|
Name |
Accession |
Description |
Interval |
E-value |
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-382 |
0e+00 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 782.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 8 VKKLNTQPRSLSPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITD 87
Cdd:PRK09452 1 SKKLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 88 VPAEHRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 167
Cdd:PRK09452 81 VPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 168 NKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLF 247
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 248 VASFIGEINIFDATVIERIDAQRVRANVEGRECVLYVAFPVTAGQKLNVLLRPEDLRVEEINGDGEADGLIGFVRERNYK 327
Cdd:PRK09452 241 VARFIGEINIFDATVIERLDEQRVRANVEGRECNIYVNFAVEPGQKLHVLLRPEDLRVEEINDDEHAEGLIGYVRERNYK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 495142058 328 GMTLESVVELENGKIVLVSEFFNEDDPDFDHSLDQKMAVTWVESWEVVLADEELA 382
Cdd:PRK09452 321 GMTLDSVVELENGKMVMVSEFFNEDDPDFDHSLGQKVAVTWVEGWEVVLADEEHK 375
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
52-376 |
0e+00 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 538.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 52 LLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPR 131
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 132 VMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHD 211
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 212 QEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGEINIFDATVIERIDAQRVRANVEGRECVLYVAFPVTAG 291
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAGVEGRRCDIYTDVPVEKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 292 QKLNVLLRPEDLRVEEINGDGEADGLIGFVRERNYKGMTLESVVELENGKIVLVSEFFNEDDPDFDHSLDQKMAVTWVES 371
Cdd:TIGR01187 241 QPLHVVLRPEKIVIEEEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQKVLVSEFFNEDDPHMSPSIGDRVGLTWHPG 320
|
....*
gi 495142058 372 WEVVL 376
Cdd:TIGR01187 321 SEVVL 325
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
19-378 |
0e+00 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 531.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNTV 98
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 99 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 179 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGEINIF 258
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 259 DATVIERiDAQRVRanVEGRECVLYVAFPVTAGQKLNVLLRPEDLRVEEingDGEADGLIGFVRERNYKGMTLESVVELE 338
Cdd:COG3842 243 PGTVLGD-EGGGVR--TGGRTLEVPADAGLAAGGPVTVAIRPEDIRLSP---EGPENGLPGTVEDVVFLGSHVRYRVRLG 316
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 495142058 339 NGKIVLVSEFFNEDDPdfdHSLDQKMAVTWVESWEVVLAD 378
Cdd:COG3842 317 DGQELVVRVPNRAALP---LEPGDRVGLSWDPEDVVVLPA 353
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
22-368 |
1.93e-151 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 431.42 E-value: 1.93e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNTVFQS 101
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 102 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 181
Cdd:COG3839 84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 182 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGE--INIFD 259
Cdd:COG3839 164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppMNLLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 260 ATVIERidaqrvRANVEGRECVLYVAFPVTAGQKLNVLLRPEDLRVeeinGDGEADGLIGFVRERNYKGMtlESVVELEN 339
Cdd:COG3839 244 GTVEGG------GVRLGGVRLPLPAALAAAAGGEVTLGIRPEHLRL----ADEGDGGLEATVEVVEPLGS--ETLVHVRL 311
|
330 340
....*....|....*....|....*....
