|
Name |
Accession |
Description |
Interval |
E-value |
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-333 |
7.93e-175 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 488.84 E-value: 7.93e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNT 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 161 PLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNV 240
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 241 FDGLMAE------KLCGMT--------------GSFALRPEHIRLNTPGEMQA-NGTIQAVQYQGAATRFELTLSGGEKL 299
Cdd:COG3842 242 LPGTVLGdegggvRTGGRTlevpadaglaaggpVTVAIRPEDIRLSPEGPENGlPGTVEDVVFLGSHVRYRVRLGDGQEL 321
|
330 340 350
....*....|....*....|....*....|....
gi 446142581 300 LVSQANMTGEELPatltPGQQVMVSWSRDVMVAL 333
Cdd:COG3842 322 VVRVPNRAALPLE----PGDRVGLSWDPEDVVVL 351
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-328 |
2.16e-135 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 388.66 E-value: 2.16e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQ 83
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 DYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:COG3839 83 SYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 164 ALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTS--NVF 241
Cdd:COG3839 163 NLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPpmNLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 242 DG-----------------LMAEKLCGMTGSFALRPEHIRLNTPGEMQANGTIQAVQYQGAATRFELTLsGGEKLLVSQA 304
Cdd:COG3839 243 PGtvegggvrlggvrlplpAALAAAAGGEVTLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVRL-GGQELVARVP 321
|
330 340
....*....|....*....|....
gi 446142581 305 NMTGeelpatLTPGQQVMVSWSRD 328
Cdd:COG3839 322 GDTR------LRPGDTVRLAFDPE 339
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-236 |
5.14e-131 |
|
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: 373.11 E-value: 5.14e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQD 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446142581 165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVG 236
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-325 |
7.28e-130 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 375.44 E-value: 7.28e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQD 84
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDGL 244
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDAT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 245 MAEKL-------------CGMTGSFA----------LRPEHIRLNTPGE-MQANGTIQAVQ---YQGAATRFELTLSGGE 297
Cdd:PRK09452 255 VIERLdeqrvranvegreCNIYVNFAvepgqklhvlLRPEDLRVEEINDdEHAEGLIGYVRernYKGMTLDSVVELENGK 334
|
330 340
....*....|....*....|....*....
gi 446142581 298 KLLVSQanMTGEELPA-TLTPGQQVMVSW 325
Cdd:PRK09452 335 MVMVSE--FFNEDDPDfDHSLGQKVAVTW 361
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-327 |
5.65e-116 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 339.04 E-value: 5.65e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPA-SNLPPWERDVNTVFQ 83
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 DYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 164 ALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVF-- 241
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLrg 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 242 ---------DGLMAEKLCGMTGSFA---LRPEHIRLNTPGEMQAN--GTIQAVQYQGAATRFELTLSGGEKLLVsQANMT 307
Cdd:COG1118 243 rviggqleaDGLTLPVAEPLPDGPAvagVRPHDIEVSREPEGENTfpATVARVSELGPEVRVELKLEDGEGQPL-EAEVT 321
|
330 340
....*....|....*....|.
gi 446142581 308 GEELPA-TLTPGQQVMVSWSR 327
Cdd:COG1118 322 KEAWAElGLAPGDPVYLRPRP 342
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
8-332 |
1.79e-112 |
|
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: 330.46 E-value: 1.79e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 8 DNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQDYAL 87
Cdd:TIGR03265 8 DNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQSYAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 88 FPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL 167
Cdd:TIGR03265 88 FPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 168 KLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDGLMAE 247
Cdd:TIGR03265 168 RVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPGTRGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 248 -----------------KLCGMTGSFALRPEHIRLNtPGEMQAN---GTIQAVQYQGAATRFELTLSG--GEKLLVSQAN 305
Cdd:TIGR03265 248 gsrarvggltlacapglAQPGASVRLAVRPEDIRVS-PAGNAANlllARVEDMEFLGAFYRLRLRLEGlpGQALVADVSA 326
|
330 340
....*....|....*....|....*..
gi 446142581 306 MTGEELPatLTPGQQVMVSWSRDVMVA 332
Cdd:TIGR03265 327 SEVERLG--IRAGQPIWIELPAERLRA 351
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-333 |
9.72e-112 |
|
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: 327.53 E-value: 9.72e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 35 MLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAM 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 115 AQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHD 194
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 195 QGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDGLMAEKL-------------CGMTGSF----- 256
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKseqvvlagvegrrCDIYTDVpvekd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 257 -----ALRPEHIRLNTPGEMQ----ANGTIQAVQYQGAATRFELTLSGGEKLLVSqANMTGEELPATLTPGQQVMVSWSR 327
Cdd:TIGR01187 241 qplhvVLRPEKIVIEEEDEANssnaIIGHVIDITYLGMTLEVHVRLETGQKVLVS-EFFNEDDPHMSPSIGDRVGLTWHP 319
|
....*.
gi 446142581 328 DVMVAL 333
Cdd:TIGR01187 320 GSEVVL 325
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-217 |
1.67e-110 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 320.24 E-value: 1.67e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQD 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446142581 165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVD 217
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-319 |
6.04e-101 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 301.38 E-value: 6.04e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLY-GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVF 82
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 83 QDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 163 GALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGT----- 237
Cdd:PRK11650 163 SNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpamnl 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 238 ---SNVFDGLMAEKLCGMTGSFA--------------LRPEHIRLnTPGEMQANGTIQAVQYQGaATRFELTLSGGEKLL 300
Cdd:PRK11650 243 ldgRVSADGAAFELAGGIALPLGggyrqyagrkltlgIRPEHIAL-SSAEGGVPLTVDTVELLG-ADNLAHGRWGGQPLV 320
|
330 340
....*....|....*....|...
gi 446142581 301 VSQAN----MTGEELPATLTPGQ 319
Cdd:PRK11650 321 VRLPHqerpAAGSTLWLHLPANQ 343
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-236 |
1.13e-97 |
|
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: 288.85 E-value: 1.13e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 3 YAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVF 82
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 83 QDYALFPHMSILDNVAYGLMVKGV----NKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 159 DEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVG 236
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-217 |
1.21e-96 |
|
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: 284.92 E-value: 1.21e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQD 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446142581 165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVD 217
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-231 |
2.96e-95 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 283.13 E-value: 2.96e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLY----GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPwerDVN 79
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---DRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:COG1116 84 VVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 160 EPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNN--GRI---EQVDSPrdlymRPRTPFV 231
Cdd:COG1116 164 EPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIveeIDVDLP-----RPRDREL 235
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-307 |
2.18e-94 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 284.30 E-value: 2.18e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQD 84
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDGL 244
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPAT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 245 MAEKLCGMTG------------------SFALRPEHIRLNTPGEMQANGTIQAVQYQGAatRFELTLSGGEKLLVSQANM 306
Cdd:PRK11432 247 LSGDYVDIYGyrlprpaafafnlpdgecTVGVRPEAITLSEQGEESQRCTIKHVAYMGP--QYEVTVDWHGQELLLQVNA 324
|
.
gi 446142581 307 T 307
Cdd:PRK11432 325 T 325
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
5-240 |
5.22e-91 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 271.67 E-value: 5.22e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQD 84
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446142581 165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNV 240
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNV 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-213 |
6.44e-91 |
|
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: 270.88 E-value: 6.44e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGD----VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPwerDVNT 80
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 161 PLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNN--GRI 213
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRI 212
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-301 |
6.48e-88 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 268.44 E-value: 6.48e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQD 84
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVG-------- 236
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGspkmnflp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 237 ---TSNVFDGLMAEKLCGM--------TG-------SFALRPEHIRLNTPGEMQANGTIQAVQYQGAATRFELTLSGGEK 298
Cdd:PRK11000 244 vkvTATAIEQVQVELPNRQqvwlpvegRGvqvganmSLGIRPEHLLPSDIADVTLEGEVQVVEQLGNETQIHIQIPAIRQ 323
|
...
gi 446142581 299 LLV 301
Cdd:PRK11000 324 NLV 326
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-240 |
7.34e-88 |
|
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: 263.43 E-value: 7.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRaVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQD 84
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446142581 165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNV 240
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-238 |
3.95e-86 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 261.56 E-value: 3.95e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYGD-VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE--RDVNTVF 82
Cdd:COG1125 3 EFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 83 QDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVAL--GFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 161 PLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTS 238
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGAD 240
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-333 |
4.24e-86 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 264.00 E-value: 4.24e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQD 84
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDGL 244
Cdd:PRK11607 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 245 MAEK------------------------LCGMTGSFALRPEHIRLNTpgEMQANGTIQAV------QYQGAATRFELTLS 294
Cdd:PRK11607 260 LKERqedglvidspglvhplkvdadasvVDNVPVHVALRPEKIMLCE--EPPADGCNFAVgevihiAYLGDLSIYHVRLK 337
|
330 340 350
....*....|....*....|....*....|....*....
gi 446142581 295 GGeKLLVSQANMTGEELPATLTPGQQVMVSWSRDVMVAL 333
Cdd:PRK11607 338 SG-QMISAQLQNAHRYRKGLPTWGDEVRLCWEADSCVVL 375
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-243 |
8.76e-85 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 260.02 E-value: 8.76e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQ 83
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 DYALFPHMSILDNVAYGLMVkgVNKKQR---HAMAQEA---LEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTV--LPRRERpnaAAIKAKVtqlLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 158 LDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGT 237
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE 239
|
....*.
gi 446142581 238 SNVFDG 243
Cdd:PRK10851 240 VNRLQG 245
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
5-301 |
3.08e-83 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 255.77 E-value: 3.08e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRaVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQD 84
Cdd:NF040840 2 IRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:NF040840 81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 165 LDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDGL 244
Cdd:NF040840 161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 245 MAEKLCGM---TGS--------------FALRPEHIRLNT-PGEMQA----NGTIQAVQYQGAATRfeLTLSGGEKLLV 301
Cdd:NF040840 241 AEKGGEGTildTGNikielpeekkgkvrIGIRPEDITISTeKVKTSArnefKGKVEEIEDLGPLVK--LTLDVGIILVA 317
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-236 |
1.29e-79 |
|
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: 242.98 E-value: 1.29e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVR-AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE--RDVNTV 81
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 82 FQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQ--QRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 160 EPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVG 236
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-214 |
3.69e-79 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 241.10 E-value: 3.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGD----VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWER 76
Cdd:COG1136 1 MSPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 77 DV--NT----VFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALV 150
Cdd:COG1136 81 ARlrRRhigfVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 151 NEPRVLLLDEPLGALDLKLREQ-MQLeLKKLQQSLGITFIFVTHDQgEALSMSDRVAVFNNGRIE 214
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEvLEL-LRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-235 |
4.47e-78 |
|
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: 239.85 E-value: 4.47e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 15 GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE------RDVNTVFQDYALF 88
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 89 PHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:cd03294 115 PHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 169 LREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFV 235
Cdd:cd03294 195 IRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-213 |
4.60e-77 |
|
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: 235.46 E-value: 4.60e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGD----VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERD--- 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 ---VNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 155 VLLLDEPLGALDLKLREQ-MQLeLKKLQQSLGITFIFVTHDQgEALSMSDRVAVFNNGRI 213
Cdd:cd03255 161 IILADEPTGNLDSETGKEvMEL-LRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-212 |
2.13e-76 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 232.08 E-value: 2.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP----ASNLPPWERDVNT 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdlEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFPHMSILDNVAYGLmvkgvnkkqrhamaqealekvalgfvqqrkpsqlSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:cd03229 81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446142581 161 PLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
2-235 |
6.20e-74 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 233.07 E-value: 6.20e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 2 TYAVEFDNVSRLYGD------------------------VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLS 57
Cdd:COG4175 1 MPKIEVRNLYKIFGKrperalklldqgkskdeilektgqTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 58 GGAISIFGTPASNLPPWE------RDVNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRK 131
Cdd:COG4175 81 AGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 132 PSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNG 211
Cdd:COG4175 161 PDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDG 240
|
250 260
....*....|....*....|....
gi 446142581 212 RIEQVDSPRDLYMRPRTPFVAGFV 235
Cdd:COG4175 241 RIVQIGTPEEILTNPANDYVADFV 264
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-229 |
5.98e-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: 226.32 E-value: 5.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY-----GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE---- 75
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 76 -RDVNTVFQD--YALFPHMSILDNVAYGLMVKGV-NKKQRHAMAQEALEKVALGF-VQQRKPSQLSGGQRQRVAIARALV 150
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 151 NEPRVLLLDEPLGALDLKLREQ-MQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTP 229
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQiLNL-LRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-229 |
7.12e-69 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 215.24 E-value: 7.12e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGT----PASNLPPWERDVNT 80
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEdltdSKKDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFPHMSILDNVAYGLM-VKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIkVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 160 EPLGALD-------LKLreqmqleLKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTP 229
Cdd:COG1126 162 EPTSALDpelvgevLDV-------MRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-213 |
4.60e-68 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 213.96 E-value: 4.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYG----DVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNlPPWERDVntV 81
Cdd:COG4525 5 TVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV--V 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 82 FQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:COG4525 82 FQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446142581 162 LGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVF--NNGRI 213
Cdd:COG4525 162 FGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRI 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-217 |
2.84e-67 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 210.68 E-value: 2.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY-GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE-----RDV 78
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 79 NTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 159 DEPLGALDLKLREQ-MQLeLKKLQQsLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVD 217
Cdd:COG2884 162 DEPTGNLDPETSWEiMEL-LEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-217 |
6.15e-66 |
|
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: 206.76 E-value: 6.15e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 29 DGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP------ASNLPPWERDVNTVFQDYALFPHMSILDNVAYGLm 102
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGL- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 103 vKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQ 182
Cdd:cd03297 101 -KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 446142581 183 SLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVD 217
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-222 |
1.31e-65 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 206.84 E-value: 1.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG-TPASNLPPWERDVNTVFQ 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGeDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 DYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 164 ALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-213 |
1.76e-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: 206.20 E-value: 1.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY----GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLP-----PWE 75
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 76 RDVNTVFQDY--ALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGF---VQQRKPSQLSGGQRQRVAIARALV 150
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLpeeVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446142581 151 NEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-237 |
1.14e-64 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 204.22 E-value: 1.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYGD--VRAvngvSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQ 83
Cdd:COG3840 3 RLDDLTYRYGDfpLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 DYALFPHMSILDNVAYGLMVKG-VNKKQRHAMAQeALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGLRPGLkLTAEQRAQVEQ-ALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 163 GALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGT 237
Cdd:COG3840 158 SALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-230 |
3.73e-64 |
|
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: 203.50 E-value: 3.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYG----DVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE--RD 77
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 VNTVFQDY--ALFPHMSILDNVAYGLMVKGVnkKQRHAMAQEALEKVALGF-VQQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446142581 155 VLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPF 230
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-228 |
3.88e-64 |
|
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: 202.56 E-value: 3.88e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY-GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE--RDVNTV 81
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 82 FQ--DYALFpHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:COG1122 81 FQnpDDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 160 EPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRT 228
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
37-243 |
1.77e-61 |
|
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: 199.94 E-value: 1.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 37 GPSGSGKTTCLRLIAGFEQLSGGAISIFGTP------ASNLPPWERDVNTVFQDYALFPHMSILDNVAYGLmvKGVNKKQ 110
Cdd:COG4148 32 GPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsarGIFLPPHRRRIGYVFQEARLFPHLSVRGNLLYGR--KRAPRAE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 111 RHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIF 190
Cdd:COG4148 110 RRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILY 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446142581 191 VTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDG 243
Cdd:COG4148 190 VSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEA 242
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-213 |
5.02e-61 |
|
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: 194.29 E-value: 5.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGT----PASNLPPWERDVNT 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltdDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFPHMSILDNVAYGLM-VKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446142581 160 EPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-238 |
7.23e-61 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 197.99 E-value: 7.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY----GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE----- 75
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 76 RDVNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 156 LLLDEPLGALD-------LKLreqmqleLKKLQQSLGITFIFVTHDqgealsMS------DRVAVFNNGRIEQVDSPRDL 222
Cdd:COG1135 162 LLCDEATSALDpettrsiLDL-------LKDINRELGLTIVLITHE------MDvvrricDRVAVLENGRIVEQGPVLDV 228
|
250
....*....|....*.
