-27 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 108.39 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVqPAGGRILIGDTDVTHLPPYK--RGLAMVVQNYALFPHLKVEDNV 111
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 112 AFGLRAQKQPKALINE--RVTQALktvGMSDYAARYPHQLSGGQQQRVAIARAIA-VRPRV------LLLDEPLSALDaq 182
Cdd:COG4138 91 ALHQPAGASSEAVEQLlaQLAEAL---GLEDKLSRPLTQLSGGEWQRVRLAAVLLqVWPTInpegqlLLLDEPMNSLD-- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 183 IRHNmveeiACLHRELPEL-----TILYVTHDQTEALTLADKIGIMKDGSLIAHGETR 235
Cdd:COG4138 166 VAQQ-----AALDRLLRELcqqgiTVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
33-234 |
2.08e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 109.79 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRI-----------------LIGDTDVTHLPPYK------ 89
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekeKVLEKLVIQKTRFKkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 90 ---RGLAMVVQ--NYALFPHlKVEDNVAFGLRAQKQPKALINERVTQALKTVGMS-DYAARYPHQLSGGQQQRVAIARAI 163
Cdd:PRK13651 102 eirRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 566074967 164 AVRPRVLLLDEPLSALDAQIRHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGET 234
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ--GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDT 249
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
33-229 |
2.91e-27 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 107.36 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAG---GRILIGDTDVT-HLppYKRGLAMVVQNYALFPHLKVE 108
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKpDQ--FQKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 109 DNVAFG--LRAQ-KQPKALINERV-TQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIR 184
Cdd:cd03234 100 ETLTYTaiLRLPrKSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 566074967 185 HNMVEEIACLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLI 229
Cdd:cd03234 180 LNLVSTLSQLARR-NRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
28-227 |
4.38e-27 |
|
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: 106.40 E-value: 4.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 28 YHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTdvthlppykrgLAMVVQNyalfPHLK- 106
Cdd:cd03250 15 QETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAYVSQE----PWIQn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 107 --VEDNVAFGLRaqkqpkaLINERVTQALK----------------TV----GMSdyaaryphqLSGGQQQRVAIARAIA 164
Cdd:cd03250 80 gtIRENILFGKP-------FDEERYEKVIKacalepdleilpdgdlTEigekGIN---------LSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566074967 165 VRPRVLLLDEPLSALDAQIRHNMVEEiaCLhreLPEL----TILYVTHdQTEALTLADKIGIMKDGS 227
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFEN--CI---LGLLlnnkTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-237 |
5.37e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 111.68 E-value: 5.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 27 AYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP---YKRGLAMVVQNYALFP 103
Cdd:PRK15439 20 QYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLVPQEPLLFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 104 HLKVEDNVAFGLraQKQPKALinERVTQALKTVGMS---DYAArypHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK15439 100 NLSVKENILFGL--PKRQASM--QKMKQLLAALGCQldlDSSA---GSLEVADRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 566074967 181 AQIRHNMVEEIaclhRELPELT--ILYVTHDQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:PRK15439 173 PAETERLFSRI----RELLAQGvgIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
10-209 |
6.30e-27 |
|
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: 111.68 E-value: 6.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 10 APASQGTSGIVLDSLRVAYHG-NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLP-- 86
Cdd:TIGR02868 326 GAVGLGKPTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqd 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 87 PYKRGLAMVVQNYALFpHLKVEDNVAFGlraqkQPKAlINERVTQALKTVGMSDYAARYPH-----------QLSGGQQQ 155
Cdd:TIGR02868 406 EVRRRVSVCAQDAHLF-DTTVRENLRLA-----RPDA-TDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 566074967 156 RVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIAclhRELPELTILYVTHD 209
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEDLL---AALSGRTVVLITHH 529
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
11-239 |
6.92e-27 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 107.57 E-value: 6.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 11 PASQGTSgIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVT--HLPPY 88
Cdd:PRK10575 5 TNHSDTT-FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 89 KRGLAMVVQNYALFPHLKVEDNVAFGLR----AQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIA 164
Cdd:PRK10575 84 ARKVAYLPQQLPAAEGMTVRELVAIGRYpwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566074967 165 VRPRVLLLDEPLSALDaqIRHNmVEEIACLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQ 239
Cdd:PRK10575 164 QDSRCLLLDEPTSALD--IAHQ-VDVLALVHRLSQErgLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-232 |
8.01e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 107.79 E-value: 8.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 16 TSGIVLDSLRVAYHGNV-----VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGD-------TDVT 83
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 84 HLPPYKRGLAMVVQ--NYALFPHlKVEDNVAFGLRAQKQPKALINERVTQALKTVGM-SDYAARYPHQLSGGQQQRVAIA 160
Cdd:PRK13645 84 EVKRLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 161 RAIAVRPRVLLLDEPLSALDAQIRHNMVEEIACLHRELPElTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKK-RIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
32-232 |
8.08e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 108.40 E-value: 8.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPY------------------KRGLA 93
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNhelitnpyskkiknfkelRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 94 MVVQ--NYALFPHlKVEDNVAFGLRAQKQPKALINERVTQALKTVGM-SDYAARYPHQLSGGQQQRVAIARAIAVRPRVL 170
Cdd:PRK13631 120 MVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 171 LLDEPLSALDAQIRHNMVEEIacLHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLI--LDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
19-253 |
1.77e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 109.16 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYK--RGLAMVV 96
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 97 QNYALFPHLKVEDNVAFGL---RAQKQPKALINER-VTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMGRtphRSRFDTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 173 DEPLSALDAqirHNMVEEIAcLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQhpPNRFAAEFL 250
Cdd:PRK09536 164 DEPTASLDI---NHQVRTLE-LVRRLVDdgKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT--ADTLRAAFD 237
|
...
gi 566074967 251 GRA 253
Cdd:PRK09536 238 ART 240
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
34-249 |
1.81e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.84 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVT------HLPPYKRGLAMVVQ--NYALFPHL 105
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 106 KVEDnVAFGLRAQKQPKALINERVTQALKTVGMS-DYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIR 184
Cdd:PRK13641 103 VLKD-VEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566074967 185 HNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP------------PNRFAAEF 249
Cdd:PRK13641 182 KEMMQLFKDYQKA--GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKewlkkhyldepaTSRFASKL 256
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
24-181 |
2.51e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 104.19 E-value: 2.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 24 LRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVtHLPPYKRGLAMVVQNYALFP 103
Cdd:PRK13539 8 LACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI-DDPDVAEACHYLGHRNAMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 104 HLKVEDNVAF--GLRAQKQPkalineRVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDA 181
Cdd:PRK13539 87 ALTVAENLEFwaAFLGGEEL------DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
33-244 |
3.15e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 105.54 E-value: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLP-----PYKRGLAMVVQNY--ALFPHL 105
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkAFRRDIQMVFQDSisAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 106 KVEDNVAFGLR-AQKQPKALINERVTQALKTVGMSD-YAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:PRK10419 107 TVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 184 RHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIahgETRAL-----YQHPPNR 244
Cdd:PRK10419 187 QAGVIRLLKKLQQQF-GTACLFITHDLRLVERFCQRVMVMDNGQIV---ETQPVgdkltFSSPAGR 248
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-237 |
1.15e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 103.94 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFV---QPAGGRI-LIGDTdVTHLPPYKRGL-- 92
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIeLLGRT-VQREGRLARDIrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 93 -----AMVVQNYALFPHLKVEDNVAFGL---------------RAQKQpkalineRVTQALKTVGMSDYAARYPHQLSGG 152
Cdd:PRK09984 84 srantGYIFQQFNLVNRLSVLENVLIGAlgstpfwrtcfswftREQKQ-------RALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 153 QQQRVAIARAIAVRPRVLLLDEPLSALD---AQIRHNMVEEIaclhRELPELTILYVTHDQTEALTLADKIGIMKDGSLI 229
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDpesARIVMDTLRDI----NQNDGITVVVTLHQVDYALRYCERIVALRQGHVF 232
|
....*...
gi 566074967 230 AHGETRAL 237
Cdd:PRK09984 233 YDGSSQQF 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-272 |
1.45e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 107.48 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 21 LDSLRVAY----HGNVVLKPLSLTIEPGEVLALIGPSGSGKT----TVLRAV-AGFVQPAGGRILIGDTDVTHLP-PYKR 90
Cdd:PRK15134 8 IENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLLHASeQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 91 GL-----AMVVQN--YALFPHLKVEDNVAFGL---RAQKQPKAliNERVTQALKTVGMSDYAAR---YPHQLSGGQQQRV 157
Cdd:PRK15134 88 GVrgnkiAMIFQEpmVSLNPLHTLEKQLYEVLslhRGMRREAA--RGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 158 AIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQEL-NMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 566074967 238 Y---QHPPNR--FAAEFLGRANILSAialgitEAPGLVDV 272
Cdd:PRK15134 245 FsapTHPYTQklLNSEPSGDPVPLPE------PASPLLDV 278
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
33-230 |
1.61e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.41 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPY---KRGLAMVVQN---YALFPHLK 106
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdaiRAGIAYVPEDrkgEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 107 VEDNVA---------FGLRAQKQPKALINERVTQ-ALKTVGMSDYAAryphQLSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:COG1129 347 IRENITlasldrlsrGGLLDRRRERALAEEYIKRlRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 177 SALD----AQIrHNMVEEIAclhRElpELTILYVTHDQTEALTLADKIGIMKDGSLIA 230
Cdd:COG1129 423 RGIDvgakAEI-YRLIRELA---AE--GKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-230 |
1.86e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.03 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 9 HAPASQGTSGIVLDSLRVA-YHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP 87
Cdd:COG3845 248 KAPAEPGEVVLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 88 YKR---GLAMVV---QNYALFPHLKVEDNVAFGL--RAQKQPKALINERVTQAL-KTVgMSDYAARYPH------QLSGG 152
Cdd:COG3845 328 RERrrlGVAYIPedrLGRGLVPDMSVAENLILGRyrRPPFSRGGFLDRKAIRAFaEEL-IEEFDVRTPGpdtparSLSGG 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 153 QQQRVAIARAIAVRPRVLLLDEPLSALDaqirhnmVEEIACLHRELPEL-----TILYVTHDQTEALTLADKIGIMKDGS 227
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLD-------VGAIEFIHQRLLELrdagaAVLLISEDLDEILALSDRIAVMYEGR 479
|
...