gi 495142058 340 GKIVLVSEFfnedDPDFDHSLDQKMAVTW 368
Cdd:COG3839 312 GGQELVARV----PGDTRLRPGDTVRLAF 336
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
22-253 |
1.30e-146 |
|
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: 414.33 E-value: 1.30e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNTVFQS 101
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 102 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 181
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 182 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIG 253
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
22-307 |
1.56e-133 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 385.65 E-value: 1.56e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDI-TDVPAEHRHVNTVFQ 100
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 101 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 180
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 181 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGEINIFDA 260
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 495142058 261 tvieRIDAQRVRANvegrECVLYVAFPVTAGQKLnVLLRPEDLRVEE 307
Cdd:COG1118 243 ----RVIGGQLEAD----GLTLPVAEPLPDGPAV-AGVRPHDIEVSR 280
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
18-345 |
3.12e-125 |
|
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: 364.74 E-value: 3.12e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 18 LSPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNT 97
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 98 VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 178 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGEINI 257
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 258 FDAtviERIDAQRVRANVEGRECVLYVAFPVTAGqklNVLLRPEDLRVEEinGDGEADGLIGFVRERNYKGMTLESVVEL 337
Cdd:TIGR03265 241 LPG---TRGGGSRARVGGLTLACAPGLAQPGASV---RLAVRPEDIRVSP--AGNAANLLLARVEDMEFLGAFYRLRLRL 312
|
330
....*....|
gi 495142058 338 EN--GKIVLV 345
Cdd:TIGR03265 313 EGlpGQALVA 322
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
22-234 |
2.38e-118 |
|
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: 341.81 E-value: 2.38e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNTVFQS 101
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 102 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 181
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495142058 182 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 234
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
15-343 |
3.02e-110 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 327.56 E-value: 3.02e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 15 PRSLSPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRH 94
Cdd:PRK11607 13 RKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 95 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 174
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 175 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGE 254
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 255 INIFDATVIERIDAQRVrANVEGRECVLYV--AFPVTAGQKLNVLLRPEDLRV-EEINGDGeADGLIGFVRERNYKGMTL 331
Cdd:PRK11607 253 VNVFEGVLKERQEDGLV-IDSPGLVHPLKVdaDASVVDNVPVHVALRPEKIMLcEEPPADG-CNFAVGEVIHIAYLGDLS 330
|
330
....*....|..
gi 495142058 332 ESVVELENGKIV 343
Cdd:PRK11607 331 IYHVRLKSGQMI 342
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
22-234 |
8.32e-110 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 320.36 E-value: 8.32e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNTVFQS 101
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 102 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 181
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495142058 182 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 234
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
22-304 |
1.06e-108 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 322.95 E-value: 1.06e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKT-VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDV-PAEhRHVNTVF 99
Cdd:PRK11650 4 LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELePAD-RDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 100 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 179
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 180 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGE--INI 257
Cdd:PRK11650 163 SNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpaMNL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 495142058 258 FDATVIERIDAQRVRANVEGRecvLYVAFPVTAGQKLNVLLRPEDLR 304
Cdd:PRK11650 243 LDGRVSADGAAFELAGGIALP---LGGGYRQYAGRKLTLGIRPEHIA 286
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-254 |
1.50e-108 |
|
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: 318.13 E-value: 1.50e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNTVFQS 101
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 102 YALFPHMTVFENVAFGLRMQK----TPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKPrserPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 178 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGE 254
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
22-261 |
1.03e-107 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 320.13 E-value: 1.03e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNTVFQS 101
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 102 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 181
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 182 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGEINIFDAT 261
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPAT 246
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
20-233 |
1.72e-101 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 300.85 E-value: 1.72e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSF----DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVpaeHRHV 95
Cdd:COG1116 6 PALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP---GPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 96 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 175
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 176 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRIEQD 233
Cdd:COG1116 163 DEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEE 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
22-262 |
5.52e-101 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 303.16 E-value: 5.52e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNTVFQS 101
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 102 YALFPHMTVFENVAFGLRM----QKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 178 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGEINI 257
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNR 242
|
....*
gi 495142058 258 FDATV 262
Cdd:PRK10851 243 LQGTI 247
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
22-230 |
3.80e-97 |
|
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: 288.22 E-value: 3.80e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGK----TVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVpaeHRHVNT 97
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP---GPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 98 VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495142058 178 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRI 230
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRI 212
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
24-303 |
9.36e-94 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 285.00 E-value: 9.36e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 24 LADIGKSFdGKTVIS-DFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNTVFQSY 102
Cdd:PRK11000 6 LRNVTKAY-GDVVISkDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 103 ALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 182
Cdd:PRK11000 85 ALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 183 DYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIG--EINIFDA 260
Cdd:PRK11000 165 DAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGspKMNFLPV 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 495142058 261 TV---------IERIDAQRVRANVEGREcvlyvafpVTAGQKLNVLLRPEDL 303
Cdd:PRK11000 245 KVtataieqvqVELPNRQQVWLPVEGRG--------VQVGANMSLGIRPEHL 288
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
36-257 |
1.36e-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: 267.28 E-value: 1.36e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 36 VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNTVFQSYALFPHMTVFENVA 115
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 116 FGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELK 195
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 196 ALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGEINI 257
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
22-256 |
1.59e-86 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 267.35 E-value: 1.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFD------GKTV-ISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH-- 92
Cdd:COG4175 21 LKLLDQGKSKDeilektGQTVgVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 93 ----RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 168
Cdd:COG4175 101 elrrKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALAT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 169 KPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFV 248
Cdd:COG4175 181 DPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYV 260
|
....*...