gi 446142581 223 YMRPRTPFVAGFVGTS 238
Cdd:COG1135 229 FANPQSELTRRFLPTV 244
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-222 |
8.35e-61 |
|
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: 194.43 E-value: 8.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERD--- 77
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 --VNTVFQDYALFPHMSILDNVAYGL-MVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:COG1127 82 rrIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 155 VLLLDEPLGALD-LKLREQMQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG1127 162 ILLYDEPTAGLDpITSAVIDEL-IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-227 |
4.71e-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: 192.41 E-value: 4.71e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGD----VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGT-----PASNLPPWE 75
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 76 RDVNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446142581 156 LLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPR 227
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-213 |
3.44e-58 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 187.96 E-value: 3.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLY-GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP-----WERD 77
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralrrLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 VNTVFQDYALFPHMSILDNVAYGL---------MVKGVNKKQRhAMAQEALEKVALG-FVQQRkPSQLSGGQRQRVAIAR 147
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGRlgrtstwrsLLGLFPPEDR-ERALEALERVGLAdKAYQR-ADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 148 ALVNEPRVLLLDEPLGALDLKLREQ-MQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQvMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-222 |
3.50e-57 |
|
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: 184.69 E-value: 3.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQL-----SGGAISIFGTP--ASNLPPWE-- 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDiyDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 76 RDVNTVFQDYALFPhMSILDNVAYGLMVKGV-NKKQRHAMAQEALEKVAL-GFVQQR-KPSQLSGGQRQRVAIARALVNE 152
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 153 PRVLLLDEPLGALDLKLREQMQLELKKLQQSlgITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-234 |
7.31e-57 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 184.53 E-value: 7.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG----TPASNLPPWERDVNT 80
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvnDPKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFPHMSILDNVAYG-LMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 160 EPLGALDLKLREqmqlELKKLQQSL---GITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGF 234
Cdd:PRK09493 162 EPTSALDPELRH----EVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-202 |
1.66e-56 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 184.13 E-value: 1.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNlPPWERDVntVFQ 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 DYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 446142581 164 ALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMS 202
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMA 196
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-227 |
6.77e-56 |
|
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: 189.73 E-value: 6.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLY--GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAG---FEQLSGGAISIFGTPASNLPPWE 75
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 76 R--DVNTVFQD--YALFPhMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVN 151
Cdd:COG1123 81 RgrRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446142581 152 EPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPR 227
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-222 |
1.07e-55 |
|
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: 181.16 E-value: 1.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE-----RDVN 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQDYALFPHMSILDNVAYGLMVKGVNKKQR-HAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446142581 159 DEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
15-229 |
5.35e-55 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 182.24 E-value: 5.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 15 GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE-----RDVNTVFQD-YA-L 87
Cdd:COG4608 29 GVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQDpYAsL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 88 FPHMSILDNVAYGLMVKGV-NKKQRHAMAQEALEKVALG--FVQqRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:COG4608 109 NPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRpeHAD-RYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 165 LDLKLREQ-MQLeLKKLQQSLGITFIFVTHDqgeaLSM----SDRVAVFNNGRIEQVDSPRDLYMRPRTP 229
Cdd:COG4608 188 LDVSIQAQvLNL-LEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIVEIAPRDELYARPLHP 252
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
15-229 |
6.25e-55 |
|
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: 181.79 E-value: 6.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 15 GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQ---LSGGAISIFGTPASNLPPWE------RDVNTVFQD- 84
Cdd:COG0444 16 GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElrkirgREIQMIFQDp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 Y-ALFPHMSILDNVAYGLMV-KGVNKKQRHAMAQEALEKVALGFVQQRK---PSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:COG0444 96 MtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQRVMIARALALEPKLLIAD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446142581 160 EPLGALDLKLREQ-MQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI-EQVDSpRDLYMRPRTP 229
Cdd:COG0444 176 EPTTALDVTIQAQiLNL-LKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIvEEGPV-EELFENPRHP 245
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-222 |
1.68e-54 |
|
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: 178.51 E-value: 1.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP-WERDVNTVFQD 84
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 165 LDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG4555 163 LDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-220 |
2.66e-54 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 177.66 E-value: 2.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 20 VNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPwERDVntVFQDYALFPHMSILDNVAy 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-DRMV--VFQNYSLLPWLTVRENIA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 100 gLMVKGVN----KKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQL 175
Cdd:TIGR01184 77 -LAVDRVLpdlsKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446142581 176 ELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNN------GRIEQVDSPR 220
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNgpaaniGQILEVPFPR 206
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
8-227 |
3.17e-54 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 178.33 E-value: 3.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 8 DNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLppwERDVNTVFQDYAL 87
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA---REDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 88 FPHMSILDNVAYGLmvKGVNKKQrhamAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL 167
Cdd:PRK11247 93 LPWKKVIDNVGLGL--KGQWRDA----ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 168 KLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIeQVDSPRDLyMRPR 227
Cdd:PRK11247 167 LTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI-GLDLTVDL-PRPR 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-212 |
9.48e-54 |
|
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: 175.35 E-value: 9.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYGD--VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE--RDVNTV 81
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 82 FQ--DYALFpHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:cd03225 81 FQnpDDQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446142581 160 EPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-229 |
5.04e-53 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 182.58 E-value: 5.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 12 RLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTC----LRLIAgfeqlSGGAISIFGTPASNLP-----PWERDVNTVF 82
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFDGQDLDGLSrralrPLRRRMQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 83 QD-YA-LFPHMSILDNVAYGLMV--KGVNKKQRHAMAQEALEKVAL-GFVQQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:COG4172 369 QDpFGsLSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446142581 158 LDEPLGALDLKLREQMqLEL-KKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI-EQVDSpRDLYMRPRTP 229
Cdd:COG4172 449 LDEPTSALDVSVQAQI-LDLlRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVvEQGPT-EQVFDAPQHP 520
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-222 |
1.26e-52 |
|
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: 174.08 E-value: 1.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE--RDVNTV 81
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 82 FQDYALFPHMSILDNVAYGLM----VKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYphlgLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446142581 158 LDEPLGALDLKLREQ-MQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG1120 161 LDEPTSHLDLAHQLEvLEL-LRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-226 |
2.39e-52 |
|
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: 173.79 E-value: 2.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYG-----DVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGT-----PASNLPPW 74
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRditakKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 75 ERDVNTVFQ--DYALFpHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGF-VQQRKPSQLSGGQRQRVAIARALVN 151
Cdd:TIGR04521 81 RKKVGLVFQfpEHQLF-EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 152 EPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-213 |
2.98e-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: 172.92 E-value: 2.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERD--- 77
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 -VNTvFQDYALFPHMSILDNVAYGLMVK------------GVNKKQRHAM---AQEALEKVALGFVQQRKPSQLSGGQRQ 141
Cdd:COG0411 81 iART-FQNPRLFPELTVLENVLVAAHARlgrgllaallrlPRARREEREArerAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446142581 142 RVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-213 |
4.08e-52 |
|
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: 172.37 E-value: 4.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYGD-VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP-----WERDVN 79
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQDYALFPHMSILDNVAYGLM--------VKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVN 151
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGRLgrrstwrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446142581 152 EPRVLLLDEPLGALDLKLREQ-MQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQvMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-213 |
6.53e-52 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 170.75 E-value: 6.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDvrAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQD 84
Cdd:cd03298 1 VRLDKIRFSYGE--QPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGLMVK-GVNKKQRHAMAQeALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:cd03298 79 NNLFAHLTVEQNVGLGLSPGlKLTAEDRQAIEV-ALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446142581 164 ALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-206 |
7.61e-52 |
|
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: 170.51 E-value: 7.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY-GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGT-----PASNLPPWERDV 78
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEdvnrlRGRQLPLLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 79 NTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446142581 159 DEPLGALDLKLREQ-MQLeLKKLQQSlGITFIFVTHDqgeaLSMSDRVA 206
Cdd:TIGR02673 162 DEPTGNLDPDLSERiLDL-LKRLNKR-GTTVIVATHD----LSLVDRVA 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-202 |
9.76e-51 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 167.66 E-value: 9.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGF--EQLSG-GAISIFGTPASNLPPWERDVNTVF 82
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSAsGEVLLNGRRLTALPAEQRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 83 QDYALFPHMSILDNVAYGLmVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:COG4136 83 QDDLLFPHLSVGENLAFAL-PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446142581 163 GALDLKLREQM-QLELKKLQQsLGITFIFVTHDQGEALSMS 202
Cdd:COG4136 162 SKLDAALRAQFrEFVFEQIRQ-RGIPALLVTHDEEDAPAAG 201
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-213 |
1.52e-50 |
|
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: 165.65 E-value: 1.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP-WERDVNTVFQ 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEeVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 DYALFPHMSILDNVayglmvkgvnkkqrhamaqealekvalgfvqqrkpsQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446142581 164 ALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
1.53e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 168.34 E-value: 1.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNlpPWER---- 76
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR--ARRRigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 77 ----DVNtvfqdyALFPhMSILDNVAYGL-----MVKGVNKKQRhAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIAR 147
Cdd:COG1121 81 pqraEVD------WDFP-ITVRDVVLMGRygrrgLFRRPSRADR-EAVDEALERVGLEDLADRPIGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 148 ALVNEPRVLLLDEPLGALDLKLREQ-MQLeLKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI-----EQVDSPRD 221
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEAlYEL-LRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVahgppEEVLTPEN 230
|
.
gi 446142581 222 L 222
Cdd:COG1121 231 L 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-232 |
2.00e-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: 171.45 E-value: 2.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 35 MLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASN------LPPWERDVNTVFQDYALFPHMSILDNVAYGLmvKGVNK 108
Cdd:TIGR02142 28 IFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVFQEARLFPHLSVRGNLRYGM--KRARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 109 KQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITF 188
Cdd:TIGR02142 106 SERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446142581 189 IFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVA 232
Cdd:TIGR02142 186 LYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-211 |
2.00e-49 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 164.24 E-value: 2.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLP------PWERDVN 79
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERkrigyvPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TvfqdyaLFPhMSILDNVAYGL-----MVKGVNKKQRHAmAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:cd03235 81 R------DFP-ISVRDVVLMGLyghkgLFRRLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 155 VLLLDEPLGALDLKLREQMQLELKKLQQsLGITFIFVTHDQGEALSMSDRVAVFNNG 211
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-213 |
5.81e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 163.06 E-value: 5.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE--RDVNTVFQ 83
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 DYALFPhMSILDNVAYGLMVKgvNKKQRHAMAQEALEKVALG-FVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:COG4619 82 EPALWG-GTVRDNLPFPFQLR--ERKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446142581 163 GALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-213 |
9.69e-49 |
|
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: 163.38 E-value: 9.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 8 DNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP---WERDVNTVFQD 84
Cdd:cd03219 4 RGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiARLGIGRTFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGL-------MVKGVNKKQRHAM---AQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:cd03219 84 PRLFPELTVLENVMVAAqartgsgLLLARARREEREArerAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 155 VLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-216 |
2.40e-48 |
|
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: 161.57 E-value: 2.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 24 SIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQDYALFPHMSILDNVAYG--- 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGlhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 101 -LMVKGVNKKQRHAMAQEalekVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKK 179
Cdd:TIGR01277 98 gLKLNAEQQEKVVDAAQQ----VGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 446142581 180 LQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQV 216
Cdd:TIGR01277 174 LCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-215 |
2.68e-48 |
|
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: 162.22 E-value: 2.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGD----VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWER--- 76
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 77 ---DVNTVFQDYALFPHMSILDNVAYGLMVKGVnkKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEP 153
Cdd:COG4181 88 rarHVGFVFQSFQLLPTLTALENVMLPLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446142581 154 RVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEAlSMSDRVAVFNNGRIEQ 215
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-238 |
3.97e-47 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 159.97 E-value: 3.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 2 TYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG-------TPASNLPPW 74
Cdd:COG4598 6 PPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpDRDGELVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 75 ERD--------VNTVFQDYALFPHMSILDNVAYG-LMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAI 145
Cdd:COG4598 86 DRRqlqrirtrLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 146 ARALVNEPRVLLLDEPLGALDLKLreqmQLELKKLQQSL---GITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPEL----VGEVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
250
....*....|....*.
gi 446142581 223 YMRPRTPFVAGFVGTS 238
Cdd:COG4598 242 FGNPKSERLRQFLSSS 257
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-222 |
7.40e-47 |
|
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: 157.92 E-value: 7.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLP-PWERDVNTVFQ 83
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPrEVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 DYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 164 ALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-213 |
1.99e-46 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 156.80 E-value: 1.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY-GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNL-----PPWERDV 78
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgraiPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 79 NTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446142581 159 DEPLGALDLKL-REQMQLeLKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03292 161 DEPTGNLDPDTtWEIMNL-LKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-227 |
2.60e-46 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 157.51 E-value: 2.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLR-------LIAGFEqlSGGAISIFGTP--ASNL 71
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEDiyDPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 72 PPWE--RDVNTVFQDYALFPhMSILDNVAYGLMVKGV-NKKQRHAMAQEALEKVAL-GFVQQR--KP-SQLSGGQRQRVA 144
Cdd:COG1117 86 DVVElrRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwDEVKDRlkKSaLGLSGGQQQRLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 145 IARALVNEPRVLLLDEPLGALD----LKLREQMQlELKKlqqslGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPR 220
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDpistAKIEELIL-ELKK-----DYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTE 238
|
....*..
gi 446142581 221 DLYMRPR 227
Cdd:COG1117 239 QIFTNPK 245
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-234 |
5.59e-46 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 156.33 E-value: 5.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG--------TPASNLPPWE 75
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 76 RDVNTVFQDYALFPHMSILDNVAYGLM-VKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEAPCrVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 155 VLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI-EQVDSprDLYMRPRTPFVAG 233
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIvEQGDA--SCFTQPQTEAFKN 238
|
.
gi 446142581 234 F 234
Cdd:PRK11124 239 Y 239
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-213 |
7.38e-46 |
|
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: 155.04 E-value: 7.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGeFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERD-VNTVFQ 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 DYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446142581 164 ALDLKLREQMQLELKKLqqSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03264 160 GLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-205 |
7.61e-46 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 154.70 E-value: 7.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 9 NVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTpaSNLPPWERDVNT-------- 80
Cdd:TIGR03608 3 NISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQ--ETPPLNSKKASKfrreklgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446142581 161 PLGALDLKLREQ-MQLeLKKLQQSlGITFIFVTHDQgEALSMSDRV 205
Cdd:TIGR03608 161 PTGSLDPKNRDEvLDL-LLELNDE-GKTIIIVTHDP-EVAKQADRV 203
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-213 |
7.71e-46 |
|
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: 154.13 E-value: 7.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERdvntvfqdy 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 86 alfphmsiLDNVAYglmvkgvnkkqrhaMAQeALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:cd03214 72 --------ARKIAY--------------VPQ-ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446142581 166 DLKlreqMQLE----LKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03214 129 DIA----HQIEllelLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-225 |
1.36e-45 |
|
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: 156.05 E-value: 1.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY--GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP---ASNLppWE--RD 77
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtldEENL--WEirKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 VNTVFQDyalfPhmsilDN----------VAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIAR 147
Cdd:TIGR04520 79 VGMVFQN----P-----DNqfvgatveddVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 148 ALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALsMSDRVAVFNNGRIEQVDSPRDLYMR 225
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-212 |
2.76e-45 |
|
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: 151.63 E-value: 2.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERdvntvfqdy 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 86 alfphmsildnvayglmvkgvnkkQRHamaqealekvaLGFVqqrkpSQLSGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:cd00267 72 ------------------------RRR-----------IGYV-----PQLSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446142581 166 DLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:cd00267 112 DPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-223 |
4.29e-45 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 153.99 E-value: 4.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYG-DVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP-----ASNLPPWERDV 78
Cdd:TIGR02315 2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDitklrGKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 79 NTVFQDYALFPHMSILDNVAYGL--------MVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALV 150
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRlgykptwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446142581 151 NEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
16-213 |
4.99e-45 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 153.28 E-value: 4.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 16 DVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWER------DVNTVFQDYALFP 89
Cdd:TIGR02211 17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkKLGFIYQFHHLLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 90 HMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKL 169
Cdd:TIGR02211 97 DFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNN 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446142581 170 REQMQLELKKLQQSLGITFIFVTHDQGEALSMsDRVAVFNNGRI 213
Cdd:TIGR02211 177 AKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-241 |
5.60e-45 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 158.27 E-value: 5.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 19 AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE------RDVNTVFQDYALFPHMS 92
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 93 ILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQ 172
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446142581 173 MQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGF---VGTSNVF 241
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFfrgVDISQVF 274
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-213 |
6.21e-45 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 153.20 E-value: 6.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 24 SIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQDYALFPHMSILDNVAYGLM- 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 103 -VKgVNKKQRHAMAQEAlEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQ 181
Cdd:PRK10771 99 gLK-LNAAQREKLHAIA-RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVC 176
|
170 180 190
....*....|....*....|....*....|..
gi 446142581 182 QSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK10771 177 QERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-234 |
5.43e-44 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 151.32 E-value: 5.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG--------TPASNLPPWE 75
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 76 RDVNTVFQDYALFPHMSILDN-VAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 155 VLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI-EQVDSprDLYMRPRTPFVAG 233
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIiEQGDA--SHFTQPQTEAFAH 238
|
.
gi 446142581 234 F 234
Cdd:COG4161 239 Y 239
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-212 |
9.26e-44 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 148.30 E-value: 9.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGD--VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP--WERDVNT 80
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLesLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFpHMSILDNVayglmvkgvnkkqrhamaqealekvalgfvqqrkpsqLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446142581 161 PLGALDLKLREQMQLELKKLQQslGITFIFVTHDQgEALSMSDRVAVFNNGR 212
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-229 |
1.98e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 152.65 E-value: 1.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY----GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE----- 75
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 76 RDVNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 156 LLLDEPLGALD-------LKLreqmqleLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRT 228
Cdd:PRK11153 162 LLCDEATSALDpattrsiLEL-------LKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKH 234
|
.
gi 446142581 229 P 229
Cdd:PRK11153 235 P 235
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-222 |
7.17e-43 |
|
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: 157.30 E-value: 7.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVS-RLYGDVRAV-NGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP--WERDVN 79
Cdd:COG2274 473 DIELENVSfRYPGDSPPVlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPasLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQDYALFpHMSILDNVAYGLmvKGVNKKQrhamAQEALEKVAL-GFVQQRkP-----------SQLSGGQRQRVAIAR 147
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLGD--PDATDEE----IIEAARLAGLhDFIEAL-PmgydtvvgeggSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 148 ALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHDQgEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-222 |
7.56e-43 |
|
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: 147.58 E-value: 7.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWER---DVNTVF 82
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 83 QDYALFPHMSILDNvaygLMVKGVNKKQRHamAQEALEKV-----ALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:cd03224 82 EGRRIFPELTVEEN----LLLGAYARRRAK--RKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 158 LDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
20-225 |
1.77e-42 |
|
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: 148.03 E-value: 1.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 20 VNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP-----WERDVNTVFQDY--ALFPHMS 92
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRkqrraFRRDVQLVFQDSpsAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 93 ILDNVAYGLM-VKGVNKKQRHAMAQEALEKVAL-GFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLR 170
Cdd:TIGR02769 107 VRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446142581 171 EQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI-EQVDSPRDLYMR 225
Cdd:TIGR02769 187 AVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIvEECDVAQLLSFK 242
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-225 |
2.00e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 148.34 E-value: 2.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVR---AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE-- 75
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 76 RDVNTVFQDY-ALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK13650 81 HKIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446142581 155 VLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEaLSMSDRVAVFNNGRIEQVDSPRDLYMR 225
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-237 |
2.92e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 146.82 E-value: 2.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISI----------FGTPASNLPP 73
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarsLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 74 WERDVNTVFQDYALFPHMSILDNVAYG-LMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNE 152
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 153 PRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTP--- 229
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPrtr 241
|
....*....
gi 446142581 230 -FVAGFVGT 237
Cdd:PRK11264 242 qFLEKFLLQ 250
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-213 |
3.73e-42 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 147.14 E-value: 3.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 20 VNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLP-----PWERDVNTVFQDY--ALFPHMS 92
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkAFRRDIQMVFQDSisAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 93 ILDNVAYGLM-VKGVNKKQRHAMAQEALEKVALGF-VQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLR 170
Cdd:PRK10419 108 VREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446142581 171 EQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK10419 188 AGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-161 |
3.06e-41 |
|
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: 141.25 E-value: 3.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 20 VNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP--ASNLPPWERDVNTVFQDYALFPHMSILDNV 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 98 AYGLMVKGVNKKQRHAMAQEALEKVALGF----VQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-222 |
4.28e-41 |
|
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: 143.03 E-value: 4.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVR--AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP-ASNLPPWERDVNTV 81
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSiRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 82 FQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446142581 162 LGALDLKLREQMQLELKKLQQslGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-213 |
2.25e-40 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 147.86 E-value: 2.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP---WERD 77
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 VNTVFQDYALFPHMSILDNVAYGLMVKG---VNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 155 VLLLDEPLGALDLKLREQMqLEL-KKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG1129 161 VLILDEPTASLTEREVERL-FRIiRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-213 |
4.64e-40 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 140.04 E-value: 4.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQD 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGLMVKGVNKKQrhamAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446142581 165 LDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03268 157 LDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-226 |
7.27e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 141.86 E-value: 7.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVR--AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGF---EQLSGGAISIFGTPASNLPPWE-RD 77
Cdd:PRK13640 5 IVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDiRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 -VNTVFQDY-ALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK13640 85 kVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446142581 156 LLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEAlSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-213 |
1.85e-39 |
|
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: 138.65 E-value: 1.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVR----AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLP-PWERDVN 79
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446142581 160 EPLGALDLkLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03266 162 EPTTGLDV-MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-194 |
4.84e-39 |
|
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: 137.23 E-value: 4.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP-WERDVNTVFQ 83
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 DYALFPHMSILDNVAYGLMVKGVnkKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|....*
gi 446142581 164 ALDLK----LREQMQLELKKlqqslGITFIFVTHD 194
Cdd:COG4133 161 ALDAAgvalLAELIAAHLAR-----GGAVLLTTHQ 190
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-222 |
9.05e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 144.54 E-value: 9.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVRAV-NGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP--WERDVNT 80
Cdd:COG1132 339 EIEFENVSFSYPGDRPVlKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLesLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFpHMSILDNVAYGlmvkgvNKKQRHAMAQEALEKV-ALGFVQqRKP-----------SQLSGGQRQRVAIARA 148
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRYG------RPDATDEEVEEAAKAAqAHEFIE-ALPdgydtvvgergVNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 149 LVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHDqgeaLS---MSDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHR----LStirNADRILVLDDGRIVEQGTHEEL 561
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-213 |
1.21e-38 |
|
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: 136.26 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLP-------PWERd 77
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEER- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 vntvfqdyALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:cd03269 80 --------GLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446142581 158 LDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-213 |
3.94e-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: 135.98 E-value: 3.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFE-QLSGGAISIFGTPASNLPPWE-RD---- 77
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERRGGEDVWElRKrigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 VNTVFQDYaLFPHMSILDNVAYGL-----MVKGVNKKQRHAmAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNE 152
Cdd:COG1119 83 VSPALQLR-FPRDETVLDVVLSGFfdsigLYREPTDEQRER-ARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446142581 153 PRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
8-213 |
5.91e-38 |
|
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: 134.98 E-value: 5.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 8 DNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWER---DVNTVFQD 84
Cdd:cd03218 4 ENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03218 84 ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446142581 165 LDLKLREQMQLELKKLQQSlGITfIFVT-HDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDR-GIG-VLITdHNVRETLSITDRAYIIYEGKV 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-213 |
5.94e-38 |
|
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: 134.64 E-value: 5.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGD--VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE--RDVN 79
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQDYALFpHMSILDNVAYG------------LMVKGVN---KKQRHAMAQEALEKvalGFvqqrkpsQLSGGQRQRVA 144
Cdd:cd03245 82 YVPQDVTLF-YGTLRDNITLGapladderilraAELAGVTdfvNKHPNGLDLQIGER---GR-------GLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 145 IARALVNEPRVLLLDEPLGALDLKLREQMqleLKKLQQSL-GITFIFVTHDQgEALSMSDRVAVFNNGRI 213
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERL---KERLRQLLgDKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-223 |
7.93e-38 |
|
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: 141.82 E-value: 7.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGD-VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP--WERDVNT 80
Cdd:COG4988 336 SIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPasWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFpHMSILDNVAYGlmvkgvnkkQRHA-MAQ--EALEKVAL-GFVQQRkP-----------SQLSGGQRQRVAI 145
Cdd:COG4988 416 VPQNPYLF-AGTIRENLRLG---------RPDAsDEEleAALEAAGLdEFVAAL-PdgldtplgeggRGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 146 ARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHDQgEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-213 |
9.71e-38 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 134.23 E-value: 9.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY-GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNL-----PPWERDV 78
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 79 NTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 159 DEPLGALDLKLREQMqLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK10908 162 DEPTGNLDDALSEGI-LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-229 |
1.18e-37 |
|
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: 140.98 E-value: 1.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 15 GDVRAVNGVSIAIKDGEFFSMLGPSGSGKT----TCLRLIAGFEQLSGGAISIFGTPASNLPPWE------RDVNTVFQD 84
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 --YALFPHMSILDNVAYGLMV-KGVNKKQRHAMAQEALEKVALGFVQQR---KPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:COG4172 101 pmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQRVMIAMALANEPDLLIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446142581 159 DEPLGALDLKLREQMqLEL-KKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTP 229
Cdd:COG4172 181 DEPTTALDVTVQAQI-LDLlKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHP 251
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-213 |
1.66e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 136.01 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLP-------PWER 76
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 77 dvntvfqdyALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:COG4152 81 ---------GLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 157 LLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
14-238 |
2.80e-37 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 134.33 E-value: 2.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 14 YGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPAS---------------NLPPWERDV 78
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadknQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 79 NTVFQDYALFPHMSILDNVAYG-LMVKGVNKKQRHAMAQEALEKVAL-GFVQQRKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 157 LLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVG 236
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
..