gi 566074967 228 LIA 230
Cdd:COG3845 480 IVG 482
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
9-237 |
2.17e-25 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 107.60 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 9 HAPASQGTSG-IVLDSLRVAYHGN-VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLP 86
Cdd:COG5265 347 DAPPLVVGGGeVRFENVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 87 P--YKRGLAMVVQNYALFpHLKVEDNVAFGlraqkQPKAlINERVTQALKTVGMSDYAARYPHQ-----------LSGGQ 153
Cdd:COG5265 427 QasLRAAIGIVPQDTVLF-NDTIAYNIAYG-----RPDA-SEEEVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 154 QQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIaclhRElpeltilyVTHDQTealTL-----------ADKIGI 222
Cdd:COG5265 500 KQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAAL----RE--------VARGRT---TLviahrlstivdADEILV 564
|
250
....*....|....*
gi 566074967 223 MKDGSLIAHGETRAL 237
Cdd:COG5265 565 LEAGRIVERGTHAEL 579
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
32-240 |
2.37e-25 |
|
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: 107.05 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRG--LAMVVQNYALFPHlKVED 109
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGkhIGYLPQDVELFPG-TVAE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 110 NVA-FGLRAQkqpkaliNERVTQALKTVGMSDYAARYPH-----------QLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:TIGR01842 411 NIArFGENAD-------PEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 566074967 178 ALDAQIRHNMVEeiACLHRELPELTILYVTHdQTEALTLADKIGIMKDGSLIAHGETRALYQH 240
Cdd:TIGR01842 484 NLDEEGEQALAN--AIKALKARGITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-232 |
2.85e-25 |
|
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: 101.06 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 24 LRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGF--VQPAGGRILIGDTDVTHLPPYKR---GLAMVVQN 98
Cdd:cd03217 6 LHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERarlGIFLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 99 YALFPHLKVEDnvaFgLRAqkqpkalINErvtqalktvgmsdyaaryphQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:cd03217 86 PPEIPGVKNAD---F-LRY-------VNE--------------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 566074967 179 LDAQIRHNMVEEIACLHRelPELTILYVTHDQTEALTL-ADKIGIMKDGSLIAHG 232
Cdd:cd03217 135 LDIDALRLVAEVINKLRE--EGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-182 |
4.94e-25 |
|
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: 100.65 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 22 DSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILI-GDTDVTHLPPYKRGLAMVVQNYA 100
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnGGPLDFQRDSIARGLLYLGHAPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 101 LFPHLKVEDNVAFGLRAQKqpkaliNERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:cd03231 84 IKTTLSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
..
gi 566074967 181 AQ 182
Cdd:cd03231 158 KA 159
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
33-213 |
5.36e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 101.39 E-value: 5.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRG------LAMVVQNYALFPHLK 106
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakhVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 107 VEDNVAFG--LRAQKQPKAliNERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIR 184
Cdd:PRK10584 105 ALENVELPalLRGESSRQS--RNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180
....*....|....*....|....*....
gi 566074967 185 HNMVEEIACLHRELPELTILyVTHDQTEA 213
Cdd:PRK10584 183 DKIADLLFSLNREHGTTLIL-VTHDLQLA 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-232 |
9.84e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 101.60 E-value: 9.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 22 DSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYK--RGLAMVVQNY 99
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 100 ALFPHLKVEDNVAFGlRAQKQP-----KALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:PRK10253 91 TTPGDITVQELVARG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 175 PLSALDAQIRHNMVEEIACLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNRE-KGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
37-241 |
2.24e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 101.74 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 37 LSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAG----GRILIGDTDVTHLPPYKR------GLAMVVQN--YALFPH 104
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 105 LKVEDNVAFGLRA-QKQPKALINERVTQALKTVGMSDYAAR---YPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK11022 106 YTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 566074967 181 AQIRHNMVEEIACLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:PRK11022 186 VTIQAQIIELLLELQQK-ENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-237 |
3.46e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.45 E-value: 3.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 11 PASQGTSGIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDV-THLPPYK 89
Cdd:PRK13536 34 PGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 90 RGLAMVVQNYALFPHLKVEDNVA-----FGLRAQKqpkalINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIA 164
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLvfgryFGMSTRE-----IEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALI 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 566074967 165 VRPRVLLLDEPLSALDAQIRHNMVEEI-ACLHRelpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLrSLLAR---GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
38-241 |
5.30e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 99.23 E-value: 5.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILI-----GDTDVTHLP-PYKRGLAMVVQNYalfphlkVEDNV 111
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdgQLRDLYALSeAERRRLLRTEWGF-------VHQHP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 112 AFGLRAQKQPKALINERvtqaLKTVGMSDY-----------------AAR---YPHQLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:PRK11701 99 RDGLRMQVSAGGNIGER----LMAVGARHYgdiratagdwlerveidAARiddLPTTFSGGMQQRLQIARNLVTHPRLVF 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 566074967 172 LDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGET-RAL--YQHP 241
Cdd:PRK11701 175 MDEPTGGLDVSVQARLLDLLRGLVREL-GLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTdQVLddPQHP 246
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
10-241 |
6.08e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 100.57 E-value: 6.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 10 APASQGTSGIVLD--SLRVAYH---GNVV-LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAG---GRILIGDT 80
Cdd:PRK09473 2 VPLAQQQADALLDvkDLRVTFStpdGDVTaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 81 DVTHLPPYK------RGLAMVVQN--YALFPHLKVEDNVAFGLRAQKQ-PKALINERVTQALKTVGMSDYAAR---YPHQ 148
Cdd:PRK09473 82 EILNLPEKElnklraEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGmSKAEAFEESVRMLDAVKMPEARKRmkmYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 149 LSGGQQQRVAIARAIAVRPRVLLLDEPLSALD----AQIRHNMVEeiacLHRELpELTILYVTHDQTEALTLADKIGIMK 224
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNE----LKREF-NTAIIMITHDLGVVAGICDKVLVMY 236
|
250
....*....|....*..
gi 566074967 225 DGSLIAHGETRALYQHP 241
Cdd:PRK09473 237 AGRTMEYGNARDVFYQP 253
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-255 |
6.75e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 99.31 E-value: 6.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 28 YHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHlppYKRGLAMVVQNYA------- 100
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY---SKRGLLALRQQVAtvfqdpe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 101 --LFpHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGmsdyAARYPHQ----LSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:PRK13638 88 qqIF-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD----AQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 175 PLSALDAQIRHNMveeIACLHRELPELT-ILYVTHDQTEALTLADKIGIMKDGSLIAHGEtralyqhPPNRFA-AEFLGR 252
Cdd:PRK13638 163 PTAGLDPAGRTQM---IAIIRRIVAQGNhVIISSHDIDLIYEISDAVYVLRQGQILTHGA-------PGEVFAcTEAMEQ 232
|
...
gi 566074967 253 ANI 255
Cdd:PRK13638 233 AGL 235
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
37-182 |
7.16e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 97.57 E-value: 7.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 37 LSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP-YKRGLAMVVQNYALFPHLKVEDNVAFGL 115
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeYHQDLLYLGHQPGIKTELTALENLRFYQ 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566074967 116 RAQKQPKAlinERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQ 182
Cdd:PRK13538 100 RLHGPGDD---EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
28-241 |
8.98e-24 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 98.75 E-value: 8.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 28 YHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILI-----GDTDVTHLPPYKRGLAMVVQnYALf 102
Cdd:TIGR02323 13 YGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAERRRLMRTE-WGF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 103 phlkVEDNVAFGLRAQKQPKALINERvtqaLKTVGMSDY-----------------AARY---PHQLSGGQQQRVAIARA 162
Cdd:TIGR02323 91 ----VHQNPRDGLRMRVSAGANIGER----LMAIGARHYgnirataqdwleeveidPTRIddlPRAFSGGMQQRLQIARN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 163 IAVRPRVLLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALY---Q 239
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDL-GLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLddpQ 241
|
..
gi 566074967 240 HP 241
Cdd:TIGR02323 242 HP 243
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
27-251 |
9.63e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 98.03 E-value: 9.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 27 AYHGNV-VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP---YKRGLAMVVQNYALF 102
Cdd:PRK11614 13 AHYGKIqALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakiMREAVAIVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 103 PHLKVEDNVAF-GLRAQKQPKALINERVTQALKTvgMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDA 181
Cdd:PRK11614 93 SRMTVEENLAMgGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 182 QIRHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAaeFLG 251
Cdd:PRK11614 171 IIIQQIFDTIEQLREQ--GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSA--YLG 236
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-239 |
1.71e-23 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 98.36 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 22 DSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAG----FVQPAG----GRILIGDTDVTHLPPYKRGLA 93
Cdd:PRK13547 5 DHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRGarvtGDVTLNGEPLAAIDAPRLARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 94 MVVQNYALFPHL--KVEDNVAFG----LRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIA--- 164
Cdd:PRK13547 85 RAVLPQAAQPAFafSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 165 ------VRPRVLLLDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALY 238
Cdd:PRK13547 165 pphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDW-NLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
.
gi 566074967 239 Q 239
Cdd:PRK13547 244 T 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-252 |
2.78e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 100.76 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 21 LDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVThlppYKR-------GLA 93
Cdd:PRK11288 7 FDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR----FASttaalaaGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 94 MVVQNYALFPHLKVEDNVAFGLRAQKQ---PKALINERVTQALKTVGMS-DYAARYPHqLSGGQQQRVAIARAIAVRPRV 169
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLYLGQLPHKGgivNRRLLNYEAREQLEHLGVDiDPDTPLKY-LSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 170 LLLDEPLSALDAQirhnmveEIACLHRELPEL-----TILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHppNR 244
Cdd:PRK11288 162 IAFDEPTSSLSAR-------EIEQLFRVIRELraegrVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVDR--DQ 232
|
....*...