gi 495142058 249 ASFIGEIN 256
Cdd:COG4175 261 ADFVEDVD 268
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
22-254 |
4.66e-85 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 258.38 E-value: 4.66e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSF-DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH--RHVNTV 98
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 99 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLE--EFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 176
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495142058 177 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGE 254
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-244 |
1.34e-83 |
|
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: 263.69 E-value: 1.34e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 4 LRDRVKKLNTQPRSLSPLLQLADIGKSFDGK-----TVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRI 78
Cdd:COG1123 243 LGAARGRAAPAAAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 79 TLDAQDITDVPAE-----HRHVNTVFQ--SYALFPHMTVFENVAFGLRMQKT-PAAEITPRVMDALKMVQL-EEFAQRKP 149
Cdd:COG1123 323 LFDGKDLTKLSRRslrelRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYP 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 150 HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 229
Cdd:COG1123 403 HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGR 482
|
250
....*....|....*
gi 495142058 230 IEQDGTPREIYEEPK 244
Cdd:COG1123 483 IVEDGPTEEVFANPQ 497
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
19-233 |
6.12e-82 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 249.58 E-value: 6.12e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSF-DGK---TVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHR- 93
Cdd:COG1136 2 SPLLELRNLTKSYgTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 94 -----HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 168
Cdd:COG1136 82 rlrrrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495142058 169 KPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqEEALTMSDRIVVMRDGRIEQD 233
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-252 |
1.24e-81 |
|
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: 250.64 E-value: 1.24e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 25 ADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE------HRHVNTV 98
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrRKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 99 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142058 179 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFI 252
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
20-252 |
7.40e-79 |
|
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: 242.19 E-value: 7.40e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH-----RH 94
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 95 VNTVFQSYALFPHMTVFENVAFGLRMQKT-PAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLL 173
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 174 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIyEEPKNLFVASFI 252
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL-LASDDPWVRQFL 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
21-245 |
6.32e-78 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 239.90 E-value: 6.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE----HRHVN 96
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinklRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 97 TVFQSYALFPHMTVFENVAFGLRM-QKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 175
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495142058 176 DESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 245
Cdd:COG1126 161 DEPTSALD----PELVGEVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
29-267 |
2.87e-77 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 242.84 E-value: 2.87e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 29 KSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDV-PAEHRHVN-----TVFQSY 102
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQsPVELREVRrkkigMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 103 ALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 182
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 183 DYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGEINIFDATV 262
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240
|
....*
gi 495142058 263 IERID 267
Cdd:TIGR01186 241 AERIA 245
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
22-230 |
2.11e-75 |
|
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: 232.77 E-value: 2.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDG----KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE------ 91
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 92 HRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPR 171
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 172 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALtMSDRIVVMRDGRI 230
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
32-246 |
1.24e-74 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 231.07 E-value: 1.24e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT--DVPAEHRHVNTVFQS--YALFpH 107
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkkNLRELRRKVGLVFQNpdDQLF-A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 108 MTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 187
Cdd:COG1122 91 PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 188 KQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNL 246
Cdd:COG1122 171 RELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
22-229 |
1.24e-73 |
|
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: 226.68 E-value: 1.24e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITD----VPAEHRHVNT 97
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 98 VFQSYALFPHMTVFENVAFGlrmqktpaaeitprvmdalkmvqleefaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495142058 178 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 229
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-234 |
2.03e-73 |
|
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: 227.56 E-value: 2.03e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 24 LADIGKSFDGKTVisDFSLTINhGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITL------DAQDITDVPAEHRHVNT 97
Cdd:cd03297 3 CVDIEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfDSRKKINLPPQQRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 98 VFQSYALFPHMTVFENVAFGLRmqKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:cd03297 80 VFQQYALFPHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 178 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 234
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
22-239 |
9.59e-73 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 226.61 E-value: 9.59e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDV-PAEHRHVNT--- 97
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLsEAELYRLRRrmg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 98 -VFQSYALFPHMTVFENVAFGLRMQ-KTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 175