gi 446142581 237 TS 238
Cdd:PRK10619 254 GS 255
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-221 |
2.86e-37 |
|
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: 141.54 E-value: 2.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLY-GDVR-AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE--RDVN 79
Cdd:TIGR03375 463 EIEFRNVSFAYpGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQDYALFpHMSILDNVAYGlmVKGVNKkqrhAMAQEALEKVALGFVQQRKPS-----------QLSGGQRQRVAIARA 148
Cdd:TIGR03375 543 YVPQDPRLF-YGTLRDNIALG--APYADD----EEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARA 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446142581 149 LVNEPRVLLLDEPLGALDLKLREQMqleLKKLQQSL-GITFIFVTHdQGEALSMSDRVAVFNNGRIeQVDSPRD 221
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMDNRSEERF---KDRLKRWLaGKTLVLVTH-RTSLLDLVDRIIVMDNGRI-VADGPKD 684
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-223 |
3.61e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 134.79 E-value: 3.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 18 RAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPAS----NLPPWERDVNTVFQ--DYALFPHm 91
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSDIRKKVGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 92 SILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGF--VQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKL 169
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446142581 170 REQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-223 |
4.76e-37 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 133.05 E-value: 4.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY---GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNL-PPWERD-VN 79
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLnLRWLRSqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQDYALFPhMSILDNVAYGL------MVKGVNKKqrhAMAQEALEKVALGF---VQQRKpSQLSGGQRQRVAIARALV 150
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRYGKpdatdeEVEEAAKK---ANIHDFIMSLPDGYdtlVGERG-SQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446142581 151 NEPRVLLLDEPLGALDLKLREQMQlelKKLQQ-SLGITFIFVTHdQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQ---EALDRaMKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-227 |
5.55e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 133.43 E-value: 5.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSG-----GAISIFG----TPASNL 71
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGrniySPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 72 PPWERDVNTVFQDYALFPHMSILDNVAYGLMVKGV--NKKQRHAMAQEALEKVAL-GFVQQR---KPSQLSGGQRQRVAI 145
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 146 ARALVNEPRVLLLDEPLGALD---LKLREQMQLELKKlqqslGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-----EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
....*
gi 446142581 223 YMRPR 227
Cdd:PRK14267 236 FENPE 240
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-222 |
9.01e-37 |
|
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: 132.03 E-value: 9.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWER---DVNTVF 82
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 83 QDYALFPHMSILDNvaygLMVKGVNKKQRHAmAQEALEKV-----ALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:COG0410 85 EGRRIFPSLTVEEN----LLLGAYARRDRAE-VRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446142581 158 LDEP-LGaLDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG0410 160 LDEPsLG-LAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-205 |
1.22e-36 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 131.86 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 23 VSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPW------ERDVNTVFQDYALFPHMSILDN 96
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaelrNQKLGFIYQFHHLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 97 VAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLE 176
Cdd:PRK11629 108 VAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQL 187
|
170 180
....*....|....*....|....*....
gi 446142581 177 LKKLQQSLGITFIFVTHDQGEALSMSDRV 205
Cdd:PRK11629 188 LGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
9-226 |
1.61e-36 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 132.21 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 9 NVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLS-----GGAISIFG----TPASNLPPWERDVN 79
Cdd:PRK14239 10 DLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGhniySPRTDTVDLRKEIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQDYALFPhMSILDNVAYGLMVKGVNKKQRhamAQEALEKVALGF-----VQQRKPSQ---LSGGQRQRVAIARALVN 151
Cdd:PRK14239 90 MVFQQPNPFP-MSIYENVVYGLRLKGIKDKQV---LDEAVEKSLKGAsiwdeVKDRLHDSalgLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 152 EPRVLLLDEPLGALDLKLREQMQLELKKLQQSLgiTFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-213 |
2.04e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 132.13 E-value: 2.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 17 VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWER--DVNTVFQDYAL--FPHMS 92
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakYIGRVFQDPMMgtAPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 93 ILDNVA--------YGLmVKGVNKKQRhAMAQEALEKVALGFvQQR---KPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:COG1101 99 IEENLAlayrrgkrRGL-RRGLTKKRR-ELFRELLATLGLGL-ENRldtKVGLLSGGQRQALSLLMATLTKPKLLLLDEH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446142581 162 LGALDLKlREQMQLEL-KKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG1101 176 TAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-213 |
3.75e-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: 128.32 E-value: 3.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWErdvntvfqd 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 yalfphmsildnvayglmvkgvnkkqrhamAQEAlekvALGFVqqrkpSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03216 72 ------------------------------ARRA----GIAMV-----YQLSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446142581 165 LDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03216 113 LTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-223 |
5.71e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.29 E-value: 5.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 19 AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE--RDVNTVFQDY-ALFPHMSILD 95
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGMVFQNPdNQFVGATVQD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 96 NVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQL 175
Cdd:PRK13635 102 DVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446142581 176 ELKKLQQSLGITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13635 182 TVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-221 |
8.36e-36 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 130.24 E-value: 8.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 8 DNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE----RDVntVFQ 83
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElarrRAV--LPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 DYAL-FPhMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALV-------NEPRV 155
Cdd:COG4559 83 HSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 156 LLLDEPLGALDLKLREQ-MQLeLKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRD 221
Cdd:COG4559 162 LFLDEPTSALDLAHQHAvLRL-ARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-235 |
8.50e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 130.03 E-value: 8.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 14 YGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRL------------IAGFEQLSGGaiSIFGTPASNLppwERDVNTV 81
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlielypearVSGEVYLDGQ--DIFKMDVIEL---RRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 82 FQDYALFPHMSILDNVAYGLMVKGV--NKKQRHAMAQEALEKVAL-GFVQQR---KPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK14247 88 FQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 156 LLLDEPLGALD----LKLrEQMQLELKKlqqslGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFV 231
Cdd:PRK14247 168 LLADEPTANLDpentAKI-ESLFLELKK-----DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
....
gi 446142581 232 AGFV 235
Cdd:PRK14247 242 EKYV 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-222 |
2.00e-35 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 134.54 E-value: 2.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 9 NVSRLY-----GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISI-FG---TPASNLPPWERD-- 77
Cdd:TIGR03269 284 NVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGdewVDMTKPGPDGRGra 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 ---VNTVFQDYALFPHMSILDNVAYGLmvkGVNKKQRHAMAQEALEKVALGF-------VQQRKPSQLSGGQRQRVAIAR 147
Cdd:TIGR03269 364 kryIGILHQEYDLYPHRTVLDNLTEAI---GLELPDELARMKAVITLKMVGFdeekaeeILDKYPDELSEGERHRVALAQ 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 148 ALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-213 |
3.33e-35 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 135.24 E-value: 3.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLY----GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE- 75
Cdd:PRK10535 1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 76 -----RDVNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALV 150
Cdd:PRK10535 81 aqlrrEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446142581 151 NEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEAlSMSDRVAVFNNGRI 213
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEI 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-230 |
4.15e-35 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 130.76 E-value: 4.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 37 GPSGSGKTTCLRLIAGFEQLSGGAISIFGTPAS------NLPPWERDVNTVFQDYALFPHMSILDNVAYGLmvkgvnkkq 110
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdaekgiCLPPEKRRIGYVFQDARLFPHYKVRGNLRYGM--------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 111 RHAMAQEALEKVAL---GFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL-KLREQMQLeLKKLQQSLGI 186
Cdd:PRK11144 102 AKSMVAQFDKIVALlgiEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLpRKRELLPY-LERLAREINI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446142581 187 TFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY----MRPRTPF 230
Cdd:PRK11144 181 PILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWassaMRPWLPK 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-222 |
4.43e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.57 E-value: 4.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVR--AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPAS--NLPPWERDVN 79
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkeNLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQ--DYAlFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:PRK13632 87 IIFQnpDNQ-FIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 158 LDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALsMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-225 |
4.78e-35 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 133.68 E-value: 4.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 12 RLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTC----LRLIAgfeqlSGGAISIFGTPASNLP-----PWERDVNTVF 82
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFDGQPLHNLNrrqllPVRHRIQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 83 QD--YALFPHMSILDNVAYGLMV--KGVNKKQRHAMAQEALEKVALG-FVQQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:PRK15134 369 QDpnSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 158 LDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGR-IEQVD------SPRDLYMR 225
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEvVEQGDcervfaAPQQEYTR 523
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
22-194 |
8.93e-35 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 126.82 E-value: 8.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 22 GVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWER------DVNTVFQDYALFPHMSILD 95
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTLNALE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 96 NVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQL 175
Cdd:PRK10584 108 NVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170
....*....|....*....
gi 446142581 176 ELKKLQQSLGITFIFVTHD 194
Cdd:PRK10584 188 LLFSLNREHGTTLILVTHD 206
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-221 |
1.23e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 127.20 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 8 DNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE----RDVntVFQ 83
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElarrRAV--LPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 DYAL-FPhMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALV------NEPRVL 156
Cdd:PRK13548 84 HSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 157 LLDEPLGALDlkLREQ---MQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRD 221
Cdd:PRK13548 163 LLDEPTSALD--LAHQhhvLRL-ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-230 |
1.39e-34 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 128.93 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 17 VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE-----RDVNTVFQD-YA-LFP 89
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQNpYGsLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 90 HMSILDNVAYGLMVK-GVNKKQRHAMAQEALEKVALGFVQ-QRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL 167
Cdd:PRK11308 108 RKKVGQILEEPLLINtSLSAAERREKALAMMAKVGLRPEHyDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446142581 168 KLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPF 230
Cdd:PRK11308 188 SVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPY 250
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-226 |
2.55e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 127.06 E-value: 2.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 18 RAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISI------FGTPASNLPPWERDVNTVFQ--DYALFP 89
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKPLRKKVGIVFQfpEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 90 HmSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGF-VQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:PRK13634 101 E-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 169 LREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
8-213 |
1.41e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 123.99 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 8 DNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWER---DVNTVFQD 84
Cdd:COG1137 7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:COG1137 87 ASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446142581 165 LDLKLREQMQLELKKLQQSlGITfIFVT-HDQGEALSMSDRVAVFNNGRI 213
Cdd:COG1137 167 VDPIAVADIQKIIRHLKER-GIG-VLITdHNVRETLGICDRAYIISEGKV 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-222 |
2.37e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 124.92 E-value: 2.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERD-VN 79
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446142581 160 EPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
14-212 |
2.68e-33 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 123.56 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 14 YGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE---RDVNTVFQDYALFPH 90
Cdd:PRK11300 15 FGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarMGVVRTFQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 91 MSILDN--VAYGLMVK-----------GVNKKQRHAMAQEA--LEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK11300 95 MTVIENllVAQHQQLKtglfsgllktpAFRRAESEALDRAAtwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 156 LLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-235 |
2.68e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 123.62 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 9 NVSRLY---GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAIS-----------IFGTPASNLppw 74
Cdd:PRK14246 12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKvdgkvlyfgkdIFQIDAIKL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 75 ERDVNTVFQDYALFPHMSILDNVAYGLMVKGV-NKKQRHAMAQEALEKVAL-GFVQQR---KPSQLSGGQRQRVAIARAL 149
Cdd:PRK14246 89 RKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIkEKREIKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 150 VNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlgITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTP 229
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNE 246
|
....*.
gi 446142581 230 FVAGFV 235
Cdd:PRK14246 247 LTEKYV 252
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-226 |
2.77e-33 |
|
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: 129.12 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 3 YAVEFDNVSRLY--GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP--WERDV 78
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEddLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 79 NTVFQDYALFpHMSILDNVAYGlmvkgvNKKQRHAMAQEALEKVALGFVQQRKP-----------SQLSGGQRQRVAIAR 147
Cdd:COG4987 412 AVVPQRPHLF-DTTLRENLRLA------RPDATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 148 ALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHDQgEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
8-213 |
6.33e-33 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 122.00 E-value: 6.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 8 DNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWER---DVNTVFQD 84
Cdd:TIGR04406 5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERarlGIGYLPQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGL-MVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:TIGR04406 85 ASIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446142581 164 ALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:TIGR04406 165 GVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKV 213
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-230 |
8.37e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 124.05 E-value: 8.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 18 RAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWER-----DVNTVFQD--YALFPH 90
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 91 MSILDNVAYGL------MVKGVNKKQRHAMaqeaLEKVAL-GFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:PRK15079 115 MTIGEIIAEPLrtyhpkLSRQEVKDRVKAM----MLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 164 ALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPF 230
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPY 257
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-223 |
9.73e-33 |
|
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: 121.57 E-value: 9.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGD--VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASN--LPPWERDVNT 80
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDytLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFpHMSILDNVAYGlmVKGVNKKQ-----RHAMAQEALEKVALGF---VQQRKpSQLSGGQRQRVAIARALVNE 152
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYG--RPGATREEveeaaRAANAHEFIMELPEGYdtvIGERG-VKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446142581 153 PRVLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHdqgeALSM---SDRVAVFNNGRIEQVDSPRDLY 223
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH----RLSTienADRIVVLEDGKIVERGTHEELL 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-223 |
1.64e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 122.25 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYG-----DVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG------TPASNLP 72
Cdd:PRK13641 2 SIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpeTGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 73 PWERDVNTVFQ--DYALFPHmSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGF-VQQRKPSQLSGGQRQRVAIARAL 149
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446142581 150 VNEPRVLLLDEPLGALDLKLREQMqLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-213 |
3.34e-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: 118.09 E-value: 3.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYGDVRA--VNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP--WERDVNTV 81
Cdd:cd03246 2 EVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPneLGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 82 FQDYALFPHmSILDNVayglmvkgvnkkqrhamaqealekvalgfvqqrkpsqLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:cd03246 82 PQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446142581 162 LGALDLKlREQMQLELKKLQQSLGITFIFVTHdQGEALSMSDRVAVFNNGRI 213
Cdd:cd03246 124 NSHLDVE-GERALNQAIAALKAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-213 |
7.12e-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: 119.11 E-value: 7.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY---GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPasnLPPWE-----R 76
Cdd:cd03248 12 VKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKP---ISQYEhkylhS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 77 DVNTVFQDYALFPHmSILDNVAYGLMVKG---VNKKQRHAMAQEALEKVALGFVQQ--RKPSQLSGGQRQRVAIARALVN 151
Cdd:cd03248 89 KVSLVGQEPVLFAR-SLQDNIAYGLQSCSfecVKEAAQKAHAHSFISELASGYDTEvgEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446142581 152 EPRVLLLDEPLGALDLKLREQMQlelKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQ---QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
5-223 |
8.80e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 119.86 E-value: 8.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY-GDVR-AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP--ASNLPPWERDVNT 80
Cdd:PRK13648 8 IVFKNVSFQYqSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQD-YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK13648 88 VFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446142581 160 EPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13648 168 EATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-230 |
1.39e-31 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 124.97 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 11 SRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGT-----PASNLPPWERDVNTVFQD- 84
Cdd:PRK10261 331 NRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlSPGKLQALRRDIQFIFQDp 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YA-LFPHMSILDNVAYGLMVKGV-NKKQRHAMAQEALEKVALGFVQQ-RKPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:PRK10261 411 YAsLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 162 LGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPF 230
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPY 559
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-223 |
2.09e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 119.08 E-value: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYG-----DVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASN------LP 72
Cdd:PRK13649 2 GINLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 73 PWERDVNTVFQdyalFPHM-----SILDNVAYGLMVKGVNKKQRHAMAQEALEKVALG-FVQQRKPSQLSGGQRQRVAIA 146
Cdd:PRK13649 82 QIRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 147 RALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-223 |
4.07e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 118.27 E-value: 4.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLY---GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGT--PASNLPPWE 75
Cdd:PRK13642 1 MNKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEllTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 76 RDVNTVFQDY-ALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK13642 81 RKIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 155 VLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-213 |
4.38e-31 |
|
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: 117.33 E-value: 4.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAV-NGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASN--LPPWERDVNTV 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVlKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 82 FQDYALFpHMSILDNVAYGLMvkGVNKKQ-----RHAMAQEALEKVALGF---VQQRKpSQLSGGQRQRVAIARALVNEP 153
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYGRP--DATDEEvieaaKAAQIHDKIMRFPDGYdtiVGERG-LKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 154 RVLLLDEPLGALDLKLREQMQLELKKLqqSLGITFIFVTHDQGEALSmSDRVAVFNNGRI 213
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-222 |
5.86e-31 |
|
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: 116.56 E-value: 5.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVR-AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLP--PWERDVNTV 81
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 82 FQDYALFPHmSILDNVAYG---LMVKGVNKKQRHAMAQEALEKVALGFVQQRKP--SQLSGGQRQRVAIARALVNEPRVL 156
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGrpnATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGEngGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 157 LLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHdqgeALSM---SDRVAVFNNGRIEQVDSPRDL 222
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH----RLSTiknADKILVLDDGKIIEEGTHDEL 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-226 |
6.08e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 117.11 E-value: 6.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPwerdvntvfQD 84
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPS---------RE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALfpHMSIL--DN-VAYGLMV------------KGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARAL 149