gi 566074967 245 FAAEFLGR 252
Cdd:PRK11288 233 LVQAMVGR 240
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-229 |
3.26e-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: 96.02 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAY--HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYK--RGLAM 94
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 95 VVQNYALF---------PHLKVEDnvafglraqkqpkalinERVTQALKTVGMSDYAARYPHQL-----------SGGQQ 154
Cdd:cd03244 83 IPQDPVLFsgtirsnldPFGEYSD-----------------EELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 566074967 155 QRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIaclHRELPELTILYVTHdQTEALTLADKIGIMKDGSLI 229
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTI---REAFKDCTVLTIAH-RLDTIIDSDRILVLDKGRVV 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-232 |
9.47e-23 |
|
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: 93.92 E-value: 9.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGN--VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVV 96
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 97 QNYalfPHLkvednvaFGlraqkqpkalinervTQALKTVGMsdyaaryphQLSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:cd03247 81 NQR---PYL-------FD---------------TTLRNNLGR---------RFSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 177 SALDAQIRHNMVEEIAclhRELPELTILYVTHDQTeALTLADKIGIMKDGSLIAHG 232
Cdd:cd03247 127 VGLDPITERQLLSLIF---EVLKDKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
33-232 |
1.18e-22 |
|
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: 94.91 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRIlIGDTDVTHLppykrgLAMvvqNYALFPHLKVEDNVA 112
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-TVRGRVSSL------LGL---GGGFNPELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 113 FGLRA----QKQPKALINE---------RVTQALKTvgmsdyaaryphqLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:cd03220 107 LNGRLlglsRKEIDEKIDEiiefselgdFIDLPVKT-------------YSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 566074967 180 DAQIRHNMVEEIACLHRELPelTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQGK--TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-241 |
1.50e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 95.15 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 18 GIVLDSLRVAYHGnvvlkpLSLTIEPGEVLALIGPSGSGKTTVLRAVAGfVQPAG-----GRILIGDTDVthLPPYKRG- 91
Cdd:PRK10418 9 NIALQAAQPLVHG------VSLTLQRGRVLALVGGSGSGKSLTCAAALG-ILPAGvrqtaGRVLLDGKPV--APCALRGr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 92 -LAMVVQN--YALFPHLKVEDNVAFGLRAQKQPKAliNERVTQALKTVGMSDYAA---RYPHQLSGGQQQRVAIARAIAV 165
Cdd:PRK10418 80 kIATIMQNprSAFNPLHTMHTHARETCLALGKPAD--DATLTAALEAVGLENAARvlkLYPFEMSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 166 RPRVLLLDEPLSALDAQIRHNMVEEIACLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIVQK-RALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
21-209 |
6.38e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.67 E-value: 6.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 21 LDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILI-GDTDVTHLPpykrglamvvQNY 99
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRIGYLP----------QEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 100 ALFPHLKVEDNVAFGLRAQKQPKALINE--------------------------------RVTQALKTVGMS-DYAARYP 146
Cdd:COG0488 71 PLDDDLTVLDTVLDGDAELRALEAELEEleaklaepdedlerlaelqeefealggweaeaRAEEILSGLGFPeEDLDRPV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 566074967 147 HQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAqirhnmvEEIACLHRELPEL--TILYVTHD 209
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-------ESIEWLEEFLKNYpgTVLVVSHD 208
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
34-244 |
6.50e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 97.23 E-value: 6.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIG-------DTDVTHLPPYK-------RG--LAMVVQ 97
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRQVIELSEQSaaqmrhvRGadMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 98 N--YALFPHLKVEDNVAFGLR----AQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRlhqgASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 172 LDEPLSALDAQIRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALY---QHPPNR 244
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEM-SMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFhapQHPYTR 266
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
11-241 |
6.51e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 97.09 E-value: 6.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 11 PASQGTSGIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTH--LPPY 88
Cdd:PRK10789 308 PEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqLDSW 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 89 KRGLAMVVQNYALFPHlKVEDNVAFGlraqkQPKAlINERVTQALKTVGMSDYAARYPH-----------QLSGGQQQRV 157
Cdd:PRK10789 388 RSRLAVVSQTPFLFSD-TVANNIALG-----RPDA-TQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRI 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 158 AIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIaclhRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:PRK10789 461 SIARALLLNAEILILDDALSAVDGRTEHQILHNL----RQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQL 536
|
....
gi 566074967 238 YQHP 241
Cdd:PRK10789 537 AQQS 540
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
29-241 |
1.06e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 94.20 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 29 HGNV-VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQP----AGGRILIGDTDVTHLPPYKR------GLAMVVQ 97
Cdd:COG4170 17 QGRVkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 98 N--YALFPHLKVEDNVAFGLRAQK------QPKALINERVTQALKTVGMSDYAA---RYPHQLSGGQQQRVAIARAIAVR 166
Cdd:COG4170 97 EpsSCLDPSAKIGDQLIEAIPSWTfkgkwwQRFKWRKKRAIELLHRVGIKDHKDimnSYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 167 PRVLLLDEPLSALD----AQI-----RHNmveeiaclhrELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:COG4170 177 PRLLIADEPTNAMEsttqAQIfrllaRLN----------QLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQI 246
|
....
gi 566074967 238 YQHP 241
Cdd:COG4170 247 LKSP 250
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-237 |
1.28e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 96.35 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPY--KRGLAMV 95
Cdd:TIGR01193 474 IVINDVSYSYgYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHtlRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 96 VQNYALFPHlKVEDNVAFGLRaqkqPKALINErVTQALKTVGMSDYAARYPH-----------QLSGGQQQRVAIARAIA 164
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAK----ENVSQDE-IWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 566074967 165 VRPRVLLLDEPLSALDAQIRHNMVEEIAclhrELPELTILYVTHDQTEAlTLADKIGIMKDGSLIAHGETRAL 237
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLL----NLQDKTIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
19-226 |
1.46e-21 |
|
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: 89.43 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTdvthlppykrglamvvqn 98
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 99 yalfphlkvednvafglraqkqpkalinervtqalKTVGmsdyaarYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:cd03221 63 -----------------------------------VKIG-------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 566074967 179 LDaqirhnmVEEIACLHRELPEL--TILYVTHDQTEALTLADKIGIMKDG 226
Cdd:cd03221 101 LD-------LESIEALEEALKEYpgTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-232 |
2.11e-21 |
|
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: 91.63 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 2 LMKTTAVHapasQGTSGIvLDSLRVAYHGN----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILI 77
Cdd:cd03267 6 LSKSYRVY----SKEPGL-IGSLKSLFKRKyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 78 GDtdvthLPPYKR--------GLAM-----------VVQNYALFPHLKVEDNVAFGLRAqkqpkalinERVTQALKTVGM 138
Cdd:cd03267 81 AG-----LVPWKRrkkflrriGVVFgqktqlwwdlpVIDSFYLLAAIYDLPPARFKKRL---------DELSELLDLEEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 139 SDYAARyphQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIACLHRElPELTILYVTHDQTEALTLAD 218
Cdd:cd03267 147 LDTPVR---QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRE-RGTTVLLTSHYMKDIEALAR 222
|
250
....*....|....
gi 566074967 219 KIGIMKDGSLIAHG 232
Cdd:cd03267 223 RVLVIDKGRLLYDG 236
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
33-239 |
7.10e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.12 E-value: 7.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLP--PYKRGLAMVVQNYALFPH-LKveD 109
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSeaALRQAISVVSQRVHLFSAtLR--D 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 110 NVAFGlraqkQPKAlINERVTQALKTVGMSDYAARYP----------HQLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:PRK11160 433 NLLLA-----APNA-SDEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 180 DAQIRHNMVEEIA--CLHRelpelTILYVTHDQTeALTLADKIGIMKDGSLIAHGETRALYQ 239
Cdd:PRK11160 507 DAETERQILELLAehAQNK-----TVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQELLA 562
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-232 |
8.84e-21 |
|
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: 94.31 E-value: 8.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 37 LSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDV-THLPPYKRGLAMVVQNYALFPHLKVEDNVAF-- 113
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVAEHILFya 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 114 GLRAQKQPKALIneRVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEeiaC 193
Cdd:TIGR01257 1029 QLKGRSWEEAQL--EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD---L 1103
|
170 180 190
....*....|....*....|....*....|....*....
gi 566074967 194 LHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:TIGR01257 1104 LLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-194 |
9.13e-21 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 93.79 E-value: 9.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAG--GRILIGDTDVTHlpPYKRGLAMVVQNYALFPHLKVEDN 110
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK--QILKRTGFVTQDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAFG--LR----AQKQPKALINERVTQ--ALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQ 182
Cdd:PLN03211 161 LVFCslLRlpksLTKQEKILVAESVISelGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170
....*....|..
gi 566074967 183 IRHNMVEEIACL 194
Cdd:PLN03211 241 AAYRLVLTLGSL 252
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
34-234 |
1.05e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 89.99 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGfVQPAGGRILIGDTDVTHLPPYK----RG---------LAMVVQNYa 100
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAElarhRAylsqqqtppFAMPVFQY- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 101 LFPHLKVEDNVAfglraqkQPKALINErVTQALKtvgMSDYAARYPHQLSGGQQQRVAIARAI-----AVRP--RVLLLD 173
Cdd:PRK03695 90 LTLHQPDKTRTE-------AVASALNE-VAEALG---LDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 174 EPLSALDaqirhnmVEEIACLHRELPEL-----TILYVTHDQTEALTLADKIGIMKDGSLIAHGET 234
Cdd:PRK03695 159 EPMNSLD-------VAQQAALDRLLSELcqqgiAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRR 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
34-233 |
1.16e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.31 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP---YKRGLAMVVQNYALFPHLKVEDN 110
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLGIGIIYQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAFGLRAQKQ-------PKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDaqi 183
Cdd:PRK09700 101 LYIGRHLTKKvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT--- 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 566074967 184 rHNMVEEIACLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGE 233
Cdd:PRK09700 178 -NKEVDYLFLIMNQLRKegTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGM 228
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
30-211 |
2.02e-20 |
|
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: 87.21 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 30 GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILI-GDTDVTHLP--PYkrglamvvqnyalFPhlk 106
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLPqrPY-------------LP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 107 vednvaFG-LRAQkqpkaLInervtqalktvgmsdyaarYP--HQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQi 183
Cdd:cd03223 77 ------LGtLREQ-----LI-------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE- 125
|
170 180 190
....*....|....*....|....*....|
gi 566074967 184 rhnmvEEIAcLHRELPEL--TILYVTHDQT 211
Cdd:cd03223 126 -----SEDR-LYQLLKELgiTVISVGHRPS 149
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
37-181 |
3.31e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.95 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 37 LSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVT--HLPPYKRGLAMVVQNYALFPHlKVEDNVAFG 114
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRtvTRASLRRNIAVVFQDAGLFNR-SIEDNIRVG 432
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 115 lraqkQPKAlINERVTQALKTVGMSDYAARYPH-----------QLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDA 181
Cdd:PRK13657 433 -----RPDA-TDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSALDV 504
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
23-232 |
4.98e-20 |
|
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: 87.08 E-value: 4.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 23 SLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLP--PYKRGLAMVVQNYA 100
Cdd:cd03369 13 SVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPleDLRSSLTIIPQDPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 101 LF-----PHLKVEDNVAfglraqkqpkaliNERVTQALKTVGMSDyaaryphQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:cd03369 93 LFsgtirSNLDPFDEYS-------------DEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 566074967 176 LSALDAQIRHNMVEEIaclHRELPELTILYVTHdQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03369 153 TASIDYATDALIQKTI---REEFTNSTILTIAH-RLRTIIDYDKILVMDAGEVKEYD 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-233 |
6.96e-20 |
|
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: 91.02 E-value: 6.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTT---VLRAVAGFvQPAGGRIL-----------------IG 78
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVlmhVLRGMDQY-EPTSGRIIyhvalcekcgyverpskVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 79 ------------------DTDVTHLPPYKRGLAMVVQ-NYALFPHLKVEDNVafgLRAQKQPKALINERVTQALKTVGMS 139
Cdd:TIGR03269 80 epcpvcggtlepeevdfwNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNV---LEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 140 DYAARYPH---QLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD---AQIRHNMVEEIAclhreLPELTILYVTHDQTEA 213
Cdd:TIGR03269 157 QLSHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVHNALEEAV-----KASGISMVLTSHWPEV 231
|
250 260
....*....|....*....|.