Cdd:cd03261 81 mLFQSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142058 176 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
22-254 |
2.12e-72 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 225.40 E-value: 2.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVisDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNTVFQS 101
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 102 YALFPHMTVFENVAFGLRmqktPAAEITP----RVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:COG3840 80 NNLFPHLTVAQNIGLGLR----PGLKLTAeqraQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 178 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGE 254
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-252 |
2.48e-72 |
|
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: 225.84 E-value: 2.48e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSF----DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVP--AEHRH 94
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRrkAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 95 VNTVFQSY--ALFPHMTVFENVAFGLRMQKTPaaEITPRVMDALKMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPR 171
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 172 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN-----L 246
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHpytreL 238
|
....*.
gi 495142058 247 FVASFI 252
Cdd:COG1124 239 LAASLA 244
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-230 |
4.45e-71 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 223.20 E-value: 4.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFDG----KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDvPAEHRHV 95
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 96 ntVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 175
Cdd:COG4525 81 --VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 176 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRI 230
Cdd:COG4525 159 DEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRI 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
22-234 |
7.93e-70 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 218.77 E-value: 7.93e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSF-DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH-----RHV 95
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 96 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 175
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 176 DESLSALDYKLRKQMQNELKALQRkLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 234
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
21-234 |
3.50e-69 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 216.99 E-value: 3.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGK----TVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE----- 91
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 92 HRHVNTVFQSY--ALFPHMTVFENVAFGLRMQK--TPAAEITPRVMDALKMVQL-EEFAQRKPHQLSGGQQQRVAIARAV 166
Cdd:cd03257 81 RKEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGklSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495142058 167 VNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 234
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
39-265 |
8.15e-69 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 220.74 E-value: 8.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 39 DFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITL------DAQDITDVPAEHRHVNTVFQSYALFPHMTVFE 112
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqDSARGIFLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 113 NVAFGLRmqKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQN 192
Cdd:COG4148 97 NLLYGRK--RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495142058 193 ELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGEINIFDATVIER 265
Cdd:COG4148 175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVAAH 247
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
22-230 |
2.81e-67 |
|
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: 211.62 E-value: 2.81e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT----DVPAEHRHVNT 97
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 98 VFQSYALFPHMTVFENVAFGLR-MQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 176
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495142058 177 ESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
20-242 |
5.75e-67 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 212.22 E-value: 5.75e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSF-DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE-----HR 93
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRalrrlRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 94 HVNTVFQSYALFPHMTVFENVAFG-----------LRMQktPAAEItPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAI 162
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGrlgrtstwrslLGLF--PPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 163 ARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDA 237
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
22-242 |
3.36e-66 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 209.92 E-value: 3.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE-HRHVNTVFQ 100
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 101 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 180
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 181 ALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
23-229 |
7.48e-66 |
|
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: 208.09 E-value: 7.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 23 QLADIGKSFDGKT--VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH--RHVNTV 98
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 99 FQsyalFP-HM----TVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLL 173
Cdd:cd03225 81 FQ----NPdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495142058 174 LLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 229
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
21-239 |
1.45e-65 |
|
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: 208.74 E-value: 1.45e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH--RHVNTV 98
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 99 FQSYALFPHMTVFENVAFG----LRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 174
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495142058 175 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
22-255 |
3.55e-65 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 210.70 E-value: 3.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGK----TVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVP-----AEH 92
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSerelrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 93 RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRL 172
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 173 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeealtMS------DRIVVMRDGRIEQDGTPREIYEEPKNL 246
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE------MDvvrricDRVAVLENGRIVEQGPVLDVFANPQSE 235
|
....*....