Cdd:COG4604 73 LAK--RLAILrqENhINSRLTVrelvafgrfpysKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 150 VNEPRVLLLDEPLGALDLKL-REQMQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLyMRP 226
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHsVQMMKL-LRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI-ITP 226
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-213 |
1.04e-30 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 116.86 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLY---------GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP--AS 69
Cdd:COG4167 1 MSALLEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKleYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 70 NLPPWERDVNTVFQD--YALFPHM---SILD-----NVAYglmvkgvNKKQRHAMAQEALEKVAL-----GFvqqrKPSQ 134
Cdd:COG4167 81 DYKYRCKHIRMIFQDpnTSLNPRLnigQILEeplrlNTDL-------TAEEREERIFATLRLVGLlpehaNF----YPHM 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 135 LSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEV 228
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-213 |
1.08e-30 |
|
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: 116.09 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWER---DVNTVF 82
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 83 QDYALFPHMSILDNVAYGLMVKGVNKKQRhamAQEALEKV-ALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKI---PDEIYELFpVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446142581 162 LGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-213 |
1.16e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 117.88 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 18 RAVNGVSIAIKDGEFFSMLGPSGSGKTTclrLIAGFEQL----SGGAISIFGTPASNLPPWE------------------ 75
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTT---FIEHLNALllpdTGTIEWIFKDEKNKKKTKEkekvleklviqktrfkki 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 76 -------RDVNTVFQ--DYALFpHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVAL--GFVQqRKPSQLSGGQRQRVA 144
Cdd:PRK13651 98 kkikeirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdeSYLQ-RSPFELSGGQKRRVA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 145 IARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-212 |
1.82e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 120.52 E-value: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPweRD--- 77
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSP--RDaia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 --VNTVFQDYALFPHMSILDNVAYGLMVKG---VNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNE 152
Cdd:COG3845 80 lgIGMVHQHFMLVPNLTVAENIVLGLEPTKggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 153 PRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:COG3845 160 ARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-213 |
1.90e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 116.37 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGD-VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP--ASNLPPWERD 77
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvnAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 VNTVFQDY--ALFPhMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK13647 81 VGLVFQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 156 LLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-220 |
4.00e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 115.50 E-value: 4.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGF---EQLSGGAISIFGTPASNLPPWERD 77
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 VNT-------VFQDYALFPHMSILDNVAYGLM---------VKGVNKKQRHAmAQEALEKVALGFVQQRKPSQLSGGQRQ 141
Cdd:PRK09984 81 IRKsrantgyIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKQR-ALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 142 RVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVA------VFNNGRIEQ 215
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIValrqghVFYDGSSQQ 239
|
....*
gi 446142581 216 VDSPR 220
Cdd:PRK09984 240 FDNER 244
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-228 |
6.19e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 115.17 E-value: 6.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGD-VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP----ASNLPPWERDVN 79
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikydKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQ--DYALF-PhmSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:PRK13639 82 IVFQnpDDQLFaP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446142581 157 LLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRT 228
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-222 |
7.00e-30 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 113.79 E-value: 7.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 30 GEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASnlpPWERDVNTVFQ------DYALFPHMSILDNVAYGLMV 103
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPG---KGWRHIGYVPQrhefawDFPISVAHTVMSGRTGHIGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 104 KGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQS 183
Cdd:TIGR03771 83 LRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELAGA 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 446142581 184 lGITFIFVTHDQGEALSMSDRVAVFnNGRIEQVDSPRDL 222
Cdd:TIGR03771 163 -GTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQL 199
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-222 |
7.59e-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: 119.44 E-value: 7.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYG--DVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASN--LPPWERDVNT 80
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADytLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFPHmSILDNVAYGLMVKGVNKKQRHAM----AQEALEKVALGFVQQ--RKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYGRTEQADRAEIERALaaayAQDFVDKLPLGLDTPigENGVLLSGGQRQRLAIARALLKDAP 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446142581 155 VLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHdqgeALSM---SDRVAVFNNGRIEQVDSPRDL 222
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAH----RLSTiekADRIVVMDDGRIVERGTHNEL 554
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-214 |
9.44e-30 |
|
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: 113.40 E-value: 9.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 14 YGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLppwerDVNTVFQdyalfPHMSI 93
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----GLGGGFN-----PELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 94 LDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQM 173
Cdd:cd03220 102 RENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446142581 174 QLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIE 214
Cdd:cd03220 182 QRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
15-233 |
2.03e-29 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 115.21 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 15 GDVRAVNGVSIAIKDGEFFSMLGPSGSGKT----TCLRLIAGFEQLSGGAIsiF-GTPASNLPpwERDVN--------TV 81
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIGGSAT--FnGREILNLP--EKELNklraeqisMI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 82 FQD--YALFPHMSILDNVAYGLMV-KGVNKKQRHAMAQEALEKVALGFVQQRK---PSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK09473 103 FQDpmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 156 LLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAG 233
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIG 260
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-209 |
2.42e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 113.34 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 2 TYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLR-------LIAGFEqlSGGAISIFGTP--ASNLP 72
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNlyAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 73 PWE--RDVNTVFQDYALFPHmSILDNVAYGLMVKGVnKKQRHAMAQEALEKVALGFVQQRKPSQ----LSGGQRQRVAIA 146
Cdd:PRK14243 86 PVEvrRRIGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 147 RALVNEPRVLLLDEPLGALD----LKLREQMQlELKKlqqslGITFIFVTHDQGEALSMSDRVAVFN 209
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDpistLRIEELMH-ELKE-----QYTIIIVTHNMQQAARVSDMTAFFN 224
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
19-226 |
2.92e-29 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 112.08 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 19 AVNGVSIAIKDGEFFSMLGPSGSGKT-TCLRLI----AGFEQLSGgAISIFGTPASNLPPWERDVNTVFQD--YALFPHM 91
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSlTCLAILgllpPGLTQTSG-EILLDGRPLLPLSIRGRHIATIMQNprTAFNPLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 92 SILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQ---RKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:TIGR02770 80 TMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEvlkKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 169 LREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:TIGR02770 160 NQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNP 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-194 |
3.36e-29 |
|
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: 117.39 E-value: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVR-AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP--WERDVNT 80
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAdsWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFPHmSILDNVAYGLmvkgvnKKQRHAMAQEALEKVAL-GFVQQR----------KPSQLSGGQRQRVAIARAL 149
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLAR------PDASDAEIREALERAGLdEFVAALpqgldtpigeGGAGLSGGQAQRLALARAF 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446142581 150 VNEPRVLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHD 194
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR 516
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-223 |
7.22e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 112.63 E-value: 7.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 3 YAVEFDNVSRLYGD-VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP----ASNLPPWERD 77
Cdd:PRK13636 4 YILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPidysRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 VNTVFQ--DYALFPhMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK13636 84 VGMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 156 LLLDEPLGALDLK-LREQMQLeLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13636 163 LVLDEPTAGLDPMgVSEIMKL-LVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-222 |
8.37e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 113.77 E-value: 8.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 2 TYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWER-DVNT 80
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARaRIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFPHMSILDN-VAYGLMVkGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK13536 119 VPQFDNLDLEFTVRENlLVFGRYF-GMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446142581 160 EPLGALDLKLREQMQLELKKLqQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
4-222 |
1.06e-28 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 116.59 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGD--VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE--RDVN 79
Cdd:TIGR03797 451 AIEVDRVTFRYRPdgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAvrRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQDYALFPHmSILDNVAYGLMVKgvnkkqrHAMAQEALEKVALGFVQQRKP-----------SQLSGGQRQRVAIARA 148
Cdd:TIGR03797 531 VVLQNGRLMSG-SIFENIAGGAPLT-------LDEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARA 602
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 149 LVNEPRVLLLDEPLGALDLKLREQMQLELKKLQqslgITFIFVTHdqgeALSM---SDRVAVFNNGRIEQVDSPRDL 222
Cdd:TIGR03797 603 LVRKPRILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAH----RLSTirnADRIYVLDAGRVVQQGTYDEL 671
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-223 |
3.23e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 111.02 E-value: 3.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYG-----DVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG------TPASNLPP 73
Cdd:PRK13646 3 IRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 74 WERDVNTVFQdyalFPHMSIL-DNVA----YGLMVKGVNKKQRHAMAQEALekVALGF---VQQRKPSQLSGGQRQRVAI 145
Cdd:PRK13646 83 VRKRIGMVFQ----FPESQLFeDTVEreiiFGPKNFKMNLDEVKNYAHRLL--MDLGFsrdVMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 146 ARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-216 |
3.73e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 110.13 E-value: 3.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSG-----GAISIFGTPA----SNLPPW 74
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 75 ERDVNTVFQDYALFPhMSILDNVAYGLMVKGVNKK-QRHAMAQEALEKVALGFVQQRK----PSQLSGGQRQRVAIARAL 149
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLWDEIKHKihksALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 150 VNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVF--NNGRIEQV 216
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRIGQL 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-223 |
6.31e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 110.10 E-value: 6.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 7 FDNVSRLYG-----DVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISI--FGTPAS-----NLPPW 74
Cdd:PRK13645 9 LDNVSYTYAkktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdYAIPANlkkikEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 75 ERDVNTVFQ--DYALFPHmSILDNVAYGLMVKGVNKKQRHAMAQEALEKVAL--GFVQqRKPSQLSGGQRQRVAIARALV 150
Cdd:PRK13645 89 RKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpeDYVK-RSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446142581 151 NEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-213 |
6.77e-28 |
|
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: 108.57 E-value: 6.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 10 VSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGtpasnLPPWERDVNTVFQ------ 83
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVPWKRRKKFLRRigvvfg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 -------------DYALFPHMSILDNVAYglmvkgvnkKQRHAMAQEALEKVALGFVQQRkpsQLSGGQRQRVAIARALV 150
Cdd:cd03267 102 qktqlwwdlpvidSFYLLAAIYDLPPARF---------KKRLDELSELLDLEELLDTPVR---QLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446142581 151 NEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
8-222 |
9.34e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 108.44 E-value: 9.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 8 DNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWER---DVNTVFQD 84
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarrGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGLMV-KGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446142581 164 ALDlklrEQMQLELKKLQQSL---GITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:PRK10895 167 GVD----PISVIDIKRIIEHLrdsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-223 |
9.47e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 109.82 E-value: 9.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 18 RAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAI---SIFGTPASN---LPPWERDVNTVFQ--DYALFP 89
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgDIVVSSTSKqkeIKPVRKKVGVVFQfpESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 90 HmSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGF-VQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:PRK13643 100 E-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 169 LREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13643 179 ARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-236 |
1.62e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 108.64 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 9 NVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGF-EQLSG---------GAISIFGTpaSNLPPWERDV 78
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSGyrysgdvllGGRSIFNY--RDVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 79 NTVFQDYALFPhMSILDNVAYGLMV-KGVNKKQRHAMAQEALEKVAL-GFVQQR---KPSQLSGGQRQRVAIARALVNEP 153
Cdd:PRK14271 104 GMLFQRPNPFP-MSIMDNVLAGVRAhKLVPRKEFRGVAQARLTEVGLwDAVKDRlsdSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 154 RVLLLDEPLGALDLKLREQMQLELKKLQQSLgiTFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPR----TP 229
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKhaetAR 260
|
....*..
gi 446142581 230 FVAGFVG 236
Cdd:PRK14271 261 YVAGLSG 267
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-227 |
1.96e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 111.09 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE--RDVNTVF 82
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 83 QDYAL--------------FPHMSILDnvayglmvkGVNKKQRHAMaQEALEKVALGFVQQRKPSQLSGGQRQRVAIARA 148
Cdd:PRK09536 84 QDTSLsfefdvrqvvemgrTPHRSRFD---------TWTETDRAAV-ERAMERTGVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 149 LVNEPRVLLLDEPLGALDLKlREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPR 227
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDIN-HQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADT 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-213 |
2.62e-27 |
|
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: 107.19 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVS-RLYGDVRAV-NGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP-ASNLPPW-ERDVNT 80
Cdd:cd03252 1 ITFEHVRfRYKPDGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlALADPAWlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFpHMSILDNVAY---GLMVKGVNKKQRHAMAQEALEKVALGF--VQQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALadpGMSMERVIEAAKLAGAHDFISELPEGYdtIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 156 LLLDEPLGALDLKLREQMQLELKKLqqSLGITFIFVTHdQGEALSMSDRVAVFNNGRI 213
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDI--CAGRTVIIIAH-RLSTVKNADRIIVMEKGRI 214
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-226 |
6.49e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 111.35 E-value: 6.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY---GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPasnLPPWE-----R 76
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVP---LVQYDhhylhR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 77 DVNTVFQDYALFPHmSILDNVAYGLmvKGVNKKQRHAMAQEALekvALGFVQQ----------RKPSQLSGGQRQRVAIA 146
Cdd:TIGR00958 556 QVALVGQEPVLFSG-SVRENIAYGL--TDTPDEEIMAAAKAAN---AHDFIMEfpngydtevgEKGSQLSGGQKQRIAIA 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 147 RALVNEPRVLLLDEPLGALDLKLrEQMQLELKKLQqslGITFIFVTHDqgeaLSM---SDRVAVFNNGRIEQVDSPRDLY 223
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAEC-EQLLQESRSRA---SRTVLLIAHR----LSTverADQILVLKKGSVVEMGTHKQLM 701
|
...
gi 446142581 224 MRP 226
Cdd:TIGR00958 702 EDQ 704
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-213 |
6.61e-27 |
|
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: 105.03 E-value: 6.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 8 DNVSRLYGDV-RAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGtpaSNLPPWER--DVNTVFQD 84
Cdd:cd03226 3 ENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERrkSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 --YALFPHmSILDNVAYGLMVKGVNKKQrhamAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:cd03226 80 vdYQLFTD-SVREELLLGLKELDAGNEQ----AETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446142581 163 GALDLKLREQMQLELKKLqQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03226 155 SGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-223 |
2.41e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.55 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVR------AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP- 73
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 74 WE--RDVNTVFQDyalfPHMSIL-----DNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIA 146
Cdd:PRK13633 81 WDirNKAGMVFQN----PDNQIVativeEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 147 RALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDSPRDLY 223
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
9-223 |
2.80e-26 |
|
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: 104.91 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 9 NVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAG----------FEQLSGGAISIFGTPASNLPPWER-D 77
Cdd:TIGR02323 8 GLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGrlapdhgtatYIMRSGAELELYQLSEAERRRLMRtE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 VNTVFQDYA--LFPHMSILDNVAYGLMVKGvnkkQRH-----AMAQEALEKVALGfvQQR---KPSQLSGGQRQRVAIAR 147
Cdd:TIGR02323 88 WGFVHQNPRdgLRMRVSAGANIGERLMAIG----ARHygnirATAQDWLEEVEID--PTRiddLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 148 ALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI------EQV-DSPR 220
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVvesgltDQVlDDPQ 241
|
...
gi 446142581 221 DLY 223
Cdd:TIGR02323 242 HPY 244
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-226 |
3.79e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.88 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY-GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPAS--NLPPWERDVNTV 81
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 82 FQ--DYALFPhMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK13652 84 FQnpDDQIFS-PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 160 EPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-213 |
4.64e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 108.51 E-value: 4.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVR-AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPAS--NLPPWERDVNT 80
Cdd:PRK13657 334 AVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRtvTRASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFpHMSILDNVAYG---LMVKGVNKKQRHAMAQEALEKVALGF---VQQRKpSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK13657 414 VFQDAGLF-NRSIEDNIRVGrpdATDEEMRAAAERAQAHDFIERKPDGYdtvVGERG-RQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446142581 155 VLLLDEPLGALDLKLREQMQLELKKLQQSLgITFIfVTHdqgeALSM---SDRVAVFNNGRI 213
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDELMKGR-TTFI-IAH----RLSTvrnADRILVFDNGRV 547
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-213 |
1.39e-25 |
|
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: 100.97 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 18 RAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVF------QDYALFPHM 91
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvpedrKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 92 SILDNVAYglmvkgvnkkqrhamaqealekvalgfvqqrkPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLRE 171
Cdd:cd03215 94 SVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446142581 172 QMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03215 142 EIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-222 |
3.28e-25 |
|
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: 106.36 E-value: 3.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYG-DVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE--RDVNTV 81
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlrQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 82 FQDYALFPHmSILDNVAYG----LMVKGVNKKQRHAMAQEALEKVALGFVQQ--RKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGakenVSQDEIWAACEIAEIKDDIENMPLGYQTElsEEGSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 156 LLLDEPLGALDLKLREQMQLELKKLQQSlgiTFIFVTHdQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-226 |
3.56e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 102.15 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGtpaSNLPPWERD------- 77
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG---ENIPAMSRSrlytvrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 -VNTVFQDYALFPHMSILDNVAYGLmvkgvnkkQRHAMAQEA---------LEKVALGFVQQRKPSQLSGGQRQRVAIAR 147
Cdd:PRK11831 85 rMSMLFQSGALFTDMNVFDNVAYPL--------REHTQLPAPllhstvmmkLEAVGLRGAAKLMPSELSGGMARRAALAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 148 ALVNEPRVLLLDEP--------LGALdLKLreqmqleLKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSP 219
Cdd:PRK11831 157 AIALEPDLIMFDEPfvgqdpitMGVL-VKL-------ISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA 228
|
....*..
gi 446142581 220 RDLYMRP 226
Cdd:PRK11831 229 QALQANP 235
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-194 |
3.97e-25 |
|
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: 105.52 E-value: 3.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 15 GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE--RDVNTVFQDYALFpHMS 92
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 93 ILDNVAYGlmvkgvNKKQRHAMAQEALEKVALGFVQQRKP-----------SQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:TIGR02868 425 VRENLRLA------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|...
gi 446142581 162 LGALDLKLREQMQLELkkLQQSLGITFIFVTHD 194
Cdd:TIGR02868 499 TEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-223 |
4.26e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 101.54 E-value: 4.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 8 DNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAG----------FEQLSGGAISIFGTPASNLPPWER- 76
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSArlapdagevhYRMRDGQLRDLYALSEAERRRLLRt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 77 DVNTVFQDYA--LFPHMSILDNVAYGLMVKGvnkkQRH-----AMAQEALEKVALGfvQQR---KPSQLSGGQRQRVAIA 146
Cdd:PRK11701 90 EWGFVHQHPRdgLRMQVSAGGNIGERLMAVG----ARHygdirATAGDWLERVEID--AARiddLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 147 RALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI------EQV-DSP 219
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVvesgltDQVlDDP 243
|
....