gi 566074967 214 LT-LADKIGIMKDGSLIAHGE 233
Cdd:TIGR03269 232 IEdLSDKAIWLENGEIKEEGT 252
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
32-239 |
1.05e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.06 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIgdtdvthlppykRG-------LAMVVQnyalfPH 104
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV------------NGrvsalleLGAGFH-----PE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 105 LKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARyP-HQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:COG1134 103 LTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQ-PvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAF 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 184 RH-------NMVEEIAclhrelpelTILYVTHDQTEALTLADKIGIMKDGSLIAHGETR---ALYQ 239
Cdd:COG1134 182 QKkclarirELRESGR---------TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEeviAAYE 238
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
38-252 |
1.42e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.99 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVAGfVQPAG---GRIL----------IGDTDvthlppyKRGLAMVVQNYALFPH 104
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIfegeelqasnIRDTE-------RAGIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 105 LKVEDNVAFGlrAQKQPKALIN-----ERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:PRK13549 97 LSVLENIFLG--NEITPGGIMDydamyLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 180 DAQirhnmveEIACLHRELPEL-----TILYVTHDQTEALTLADKIGIMKDGSLIAhgeTRALYQHPPNRFAAEFLGR 252
Cdd:PRK13549 175 TES-------ETAVLLDIIRDLkahgiACIYISHKLNEVKAISDTICVIRDGRHIG---TRPAAGMTEDDIITMMVGR 242
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
19-229 |
2.00e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDT-DVTHLPpykrglamvvQ 97
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETvKIGYFD----------Q 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 98 NYALF-PHLKVEDNVAfGLRAQKQPKALIN--ERV----TQALKTVGmsdyaaryphQLSGGQQQRVAIARAIAVRPRVL 170
Cdd:COG0488 386 HQEELdPDKTVLDELR-DGAPGGTEQEVRGylGRFlfsgDDAFKPVG----------VLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 566074967 171 LLDEPLSALDAQIRhNMVEEIaclhrelpeL-----TILYVTHDQtEAL-TLADKIGIMKDGSLI 229
Cdd:COG0488 455 LLDEPTNHLDIETL-EALEEA---------LddfpgTVLLVSHDR-YFLdRVATRILEFEDGGVR 508
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
34-255 |
4.57e-19 |
|
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: 88.34 E-value: 4.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGfVQPAG---GRIL----------IGDTDvthlppyKRGLAMVVQNYA 100
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYwsgsplkasnIRDTE-------RAGIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 101 LFPHLKVEDNVAFG----LRAQKQPKALINERVTQALKTVGMSDY-AARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:TIGR02633 89 LVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 176 LSALDAQ--------IRHNMVEEIAClhrelpeltiLYVTHDQTEALTLADKIGIMKDGSLIAHG--------------- 232
Cdd:TIGR02633 169 SSSLTEKeteilldiIRDLKAHGVAC----------VYISHKLNEVKAVCDTICVIRDGQHVATKdmstmseddiitmmv 238
|
250 260
....*....|....*....|....*
gi 566074967 233 --ETRALYQHPPNRFAAEFLGRANI 255
Cdd:TIGR02633 239 grEITSLYPHEPHEIGDVILEARNL 263
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
34-240 |
1.08e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.38 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTH--LPPYKRGLAMVVQNYALFpHLKVEDNV 111
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLASLRNQVALVSQNVHLF-NDTIANNI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 112 AFG----------LRAQKQPKAL--InERVTQALKTV----GMSdyaaryphqLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:PRK11176 438 AYArteqysreqiEEAARMAYAMdfI-NKMDNGLDTVigenGVL---------LSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 566074967 176 LSALDAQirhnmvEEIAcLHRELPEL----TILYVTHdQTEALTLADKIGIMKDGSLIAHGETRALYQH 240
Cdd:PRK11176 508 TSALDTE------SERA-IQAALDELqknrTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
34-232 |
2.20e-18 |
|
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: 82.31 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAG---GRILIGDTDVTH-LPPYKRGLAMVVQNYALFPHLKVED 109
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEfAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 110 NVAFGLRAQkqpkalinervtqalktvgmsdyAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVE 189
Cdd:cd03233 103 TLDFALRCK-----------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 566074967 190 EIACLHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03233 160 CIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
34-250 |
3.62e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.87 E-value: 3.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAgFVQPAG----GRILIGDTDVThLPPYKRGLAMVVQNYALFPHLKVED 109
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGvkgsGSVLLNGMPID-AKEMRAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 110 NVAFG--LRAQKQ-PKALINERVTQALKTVGMSDYA------ARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:TIGR00955 119 HLMFQahLRMPRRvTKKEKRERVDEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 181 AQIRHNMVeeiaclhRELPEL-----TILYVTHDQT-EALTLADKIGIMKDGSLIAHGETRAL--------YQHPPNRFA 246
Cdd:TIGR00955 199 SFMAYSVV-------QVLKGLaqkgkTIICTIHQPSsELFELFDKIILMAEGRVAYLGSPDQAvpffsdlgHPCPENYNP 271
|
....
gi 566074967 247 AEFL 250
Cdd:TIGR00955 272 ADFY 275
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
33-210 |
1.29e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.77 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFV--QPAGGRILIGDTDVThlppykrglamvvQNYALFPHLKVEDN 110
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG-------------REASLIDAIGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAfglraqkqpkalineRVTQALKTVGMSD---YAARYPHqLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNM 187
Cdd:COG2401 112 FK---------------DAVELLNAVGLSDavlWLRRFKE-LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180
....*....|....*....|...
gi 566074967 188 VEEIACLHRELpELTILYVTHDQ 210
Cdd:COG2401 176 ARNLQKLARRA-GITLVVATHHY 197
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
29-251 |
2.21e-17 |
|
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: 81.44 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 29 HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRIligdtdvthlpPYKRGLAMVVQNYALFPHlKVE 108
Cdd:cd03291 48 VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------KHSGRISFSSQFSWIMPG-TIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 109 DNVAFGLRAQKQpkalineRVTQALKTVGMSDYAARYPHQ-----------LSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:cd03291 116 ENIIFGVSYDEY-------RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 566074967 178 ALDAQIRHNMVEeiACLHRELPELTILYVThDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNrFAAEFLG 251
Cdd:cd03291 189 YLDVFTEKEIFE--SCVCKLMANKTRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQSLRPD-FSSKLMG 258
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-251 |
2.96e-17 |
|
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: 83.42 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 13 SQGTSGIVLDSLrvAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRIligdtdvthlpPYKRGL 92
Cdd:TIGR01271 423 PNGDDGLFFSNF--SLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----------KHSGRI 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 93 AMVVQNYALFPHlKVEDNVAFGLRAQKQpkalineRVTQALKTVGMSDYAARYPHQ-----------LSGGQQQRVAIAR 161
Cdd:TIGR01271 490 SFSPQTSWIMPG-TIKDNIIFGLSYDEY-------RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLAR 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 162 AIAVRPRVLLLDEPLSALDAQIRHNMVEeiACLHRELPELTILYVThDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:TIGR01271 562 AVYKDADLYLLDSPFTHLDVVTEKEIFE--SCLCKLMSNKTRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
250
....*....|
gi 566074967 242 PNrFAAEFLG 251
Cdd:TIGR01271 639 PD-FSSLLLG 647
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-237 |
7.47e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 81.94 E-value: 7.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 23 SLR-VAYH---GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP--YKRGLAMVV 96
Cdd:PRK10522 324 ELRnVTFAyqdNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPedYRKLFSAVF 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 97 QNYALFPHLkvednvafgLRAQKQPKAliNERVTQALKTVGMSDYAARYPH-----QLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:PRK10522 404 TDFHLFDQL---------LGPEGKPAN--PALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566074967 172 LDEPLSALDAQIRHNMVEEIACLHRELPElTILYVTHDQtEALTLADKIGIMKDGSLIA-HGETRAL 237
Cdd:PRK10522 473 LDEWAADQDPHFRREFYQVLLPLLQEMGK-TIFAISHDD-HYFIHADRLLEMRNGQLSElTGEERDA 537
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
35-228 |
1.67e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.60 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 35 KPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPY---KRGLAMVVQNY---ALFPHLKVE 108
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdavKKGMAYITESRrdnGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 109 DNVAFgLRAQKQPK-----ALINERVTQALKTVGMSDYAARYPH------QLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:PRK09700 360 QNMAI-SRSLKDGGykgamGLFHEVDEQRTAENQRELLALKCHSvnqnitELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 566074967 178 ALDAQIRhnmvEEIACLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSL 228
Cdd:PRK09700 439 GIDVGAK----AEIYKVMRQLADdgKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-209 |
1.74e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.23 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILigdtdvtHLPPYKRGlaMVVQN 98
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------RNGKLRIG--YVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 99 YALFPHLKVEDNVAFGLRAQKQPKALInervtQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:PRK09544 76 LYLDTTLPLTVNRFLRLRPGTKKEDIL-----PALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190
....*....|....*....|....*....|.
gi 566074967 179 LDAQIRHNMVEEIACLHRELpELTILYVTHD 209
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRREL-DCAVLMVSHD 180
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
33-180 |
1.99e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 77.20 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIgDTDVTHLPPYKRGLAMVVQNYALFPHLKVEDNVA 112
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATRGDRSRFMAYLGHLPGLKADLSTLENLH 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 566074967 113 F-----GLRAQKQPkalinervTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK13543 105 FlcglhGRRAKQMP--------GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
37-228 |
2.35e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 37 LSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVV------QNYALFPHLKVEDN 110
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 V--------AFGLRAQKQPKALinERVTQALKT-VGMSDYAARyphQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDA 181
Cdd:PRK15439 362 VcalthnrrGFWIKPARENAVL--ERYRRALNIkFNHAEQAAR---TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 566074967 182 QIRHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGSL 228
Cdd:PRK15439 437 SARNDIYQLIRSIAAQ--NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
38-248 |
5.25e-16 |
|
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: 76.68 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPG-----EVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPY-KRGLAMVVQNyalFPHLKVEDnv 111
Cdd:cd03237 14 TLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYiKADYEGTVRD---LLSSITKD-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 112 aFGLRAQKQpkalinervTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRhNMVEEI 191
Cdd:cd03237 89 -FYTHPYFK---------TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR-LMASKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 566074967 192 ACLHRELPELTILYVTHDQTEALTLADKIgIMKDGSLIAHGETralyqHPP-------NRFAAE 248
Cdd:cd03237 158 IRRFAENNEKTAFVVEHDIIMIDYLADRL-IVFEGEPSVNGVA-----NPPqslrsgmNRFLKN 215
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
24-232 |
9.93e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 75.83 E-value: 9.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 24 LRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGfvQPA----GGRILIGDTDVTHLPPYKR---GLAMVV 96
Cdd:CHL00131 13 LHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERahlGIFLAF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 97 QNYALFPHLKVED--NVAFGLRAQKQPKALIN-----ERVTQALKTVGMSD-YAARYPHQ-LSGGQQQRVAIARAIAVRP 167
Cdd:CHL00131 91 QYPIEIPGVSNADflRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMALLDS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566074967 168 RVLLLDEPLSALDAQIRHNMVEEIACLHRelPELTILYVTHDQtEAL--TLADKIGIMKDGSLIAHG 232
Cdd:CHL00131 171 ELAILDETDSGLDIDALKIIAEGINKLMT--SENSIILITHYQ-RLLdyIKPDYVHVMQNGKIIKTG 234
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
33-209 |
1.51e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 77.67 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGdtdvthlPPYKRGlaMVVQNYALFPHLKVEDNVA 112
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-------PGIKVG--YLPQEPQLDPTKTVRENVE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 113 FGLRAQKQPKALINE--------------------RVTQALKTVGMSDY---------AARYP------HQLSGGQQQRV 157
Cdd:TIGR03719 91 EGVAEIKDALDRFNEisakyaepdadfdklaaeqaELQEIIDAADAWDLdsqleiamdALRCPpwdadvTKLSGGERRRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 566074967 158 AIARAIAVRPRVLLLDEPLSALDAqirhnmvEEIACLHRELPEL--TILYVTHD 209
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHLDA-------ESVAWLERHLQEYpgTVVAVTHD 217
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
34-227 |
2.03e-15 |
|
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: 74.67 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRI-----LIGDTDVTHLPPYKRGLAMVVQNYALFPHLKVE 108
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 109 DNVAFGLRAQKQP-KALINERVTQA---LKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIR 184
Cdd:cd03290 97 ENITFGSPFNKQRyKAVTDACSLQPdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 566074967 185 -HNMVEEIACLHRElPELTILYVTHdQTEALTLADKIGIMKDGS 227
Cdd:cd03290 177 dHLMQEGILKFLQD-DKRTLVLVTH-KLQYLPHADWIIAMKDGS 218
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-250 |
2.85e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 77.46 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVA----GFVQPAGGRILIGDTDVTHLPPYKRG-LAMVVQNYALFPHLKV 107
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGdVVYNAETDVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 108 EDNVAFGLR---AQKQPKALINERVTQALKTVGMSDYAARYPHQ----------LSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:TIGR00956 156 GETLDFAARcktPQNRPDGVSREEYAKHIADVYMATYGLSHTRNtkvgndfvrgVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 175 PLSALDAQIRHNMV---EEIACLHRELPELTILYVTHDqteALTLADKIGIMKDGSLIAHGE-TRAL-------YQHPPN 243
Cdd:TIGR00956 236 ATRGLDSATALEFIralKTSANILDTTPLVAIYQCSQD---AYELFDKVIVLYEGYQIYFGPaDKAKqyfekmgFKCPDR 312
|
....*..