gi 495142058 247 FVASFIGEI 255
Cdd:COG1135 236 LTRRFLPTV 244
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-246 |
4.45e-65 |
|
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: 215.54 E-value: 4.45e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSFDG--KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADA---GRITLDAQDITDVPAEHR 93
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 94 --HVNTVFQS--YALFPhMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 169
Cdd:COG1123 82 grRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 170 PRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNL 246
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-244 |
1.25e-63 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 206.12 E-value: 1.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFD------GKTV-----ISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDV 88
Cdd:COG4608 6 PLLEVRDLKKHFPvrgglfGRTVgvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 89 PAE-----HRHVNTVFQ-SYA-LFPHMTVFENVAFGLRMQK-TPAAEITPRVMDALKMVQL-EEFAQRKPHQLSGGQQQR 159
Cdd:COG4608 86 SGRelrplRRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 160 VAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLTM----SDRIVVMRDGRIEQDGT 235
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIVEIAP 241
|
....*....
gi 495142058 236 PREIYEEPK 244
Cdd:COG4608 242 RDELYARPL 250
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
21-244 |
6.26e-63 |
|
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: 201.27 E-value: 6.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGK----TVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVP-----AE 91
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 92 HRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPR 171
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495142058 172 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 244
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
32-246 |
1.04e-60 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 196.88 E-value: 1.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRI------TLDAQDITDVpaeHRHVNTVFQSyalf 105
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVtvdgldTLDEENLWEI---RKKVGMVFQN---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 106 PH-----MTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 180
Cdd:TIGR04520 86 PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495142058 181 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALtMSDRIVVMRDGRIEQDGTPREIYEEPKNL 246
Cdd:TIGR04520 166 MLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQVELL 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
22-242 |
2.08e-60 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 195.09 E-value: 2.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSF-DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH-----RHV 95
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 96 NTVFQSYALFPHMTVFENVAFGLRMQKT---------PAAEItPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAV 166
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRStwrslfglfPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495142058 167 VNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
21-252 |
1.29e-58 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 190.30 E-value: 1.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHV----N 96
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 97 TVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 175
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 176 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFI 252
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
21-228 |
3.34e-58 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 189.91 E-value: 3.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEhRHVntVFQ 100
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE-RGV--VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 101 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 180
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495142058 181 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 228
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
19-239 |
3.66e-58 |
|
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: 189.86 E-value: 3.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRH---- 94
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 95 VNTvFQSYALFPHMTVFENVA---------------FGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQR 159
Cdd:COG0411 82 ART-FQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 160 VAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-227 |
1.26e-57 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 186.92 E-value: 1.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADA---GRITLDAQDITDVPAEHRHVNTV 98
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALPAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 99 FQSYALFPHMTVFENVAFGLRmQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:COG4136 82 FQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495142058 179 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSdRIVVMRD 227
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAG-RVLDLGN 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
32-241 |
1.96e-57 |
|
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: 198.90 E-value: 1.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH--RHVNTVFQSYALFpHMT 109
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFLF-SGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 110 VFENVAFGlrmqktpAAEITP-RVMDALKMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:COG2274 565 IRENITLG-------DPDATDeEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142058 178 SLSALDYKLRKQMQNELKALQRklGITFVFVTHDqEEALTMSDRIVVMRDGRIEQDGTPREIYE 241
Cdd:COG2274 638 ATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
15-238 |
2.60e-57 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 186.87 E-value: 2.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 15 PRSLSPLLQLADIGKSFDGK----TVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT---- 86
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFalde 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 87 DVPAEHR--HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEitPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIAR 164
Cdd:COG4181 82 DARARLRarHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142058 165 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALtMSDRIVVMRDGRIEQDGTPRE 238
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLVEDTAATA 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
22-230 |
5.78e-57 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 185.02 E-value: 5.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH--RHVNTVF 99
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 100 QSYALFPhMTVFENVAFGLRMQKTPAAEitPRVMDALKMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:COG4619 81 QEPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495142058 179 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-244 |
1.68e-56 |
|
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: 187.57 E-value: 1.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGK----TVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENA---DAGRITLDAQDITDVPAE-- 91
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 92 ----HRHVNTVFQ-SY-ALFPHMTVFENVAFGLRM-QKTPAAEITPRVMDALKMVQL---EEFAQRKPHQLSGGQQQRVA 161
Cdd:COG0444 81 rkirGREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 162 IARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI-EQdGTPREIY 240
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIvEE-GPVEELF 239
|
....