gi 446142581 220 RDLY 223
Cdd:PRK11701 244 QHPY 247
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-213 |
1.65e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 99.27 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 16 DVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQ---LSGGAISIFGTPaSNLPPWERDVNTVFQDYALFPHMS 92
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQP-RKPDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 93 ILDNVAYGLMVKGVN---KKQRHAM-AQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:cd03234 98 VRETLTYTAILRLPRkssDAIRKKRvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446142581 169 LREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-236 |
1.67e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 103.84 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP---ASNLPPWERD 77
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 VNTVFQDYALFPHMSILDNVAYG-LMVKG--VNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGqLPHKGgiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 155 VLLLDEPLGALDLKLREQmqleLKKLQQSL---GITFIFVTHDQGEALSMSDRVAVFNNGRieQVDSPRDLYMRPRTPFV 231
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQ----LFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDGR--YVATFDDMAQVDRDQLV 234
|
....*
gi 446142581 232 AGFVG 236
Cdd:PRK11288 235 QAMVG 239
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-221 |
1.75e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.77 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVS---RLY-------------------GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSG 58
Cdd:COG1134 1 MSSMIEVENVSksyRLYhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 59 GAISIFGTPASNLppwerDVNTVFQdyalfPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALG-FVQQrkP-SQLS 136
Cdd:COG1134 81 GRVEVNGRVSALL-----ELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGdFIDQ--PvKTYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 137 GGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQV 216
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
....*
gi 446142581 217 DSPRD 221
Cdd:COG1134 228 GDPEE 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-226 |
4.31e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 100.31 E-value: 4.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 16 DVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISI--------FGTPASNLPPWERD---------- 77
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkKNNHELITNPYSKKiknfkelrrr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 VNTVFQ--DYALFPHmSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGF-VQQRKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK13631 118 VSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446142581 155 VLLLDEPLGALDLK-LREQMQLELKKLQQslGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:PRK13631 197 ILIFDEPTAGLDPKgEHEMMQLILDAKAN--NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-212 |
4.94e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 102.31 E-value: 4.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLiagfeqLSG--------GAISIFGTP--ASN 70
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKV------LSGvyphgtyeGEIIFEGEElqASN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 71 LPPWERD-VNTVFQDYALFPHMSILDNVAYG--LMVKGV-NKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIA 146
Cdd:PRK13549 76 IRDTERAgIAIIHQELALVKELSVLENIFLGneITPGGImDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446142581 147 RALVNEPRVLLLDEPLGALDLKLREQMqLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVL-LDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-227 |
5.64e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.55 E-value: 5.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 8 DNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPwerdvNTVFQDYAL 87
Cdd:PRK11231 6 ENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-----RQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 88 FP--HM-----SILDNVAYG----LMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:PRK11231 81 LPqhHLtpegiTVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446142581 157 LLDEPLGALDLklreQMQLELKKLQQSL---GITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLyMRPR 227
Cdd:PRK11231 161 LLDEPTTYLDI----NHQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV-MTPG 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-218 |
7.80e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 97.64 E-value: 7.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP---WERD 77
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakiMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 VNTVFQDYALFPHMSILDNVAYGLMVkgVNKKQRhamaQEALEKVALGF--VQQRKPSQ---LSGGQRQRVAIARALVNE 152
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMGGFF--AERDQF----QERIKWVYELFprLHERRIQRagtMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446142581 153 PRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDS 218
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-213 |
1.40e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 99.01 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 10 VSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGtpasnLPPWE------RDVNTVF- 82
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-----YVPFKrrkefaRRIGVVFg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 83 QDYALFPHMSILDNvaYGLM--VKGVNK---KQRHAMAQEALEkvaLG-FVQQ--RkpsQLSGGQRQRVAIARALVNEPR 154
Cdd:COG4586 103 QRSQLWWDLPAIDS--FRLLkaIYRIPDaeyKKRLDELVELLD---LGeLLDTpvR---QLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446142581 155 VLLLDEP-LGaLDLKLREQMQLELKKLQQSLGITFIFVTHDQG--EALsmSDRVAVFNNGRI 213
Cdd:COG4586 175 ILFLDEPtIG-LDVVSKEAIREFLKEYNRERGTTILLTSHDMDdiEAL--CDRVIVIDHGRI 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-230 |
1.45e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 101.47 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 17 VRAVNGVSIAIKDGEFFSMLGPSGSGKT-TCLRLIAGFEQLSGGA--------------ISIFGTPASNLPPWE-RDVNT 80
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGLVqcdkmllrrrsrqvIELSEQSAAQMRHVRgADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQD--YALFPHMSILDNVAYGLMV-KGVNKKQRHAMAQEALEKVALGFVQQ---RKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTilsRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446142581 155 VLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPF 230
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPY 264
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-194 |
1.80e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 7 FDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIfgtpasnlPPWERdVNTVFQDYA 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--------PKGLR-IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 87 LFPHMSILDNV----------------AYGLMVKGVNKKQRHAMAQEALE---------KVA-----LGF---VQQRKPS 133
Cdd:COG0488 72 LDDDLTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAELQEEFEalggweaeaRAEeilsgLGFpeeDLDRPVS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 134 QLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK----LREQmqlelkkLQQSLGiTFIFVTHD 194
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLEsiewLEEF-------LKNYPG-TVLVVSHD 208
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-213 |
1.83e-23 |
|
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: 95.70 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 20 VNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGfeQLSGGAIS----IFGTPaSNLPPWERDVNTVFQDYALFPHMSIld 95
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG--RRTGLGVSgevlINGRP-LDKRSFRKIIGYVPQDDILHPTLTV-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 96 nvayglmvkgvnkkqrhamaQEALEKVAlgfvqqrKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQL 175
Cdd:cd03213 100 --------------------RETLMFAA-------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 446142581 176 ELKKLQQSlGITFIFVTHD-QGEALSMSDRVAVFNNGRI 213
Cdd:cd03213 153 LLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
4-213 |
3.15e-23 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 100.59 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVRAV--NGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNL-PPW-ERDVN 79
Cdd:TIGR01846 455 AITFENIRFRYAPDSPEvlSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIAdPAWlRRQMG 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQDYALFPHmSILDNVAY---GLMVKGVNKKQRHAMAQEALEKVALGFVQQ--RKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:TIGR01846 535 VVLQENVLFSR-SIRDNIALcnpGAPFEHVIHAAKLAGAHDFISELPQGYNTEvgEKGANLSGGQRQRIAIARALVGNPR 613
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 155 VLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHdQGEALSMSDRVAVFNNGRI 213
Cdd:TIGR01846 614 ILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQI 669
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-226 |
3.30e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.98 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGD-VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPA---SNLPPWERDVNT 80
Cdd:PRK13644 2 IRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQD-YALFPHMSILDNVAYG---LMVKGVNKKQRHAMAqeaLEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGpenLCLPPIEIRKRVDRA---LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 157 LLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQgEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNL-EELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
12-229 |
5.79e-23 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 95.92 E-value: 5.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 12 RLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKT-TCLRLI----AGFEQLSGgAISIFGTPASNLPPWERDVNTVFQD-- 84
Cdd:PRK10418 11 ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQTAG-RVLLDGKPVAPCALRGRKIATIMQNpr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 YALFPHMSILDNVAYGLMVKGvnKKQRHAMAQEALEKVALGFVQ---QRKPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:PRK10418 90 SAFNPLHTMHTHARETCLALG--KPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 162 LGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTP 229
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-221 |
6.51e-23 |
|
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: 99.44 E-value: 6.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVS-RLYGDVRAV-NGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNlppWERDVNTVF 82
Cdd:COG4618 331 LSVENLTvVPPGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ---WDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 83 -----QDYALFPHmSILDNVAyglmvkgvnkkqRhaMAQEALEKValgfVQ-----------QRKP-----------SQL 135
Cdd:COG4618 408 igylpQDVELFDG-TIAENIA------------R--FGDADPEKV----VAaaklagvhemiLRLPdgydtrigeggARL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 136 SGGQRQRVAIARALVNEPRVLLLDEPLGALD----LKLREQMQlELKKlqqsLGITFIFVTHDQGeALSMSDRVAVFNNG 211
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeAALAAAIR-ALKA----RGATVVVITHRPS-LLAAVDKLLVLRDG 542
|
250
....*....|
gi 446142581 212 RIEQVDsPRD 221
Cdd:COG4618 543 RVQAFG-PRD 551
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-193 |
6.94e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 99.11 E-value: 6.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVS-RLYGDVRAVNGVSIAIKDGEffSML--GPSGSGKTTCLRLIAGFEQLSGGAISifgtpasnLPPWERdvnt 80
Cdd:COG4178 362 ALALEDLTlRTPDGRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIA--------RPAGAR---- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 vfqdyALF----PHM---SILDNVAYGLMVKGVNkkqrHAMAQEALEKVALG------FVQQRKPSQLSGGQRQRVAIAR 147
Cdd:COG4178 428 -----VLFlpqrPYLplgTLREALLYPATAEAFS----DAELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFAR 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446142581 148 ALVNEPRVLLLDEPLGALDLKLREQMqleLKKLQQSL-GITFIFVTH 193
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-213 |
1.32e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.17 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRlygdVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE---------- 75
Cdd:COG1129 258 EVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagiayvp 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 76 --RdvntvfQDYALFPHMSILDNVAYGLMVKG-----VNKKQRHAMAQEALEKVALgfvqqRKPS------QLSGGQRQR 142
Cdd:COG1129 334 edR------KGEGLVLDLSIRENITLASLDRLsrgglLDRRRERALAEEYIKRLRI-----KTPSpeqpvgNLSGGNQQK 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 143 VAIARALVNEPRVLLLDEP-----LGAldlKlREQMQLeLKKL-QQSLGItfIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPtrgidVGA---K-AEIYRL-IRELaAEGKAV--IVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-205 |
2.17e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.63 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP--WERDVNTVFQ 83
Cdd:PRK10247 9 QLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiYRQQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 DYALFPHmSILDNVAYGLMVKGVN---KKQRHAMAQEALEKVALgfvqQRKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:PRK10247 89 TPTLFGD-TVYDNLIFPWQIRNQQpdpAIFLDDLERFALPDTIL----TKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446142581 161 PLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEaLSMSDRV 205
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKV 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-214 |
2.42e-22 |
|
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: 91.99 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYG--DVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVF 82
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 83 QDYALFPHMSILDNVAyglmvkgvnkkqrhamaqealekvalgfvqqrkpSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:cd03247 81 NQRPYLFDTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446142581 163 GALDlKLREQMQLELkKLQQSLGITFIFVTHdQGEALSMSDRVAVFNNGRIE 214
Cdd:cd03247 127 VGLD-PITERQLLSL-IFEVLKDKTLIWITH-HLTGIEHMDKILFLENGKII 175
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-219 |
2.67e-22 |
|
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: 97.57 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAG---FEQLSGGAI---------------SIFGT 66
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqYEPTSGRIIyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 67 P----ASNLPPWERDV----NTVFQD------------YALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGF 126
Cdd:TIGR03269 81 PcpvcGGTLEPEEVDFwnlsDKLRRRirkriaimlqrtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 127 VQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVA 206
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|...
gi 446142581 207 VFNNGRIEQVDSP 219
Cdd:TIGR03269 241 WLENGEIKEEGTP 253
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-215 |
3.42e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.22 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 23 VSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFeqLS-GGAISIFGTPASNLPP--WERDVNTVFQDYALFpHMSILDNVAY 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF--LPyQGSLKINGIELRELDPesWRKHLSWVGQNPQLP-HGTLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 100 GlmvkgvnkkqRHAMAQEALEKV-----ALGFVQQRKP----------SQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:PRK11174 446 G----------NPDASDEQLQQAlenawVSEFLPLLPQgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446142581 165 LDLKLREQMQLELKklQQSLGITFIFVTHdQGEALSMSDRVAVFNNGRIEQ 215
Cdd:PRK11174 516 LDAHSEQLVMQALN--AASRRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQ 563
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-213 |
4.21e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.66 E-value: 4.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP---WERD 77
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 VNTVFQDYALFPHMSILDNVAYGLmvkgvnkkQRHAMAQEALEKVALGFVQQRKPSQLSG----GQRQRVAIARALVNEP 153
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGL--------PKRQASMQKMKQLLAALGCQLDLDSSAGslevADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 154 RVLLLDEPLGALDLKLREQMQLELKKLQQsLGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-215 |
6.82e-22 |
|
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: 96.43 E-value: 6.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVRAV-NGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG------TPASnLppwER 76
Cdd:COG5265 357 EVRFENVSFGYDPERPIlKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvTQAS-L---RA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 77 DVNTVFQDYALFpHMSILDNVAYGlmvkgvnkkqRHAMAQEALEKVA-----LGFVQQ-----------R--KpsqLSGG 138
Cdd:COG5265 433 AIGIVPQDTVLF-NDTIAYNIAYG----------RPDASEEEVEAAAraaqiHDFIESlpdgydtrvgeRglK---LSGG 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 139 QRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLqqSLGITFIFVTHdqgeALSM---SDRVAVFNNGRI-E 214
Cdd:COG5265 499 EKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV--ARGRTTLVIAH----RLSTivdADEILVLEAGRIvE 572
|
.
gi 446142581 215 Q 215
Cdd:COG5265 573 R 573
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-213 |
8.86e-22 |
|
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: 95.88 E-value: 8.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 20 VNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGtpaSNLPPWERD-----VNTVFQDYALFPHmSIL 94
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG---ADLKQWDREtfgkhIGYLPQDVELFPG-TVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 95 DNVAyglmvkgvnKKQRHAMAQEALEKVALGFVQ---QRKP-----------SQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:TIGR01842 410 ENIA---------RFGENADPEKIIEAAKLAGVHeliLRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 161 PLGALD----LKLREQMQlELKKlqqsLGITFIFVTHDQGeALSMSDRVAVFNNGRI 213
Cdd:TIGR01842 481 PNSNLDeegeQALANAIK-ALKA----RGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
8-230 |
1.39e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 93.27 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 8 DNVSRLYGDV----RAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGF----EQLSGGAISIFGTPASNLPPWER--- 76
Cdd:PRK11022 7 DKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERrnl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 77 ---DVNTVFQDyalfpHMSILD---NVAYGLMV-----KGVNKKQRHAMAQEALEKVALGFVQQR---KPSQLSGGQRQR 142
Cdd:PRK11022 87 vgaEVAMIFQD-----PMTSLNpcyTVGFQIMEaikvhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 143 VAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
....*...
gi 446142581 223 YMRPRTPF 230
Cdd:PRK11022 242 FRAPRHPY 249
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-226 |
1.63e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 92.16 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 17 VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPAS--NLPPWERDVNTVFQD--YALFPHMS 92
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDpsTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 93 ILDNVAYGLMVK-GVNKKQRHAMAQEALEKVALGFVQQRK-PSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLR 170
Cdd:PRK15112 106 ISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLPDHASYyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446142581 171 EQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-205 |
1.68e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.37 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 14 YGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTpasnlppweRDVNTVFQDYAL---FPh 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------ARVAYVPQRSEVpdsLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 91 MSILDNVAYGLMVK----GVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:NF040873 72 LTVRDLVAMGRWARrglwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 446142581 167 LKLREQMqLELKKLQQSLGITFIFVTHDQGEALSMSDRV 205
Cdd:NF040873 152 AESRERI-IALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-212 |
1.71e-21 |
|
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: 94.89 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSG--GAISIFGTP--ASNLPPWERD-VN 79
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPlkASNIRDTERAgIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQDYALFPHMSILDNVAYG--LMVKG--VNKKQRHAMAQEALEKVALGFVQQRKP-SQLSGGQRQRVAIARALVNEPR 154
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGneITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 155 VLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-230 |
1.92e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.77 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 18 RAVNGVSIAIKDGEFFSMLGPSGSGKT----TCLRLI--------------AG----------FEQLSGGAIS-IFGTPA 68
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypsgdirfHGesllhaseqtLRGVRGNKIAmIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 69 SNLPPW---ERDVNTVfqdyaLFPHmsildnvayglmvKGVNKKQRHAMAQEALEKVALGFVQQRK---PSQLSGGQRQR 142
Cdd:PRK15134 103 VSLNPLhtlEKQLYEV-----LSLH-------------RGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 143 VAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
....*...
gi 446142581 223 YMRPRTPF 230
Cdd:PRK15134 245 FSAPTHPY 252
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-214 |
2.00e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIfGTpasnlppwerdvnTVFQD 84
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-------------TVKIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 Y------ALFPHMSILDNVAYGlmvkGVNKKQRHAMAQeaLEkvALGFV--QQRKP-SQLSGGQRQRVAIARALVNEPRV 155
Cdd:COG0488 382 YfdqhqeELDPDKTVLDELRDG----APGGTEQEVRGY--LG--RFLFSgdDAFKPvGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446142581 156 LLLDEPLGALDLKLREQmqlelkkLQQSL----GiTFIFVTHDQgEAL-SMSDRVAVFNNGRIE 214
Cdd:COG0488 454 LLLDEPTNHLDIETLEA-------LEEALddfpG-TVLLVSHDR-YFLdRVATRILEFEDGGVR 508
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-221 |
2.66e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.47 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLygDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG---TPASNLPPWERDVNTVF 82
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdiSPRSPLDAVKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 83 Q---DYALFPHMSILDNVA---------YGLMVKGVNKKQRHAMAQEALEKVAL--GFVQQrKPSQLSGGQRQRVAIARA 148
Cdd:PRK09700 345 EsrrDNGFFPNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQRELLALkcHSVNQ-NITELSGGNQQKVLISKW 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446142581 149 LVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRD 221
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-211 |
3.25e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.08 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP---WERD 77
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 VNTVFQDYALFPHMSILDNVAYG-LMVK---GVN----KKQRhAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARAL 149
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGrHLTKkvcGVNiidwREMR-VRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446142581 150 VNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNG 211
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-212 |
4.02e-20 |
|
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: 87.49 E-value: 4.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSR-----LYGDVR--AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAI---SIFG-TPAS 69
Cdd:COG4778 1 MTTLLEVENLSKtftlhLQGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrHDGGwVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 70 NLPPWE------RDVNTVFQdyalF----PHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKvaLGfVQQR----KPSQL 135
Cdd:COG4778 81 QASPREilalrrRTIGYVSQ----FlrviPRVSALDVVAEPLLERGVDREEARARARELLAR--LN-LPERlwdlPPATF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 136 SGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLRE---QMQLELKklqqSLGITFIFVTHDQG--EALsmSDRVAVFNN 210
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAvvvELIEEAK----ARGTAIIGIFHDEEvrEAV--ADRVVDVTP 227
|
..
gi 446142581 211 GR 212
Cdd:COG4778 228 FS 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
8-166 |
9.05e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.08 E-value: 9.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 8 DNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQDyAL 87
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRN-AM 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 88 FPHMSILDNVAYGLMVKGvnkkQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:PRK13539 85 KPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-166 |
4.19e-19 |
|
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: 83.95 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 15 GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP-WERDVNTVFQDYALFPHMSI 93
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDePHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446142581 94 LDNVAYGLMVKGvnKKQRhaMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:TIGR01189 91 LENLHFWAAIHG--GAQR--TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-213 |
4.20e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.15 E-value: 4.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY--GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGT-----PASNLppwERD 77
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdyTLASL---RNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 VNTVFQDYALFpHMSILDNVAYGLMVK----GVNKKQRHAMAQEALEKVALGF--VQQRKPSQLSGGQRQRVAIARALVN 151
Cdd:PRK11176 419 VALVSQNVHLF-NDTIANNIAYARTEQysreQIEEAARMAYAMDFINKMDNGLdtVIGENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 152 EPRVLLLDEPLGALDLKLREQMQLELKKLQQSLgiTFIFVTHdqgeALSM---SDRVAVFNNGRI 213
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAH----RLSTiekADEILVVEDGEI 556
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-234 |
4.34e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.44 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 14 YGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPAS----NLPPWERDVNTVFQD--YAL 87
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQDpeQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 88 FpHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKV-ALGFVQQrkPSQ-LSGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:PRK13638 91 F-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVdAQHFRHQ--PIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 166 DLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGF 234
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGL 235
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-213 |
4.53e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.96 E-value: 4.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 3 YAVEFDNVSRLYGD--VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPpwERD--- 77
Cdd:PRK11160 337 VSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS--EAAlrq 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 -VNTVFQDYALFPHmSILDNVAYGLmvkgvNKKQRHAMAqEALEKVALG-FVQQRKP---------SQLSGGQRQRVAIA 146
Cdd:PRK11160 415 aISVVSQRVHLFSA-TLRDNLLLAA-----PNASDEALI-EVLQQVGLEkLLEDDKGlnawlgeggRQLSGGEQRRLGIA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 147 RALVNEPRVLLLDEPLGALDlKLREQMQLELkKLQQSLGITFIFVTHdQGEALSMSDRVAVFNNGRI 213
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLD-AETERQILEL-LAEHAQNKTVLMITH-RLTGLEQFDRICVMDNGQI 551
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-166 |
6.66e-19 |
|
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: 83.31 E-value: 6.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 16 DVRAV-NGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP-ASNLPPWERDVNTVFQDYALFPHMSI 93
Cdd:cd03231 11 DGRALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPlDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 94 LDNVAYglmvkgvnKKQRHAMAQ--EALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:cd03231 91 LENLRF--------WHADHSDEQveEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
5-215 |
1.50e-18 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 86.54 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRA--VNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPwERDVN--- 79
Cdd:TIGR03796 478 VELRNITFGYSPLEPplIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPR-EVLANsva 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQDYALFpHMSILDNVAygLMVKGVNKKQRHAMAQEAlekvALGFVQQRKP-----------SQLSGGQRQRVAIARA 148
Cdd:TIGR03796 557 MVDQDIFLF-EGTVRDNLT--LWDPTIPDADLVRACKDA----AIHDVITSRPggydaelaeggANLSGGQRQRLEIARA 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446142581 149 LVNEPRVLLLDEPLGALDlklreqMQLElKKLQQSL---GITFIFVTHdqgeALSM---SDRVAVFNNGRIEQ 215
Cdd:TIGR03796 630 LVRNPSILILDEATSALD------PETE-KIIDDNLrrrGCTCIIVAH----RLSTirdCDEIIVLERGKVVQ 691
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-219 |
1.64e-18 |
|
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: 82.93 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGD--VRAVNGVSIAIKDGEFFSMLGPSGSGKTTC----LRLIagfeQLSGGAISIFGTPASNLPP--WER 76
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLhdLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 77 DVNTVFQDYALFPhmsildnvayGLMVKGVNKKQRH--AMAQEALEKVALGFVQQRKP-----------SQLSGGQRQRV 143
Cdd:cd03244 79 RISIIPQDPVLFS----------GTIRSNLDPFGEYsdEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 144 AIARALVNEPRVLLLDEPLGALDLKLREQMQlelKKLQQSL-GITFIFVTH------DqgealsmSDRVAVFNNGRIEQV 216
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQ---KTIREAFkDCTVLTIAHrldtiiD-------SDRILVLDKGRVVEF 218
|
...