gi 566074967 244 RFAAEFL 250
Cdd:TIGR00956 313 QTTADFL 319
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
38-230 |
3.03e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.97 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPP---YKRGLAMVVQNYALFPHLKVEDNVAFG 114
Cdd:PRK10762 24 ALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkssQEAGIGIIHQELNLIPQLTIAENIFLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 115 lRAQKQPKALIN-----ERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL-DAqirhnmv 188
Cdd:PRK10762 104 -REFVNRFGRIDwkkmyAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDT------- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 566074967 189 eEIACLHRELPELT-----ILYVTHDQTEALTLADKIGIMKDGSLIA 230
Cdd:PRK10762 176 -ETESLFRVIRELKsqgrgIVYISHRLKEIFEICDDVTVFRDGQFIA 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
34-232 |
5.00e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 76.70 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQP-AGGRILIgdtdvthlppykRG-LAMVVQNYALFpHLKVEDNV 111
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVI------------RGtVAYVPQVSWIF-NATVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 112 AFGLRAQKqpkalinERVTQALKTVGMSDYAARYPH-----------QLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PLN03130 700 LFGSPFDP-------ERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 566074967 181 AQIRHNMVEEiaCLHRELPELTILYVThDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:PLN03130 773 AHVGRQVFDK--CIKDELRGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEG 821
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-257 |
5.29e-15 |
|
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: 76.98 E-value: 5.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 37 LSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQ-PAGGRILIGDTDVTHLPPYKRGLAMVVQNYALFPHLKVEDNVAFGL 115
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTvTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 116 RAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIACLH 195
Cdd:TIGR01257 2038 RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII 2117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 196 RElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETralyQHPPNRFAAEFLGRANILS 257
Cdd:TIGR01257 2118 RE--GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTI----QHLKSKFGDGYIVTMKIKS 2173
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
34-248 |
5.65e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.74 E-value: 5.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDvthlpPYKR--GLAM---VV--QNYALFPHLK 106
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PFKRrkEFARrigVVfgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 107 VEDNvafgLRAQKQ----PKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQ 182
Cdd:COG4586 113 AIDS----FRLLKAiyriPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVV 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 183 IRHNMVEEIACLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALyqhpPNRFAAE 248
Cdd:COG4586 189 SKEAIREFLKEYNRER-GTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEEL----KERFGPY 249
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-241 |
6.10e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 76.36 E-value: 6.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIgdtdvthlppyKRGLAMVVQNyALFPHLKVEDNV 111
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-----------ERSIAYVPQQ-AWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 112 AF--GLRAQKQPKALineRVTQ-----ALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIR 184
Cdd:PTZ00243 742 LFfdEEDAARLADAV---RVSQleadlAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 566074967 185 HNMVEEiaCLHRELPELTILYVTHdQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:PTZ00243 819 ERVVEE--CFLGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
42-223 |
7.03e-15 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 73.55 E-value: 7.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 42 EPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRiLIGDTDVTHLPPYKRGLAMvvQNYalFPHLKvEDNVAFGLRAQ--- 118
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEILDEFRGSEL--QNY--FTKLL-EGDVKVIVKPQyvd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 119 ---KQPKALINERVTQALKTvGMSDYAA----------RYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRH 185
Cdd:cd03236 98 lipKAVKGKVGELLKKKDER-GKLDELVdqlelrhvldRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 566074967 186 NMveeiACLHREL--PELTILYVTHDQTEALTLADKIGIM 223
Cdd:cd03236 177 NA----ARLIRELaeDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-239 |
1.39e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.14 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 11 PASQGTsgIVLDSLRVAY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLP--P 87
Cdd:PRK10790 335 PLQSGR--IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 88 YKRGLAMVVQNYALFPHlKVEDNVAFGlraqkqpKALINERVTQALKTVGMSDYAARYP-----------HQLSGGQQQR 156
Cdd:PRK10790 413 LRQGVAMVQQDPVVLAD-TFLANVTLG-------RDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 157 VAIARAIAVRPRVLLLDEPLSALDAQIRhnmvEEIACLHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRA 236
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDSGTE----QAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQ 560
|
...
gi 566074967 237 LYQ 239
Cdd:PRK10790 561 LLA 563
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
37-241 |
2.41e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 73.30 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 37 LSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQP----AGGRILIGDTDVTHLPPYKR------GLAMVVQ--NYALFPH 104
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERrklvghNVSMIFQepQSCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 105 LKVEDNVA---------------FGLRAQkqpkalineRVTQALKTVGMSDYAA---RYPHQLSGGQQQRVAIARAIAVR 166
Cdd:PRK15093 106 ERVGRQLMqnipgwtykgrwwqrFGWRKR---------RAIELLHRVGIKDHKDamrSFPYELTEGECQKVMIAIALANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 566074967 167 PRVLLLDEPLSALDAQIRHNMVEEIACLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHP 241
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQN-NNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
31-239 |
3.57e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.24 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 31 NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPpykrglamvvQNYALFpHLKVEDN 110
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVP----------QVSWIF-NATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAFGLRAQkqpkaliNERVTQALKTVGMSDYAARYPHQ-----------LSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:PLN03232 699 ILFGSDFE-------SERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 180 DAQIRHNMVEeiACLHRELPELTILYVThDQTEALTLADKIGIMKDGSLIAHGETRALYQ 239
Cdd:PLN03232 772 DAHVAHQVFD--SCMKDELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-245 |
5.25e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.47 E-value: 5.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTH--LPPYKRGLAMVVQNYALFphlkvEDN 110
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLF-----SGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAFGLraqkQPKALINER-VTQALKTVGMSDYAARYPHQL-----------SGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:PLN03232 1326 VRFNI----DPFSEHNDAdLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566074967 179 LDAQIRHNMVEEIaclHRELPELTILYVTHdQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRF 245
Cdd:PLN03232 1402 VDVRTDSLIQRTI---REEFKSCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-209 |
8.80e-14 |
|
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: 72.52 E-value: 8.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 5 TTAVHAPASQGTSGIVLDSLRVAYHG-----NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGD 79
Cdd:COG4615 314 ADAAAPPAPADFQTLELRGVTYRYPGedgdeGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 80 TDVT--HLPPYKRGLAMVVQNYALFPHLkvednvaFGLRAQKQPkalinERVTQALKTVGMSdyaarypH---------- 147
Cdd:COG4615 394 QPVTadNREAYRQLFSAVFSDFHLFDRL-------LGLDGEADP-----ARARELLERLELD-------Hkvsvedgrfs 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 148 --QLSGGQQQRVAIARAIAV-RPrVLLLDEPLSALDAQIRHNMVEEIaclhreLPEL-----TILYVTHD 209
Cdd:COG4615 455 ttDLSQGQRKRLALLVALLEdRP-ILVFDEWAADQDPEFRRVFYTEL------LPELkargkTVIAISHD 517
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
38-229 |
1.30e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.74 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVAGfVQPAG---GRIL----------IGDTDvthlppyKRGLAMVVQNYALFPH 104
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHGsyeGEILfdgevcrfkdIRDSE-------ALGIVIIHQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 105 LKVEDNVAFGLRAQKqpKALIN-----ERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:NF040905 93 LSIAENIFLGNERAK--RGVIDwnetnRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 566074967 180 DAQIRHNMVEeiacLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLI 229
Cdd:NF040905 171 NEEDSAALLD----LLLELKAqgITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
36-233 |
1.46e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 36 PLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILI-GDTDVTHLPP--YKRGLAMVVQNY---ALFPHLKVED 109
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdGKPIDIRSPRdaIRAGIMLCPEDRkaeGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 110 NVAFGLRAQKQP-KALINERVTQALKTVGMSDYAARYPH------QLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQ 182
Cdd:PRK11288 351 NINISARRHHLRaGCLINNRWEAENADRFIRSLNIKTPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVG 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 183 IRHnmveEIACLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSL---IAHGE 233
Cdd:PRK11288 431 AKH----EIYNVIYELAAqgVAVLFVSSDLPEVLGVADRIVVMREGRIageLAREQ 482
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-180 |
1.53e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.82 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 23 SLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILI-GDTDVTHLPPYKRGLAMVVQNYAL 101
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKKDLCTYQKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 102 FPHLKVEDNVAFGLRAQKQpkaliNERVTQALKTVGMSDYaARYP-HQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK13540 86 NPYLTLRENCLYDIHFSPG-----AVGITELCRLFSLEHL-IDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-180 |
1.57e-13 |
|
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: 71.50 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 24 LRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVthlppykrgLAMVVQNY-ALF 102
Cdd:TIGR03719 328 LTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK---------LAYVDQSRdALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 103 PHLKVEDNVAFGLRAQKQPKALINERV---------TQALKTVGmsdyaaryphQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:TIGR03719 399 PNKTVWEEISGGLDIIKLGKREIPSRAyvgrfnfkgSDQQKKVG----------QLSGGERNRVHLAKTLKSGGNVLLLD 468
|
....*..