gi 446142581 217 DSP 219
Cdd:cd03244 219 DSP 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-213 |
2.84e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.48 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 21 NGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAgFEQLSG----GAISIFGTPAsNLPPWERDVNTVFQDYALFPHMSILDN 96
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGvkgsGSVLLNGMPI-DAKEMRAISAYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 97 VAYGLMVK---GVNKKQRHAMAQEALEKVALGFVQQRK---PSQ---LSGGQRQRVAIARALVNEPRVLLLDEPLGALDL 167
Cdd:TIGR00955 120 LMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446142581 168 KLREQMQLELKKLQQSlGITFIFVTHD-QGEALSMSDRVAVFNNGRI 213
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRV 245
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-209 |
4.15e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.47 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAIsifgtpasnlppwERD--- 77
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNgkl 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 -VNTVFQDYALFPHMSIldNVAYGLMVKGVNKKqrhAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:PRK09544 68 rIGYVPQKLYLDTTLPL--TVNRFLRLRPGTKK---EDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446142581 157 LLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFN 209
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-213 |
4.15e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.69 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 17 VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWER---DVNTVFQD---YALFPH 90
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYIPEDrlgRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 91 MSILDNVAYGL-----MVKG--VNKKQRHAMAQEALEK--VALGFVQQRkPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:COG3845 351 MSVAENLILGRyrrppFSRGgfLDRKAIRAFAEELIEEfdVRTPGPDTP-ARSLSGGNQQKVILARELSRDPKLLIAAQP 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446142581 162 LGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG3845 430 TRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-195 |
4.77e-18 |
|
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: 79.41 E-value: 4.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAIsifgtpasnlppwerdvntvfqd 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 yalfphmsildnvayglmvkgvnkkqrhamaqEALEKVALGFVqqrkpSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03221 58 --------------------------------TWGSTVKIGYF-----EQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190
....*....|....*....|....*....|.
gi 446142581 165 LDLKLREQMQLELKKLQQslgiTFIFVTHDQ 195
Cdd:cd03221 101 LDLESIEALEEALKEYPG----TVILVSHDR 127
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-219 |
6.27e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 85.07 E-value: 6.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 19 AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP-ASNLPPWERDVNTVFQDYALFPHMSILDNV 97
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDiETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 98 AYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLEL 177
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446142581 178 KKLQQslGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSP 219
Cdd:TIGR01257 1105 LKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-212 |
1.06e-17 |
|
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: 80.21 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 21 NGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPA-SNLPPW-----------------ERDVNTVF 82
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAyVSQEPWiqngtirenilfgkpfdEERYEKVI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 83 QDYALFPHMSILDNvayGLMV----KGVNkkqrhamaqealekvalgfvqqrkpsqLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:cd03250 102 KACALEPDLEILPD---GDLTeigeKGIN---------------------------LSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446142581 159 DEPLGALDLKLREQM--QLELKKLQqsLGITFIFVTHdQGEALSMSDRVAVFNNGR 212
Cdd:cd03250 152 DDPLSAVDAHVGRHIfeNCILGLLL--NNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-207 |
1.07e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 82.65 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 15 GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTtclrLIAGfeqlsggaiSIFGTPASN-----------------LPPWER- 76
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKS----LIAK---------AICGITKDNwhvtadrfrwngidllkLSPRERr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 77 -----DVNTVFQDyalfPhMSILD---NVAYGLM-------VKGV---NKKQRHAMAQEALEKValGFVQQRK-----PS 133
Cdd:COG4170 85 kiigrEIAMIFQE----P-SSCLDpsaKIGDQLIeaipswtFKGKwwqRFKWRKKRAIELLHRV--GIKDHKDimnsyPH 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446142581 134 QLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAV 207
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITV 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-193 |
1.86e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 78.35 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSrLY---GDVRaVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIfgtpasnlpPWERDVntv 81
Cdd:cd03223 1 IELENLS-LAtpdGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDL--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 82 fqdyaLF----PHM---SILDNVAYglmvkgvnkkqrhamaqeALEKValgfvqqrkpsqLSGGQRQRVAIARALVNEPR 154
Cdd:cd03223 67 -----LFlpqrPYLplgTLREQLIY------------------PWDDV------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*....
gi 446142581 155 VLLLDEPLGALDlklrEQMQLELKKLQQSLGITFIFVTH 193
Cdd:cd03223 112 FVFLDEATSALD----EESEDRLYQLLKELGITVISVGH 146
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-193 |
3.99e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.69 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 22 GVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPwerdvntVFQDYALF--------PHMSI 93
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-------EYHQDLLYlghqpgikTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 94 LDNVAYGLMVKGVnkkQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQM 173
Cdd:PRK13538 92 LENLRFYQRLHGP---GDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL 168
|
170 180
....*....|....*....|.
gi 446142581 174 -QLELKKLQQslGITFIFVTH 193
Cdd:PRK13538 169 eALLAQHAEQ--GGMVILTTH 187
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-213 |
4.05e-16 |
|
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: 75.64 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 15 GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFE--QLSGGAISIFGTPASNLPPWERDVNTV---FQDYALFP 89
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIflaFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 90 HMSILDnvayglMVKGVNKkqrhamaqealekvalGFvqqrkpsqlSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKL 169
Cdd:cd03217 91 GVKNAD------FLRYVNE----------------GF---------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446142581 170 REQMQLELKKLqQSLGITFIFVTHDQGEALSM-SDRVAVFNNGRI 213
Cdd:cd03217 140 LRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRI 183
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-327 |
4.91e-16 |
|
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: 79.29 E-value: 4.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 19 AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNlppwerDVNTVFQDYALFPHMSILDNVA 98
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISDVHQNMGYCPQFDAIDDLL 2027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 99 YG-------LMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLRE 171
Cdd:TIGR01257 2028 TGrehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 172 QMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLymrpRTPFVAGFVGTSNVF---DGLMAEk 248
Cdd:TIGR01257 2108 MLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL----KSKFGDGYIVTMKIKspkDDLLPD- 2181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 249 lcgmtgsfaLRP--EHIRLNTPGEMQANGTIQAVQYQGAATR----FELTLSGGEKLLVsqanmtgEELPATLTPGQQVM 322
Cdd:TIGR01257 2182 ---------LNPveQFFQGNFPGSVQRERHYNMLQFQVSSSSlariFQLLISHKDSLLI-------EEYSVTQTTLDQVF 2245
|
....*
gi 446142581 323 VSWSR 327
Cdd:TIGR01257 2246 VNFAK 2250
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
15-230 |
6.09e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 77.54 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 15 GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGF---------------------------EQLSGGAIS-IFGT 66
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrvtadrmrfddidllrlsprerRKLVGHNVSmIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 67 PASNLPPWERDVNTVFQdyalfphmSILDNVAYGLMVKGVNKKQRHAMaqEALEKValGFVQQRK-----PSQLSGGQRQ 141
Cdd:PRK15093 98 PQSCLDPSERVGRQLMQ--------NIPGWTYKGRWWQRFGWRKRRAI--ELLHRV--GIKDHKDamrsfPYELTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 142 RVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRD 221
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKE 245
|
....*....
gi 446142581 222 LYMRPRTPF 230
Cdd:PRK15093 246 LVTTPHHPY 254
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-213 |
6.63e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.12 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 20 VNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVF---QDY---ALFPHMSI 93
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVyisEDRkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 94 LDNVAYGLMVKGVNK--KQRHAMAQEALEKVALGFvQQRKPSQ------LSGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:PRK10762 348 KENMSLTALRYFSRAggSLKHADEQQAVSDFIRLF-NIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446142581 166 DLKL-REQMQLeLKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK10762 427 DVGAkKEIYQL-INQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-212 |
7.55e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.38 E-value: 7.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 20 VNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFQDYALFPHMSILDNVAY 99
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 100 GLMV---KGVNKKQRHAMAQEALEKVALG-----FVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLRE 171
Cdd:PLN03211 164 CSLLrlpKSLTKQEKILVAESVISELGLTkcentIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446142581 172 QMQLELKKLQQSlGITFIFVTHD-QGEALSMSDRVAVFNNGR 212
Cdd:PLN03211 244 RLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-222 |
7.70e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.18 E-value: 7.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 8 DNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE--RDVNTVFQDY 85
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 86 ALFPHMSILDNVAYG------LMVKGvnKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK10253 91 TTPGDITVQELVARGryphqpLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446142581 160 EPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-213 |
7.86e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.09 E-value: 7.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVR-AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP--ASNLPPWERDVNTV 81
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPvtAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 82 FQDYALFPHmsildnvayglMVKGVNKKQRHAMAQEALEKVALgfvqQRKPS---------QLSGGQRQRVAIARALVNE 152
Cdd:PRK10522 403 FTDFHLFDQ-----------LLGPEGKPANPALVEKWLERLKM----AHKLEledgrisnlKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446142581 153 PRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQgEALSMSDRVAVFNNGRI 213
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQL 527
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-228 |
8.42e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.98 E-value: 8.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 23 VSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPAS--NLPPWERDVNTVFQDYALFPHMSILDNVAYG 100
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVAYLPQQLPAAEGMTVRELVAIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 101 -------LMVKGVNKKQRhamAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQM 173
Cdd:PRK10575 110 rypwhgaLGRFGAADREK---VEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 174 QLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLyMRPRT 228
Cdd:PRK10575 187 LALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL-MRGET 240
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-203 |
8.82e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.07 E-value: 8.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 19 AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPAS-----NL---PPWERDVNTVF----QDYA 86
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqalqkNLvayVPQSEEVDWSFpvlvEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 87 L---FPHMSILDnvayglmvkgVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:PRK15056 102 MmgrYGHMGWLR----------RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446142581 164 ALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSD 203
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD 210
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-195 |
9.22e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.99 E-value: 9.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 18 RAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGfeQLSGGAISIFGTPASNlpPWERDVntvfqdyalfphmSILDNV 97
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--ALKGTPVAGCVDVPDN--QFGREA-------------SLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 98 AyglmvKGVNKKQrhamAQEALEKVALGFVQ--QRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQL 175
Cdd:COG2401 107 G-----RKGDFKD----AVELLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180
....*....|....*....|
gi 446142581 176 ELKKLQQSLGITFIFVTHDQ 195
Cdd:COG2401 178 NLQKLARRAGITLVVATHHY 197
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-166 |
1.23e-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: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDvntvfqd 84
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRD------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 yALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEAlekvALGFV---QQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:TIGR03719 396 -ALDPNKTVWEEISGGLDIIKLGKREIPSRAYVG----RFNFKgsdQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
....*
gi 446142581 162 LGALD 166
Cdd:TIGR03719 471 TNDLD 475
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-208 |
2.17e-15 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 74.75 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 27 IKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPW-ERDVNTVFQDYAlfphMSILDNVAYGLMVKg 105
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYiKADYEGTVRDLL----SSITKDFYTHPYFK- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 106 vnkkqrhamaQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLG 185
Cdd:cd03237 97 ----------TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
170 180
....*....|....*....|...
gi 446142581 186 ITFIFVTHDQGEALSMSDRVAVF 208
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLIVF 189
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-215 |
2.73e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 76.67 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 19 AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASN--LPPWERDVNTVFQDYALFPHmSILDN 96
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqLDSWRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 97 VAYGlmvkgvnkkqRHAMAQEALEKVA-LGFVQQ---RKPS-----------QLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:PRK10789 409 IALG----------RPDATQQEIEHVArLASVHDdilRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 162 LGALDLKLREQMqleLKKLQQ-SLGITFIFVTHdQGEALSMSDRVAVFNNGRIEQ 215
Cdd:PRK10789 479 LSAVDGRTEHQI---LHNLRQwGEGRTVIISAH-RLSALTEASEILVMQHGHIAQ 529
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-205 |
4.21e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.14 E-value: 4.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 14 YGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIfgtpASNL--------PPweRDVN-TVFqD 84
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY----EQDLivarlqqdPP--RNVEgTVY-D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 Y----------ALFPHMSILDNVAYGLMVKGVNKKQRhamAQEALEK--------------VALGFVQQRKPSQLSGGQR 140
Cdd:PRK11147 86 FvaegieeqaeYLKRYHDISHLVETDPSEKNLNELAK---LQEQLDHhnlwqlenrinevlAQLGLDPDAALSSLSGGWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 141 QRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLgitfIFVTHDQGEALSMSDRV 205
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSI----IFISHDRSFIRNMATRI 223
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-226 |
4.98e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.09 E-value: 4.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 18 RAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGfeQLSGGA----------ISIFGTPASNLPPWE----RDVNTVFQ 83
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGGGaprgarvtgdVTLNGEPLAAIDAPRlarlRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 DYAlFPhMSILDNVAYG----LMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVN-------- 151
Cdd:PRK13547 93 QPA-FA-FSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaa 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446142581 152 -EPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLyMRP 226
Cdd:PRK13547 171 qPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV-LTP 245
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-210 |
1.01e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.45 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 24 SIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFgtpasNLPPWERDVNTVFQDYALFpHMSILDNVAYG--- 100
Cdd:PTZ00265 1249 NVGMKNVNEFSLTKEGGSGEDSTVFKNSGKILLDGVDICDY-----NLKDLRNLFSIVSQEPMLF-NMSIYENIKFGked 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 101 LMVKGVNKKQRHAMAQEALEKVALGFVQQRKP--SQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELK 178
Cdd:PTZ00265 1323 ATREDVKRACKFAAIDEFIESLPNKYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1402
|
170 180 190
....*....|....*....|....*....|..
gi 446142581 179 KLQQSLGITFIFVTHdQGEALSMSDRVAVFNN 210
Cdd:PTZ00265 1403 DIKDKADKTIITIAH-RIASIKRSDKIVVFNN 1433
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-222 |
1.09e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.16 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 3 YAVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP--ASNLPPWERdVNT 80
Cdd:NF033858 265 PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPvdAGDIATRRR-VGY 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFPHMSILDNVAygLMVK--GVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:NF033858 344 MSQAFSLYGELTVRQNLE--LHARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLIL 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 159 DEPLGALDLKLREQMQLELKKLQQSLGITfIFV-THDQGEALSmSDRVAVFNNGRIEQVDSPRDL 222
Cdd:NF033858 422 DEPTSGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-226 |
1.50e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 73.62 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTtclrliagfeqlSGGAISIFGTPASNLPPWeRDVNTVFQ 83
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**------------RGALPAHV*GPDAGRRPW-RF*TWCAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 DYALFPHMSILDNVAYG----------LMVKG----VNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARAL 149
Cdd:NF000106 80 RRALRRTIG*HRPVR*GrresfsgrenLYMIGr*ldLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 150 VNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEA------LSMSDRVAVFNNGRIEQVDSP---R 220
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAeqlaheLTVIDRGRVIADGKVDELKTKvggR 238
|
....*.
gi 446142581 221 DLYMRP 226
Cdd:NF000106 239 TLQIRP 244
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-211 |
2.70e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.50 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 17 VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPP---WERDVNTVFQDYALFPHMSI 93
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkssQEAGIGIIHQELNLIPQLTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 94 LDNVAYGLMVK----GVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGAL-Dlk 168
Cdd:PRK10762 97 AENIFLGREFVnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtD-- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446142581 169 lREQMQL-----ELKklQQSLGITFIfvTHDQGEALSMSDRVAVFNNG 211
Cdd:PRK10762 175 -TETESLfrvirELK--SQGRGIVYI--SHRLKEIFEICDDVTVFRDG 217
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
257-333 |
4.82e-14 |
|
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: 66.10 E-value: 4.82e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 257 ALRPEHIRLNTPGEmQANGTIQAVQYQGAATRFELTLSGGEKLLVSQANMTgeelPATLTPGQQVMVSWSRDVMVAL 333
Cdd:pfam08402 2 AIRPEKIRLAAAAN-GLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAH----ARPPAPGDRVGLGWDPEDAHVL 73
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
27-167 |
6.70e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.88 E-value: 6.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 27 IKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLppwERDVNTVFQDY--ALFPHMSILDNVAYGLMVK 104
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRFMAYLGHlpGLKADLSTLENLHFLCGLH 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446142581 105 GVNKKQrhaMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL 167
Cdd:PRK13543 111 GRRAKQ---MPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-217 |
8.87e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.74 E-value: 8.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLiagfeqLSG--------GAISIFGTPA--SNLPPWE 75
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKV------LSGvyphgsyeGEILFDGEVCrfKDIRDSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 76 RD-VNTVFQDYALFPHMSILDNVAYG--LMVKGV-NKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVN 151
Cdd:NF040905 77 ALgIVIIHQELALIPYLSIAENIFLGneRAKRGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446142581 152 EPRVLLLDEPLGALD----LKLREQMqLELKKlQqslGITFIFVTHDQGEALSMSDRVAVFNNGR-IEQVD 217
Cdd:NF040905 157 DVKLLILDEPTAALNeedsAALLDLL-LELKA-Q---GITSIIISHKLNEIRRVADSITVLRDGRtIETLD 222
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-166 |
3.00e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.15 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIfGtpasnlppwerdvNTVFQD 84
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G-------------ETVKLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 Y------ALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEAlekvALGFV---QQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK11819 391 YvdqsrdALDPNKTVWEEISGGLDIIKVGNREIPSRAYVG----RFNFKggdQQKKVGVLSGGERNRLHLAKTLKQGGNV 466
|
170
....*....|.
gi 446142581 156 LLLDEPLGALD 166
Cdd:PRK11819 467 LLLDEPTNDLD 477
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-193 |
1.07e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.59 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVRAV-NGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLP--PWERDVNT 80
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFPHmSILDNVAYGlmvkgvnKKQRHAMAQEALEKVALGFVQQRKP-----------SQLSGGQRQRVAIARAL 149
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTLG-------RDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446142581 150 VNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlgITFIFVTH 193
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAH 533
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-193 |
2.96e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.75 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYG---DVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISI---FGTPASNLPPWERDV 78
Cdd:PTZ00265 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndsHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 79 NTVFQDYALFPHmSILDNVAYGLM-VKGV----------------NKKQRHAMAQEALEKVAL--------GFVQQRK-- 131
Cdd:PTZ00265 463 GVVSQDPLLFSN-SIKNNIKYSLYsLKDLealsnyynedgndsqeNKNKRNSCRAKCAGDLNDmsnttdsnELIEMRKny 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 132 -----------------------------------PSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLE 176
Cdd:PTZ00265 542 qtikdsevvdvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250
....*....|....*..
gi 446142581 177 LKKLQQSLGITFIFVTH 193
Cdd:PTZ00265 622 INNLKGNENRITIIIAH 638
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-161 |
4.01e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.07 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNlppwERDVNTVFQ 83
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD----ARHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 84 DYA---------LFPHMSILDNVA-----YGLmvkgvNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARAL 149
Cdd:NF033858 77 RIAympqglgknLYPTLSVFENLDffgrlFGQ-----DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCAL 151
|
170
....*....|..