gi 566074967 174 EPLSALD 180
Cdd:TIGR03719 469 EPTNDLD 475
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-209 |
2.01e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.52 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 17 SG-IVLDSLRVAYH--GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDT-DVTHLPPYKRgl 92
Cdd:PRK11147 315 SGkIVFEMENVNYQidGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFDQHRA-- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 93 amvvqnyALFPHLKVEDNVAFGlraqKQpKALINERVTQALKTvgMSDY-----AARYP-HQLSGGQQQRVAIARaIAVR 166
Cdd:PRK11147 393 -------ELDPEKTVMDNLAEG----KQ-EVMVNGRPRHVLGY--LQDFlfhpkRAMTPvKALSGGERNRLLLAR-LFLK 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 566074967 167 PRVLL-LDEPLSALDaqirhnmVEEIACLHRELPEL--TILYVTHD 209
Cdd:PRK11147 458 PSNLLiLDEPTNDLD-------VETLELLEELLDSYqgTVLLVSHD 496
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
34-250 |
2.22e-13 |
|
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: 71.90 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIgdtdvthlppyKRGLAMVVQNyALFPHLKVEDNVAF 113
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-----------KGSVAYVPQQ-AWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 114 GlraqkqpKALINERVTQALKTVGMSDYAARYPH-----------QLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQ 182
Cdd:TIGR00957 722 G-------KALNEKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 183 IRHNMVEEIACLHRELPELTILYVTHDQTeALTLADKIGIMKDGSLIAHGETRALYQHppNRFAAEFL 250
Cdd:TIGR00957 795 VGKHIFEHVIGPEGVLKNKTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELLQR--DGAFAEFL 859
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
33-180 |
3.09e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.21 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDT----DVtHLPPYKRGLAMVVQNYALFPHlKVE 108
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkDI-NLKWWRSKIGVVSQDPLLFSN-SIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 109 DNVAFGLRAQKQPKALINE---------------------------------------------------RVTQALKTVG 137
Cdd:PTZ00265 478 NNIKYSLYSLKDLEALSNYynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVL 557
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 566074967 138 MSDYAARYP-----------HQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PTZ00265 558 IHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
43-220 |
5.37e-13 |
|
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: 65.86 E-value: 5.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 43 PGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAmvvqnyalfphlkvednvafglraqkqpk 122
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLL----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 123 alinervtqalktvgmsDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIACLHRELPE-- 200
Cdd:smart00382 52 -----------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKse 114
|
170 180
....*....|....*....|..
gi 566074967 201 --LTILYVTHDQTEALTLADKI 220
Cdd:smart00382 115 knLTVILTTNDEKDLGPALLRR 136
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
19-229 |
1.62e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.38 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRIligdtdvthlppykrglamvvqn 98
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------------------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 99 yalfphlKVEDNVAFGLRAQ-------------------KQPKAliNERVTQAlkTVGM----SDYAARYPHQLSGGQQQ 155
Cdd:PRK15064 377 -------KWSENANIGYYAQdhaydfendltlfdwmsqwRQEGD--DEQAVRG--TLGRllfsQDDIKKSVKVLSGGEKG 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 156 RVAIARAIAVRPRVLLLDEPLSALDaqirhnmVEEIACLHR--ELPELTILYVTHDQTEALTLADKIGIMKDGSLI 229
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMD-------MESIESLNMalEKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
39-209 |
2.00e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.44 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 39 LTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILI-GDTDVTHL---PPykRGLAMVVQNY------ALFPHLKVE 108
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDLIVARLqqdPP--RNVEGTVYDFvaegieEQAEYLKRY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 109 DNVAFgLRAQKQPKALINE------------------RVTQALKTVGMSdyaaryPHQ----LSGGQQQRVAIARAIAVR 166
Cdd:PRK11147 102 HDISH-LVETDPSEKNLNElaklqeqldhhnlwqlenRINEVLAQLGLD------PDAalssLSGGWLRKAALGRALVSN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 566074967 167 PRVLLLDEPLSALDaqirhnmVEEIACLHRELPEL--TILYVTHD 209
Cdd:PRK11147 175 PDVLLLDEPTNHLD-------IETIEWLEGFLKTFqgSIIFISHD 212
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
41-189 |
6.77e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 63.80 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 41 IEPGEVLALIGPSGSGKTTVL-----RAVAGFVqpaGGRILIGDTDVThlPPYKRGLAMVVQNYALFPHLKVEDNVAFG- 114
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLdvlagRKTAGVI---TGEILINGRPLD--KNFQRSTGYVEQQDVHSPNLTVREALRFSa 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 115 -LRAqkqpkalinervtqalktvgmsdyaaryphqLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVE 189
Cdd:cd03232 105 lLRG-------------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
37-235 |
7.98e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.39 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 37 LSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPA-GGRILIGDTDVTHLPPYK---RGLAMVVQN---YALFPHLKVED 109
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 110 NVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPH------QLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:TIGR02633 359 NITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpflpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 184 RHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDG----SLIAHGETR 235
Cdd:TIGR02633 439 KYEIYKLINQLAQE--GVAIIVVSSELAEVLGLSDRVLVIGEGklkgDFVNHALTQ 492
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
34-230 |
1.06e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDV---THLPPYKRGLAMVVQNYALFPHLKVEDN 110
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAFGLRAQKQPkaLINE----RVTQAL-KTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQirh 185
Cdd:PRK10982 94 MWLGRYPTKGM--FVDQdkmyRDTKAIfDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK--- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 566074967 186 nMVEEIACLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIA 230
Cdd:PRK10982 169 -EVNHLFTIIRKLKErgCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
31-184 |
1.06e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 63.35 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 31 NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLP-PYkrgLAMVVQNYALFPHLKVED 109
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkPY---CTYIGHNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 566074967 110 NVAFGLRAQKQpkaliNERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIR 184
Cdd:PRK13541 90 NLKFWSEIYNS-----AETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
73-232 |
1.12e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.59 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 73 GRILIGDTDVT--HLPPYKRGLAMVVQNYALFpHLKVEDNVAFGlraqKQPKALinERVTQALKTVGMSDYAARYPHQ-- 148
Cdd:PTZ00265 1277 GKILLDGVDICdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFG----KEDATR--EDVKRACKFAAIDEFIESLPNKyd 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 149 ---------LSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQiRHNMVEEIACLHRELPELTILYVTHdQTEALTLADK 219
Cdd:PTZ00265 1350 tnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427
|
170
....*....|....*...
gi 566074967 220 IGIM----KDGSLI-AHG 232
Cdd:PTZ00265 1428 IVVFnnpdRTGSFVqAHG 1445
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-209 |
1.28e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.91 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGriligdtDVTHLPPYKRGLAMvvQNYALFPHLKVEDNV 111
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------EARPAPGIKVGYLP--QEPQLDPEKTVRENV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 112 AFGLRAQKQPKALINE--------------------RVTQALKTVGMSDY---------AARYPH------QLSGGQQQR 156
Cdd:PRK11819 92 EEGVAEVKAALDRFNEiyaayaepdadfdalaaeqgELQEIIDAADAWDLdsqleiamdALRCPPwdakvtKLSGGERRR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 566074967 157 VAIARAIAVRPRVLLLDEPLSALDAqirhnmvEEIACLHRELPEL--TILYVTHD 209
Cdd:PRK11819 172 VALCRLLLEKPDMLLLDEPTNHLDA-------ESVAWLEQFLHDYpgTVVAVTHD 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
40-223 |
2.75e-11 |
|
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: 64.81 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 40 TIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRIligDTDvthlPPYKRglamVVQNYA---LFPHL-KVEDNvafGL 115
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEE----PSWDE----VLKRFRgteLQDYFkKLANG---EI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 116 R-AQK-Q-----PKALiNERVTQALKTV---GMSDYAA----------RYPHQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:COG1245 161 KvAHKpQyvdliPKVF-KGTVRELLEKVderGKLDELAeklglenildRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 566074967 176 LSALDAQIRHNMVEEIaclhRELPEL--TILYVTHDqteaLT----LADKIGIM 223
Cdd:COG1245 240 SSYLDIYQRLNVARLI----RELAEEgkYVLVVEHD----LAildyLADYVHIL 285
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-182 |
2.90e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.13 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVqpAGGRILIGDTDVTHLP---PYKRGLAMVVQNYALFPHLKVE 108
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGDRLVNGRPldsSFQRSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 109 DNVAFG--LR-AQKQPKALINERVTQALKTVGMSDYA---ARYPHQ-LSGGQQQRVAIARAIAVRPRVLL-LDEPLSALD 180
Cdd:TIGR00956 855 ESLRFSayLRqPKSVSKSEKMEYVEEVIKLLEMESYAdavVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
..
gi 566074967 181 AQ 182
Cdd:TIGR00956 935 SQ 936
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-180 |
3.65e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.50 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 21 LDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGF--VQPAGGRILIGDTDVTHLPPYKR---GLAMV 95
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRageGIFMA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 96 VQNYALFPhlkvedNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQL---------------SGGQQQRVAIA 160
Cdd:PRK09580 84 FQYPVEIP------GVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDIL 157
|
170 180
....*....|....*....|
gi 566074967 161 RAIAVRPRVLLLDEPLSALD 180
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLD 177
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
6-247 |
5.35e-11 |
|
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: 62.23 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 6 TAVHAPASQGTSG----IVLDSLRVAYHGNV--VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGD 79
Cdd:cd03288 3 ASISGSSNSGLVGlggeIKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 80 TDVTHLPPY--KRGLAMVVQNYALFphlkvEDNVAFGLRAQKQpkaLINERVTQALKTVGMSDYAARYPHQL-------- 149
Cdd:cd03288 83 IDISKLPLHtlRSRLSIILQDPILF-----SGSIRFNLDPECK---CTDDRLWEALEIAQLKNMVKSLPGGLdavvtegg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 150 ---SGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIrHNMVEEIacLHRELPELTILYVTHDQTEALTlADKIGIMKDG 226
Cdd:cd03288 155 enfSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-ENILQKV--VMTAFADRTVVTIAHRVSTILD-ADLVLVLSRG 230
|
250 260
....*....|....*....|.
gi 566074967 227 SLIAHGETRALYQHPPNRFAA 247
Cdd:cd03288 231 ILVECDTPENLLAQEDGVFAS 251
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
38-228 |
5.50e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRI-LIGDTDVTHLPpyKRGLA------------------MVV-Q 97
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVtLDGHEVVTRSP--QDGLAngivyisedrkrdglvlgMSVkE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 98 NYALfPHLKVEDNVAFGLRAQKQPKA------LINERVTQALKTVGMsdyaaryphqLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:PRK10762 350 NMSL-TALRYFSRAGGSLKHADEQQAvsdfirLFNIKTPSMEQAIGL----------LSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 566074967 172 LDEPLSALDAQIRhnmvEEIACLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSL 228
Cdd:PRK10762 419 LDEPTRGVDVGAK----KEIYQLINQFKAegLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
40-223 |
1.14e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 40 TIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAggrilIGDTDVthlPP-------YKRGLAMvvQNYalFPHLKveDNva 112
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPN-----LGDYEE---EPswdevlkRFRGTEL--QNY--FKKLY--NG-- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 113 fGLR-AQK-Q-----PKALiNERVTQALKTV---GMSDYAA----------RYPHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:PRK13409 159 -EIKvVHKpQyvdliPKVF-KGKVRELLKKVderGKLDEVVerlglenildRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 173 DEPLSALDAQIRHNMVEEIaclhREL-PELTILYVTHDqteaLT----LADKIGIM 223
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLI----RELaEGKYVLVVEHD----LAvldyLADNVHIA 284
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-180 |
1.48e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.44 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTdVThlppykrgLAMVVQN 98
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET-VK--------LAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 99 Y-ALFPHLKVEDNVAFGLRAQKQPKALINERVtqalktvgmsdYAARY----PHQ------LSGGQQQRVAIARAIAVRP 167
Cdd:PRK11819 396 RdALDPNKTVWEEISGGLDIIKVGNREIPSRA-----------YVGRFnfkgGDQqkkvgvLSGGERNRLHLAKTLKQGG 464
|
170
....*....|...