gi 446142581 150 VNEPRVLLLDEP 161
Cdd:NF033858 152 IHDPDLLILDEP 163
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-194 |
4.48e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.90 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 6 EFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIfGTpasnlppwERDVnTVFQDY 85
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GT--------KLEV-AYFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 86 --ALFPHMSILDNVAYGLMVKGVNKKQRHAmaqealekvaLGFVQQ--------RKPSQ-LSGGQRQRVAIARALVNEPR 154
Cdd:PRK11147 391 raELDPEKTVMDNLAEGKQEVMVNGRPRHV----------LGYLQDflfhpkraMTPVKaLSGGERNRLLLARLFLKPSN 460
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446142581 155 VLLLDEPLGALDLklrEQMQLeLKKLQQSLGITFIFVTHD 194
Cdd:PRK11147 461 LLILDEPTNDLDV---ETLEL-LEELLDSYQGTVLLVSHD 496
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-214 |
6.56e-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: 66.00 E-value: 6.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 17 VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAG-FEQLSGGAISIFGTPASNLPPW---ERDVNTVFQD---YALFP 89
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDIRNPAqaiRAGIAMVPEDrkrHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 90 HMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPS------QLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:TIGR02633 353 ILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpflpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446142581 164 ALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRIE 214
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-193 |
7.87e-12 |
|
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: 63.89 E-value: 7.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 16 DVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAG-FEQLSGGAISIFGTPASNLPPWERDVNTVFQDYA----LFPH 90
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAaqkpWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 91 MSILDNVAYGlmvkGVNKKQRHAMAQEALEKVA----LGFVQQRKPSQ----LSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:cd03290 93 ATVEENITFG----SPFNKQRYKAVTDACSLQPdidlLPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190
....*....|....*....|....*....|..
gi 446142581 163 GALDLKLREQ-MQLELKKLQQSLGITFIFVTH 193
Cdd:cd03290 169 SALDIHLSDHlMQEGILKFLQDDKRTLVLVTH 200
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-213 |
8.64e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.72 E-value: 8.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 17 VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAG-FEQLSGGAISIFGTPASNLPPWE---RDVNTVFQD---YALFP 89
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 90 HMSILDNVAygLMVkgVNKKQRHAMAQEALE-KVALGFVQQRK---PS------QLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK13549 355 VMGVGKNIT--LAA--LDRFTGGSRIDDAAElKTILESIQRLKvktASpelaiaRLSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 160 EPLGALDLKLReqmqLELKKLQQSL---GITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK13549 431 EPTRGIDVGAK----YEIYKLINQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
11-213 |
9.69e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 9.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 11 SRLYGDVR----AVNG------VSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPAS----------- 69
Cdd:PRK11288 250 PRPLGEVRlrldGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprdairag 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 70 -NLPPWERDvntvfQDyALFPHMSILDNVA---------YGLMVkgvNKKQRHAMAQEALEKVAlgfVQQRKPSQ----L 135
Cdd:PRK11288 330 iMLCPEDRK-----AE-GIIPVHSVADNINisarrhhlrAGCLI---NNRWEAENADRFIRSLN---IKTPSREQlimnL 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446142581 136 SGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK11288 398 SGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
11-213 |
1.29e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 63.71 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 11 SRLYGdvravngVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQlSGGAISIFGTPASNLPPWE--------------R 76
Cdd:COG4138 10 GRLGP-------ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElarhraylsqqqspP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 77 DVNTVFQDYALfpHMSildnvayglmVKGVNKKQRHAMAQEAlEKVALGFVQQRKPSQLSGGQRQRVAIARAL------V 150
Cdd:COG4138 82 FAMPVFQYLAL--HQP----------AGASSEAVEQLLAQLA-EALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 151 N-EPRVLLLDEPLGALDLklreQMQLELKKLQQSL---GITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG4138 149 NpEGQLLLLDEPMNSLDV----AQQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-219 |
1.59e-11 |
|
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: 62.81 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGD--VRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLP--PWERDVNT 80
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPleDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFPHmSILDNVayglmvkGVNKKQRHAMAQEALeKVALGfvqqrkPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:cd03369 87 IPQDPTLFSG-TIRSNL-------DPFDEYSDEEIYGAL-RVSEG------GLNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 161 PLGALDLKLREQMQLELKKLQQslGITFIFVTHDQGEALSMsDRVAVFNNGRIEQVDSP 219
Cdd:cd03369 152 ATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
14-203 |
1.89e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.27 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 14 YGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG-TPASNLPPWERDVNTVFQDYALFPHMS 92
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqSIKKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 93 ILDNVAYGLMVKGVNKKqrhamAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQ 172
Cdd:PRK13540 91 LRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180 190
....*....|....*....|....*....|.
gi 446142581 173 MQLELKKLQQSLGItfIFVTHDQGEALSMSD 203
Cdd:PRK13540 166 IITKIQEHRAKGGA--VLLTSHQDLPLNKAD 194
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-212 |
2.16e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.75 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 9 NVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP---ASNLPPWERDVNTVFQDY 85
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfKSSKEALENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 86 ALFPHMSILDNVAYGLM-VKG--VNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:PRK10982 83 NLVLQRSVMDNMWLGRYpTKGmfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446142581 163 GALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-194 |
2.20e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 63.15 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 28 KDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAisiFGTPasnlPPWERDVN----TVFQDY-----------ALFP-HM 91
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK---FDDP----PDWDEILDefrgSELQNYftkllegdvkvIVKPqYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 92 SILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLRE 171
Cdd:cd03236 97 DLIPKAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|...
gi 446142581 172 QMQLELKKLQQSlGITFIFVTHD 194
Cdd:cd03236 177 NAARLIRELAED-DNYVLVVEHD 198
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-204 |
4.58e-11 |
|
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: 60.08 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 30 GEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWERDVNTVFqdyalfphmsildnvayglmvkgvnkk 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 110 qrhamaqealekvalgfvqQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLE-----LKKLQQSL 184
Cdd:smart00382 55 -------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEK 115
|
170 180
....*....|....*....|
gi 446142581 185 GITFIFVTHDQGEALSMSDR 204
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLR 135
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
5-208 |
6.15e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 60.66 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRaVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISifgtpasnlppWERDvntvfqd 84
Cdd:cd03222 1 QLYPDCVKRYGVFF-LLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE-----------WDGI------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 85 yalfphmsildNVAYglmvkgvnkkqrhamaqealekvalgfvqqrKPS--QLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:cd03222 62 -----------TPVY-------------------------------KPQyiDLSGGELQRVAIAAALLRNATFYLFDEPS 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446142581 163 GALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVF 208
Cdd:cd03222 100 AYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-194 |
9.03e-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: 62.88 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 26 AIKDGEFFSMLGPSGSGKTTCLRLiagfeqLSGGAISIFGTPaSNLPPWErDVNTVFQDYALFPHMSILDN----VAY-- 99
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKI------LSGELKPNLGDY-DEEPSWD-EVLKRFRGTELQDYFKKLANgeikVAHkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 100 ------GLMVKGV-----NKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:COG1245 167 qyvdliPKVFKGTvrellEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246
|
170 180
....*....|....*....|....*....
gi 446142581 169 LReqmqLELKKLQQSL---GITFIFVTHD 194
Cdd:COG1245 247 QR----LNVARLIRELaeeGKYVLVVEHD 271
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
14-194 |
1.07e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 14 YGdvraVNGVSI----AIKDGEFFSMLGPSGSGKTTCLRLiagfeqLSGGAISIFGTPASNlPPWERDVN----TVFQDY 85
Cdd:PRK13409 83 YG----VNGFKLyglpIPKEGKVTGILGPNGIGKTTAVKI------LSGELIPNLGDYEEE-PSWDEVLKrfrgTELQNY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 86 alfphmsiLDNVAYGLM---------------VKG-----VNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQRQRVAI 145
Cdd:PRK13409 152 --------FKKLYNGEIkvvhkpqyvdlipkvFKGkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAI 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446142581 146 ARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQslGITFIFVTHD 194
Cdd:PRK13409 224 AAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHD 270
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-213 |
1.32e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 60.85 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 21 NGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFE--QLSGGAISIFGTPASNLPPWER---DVNTVFQDYALFPHMSILD 95
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGIFLAFQYPVEIPGVSVSN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 96 --NVAYG----------LMVKGVNKKQRH-AMAQEALEK-VALGFvqqrkpsqlSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:COG0396 97 flRTALNarrgeelsarEFLKLLKEKMKElGLDEDFLDRyVNEGF---------SGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 162 LGALDL-----------KLREQmqlelkklqqslGITFIFVTHdQGEALSM--SDRVAVFNNGRI 213
Cdd:COG0396 168 DSGLDIdalrivaegvnKLRSP------------DRGILIITH-YQRILDYikPDFVHVLVDGRI 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-250 |
1.41e-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: 62.66 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 15 GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLR-LIAGFEQLSG-----GAIS-----------------IFGTPASnl 71
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGhvhmkGSVAyvpqqawiqndslreniLFGKALN-- 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 72 PPWERdvnTVFQDYALFPHMSIL---DNVAYGlmVKGVNkkqrhamaqealekvalgfvqqrkpsqLSGGQRQRVAIARA 148
Cdd:TIGR00957 727 EKYYQ---QVLEACALLPDLEILpsgDRTEIG--EKGVN---------------------------LSGGQKQRVSLARA 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 149 LVNEPRVLLLDEPLGALDLKLREQMqleLKKLQQSLGI----TFIFVTHDQgEALSMSDRVAVFNNGRIEQVDSPRDLYM 224
Cdd:TIGR00957 775 VYSNADIYLFDDPLSAVDAHVGKHI---FEHVIGPEGVlknkTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELLQ 850
|
250 260
....*....|....*....|....*.
gi 446142581 225 RprtpfvagfvgtsnvfDGLMAEKLC 250
Cdd:TIGR00957 851 R----------------DGAFAEFLR 860
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-228 |
1.95e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 23 VSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFeqLSG-GAISIFGTPASNLPPWE---------RDVNT-----VFQDYAL 87
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL--LPGsGSIQFAGQPLEAWSAAElarhraylsQQQTPpfampVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 88 FphmsildnvayglmvkgvnkkqRHAMAQEALEKVALGFVQQ---------RKPSQLSGGQRQRVAIA-------RALVN 151
Cdd:PRK03695 93 H----------------------QPDKTRTEAVASALNEVAEalglddklgRSVNQLSGGEWQRVRLAavvlqvwPDINP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 152 EPRVLLLDEPLGALDLKLREQMQLELKKLQQsLGITFIFVTHDQGEALSMSDRVAVFNNGRIeQVDSPRDLYMRPRT 228
Cdd:PRK03695 151 AGQLLLLDEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKL-LASGRRDEVLTPEN 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-213 |
2.20e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 23 VSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWER-DVNTVF-----QDYALFPHMSILDN 96
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 97 VaYGLMVKGVNKKQRHAMAQEALEKV--ALG--FVQQRKPSQ-LSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLRE 171
Cdd:PRK15439 362 V-CALTHNRRGFWIKPARENAVLERYrrALNikFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446142581 172 QMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK15439 441 DIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-194 |
2.75e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.06 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISifGTPASNLPPWERDVNTVF- 82
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK--WSENANIGYYAQDHAYDFe 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 83 QDYALFPHMSILDNVAYG-LMVKGVnkkqrhamaqealekvaLG---FVQ---QRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK15064 397 NDLTLFDWMSQWRQEGDDeQAVRGT-----------------LGrllFSQddiKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190
....*....|....*....|....*....|....*....
gi 446142581 156 LLLDEPLGALDLKLREQMQLELKKLQQSLgitfIFVTHD 194
Cdd:PRK15064 460 LVMDEPTNHMDMESIESLNMALEKYEGTL----IFVSHD 494
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
5-193 |
4.01e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 60.92 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY--GDVrAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIfgtPASN----LPPWERDV 78
Cdd:TIGR00954 452 IKFENIPLVTpnGDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---PAKGklfyVPQRPYMT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 79 NTVFQDYALFPhMSILDnvaygLMVKGVNKKQRHAMaqeaLEKVALGFVQQRKPS---------QLSGGQRQRVAIARAL 149
Cdd:TIGR00954 528 LGTLRDQIIYP-DSSED-----MKRRGLSDKDLEQI----LDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLF 597
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446142581 150 VNEPRVLLLDEPLGALDLKLREQMQlelkKLQQSLGITFIFVTH 193
Cdd:TIGR00954 598 YHKPQFAILDECTSAVSVDVEGYMY----RLCREFGITLFSVSH 637
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-198 |
6.30e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAG-FEQLSGGAISIFGTP-ASNLPPWE--RDV-- 78
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQGYSNDLTLFGRRrGSGETIWDikKHIgy 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 79 --NTVFQDYALfpHMSILDNVAYGL-----MVKGVNKKQRHaMAQEALEKVALGFVQQRKPSQ-LSGGQRQRVAIARALV 150
Cdd:PRK10938 341 vsSSLHLDYRV--STSVRNVILSGFfdsigIYQAVSDRQQK-LAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALV 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446142581 151 NEPRVLLLDEPLGALDLKLReqmQLELKKLQQSLG---ITFIFVTHDQGEA 198
Cdd:PRK10938 418 KHPTLLILDEPLQGLDPLNR---QLVRRFVDVLISegeTQLLFVSHHAEDA 465
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-194 |
6.97e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.95 E-value: 6.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 3 YAVEFDNVSRLYGDVRAV-NGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQ-LSGGAISIFGTPASNLPpwerdvnt 80
Cdd:TIGR03719 3 YIYTMNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKdFNGEARPQPGIKVGYLP-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 vfQDYALFPHMSILDNVAYGLMVKgVNKKQRH-----AMAQEALEKVALGFVQQR------------------------- 130
Cdd:TIGR03719 75 --QEPQLDPTKTVRENVEEGVAEI-KDALDRFneisaKYAEPDADFDKLAAEQAElqeiidaadawdldsqleiamdalr 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446142581 131 ------KPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDlklREQMQ-LElKKLQQSLGiTFIFVTHD 194
Cdd:TIGR03719 152 cppwdaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAwLE-RHLQEYPG-TVVAVTHD 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
5-208 |
7.21e-10 |
|
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: 60.18 E-value: 7.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVR-AVNGVSIaiKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAIS---------------IFGTPA 68
Cdd:COG1245 342 VEYPDLTKSYGGFSlEVEGGEI--REGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkisykpqyispdYDGTVE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 69 SNLppweRDVNTVFQDYALFPHmsildnvayglmvkgvnkkqrhamaqEALEKVALGFVQQRKPSQLSGGQRQRVAIARA 148
Cdd:COG1245 420 EFL----RSANTDDFGSSYYKT--------------------------EIIKPLGLEKLLDKNVKDLSGGELQRVAIAAC 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446142581 149 LVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDqgeaLSM----SDRVAVF 208
Cdd:COG1245 470 LSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLidyiSDRLMVF 529
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
40-222 |
1.03e-09 |
|
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: 59.43 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 40 GSGKTTCLRLIAGFEQLSGGAISIFGTP--ASNLpPWERD-VNTVFQDYALFPHmsildnvaygLMvkGVNKKQRHAMAQ 116
Cdd:COG4615 368 GSGKSTLAKLLTGLYRPESGEILLDGQPvtADNR-EAYRQlFSAVFSDFHLFDR----------LL--GLDGEADPARAR 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 117 EALEKVALgfvqQRKPS---------QLSGGQRQRVAIARALVnEPR-VLLLDE------PLgaldlkLR----EQMQLE 176
Cdd:COG4615 435 ELLERLEL----DHKVSvedgrfsttDLSQGQRKRLALLVALL-EDRpILVFDEwaadqdPE------FRrvfyTELLPE 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446142581 177 LKKlqqsLGITFIFVTHDQ---GEAlsmsDRVAVFNNGRIEQVDSPRDL 222
Cdd:COG4615 504 LKA----RGKTVIAISHDDryfDLA----DRVLKMDYGKLVELTGPAAL 544
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-230 |
2.01e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.22 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVSRLY--GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASN--LPPWERDVN 79
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQDYALFPhmsildnvayGLMVKGVNKKQRHAMAQ--EALEKVALGFVQQRKPSQL-----------SGGQRQRVAIA 146
Cdd:PLN03232 1314 IIPQSPVLFS----------GTVRFNIDPFSEHNDADlwEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLA 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 147 RALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlgITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:PLN03232 1384 RALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
....
gi 446142581 227 RTPF 230
Cdd:PLN03232 1461 TSAF 1464
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-211 |
5.15e-09 |
|
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: 56.40 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 23 VSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTpasnlppwerdVNTVFQDYALFPHmSILDNVAYGLM 102
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENIIFGVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 103 VKGVNKKQRHAMAQeaLEKVALGFVQQRKPS------QLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQM-QL 175
Cdd:cd03291 124 YDEYRYKSVVKACQ--LEEDITKFPEKDNTVlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfES 201
|
170 180 190
....*....|....*....|....*....|....*.
gi 446142581 176 ELKKLQQSLgiTFIFVThDQGEALSMSDRVAVFNNG 211
Cdd:cd03291 202 CVCKLMANK--TRILVT-SKMEHLKKADKILILHEG 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-236 |
7.30e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 23 VSIAIKDGEFFSMLGPSGSGKTTCLR-LIAGFEQLSG---GAISIFGTPASnlpPWerDVNTVFQDYALFphmsiLDNVA 98
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFEISEGrvwAERSIAYVPQQ---AW--IMNATVRGNILF-----FDEED 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 99 YGLMVKGVNKKQRHA-MAQEA--LEkVALGfvqqRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQL 175
Cdd:PTZ00243 749 AARLADAVRVSQLEAdLAQLGggLE-TEIG----EKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVE 823
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446142581 176 ELkKLQQSLGITFIFVTHdQGEALSMSDRVAVFNNGRIEQVDSPRDlYMrpRTPFVAGFVG 236
Cdd:PTZ00243 824 EC-FLGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSAD-FM--RTSLYATLAA 879
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-213 |
8.19e-09 |
|
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: 54.96 E-value: 8.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 20 VNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGfeqLSGGAISIFG-------TPASNLPPWERDVNTVFQDYALFPHMS 92
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGdihyngiPYKEFAEKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 93 ILDNVAYGLMVKGvnkkqrHAMAqealekvalgfvqqRKpsqLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQ 172
Cdd:cd03233 100 VRETLDFALRCKG------NEFV--------------RG---ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446142581 173 MQLELKKLQQSLGITfIFVTHDQ--GEALSMSDRVAVFNNGRI 213
Cdd:cd03233 157 ILKCIRTMADVLKTT-TFVSLYQasDEIYDLFDKVLVLYEGRQ 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
128-213 |
8.32e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 128 QQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLR-EQMQLELKKLQQSLGItfIFVTHDQGEALSMSDRVA 206
Cdd:PRK10982 385 HRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGI--IIISSEMPELLGITDRIL 462
|
....*..