gi 566074967 168 RVLLLDEPLSALD 180
Cdd:PRK11819 465 NVLLLDEPTNDLD 477
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
8-209 |
1.68e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 8 VHAPASQGTSGIVLD--SLRVAYhGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIgDTDVTHL 85
Cdd:PRK13409 328 ERPPRDESERETLVEypDLTKKL-GDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELKISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 86 PPYKRGlamvvqnyalfphlKVEDNVAFGLRAQKQP--KALINERVTQALKTVGMSDyaaRYPHQLSGGQQQRVAIARAI 163
Cdd:PRK13409 406 PQYIKP--------------DYDGTVEDLLRSITDDlgSSYYKSEIIKPLQLERLLD---KNVKDLSGGELQRVAIAACL 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 566074967 164 AVRPRVLLLDEPLSALDAQ--------IRHnMVEEiaclhrelPELTILYVTHD 209
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDVEqrlavakaIRR-IAEE--------REATALVVDHD 513
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
294-367 |
2.88e-10 |
|
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: 55.70 E-value: 2.88e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 294 LCIRPQHLSLtprSAYSNRFNATLQSVHWQGDLTHLLCDVAGETVRMVLTHVN--PLPRVGDKLALWFEPDDAVLI 367
Cdd:pfam08402 1 LAIRPEKIRL---AAAANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAhaRPPAPGDRVGLGWDPEDAHVL 73
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-219 |
3.24e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.89 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 23 SLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVThlppyKRGLAMVVQNYALF 102
Cdd:TIGR00957 1291 CLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA-----KIGLHDLRFKITII 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 103 PhlkvEDNVAFG--LRAQKQP-KALINERVTQALKTVGMSDYAARYP----HQ-------LSGGQQQRVAIARAIAVRPR 168
Cdd:TIGR00957 1366 P----QDPVLFSgsLRMNLDPfSQYSDEEVWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTK 1441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 566074967 169 VLLLDEPLSALDAQIrHNMVEeiACLHRELPELTILYVTH------DQTEALTLaDK 219
Cdd:TIGR00957 1442 ILVLDEATAAVDLET-DNLIQ--STIRTQFEDCTVLTIAHrlntimDYTRVIVL-DK 1494
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
128-237 |
5.06e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.13 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 128 RVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIACLHRElpELTILYVT 207
Cdd:NF000106 124 RADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD--GATVLLTT 201
|
90 100 110
....*....|....*....|....*....|
gi 566074967 208 HDQTEALTLADKIGIMKDGSLIAHGETRAL 237
Cdd:NF000106 202 QYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
19-180 |
5.16e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAG------------FVQPAGGriliGDT--DVth 84
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltlFGRRRGS----GETiwDI-- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 85 lppyKRGLAMVVQNYalfpHL--KVEDNV----------AFGLRaQKQPKALiNERVTQALKTVGMSDYAARYP-HQLSG 151
Cdd:PRK10938 335 ----KKHIGYVSSSL----HLdyRVSTSVrnvilsgffdSIGIY-QAVSDRQ-QKLAQQWLDILGIDKRTADAPfHSLSW 404
|
170 180
....*....|....*....|....*....
gi 566074967 152 GQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK10938 405 GQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-232 |
1.03e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.14 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVThlppyKRGLAMVVQNYALFPHLKV--EDN 110
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS-----KFGLMDLRKVLGIIPQAPVlfSGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAFGLRA-QKQPKALINERVTQA-LKTV------GMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL--- 179
Cdd:PLN03130 1329 VRFNLDPfNEHNDADLWESLERAhLKDVirrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVdvr 1408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 566074967 180 -DAQIRHNMVEEI-AClhrelpelTILYVTHdQTEALTLADKIGIMKDGSLIAHG 232
Cdd:PLN03130 1409 tDALIQKTIREEFkSC--------TMLIIAH-RLNTIIDCDRILVLDAGRVVEFD 1454
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
19-180 |
1.77e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 57.94 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAY--HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDT-DVTHLPPYKRGLAMV 95
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSwNSVPLQKWRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 96 VQNYALFphlkvednvAFGLRAQKQPKALIN-ERVTQALKTVGMSDYAARYPHQ-----------LSGGQQQRVAIARAI 163
Cdd:cd03289 83 PQKVFIF---------SGTFRKNLDPYGKWSdEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSV 153
|
170
....*....|....*..
gi 566074967 164 AVRPRVLLLDEPLSALD 180
Cdd:cd03289 154 LSKAKILLLDEPSAHLD 170
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-226 |
2.37e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.72 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 30 GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILigdtdvthlppykRGLAMVVqnyALFPHLKVEd 109
Cdd:PLN03073 521 GPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-------------RSAKVRM---AVFSQHHVD- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 110 nvafGLRAQKQP--------KALINERVTQALKTVGMSDYAARYP-HQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PLN03073 584 ----GLDLSSNPllymmrcfPGVPEQKLRAHLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 566074967 181 AQIRHNMVEEIAclhreLPELTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:PLN03073 660 LDAVEALIQGLV-----LFQGGVLMVSHDEHLISGSVDELWVVSEG 700
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-184 |
3.26e-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: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 8 VHAPASQGTSGIVL--DSLRVAYHGnvvlkpLSLTIEPG-----EVLALIGPSGSGKTTVLRAVAGFVQPAGGRIlIGDT 80
Cdd:COG1245 329 VHAPRREKEEETLVeyPDLTKSYGG------FSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-DEDL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 81 DVTHLPPYkrglamVVQNYalfpHLKVEDNVaFGLRAQKQPKALINERVTQALKTVGMSDyaaRYPHQLSGGQQQRVAIA 160
Cdd:COG1245 402 KISYKPQY------ISPDY----DGTVEEFL-RSANTDDFGSSYYKTEIIKPLGLEKLLD---KNVKDLSGGELQRVAIA 467
|
170 180
....*....|....*....|....
gi 566074967 161 RAIAVRPRVLLLDEPLSALDAQIR 184
Cdd:COG1245 468 ACLSRDADLYLLDEPSAHLDVEQR 491
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
38-239 |
3.51e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.10 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPpYKRGLAMVVQNYALFPH-LKVEDNVAFGLR 116
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS-FEQLQKLVSDEWQRNNTdMLSPGEDDTGRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 117 A----QKQPKAliNERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIA 192
Cdd:PRK10938 102 TaeiiQDEVKD--PARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 566074967 193 CLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQ 239
Cdd:PRK10938 180 SLHQS--GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-180 |
3.66e-09 |
|
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: 58.38 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 30 GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDT-DVTHLPPYKRGLAMVVQNYALFphlkve 108
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSwNSVTLQTWRKAFGVIPQKVFIF------ 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 109 dnvAFGLRAQKQPKA-LINERVTQALKTVGMSDYAARYPHQ-----------LSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:TIGR01271 1305 ---SGTFRKNLDPYEqWSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
....
gi 566074967 177 SALD 180
Cdd:TIGR01271 1382 AHLD 1385
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
8-182 |
7.13e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.55 E-value: 7.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 8 VHAPASQGTSGIVLDSLRVayhgnvvLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGfvQPAGGRILiGDTDVTHLPP 87
Cdd:PLN03140 877 VDMPAEMKEQGVTEDRLQL-------LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPK 946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 88 YKRGLAMVV----QNYALFPHLKVEDNVAFG--LR----AQKQPKALINERVTQALKTVGMSDYAARYP--HQLSGGQQQ 155
Cdd:PLN03140 947 KQETFARISgyceQNDIHSPQVTVRESLIYSafLRlpkeVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRK 1026
|
170 180
....*....|....*....|....*..
gi 566074967 156 RVAIARAIAVRPRVLLLDEPLSALDAQ 182
Cdd:PLN03140 1027 RLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-179 |
7.40e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.45 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 17 SGIVLDSLRVAY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILI-GDTDVTHLP--PY-KRG 91
Cdd:TIGR00954 450 NGIKFENIPLVTpNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpAKGKLFYVPqrPYmTLG 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 92 lamVVQNYALFPHlKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:TIGR00954 530 ---TLRDQIIYPD-SSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAI 605
|
....*...
gi 566074967 172 LDEPLSAL 179
Cdd:TIGR00954 606 LDECTSAV 613
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
34-250 |
9.54e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 9.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYK---RGLAMVVQ---NYALFPHLKV 107
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainHGFALVTEerrSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 108 EDN-VAFGLRAQKQPKALI-NERVTQALKTVGMSDYAARYPHQ-----LSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK10982 344 GFNsLISNIRNYKNKVGLLdNSRMKSDTQWVIDSMRVKTPGHRtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 181 AQIRHNMVEEIACLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFL 250
Cdd:PRK10982 424 VGAKFEIYQLIAELAKK--DKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQNEILRLASLHL 491
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
10-228 |
1.58e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 10 APASQGTSGIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRIligdtdvthlppyk 89
Cdd:PRK10636 304 APESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 90 rGLAMVVQnYALFPHLKVEdnvafGLRAQKQP---KALINERVT-QALKtvgmsDYAARYPHQ----------LSGGQQQ 155
Cdd:PRK10636 370 -GLAKGIK-LGYFAQHQLE-----FLRADESPlqhLARLAPQELeQKLR-----DYLGGFGFQgdkvteetrrFSGGEKA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 566074967 156 RVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIACLhrelpELTILYVTHDQTEALTLADKIGIMKDGSL 228
Cdd:PRK10636 438 RLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF-----EGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-240 |
2.32e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRI--LIGD-TDVTH----------L 85
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevLGGDmADARHrravcpriayM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 86 PpykRGLAmvvQNyaLFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAV 165
Cdd:NF033858 82 P---QGLG---KN--LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIH 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 566074967 166 RPRVLLLDEPLSALDAQIRHNMVEEIACLHRELPELTILYVTHDQTEALTLaDKIGIMKDGSLIAHGETRALYQH 240
Cdd:NF033858 154 DPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLAR 227
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
41-220 |
3.88e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.57 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 41 IEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKrglamvvqnyalfphlkvednvafglraqkq 120
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 121 pkalinervtqalktvgmsdyaaryphQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIACLHRElPE 200
Cdd:cd03222 71 ---------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE-GK 122
|
170 180
....*....|....*....|
gi 566074967 201 LTILYVTHDQTEALTLADKI 220
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRI 142
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
38-237 |
3.98e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILI-------GDTDVthlppyKRGLAMVVQNYALFPHLKVEDN 110
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvdaGDIAT------RRRVGYMSQAFSLYGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VA-----FGLraqkqPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRH 185
Cdd:NF033858 360 LElharlFHL-----PAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 566074967 186 NMVEEIACLHRElPELTILYVTHDQTEALtLADKIGIMKDGSLIAHGETRAL 237
Cdd:NF033858 435 MFWRLLIELSRE-DGVTIFISTHFMNEAE-RCDRISLMHAGRVLASDTPAAL 484
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
32-224 |
6.42e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.59 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVaGFVqpAGGRiligdtdvtHLPPYKRGLAMVVQNYALFphlKVEDNV 111
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAI-GLA--LGGA---------QSATRRRSGVKAGCIVAAV---SAELIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 112 AFglraqkqpkalinervtqalktvgmsdyaarypHQLSGGQQQRVAIARAIA---VRPRVL-LLDEPLSALDAQIRHNM 187
Cdd:cd03227 74 TR---------------------------------LQLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQAL 120
|
170 180 190
....*....|....*....|....*....|....*..