gi 446142581 207 VFNNGRI 213
Cdd:PRK10982 463 VMSNGLV 469
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
5-208 |
9.25e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 9.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLYGDVR-AVNGVSIaiKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISifgtpaSNL-----PPW-ERD 77
Cdd:PRK13409 341 VEYPDLTKKLGDFSlEVEGGEI--YEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------PELkisykPQYiKPD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 78 VNTVFQDYaLFPHMSILDNVAYglmvkgvnkkqrhamAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:PRK13409 413 YDGTVEDL-LRSITDDLGSSYY---------------KSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 158 LDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDqgeaLSM----SDRVAVF 208
Cdd:PRK13409 477 LDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD----IYMidyiSDRLMVF 527
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-211 |
1.08e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.84 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 7 FDNVSRLYGDVraVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPA-SNLPPWerdvntvfqdy 85
Cdd:TIGR01271 431 FSNFSLYVTPV--LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISfSPQTSW----------- 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 86 aLFPHmSILDNVAYGL---------MVKGVNKKQRHAMAQEAlEKVALGfvqqRKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:TIGR01271 498 -IMPG-TIKDNIIFGLsydeyrytsVIKACQLEEDIALFPEK-DKTVLG----EGGITLSGGQRARISLARAVYKDADLY 570
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 157 LLDEPLGALDLkLREQMQLE--LKKLQQSLgiTFIFVThDQGEALSMSDRVAVFNNG 211
Cdd:TIGR01271 571 LLDSPFTHLDV-VTEKEIFEscLCKLMSNK--TRILVT-SKLEHLKKADKILLLHEG 623
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-215 |
1.26e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.21 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 19 AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGtpasnlppwerDVNTVFQDYALFPHMSILDNVA 98
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------EVSVIAISAGLSGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 99 YGLMVKGVNKKQRHAMAQEALEKVALG-FVQQrKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLreqMQLEL 177
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKIIEFSELGeFIYQ-PVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF---AQKCL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446142581 178 KKLQQ--SLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQ 215
Cdd:PRK13546 184 DKIYEfkEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
15-213 |
1.60e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 15 GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFE--QLSGGAISIFGTPASNLPPWERdvntvfqdyalfPHMS 92
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEER------------AHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 93 ILDNVAYGLMVKGV----------NKKQRHamaQEALEKVALGFVQ---------QRKPSQL--------SGGQRQRVAI 145
Cdd:CHL00131 86 IFLAFQYPIEIPGVsnadflrlayNSKRKF---QGLPELDPLEFLEiineklklvGMDPSFLsrnvnegfSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 146 ARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQgEALS--MSDRVAVFNNGRI 213
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQ-RLLDyiKPDYVHVMQNGKI 230
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-213 |
2.32e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 34 SMLGPSGSGKTTCLRLIAGFEQLSGGaiSIFGTPASNLppwerdvnTVFQDYalfpHMSILDNVAYGL--MVK---GV-N 107
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSG--TVFRSAKVRM--------AVFSQH----HVDGLDLSSNPLlyMMRcfpGVpE 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 108 KKQRHAMAQEALEkvalGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLgit 187
Cdd:PLN03073 605 QKLRAHLGSFGVT----GNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGV--- 677
|
170 180
....*....|....*....|....*.
gi 446142581 188 fIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PLN03073 678 -LMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1-166 |
2.84e-08 |
|
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: 53.02 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRlygdvRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLS--GGAISIFGTPasNLPPWERDV 78
Cdd:cd03232 9 LNYTVPVKGGKR-----QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRP--LDKNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 79 NTVFQDYALFPHMSIldnvayglmvkgvnkkqrhamaQEALEKVAL--GfvqqrkpsqLSGGQRQRVAIARALVNEPRVL 156
Cdd:cd03232 82 GYVEQQDVHSPNLTV----------------------REALRFSALlrG---------LSVEQRKRLTIGVELAAKPSIL 130
|
170
....*....|
gi 446142581 157 LLDEPLGALD 166
Cdd:cd03232 131 FLDEPTSGLD 140
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
127-193 |
3.55e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 3.55e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 127 VQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQslgiTFIFVTH 193
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSH 399
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-210 |
6.54e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 12 RLYgDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAG-FEQLSGGAISIFGTPAsNLP----------PWERDvNT 80
Cdd:PRK10938 12 RLS-DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGeLPLLSGERQSQFSHIT-RLSfeqlqklvsdEWQRN-NT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VF-----QDYALFPHMSILDnvayglmvkGVNKKQRhamAQEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK10938 89 DMlspgeDDTGRTTAEIIQD---------EVKDPAR---CEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 156 LLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQGEALSMSDRVAVFNN 210
Cdd:PRK10938 157 LILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1-193 |
8.07e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.74 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 1 MTYAVEFDNVSRLY-------------------GDVR-AVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGA 60
Cdd:PRK13545 1 MNYKVKFEHVTKKYkmynkpfdklkdlffrskdGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 61 ISIFGTPAsnlppwerdvnTVFQDYALFPHMSILDNVAY-GLMVkGVNKKQRHAMAQEALEKVALGFVQQRKPSQLSGGQ 139
Cdd:PRK13545 81 VDIKGSAA-----------LIAISSGLNGQLTGIENIELkGLMM-GLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGM 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446142581 140 RQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTH 193
Cdd:PRK13545 149 KSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISH 201
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-166 |
9.93e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 27 IKDGEFFSMLGPSGSGKTTCLRLIA----GFEQLSGGAISIFG-TPASNLPPWERDVNTVFQDYALFPHMSI---LDNVA 98
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGiTPEEIKKHYRGDVVYNAETDVHFPHLTVgetLDFAA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 99 Y----GLMVKGVNKKQR------HAMAQEALE-----KVALGFVQQrkpsqLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:TIGR00956 164 RcktpQNRPDGVSREEYakhiadVYMATYGLShtrntKVGNDFVRG-----VSGGERKRVSIAEASLGGAKIQCWDNATR 238
|
...
gi 446142581 164 ALD 166
Cdd:TIGR00956 239 GLD 241
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-194 |
1.12e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 35 MLGPSGSGKTTCLRLIAGFEQLSGG-AISIFGTPASNLPpwerdvntvfQDYALFPHMSILDNVAYGLMVKgVNKKQRH- 112
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGeARPAPGIKVGYLP----------QEPQLDPEKTVRENVEEGVAEV-KAALDRFn 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 113 ----AMAQEALEKVAL----GFVQQ---------------------RKP------SQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:PRK11819 107 eiyaAYAEPDADFDALaaeqGELQEiidaadawdldsqleiamdalRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLL 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 446142581 158 LDEPLGALDlklREQMQ-LElKKLQQSLGiTFIFVTHD 194
Cdd:PRK11819 187 LDEPTNHLD---AESVAwLE-QFLHDYPG-TVVAVTHD 219
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
8-205 |
1.14e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.17 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 8 DNVSRLYgdVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLrliagfeqLSGGAISIFGTPASNLPPWERDvNTVFQDyal 87
Cdd:cd03238 1 LTVSGAN--VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV--------NEGLYASGKARLISFLPKFSRN-KLIFID--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 88 fphmsildnvayglmvkgvnkkQRHAMAQEALEKVALGfvqqRKPSQLSGGQRQRVAIARALVNEPR--VLLLDEPLGAL 165
Cdd:cd03238 67 ----------------------QLQFLIDVGLGYLTLG----QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446142581 166 DLKLREQMQLELKKLQQsLGITFIFVTHDQgEALSMSDRV 205
Cdd:cd03238 121 HQQDINQLLEVIKGLID-LGNTVILIEHNL-DVLSSADWI 158
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
135-222 |
1.69e-07 |
|
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: 53.03 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 135 LSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKklQQSLGITFIFVTHDQGEALSMSdRVAVFNNGRIE 214
Cdd:TIGR00957 1422 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVA 1498
|
....*...
gi 446142581 215 QVDSPRDL 222
Cdd:TIGR00957 1499 EFGAPSNL 1506
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
5-230 |
3.99e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.70 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 5 VEFDNVSRLY--GDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTP--ASNLPPWERDVNT 80
Cdd:PTZ00243 1309 LVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREigAYGLRELRRQFSM 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 81 VFQDYALFPHmSILDNVAYGL---------MVKGVNKKQRHAMAQEALEKVALgfvqqRKPSQLSGGQRQRVAIARALVN 151
Cdd:PTZ00243 1389 IPQDPVLFDG-TVRQNVDPFLeassaevwaALELVGLRERVASESEGIDSRVL-----EGGSNYSVGQRQLMCMARALLK 1462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 152 EPR-VLLLDEPLGALDLKLREQMQLELkkLQQSLGITFIFVTHdQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPF 230
Cdd:PTZ00243 1463 KGSgFILMDEATANIDPALDRQIQATV--MSAFSAYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
23-222 |
4.11e-07 |
|
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: 50.62 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 23 VSIAIKDGEFFSMLGPSGSGKTTclrLIAGFEQL--SGGAISIFGTPASNLP--PWERDVNTVFQDYALFPhmsildnva 98
Cdd:cd03289 23 ISFSISPGQRVGLLGRTGSGKST---LLSAFLRLlnTEGDIQIDGVSWNSVPlqKWRKAFGVIPQKVFIFS--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 99 yGLMVKGVNKKQRHAMAQ--EALEKVALGFVQQRKPSQL-----------SGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:cd03289 91 -GTFRKNLDPYGKWSDEEiwKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 166 DlklREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:cd03289 170 D---PITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKL 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-215 |
4.66e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 23 VSIAIKDGEFFSMLGPSGSGKTTCLRLIAG-FEQLSGGAISIFGTPAsnlppWERDVNTVFqdyalfpHMSILDNVAYGL 101
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTVA-----YVPQVSWIF-------NATVRDNILFGS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 102 MVKGV--NKKQRHAMAQEALEKVALGFVQQ--RKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQ----- 172
Cdd:PLN03130 704 PFDPEryERAIDVTALQHDLDLLPGGDLTEigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQvfdkc 783
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446142581 173 MQLELKklqqslGITFIFVThDQGEALSMSDRVAVFNNGRIEQ 215
Cdd:PLN03130 784 IKDELR------GKTRVLVT-NQLHFLSQVDRIILVHEGMIKE 819
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
20-213 |
1.14e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.02 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 20 VNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFE--QLSGGAISIFGTPASNLPPWERDVNTVFQdyaLFPHMSILDNV 97
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFM---AFQYPVEIPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 98 AYGLMVKGVNKKQRHAMAQEALEKVALGFVQQRKPSQL---------------SGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:PRK09580 94 SNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446142581 163 GALD---LKLREQMQLELKKLQQSlgitFIFVTHDQgEALSM--SDRVAVFNNGRI 213
Cdd:PRK09580 174 SGLDidaLKIVADGVNSLRDGKRS----FIIVTHYQ-RILDYikPDYVHVLYQGRI 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
23-237 |
2.97e-06 |
|
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: 47.98 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 23 VSIAIKDGEFFSMLGPSGSGKTTC----LRLIAGFEqlsgGAISIFGTPASNLP--PWERDVNTVFQDYALFPHmSILDN 96
Cdd:cd03288 40 VKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPlhTLRSRLSIILQDPILFSG-SIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 97 VayglmvkGVNKKQRHAMAQEALEKVALGFVQQRKPSQL-----------SGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:cd03288 115 L-------DPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446142581 166 DLKLREQMQlelKKLQQSLG-ITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDSPRDLYMRPRTPFvAGFVGT 237
Cdd:cd03288 188 DMATENILQ---KVVMTAFAdRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVF-ASLVRT 255
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-222 |
3.32e-06 |
|
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: 48.75 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 18 RAV-NGVSIAIKDGEFFSMLGPSGSGKTTclrLIAGFEQL--SGGAISIFGTP--ASNLPPWERDVNTVFQDYALFPhms 92
Cdd:TIGR01271 1232 RAVlQDLSFSVEGGQRVGLLGRTGSGKST---LLSALLRLlsTEGEIQIDGVSwnSVTLQTWRKAFGVIPQKVFIFS--- 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 93 ildnvayGLMVKGVNKKQRHAmaQEALEKVA---------------LGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:TIGR01271 1306 -------GTFRKNLDPYEQWS--DEEIWKVAeevglksvieqfpdkLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446142581 158 LDEPLGALDlklREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDL 222
Cdd:TIGR01271 1377 LDEPSAHLD---PVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKL 1438
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-239 |
4.43e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 4 AVEFDNVS-RLYGDVRAV-NGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLPPWE--RDVN 79
Cdd:PLN03130 1237 SIKFEDVVlRYRPELPPVlHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLG 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 80 TVFQDYALFPhmsildnvayGLMVKGVNKKQRHAMAQ--EALEKVALGFVQQRKPSQL-----------SGGQRQRVAIA 146
Cdd:PLN03130 1317 IIPQAPVLFS----------GTVRFNLDPFNEHNDADlwESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLA 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 147 RALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSlgITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDSPRDLYMRP 226
Cdd:PLN03130 1387 RALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKS--CTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNE 1463
|
250
....*....|....*.
gi 446142581 227 RTPFvAGFV---GTSN 239
Cdd:PLN03130 1464 GSAF-SKMVqstGAAN 1478
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
135-215 |
5.10e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 135 LSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQ-----MQLELKklqqslGITFIFVThDQGEALSMSDRVAVFN 209
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQvfdscMKDELK------GKTRVLVT-NQLHFLPLMDRIILVS 813
|
....*.
gi 446142581 210 NGRIEQ 215
Cdd:PLN03232 814 EGMIKE 819
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
8-225 |
1.24e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 8 DNVSRLYGDVRAVNGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISI-----FGTPASNLPPWERDVNTVF 82
Cdd:PRK10636 316 EKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLakgikLGYFAQHQLEFLRADESPL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 83 QdyalfpHMSildnvayGLMVKGVNKKQRHAMAqealekvALGFvQQRKPS----QLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:PRK10636 396 Q------HLA-------RLAPQELEQKLRDYLG-------GFGF-QGDKVTeetrRFSGGEKARLVLALIVWQRPNLLLL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446142581 159 DEPLGALDLKLREQMQLELKKLQQSLgitfIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMR 225
Cdd:PRK10636 455 DEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQ 517
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
22-166 |
1.62e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.76 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 22 GVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGfEQLSG---GAISIFGTPaSNLPPWERDVNTVFQDYALFPHMSILDNVA 98
Cdd:PLN03140 898 EVTGAFRPGVLTALMGVSGAGKTTLMDVLAG-RKTGGyieGDIRISGFP-KKQETFARISGYCEQNDIHSPQVTVRESLI 975
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446142581 99 YGLMV---KGVNKKQRHAMAQEALEKVAL-----GFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:PLN03140 976 YSAFLrlpKEVSKEEKMMFVDEVMELVELdnlkdAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-194 |
2.06e-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: 44.91 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 31 EFFSML----GPSGSGKTT---CLRLiagfeqlsggaiSIFGT--PASNLPPWERDVNT----------VFQ-----DYA 86
Cdd:cd03240 19 EFFSPLtlivGQNGAGKTTiieALKY------------ALTGElpPNSKGGAHDPKLIRegevraqvklAFEnangkKYT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 87 LFPHMSILDNVAYglmvkgvnkkqrhaMAQEALEKVALgfvqqRKPSQLSGGQRQ------RVAIARALVNEPRVLLLDE 160
Cdd:cd03240 87 ITRSLAILENVIF--------------CHQGESNWPLL-----DMRGRCSGGEKVlasliiRLALAETFGSNCGILALDE 147
|
170 180 190
....*....|....*....|....*....|....*
gi 446142581 161 PLGALDLKLREQMQLELKKLQQSLGI-TFIFVTHD 194
Cdd:cd03240 148 PTTNLDEENIEESLAEIIEERKSQKNfQLIVITHD 182
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
92-195 |
2.73e-05 |
|
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: 43.89 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 92 SILDNVAYGL---MVKGVNKKQRHAMAQEALekVALGFVQQRKpsQLSGGQRQRVAIARALVNE---PRVL-LLDEPLGA 164
Cdd:cd03227 36 TILDAIGLALggaQSATRRRSGVKAGCIVAA--VSAELIFTRL--QLSGGEKELSALALILALAslkPRPLyILDEIDRG 111
|
90 100 110
....*....|....*....|....*....|...
gi 446142581 165 LDlkLREQMQLE--LKKLQQSlGITFIFVTHDQ 195
Cdd:cd03227 112 LD--PRDGQALAeaILEHLVK-GAQVIVITHLP 141
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-195 |
3.32e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 24 SIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFG----------TPASNLPPWERDVNTVFQDYALFPHMSI 93
Cdd:PRK10636 21 TATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqeTPALPQPALEYVIDGDREYRQLEAQLHD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 94 LDNVAYGLMVKGVNKKQRHAMAQEALEKVA-----LGFVQ---QRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:PRK10636 101 ANERNDGHAIATIHGKLDAIDAWTIRSRAAsllhgLGFSNeqlERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHL 180
|
170 180 190
....*....|....*....|....*....|
gi 446142581 166 DLklreQMQLELKKLQQSLGITFIFVTHDQ 195
Cdd:PRK10636 181 DL----DAVIWLEKWLKSYQGTLILISHDR 206
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
26-57 |
1.56e-04 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 43.15 E-value: 1.56e-04
10 20 30
....*....|....*....|....*....|....*....
gi 446142581 26 AIKDGEFFSML--GPSGSGKTTCLRLIAG-----FEQLS 57
Cdd:PRK13342 30 MIEAGRLSSMIlwGPPGTGKTTLARIIAGatdapFEALS 68
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
135-213 |
1.97e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 135 LSGGQRQRVAIARALVNEPRVLLLDEP-----LGAldlklreqmQLELKKLQQSL---GITFIFVTHDQGEALSMSDRVA 206
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPtrgidVGA---------KYEIYTIINELaaeGKGVIVISSELPELLGMCDRIY 475
|
....*..
gi 446142581 207 VFNNGRI 213
Cdd:NF040905 476 VMNEGRI 482
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
120-205 |
2.82e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 120 EKVALGFV---QQRKPSQLSGGQRQ------RVAIARALVNEPRVLLLDEPLGALD----LKLREQMQLELKKLQQslgi 186
Cdd:PRK03918 771 NKVKLFVVyqgKERPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDeerrRKLVDIMERYLRKIPQ---- 846
|
90
....*....|....*....
gi 446142581 187 tFIFVTHDQgEALSMSDRV 205
Cdd:PRK03918 847 -VIIVSHDE-ELKDAADYV 863
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
76-205 |
1.16e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 76 RDVNTVF---QDYALFPHMSILDNVAY--GLMVKGVNKKqrhaMAQEALEKVA--LGFVQ---------QRKPSQLSGGQ 139
Cdd:TIGR00630 418 PEALAVTvggKSIADVSELSIREAHEFfnQLTLTPEEKK----IAEEVLKEIRerLGFLIdvgldylslSRAAGTLSGGE 493
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446142581 140 RQRVAIAR----ALVNeprVL-LLDEPlgALDLKLREQMQL--ELKKLqQSLGITFIFVTHDQgEALSMSDRV 205
Cdd:TIGR00630 494 AQRIRLATqigsGLTG---VLyVLDEP--SIGLHQRDNRRLinTLKRL-RDLGNTLIVVEHDE-DTIRAADYV 559
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-160 |
1.29e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 37 GPSGSGKTTCLRLIAGFEQLSGGAISIFGTPASNLP-PWerdVNTVFQDYALFPHMSILDNVAYGLMVkgvnkKQRHAMA 115
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkPY---CTYIGHNLGLKLEMTVFENLKFWSEI-----YNSAETL 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446142581 116 QEALEKVALGFVQQRKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:PRK13541 105 YAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
23-194 |
1.50e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 23 VSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISifgtpasnLPPWERdVNTVFQDYALFPHMSILDNVAYGLM 102
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVS--------LDPNER-LGKLRQDQFAFEEFTVLDTVIMGHT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446142581 103 VKGVNKKQRHAM--------------------------------AQEALEKVALGFVQQRKP-SQLSGGQRQRVAIARAL 149
Cdd:PRK15064 91 ELWEVKQERDRIyalpemseedgmkvadlevkfaemdgytaearAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446142581 150 VNEPRVLLLDEPLGALDLKLREQMQLELKKLQQslgiTFIFVTHD 194
Cdd:PRK15064 171 FSNPDILLLDEPTNNLDINTIRWLEDVLNERNS----TMIIISHD 211
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
129-205 |
5.43e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.66 E-value: 5.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446142581 129 QRKPSQLSGGQRQRVAIARALVNEPR--VLLLDEPLGALDLKLREQMQLELKKLQQSlGITFIFVTHDQgEALSMSDRV 205
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDE-QMISLADRI 547
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
37-63 |
7.29e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 36.31 E-value: 7.29e-03
10 20 30
....*....|....*....|....*....|
gi 446142581 37 GPSGSGKTTCLRLIA---GFEQLSGGAISI 63
Cdd:cd02020 6 GPAGSGKSTVAKLLAkklGLPYLDTGGIRT 35
|
|
|