gi 566074967 188 VEeiACLHRELPELTILYVTHDQTEALtLADKIGIMK 224
Cdd:cd03227 121 AE--AILEHLVKGAQVIVITHLPELAE-LADKLIHIK 154
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
38-234 |
6.64e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPA-GGRILIGDTDVTHLPP---YKRGLAMVVQN---YALFPHLKVEDN 110
Cdd:PRK13549 282 SFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNPqqaIAQGIAMVPEDrkrDGIVPVMGVGKN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 111 VAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPH------QLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIR 184
Cdd:PRK13549 362 ITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAK 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 566074967 185 HnmveEIACLHRELPE--LTILYVTHDQTEALTLADKIGIMKDG----SLIAHGET 234
Cdd:PRK13549 442 Y----EIYKLINQLVQqgVAIIVISSELPEVLGLSDRVLVMHEGklkgDLINHNLT 493
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
34-233 |
1.17e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.51 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRI-LIGDTDVthlppykrglamVVQNYALFPHLKVEDNVA 112
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdRNGEVSV------------IAISAGLSGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 113 FGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIa 192
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKI- 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 566074967 193 clhRELPEL--TILYVTHDQTEALTLADKIGIMKDGSLIAHGE 233
Cdd:PRK13546 187 ---YEFKEQnkTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
6-252 |
7.59e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 6 TAVHAPASQGTSG--------IVLDSLRVAYHGNV--VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRI 75
Cdd:PTZ00243 1288 TVVIEPASPTSAAphpvqagsLVFEGVQMRYREGLplVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEI 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 76 LIGDTDVTH--LPPYKRGLAMVVQNYALFPHlKVEDNVAFGLRAQkqpkaliNERVTQALKTVGMSDYAARYPHQL---- 149
Cdd:PTZ00243 1368 RVNGREIGAygLRELRRQFSMIPQDPVLFDG-TVRQNVDPFLEAS-------SAEVWAALELVGLRERVASESEGIdsrv 1439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 150 -------SGGQQQRVAIARAIAVRPR-VLLLDEPLS----ALDAQIRhnmveeiACLHRELPELTILYVTHdQTEALTLA 217
Cdd:PTZ00243 1440 leggsnySVGQRQLMCMARALLKKGSgFILMDEATAnidpALDRQIQ-------ATVMSAFSAYTVITIAH-RLHTVAQY 1511
|
250 260 270
....*....|....*....|....*....|....*..
gi 566074967 218 DKIGIMKDGSLIAHGETRALYQHPPNRFAA--EFLGR 252
Cdd:PTZ00243 1512 DKIIVMDHGAVAEMGSPRELVMNRQSIFHSmvEALGR 1548
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-232 |
1.59e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.23 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPA---GGRILIGDTDVTHLPPYKRGlAMVVQNYALFPHLKVED 109
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRKTS-AYISQNDVHVGVMTVKE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 110 NVAFGLRAQ--------------KQPKALI--NERVTQALKTVGM--------SDYAAR---------------YPHQLS 150
Cdd:PLN03140 259 TLDFSARCQgvgtrydllselarREKDAGIfpEAEVDLFMKATAMegvkssliTDYTLKilgldickdtivgdeMIRGIS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 151 GGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEeiaCLHR--ELPELTILY-VTHDQTEALTLADKIGIMKDGS 227
Cdd:PLN03140 339 GGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVK---CLQQivHLTEATVLMsLLQPAPETFDLFDDIILLSEGQ 415
|
....*
gi 566074967 228 LIAHG 232
Cdd:PLN03140 416 IVYQG 420
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-220 |
1.66e-06 |
|
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: 47.70 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 22 DSLRVAYHGNvvLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAgfvqpaggriligdtdvthlppYKRGLAMVVQNYAL 101
Cdd:cd03238 1 LTVSGANVHN--LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----------------------YASGKARLISFLPK 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 102 FPHLKVednVAFGlraqkQPKALINE-----RVTQALKTvgmsdyaaryphqLSGGQQQRVAIARAIAVRPR--VLLLDE 174
Cdd:cd03238 57 FSRNKL---IFID-----QLQFLIDVglgylTLGQKLST-------------LSGGELQRVKLASELFSEPPgtLFILDE 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 566074967 175 PLSALDAQIRHNMVEEIaclhRELPEL--TILYVTHDQTeALTLADKI 220
Cdd:cd03238 116 PSTGLHQQDINQLLEVI----KGLIDLgnTVILIEHNLD-VLSSADWI 158
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-180 |
2.95e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVA-----GFvqPAGGRIL------IGDtDVTHLP- 86
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGI--PKNCQILhveqevVGD-DTTALQc 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 87 ------PYKRGLAMVVQNYALFPHLKVEDNVAFGLRAQKQ--PKALINERVTQALKTVGMSD-YAA-------------- 143
Cdd:PLN03073 255 vlntdiERTQLLEEEAQLVAQQRELEFETETGKGKGANKDgvDKDAVSQRLEEIYKRLELIDaYTAearaasilaglsft 334
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 566074967 144 -----RYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PLN03073 335 pemqvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-220 |
4.28e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 19 IVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIgdtdvthlpPYKRGLAMVVQN 98
Cdd:PRK10636 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF---------PGNWQLAWVNQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 99 YalfPHLKVE--DNVAFGLRAQKQPKA---------------------------LINERVTQALKTVGMSDYAARYP-HQ 148
Cdd:PRK10636 73 T---PALPQPalEYVIDGDREYRQLEAqlhdanerndghaiatihgkldaidawTIRSRAASLLHGLGFSNEQLERPvSD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 566074967 149 LSGGQQQRVAIARAIAVRPRVLLLDEPLSALDaqirhnmVEEIACLHRELPEL--TILYVTHDQTEALTLADKI 220
Cdd:PRK10636 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAVIWLEKWLKSYqgTLILISHDRDFLDPIVDKI 216
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
48-220 |
1.10e-05 |
|
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: 45.68 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 48 ALIGPSGSGKTTVLRAV--AGF-VQPAGGRILIGDTDVT-----------HLPPYKRGLAMVVQNYALFphlkveDNVAF 113
Cdd:cd03240 26 LIVGQNGAGKTTIIEALkyALTgELPPNSKGGAHDPKLIregevraqvklAFENANGKKYTITRSLAIL------ENVIF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 114 gLRaQKQPKALInervtqalktvgmsdyaARYPHQLSGGQQQ------RVAIARAIAVRPRVLLLDEPLSALDAQIRHNM 187
Cdd:cd03240 100 -CH-QGESNWPL-----------------LDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEES 160
|
170 180 190
....*....|....*....|....*....|...
gi 566074967 188 VEEIACLHRELPELTILYVTHDQtEALTLADKI 220
Cdd:cd03240 161 LAEIIEERKSQKNFQLIVITHDE-ELVDAADHI 192
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
28-208 |
8.23e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.50 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 28 YHgnVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIgdtdvthlppyKRGLAMVVQNYALFPHLKV 107
Cdd:PRK13545 36 YH--YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-----------KGSAALIAISSGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 108 EDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNM 187
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180
....*....|....*....|...
gi 566074967 188 VEEIaclhRELPE--LTILYVTH 208
Cdd:PRK13545 183 LDKM----NEFKEqgKTIFFISH 201
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
149-258 |
5.24e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 149 LSGGQQQRVAIARAIAVRPR--VLLLDEPLSALDAQIRHNMVEEIACLHRElpELTILYVTHDQtEALTLADKIGIMKDG 226
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQ--GNTVLLVEHDE-QMISLADRIIDIGPG 553
|
90 100 110
....*....|....*....|....*....|..
gi 566074967 227 SLIAHGETraLYQHPPnrfaAEFLGRANILSA 258
Cdd:PRK00635 554 AGIFGGEV--LFNGSP----REFLAKSDSLTA 579
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
47-77 |
1.90e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 38.28 E-value: 1.90e-03
10 20 30
....*....|....*....|....*....|.
gi 566074967 47 LALIGPSGSGKTTVLRAVAGFVQPAGGRILI 77
Cdd:cd00009 22 LLLYGPPGTGKTTLARAIANELFRPGAPFLY 52
|
|
| VirB11 |
COG0630 |
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ... |
20-80 |
2.93e-03 |
|
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440395 [Multi-domain] Cd Length: 462 Bit Score: 39.29 E-value: 2.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566074967 20 VLDSLRVAYhgnvvlkpLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVqPAGGRIL-IGDT 80
Cdd:COG0630 274 TLSPELAAY--------LWLLLENGKSVLVAGGTASGKTTLLNALLSFI-PPDAKIVtIEDT 326
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
148-220 |
5.03e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.01 E-value: 5.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 566074967 148 QLSGGQQQRVAIARAIAVRpRV-----LLLDEPLSALDAQIRHNmveeIACLHRELPELTILYVTHDQTEALTLADKI 220
Cdd:cd03272 158 QLSGGQKSLVALALIFAIQ-KCdpapfYLFDEIDAALDAQYRTA----VANMIKELSDGAQFITTTFRPELLEVADKF 230
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
149-230 |
5.42e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.62 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566074967 149 LSGGQQQRVAIARAIAVRPRVLLLDEPLSALDA-------QIRHNMVEE---IACLHRELPELtilyvthdqteaLTLAD 218
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyeiyTIINELAAEgkgVIVISSELPEL------------LGMCD 472
|
90
....*....|..
gi 566074967 219 KIGIMKDGSLIA 230
Cdd:NF040905 473 RIYVMNEGRITG 484
|
|
| Kti12 |
COG4088 |
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ... |
44-81 |
7.80e-03 |
|
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];
Pssm-ID: 443264 [Multi-domain] Cd Length: 179 Bit Score: 37.01 E-value: 7.80e-03
10 20 30
....*....|....*....|....*....|....*...
gi 566074967 44 GEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTD 81
Cdd:COG4088 4 PMLLILTGPPGSGKTTFAKALAQRLYAEGIAVALLHSD 41
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
38-65 |
9.86e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.11 E-value: 9.86e-03
10 20
....*....|....*....|....*...
gi 566074967 38 SLTIEPGEVLALIGPSGSGKTTVLRAVA 65
Cdd:pfam13555 16 TIPIDPRGNTLLTGPSGSGKSTLLDAIQ 43
|
|
| |