gi 495142058 241 EEPK 244
Cdd:COG0444 240 ENPR 243
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
21-242 |
2.42e-56 |
|
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: 184.81 E-value: 2.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSF-DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE-----HRH 94
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrklRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 95 VNTVFQSYALFPHMTVFENVAFGlRMQKTPA---------AEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARA 165
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHG-RLGYKPTwrsllgrfsEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 166 VVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
21-242 |
2.96e-56 |
|
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: 184.29 E-value: 2.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHR-HVNTVF 99
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 100 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 179
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495142058 180 SALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:COG4555 161 NGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
23-255 |
2.11e-55 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 185.39 E-value: 2.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 23 QLADIGKSFDGK----TVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT-----DVPAEHR 93
Cdd:PRK11153 3 ELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalsekELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 94 HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLL 173
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 174 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIG 253
Cdd:PRK11153 163 LCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQ 242
|
..
gi 495142058 254 EI 255
Cdd:PRK11153 243 ST 244
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
39-264 |
2.34e-55 |
|
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: 185.70 E-value: 2.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 39 DFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLD-------AQDItDVPAEHRHVNTVFQSYALFPHMTVF 111
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtlfdsRKGI-FLPPEKRRIGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 112 ENVAFGLRMQKTPAAEITP-RVMDalkMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQM 190
Cdd:TIGR02142 94 GNLRYGMKRARPSERRISFeRVIE---LLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142058 191 QNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPkNLFVASFIGEINIFDATVIE 264
Cdd:TIGR02142 171 LPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP-DLPWLAREDQGSLIEGVVAE 243
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
22-239 |
8.93e-55 |
|
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: 180.07 E-value: 8.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENA-----DAGRITLDAQDI----TDVPAEH 92
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydldVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 93 RHVNTVFQSYALFPhMTVFENVAFGLRMQKT-PAAEITPRVMDALKMVQL-EEFAQR-KPHQLSGGQQQRVAIARAVVNK 169
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 170 PRLLLLDESLSALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-239 |
2.26e-54 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 179.17 E-value: 2.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAeHRHVNT---- 97
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP-HEIARLgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 98 VFQSYALFPHMTVFENVAFGLRMQKTPA----------AEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 167
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 168 NKPRLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-243 |
2.35e-54 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 179.51 E-value: 2.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVpaeHRHVNTV 98
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA---RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 99 FQSYAL---FPhMTVFENVAFGL----RMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPR 171
Cdd:COG1121 81 PQRAEVdwdFP-ITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 172 LLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEqDGTPREIYEEP 243
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVA-HGPPEEVLTPE 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
39-234 |
7.24e-54 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 177.30 E-value: 7.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 39 DFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNTVFQSYALFPHMTVFENVAFGL 118
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 119 rmqkTPAAEITP----RVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNEL 194
Cdd:cd03298 96 ----SPGLKLTAedrqAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495142058 195 KALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 234
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-254 |
1.30e-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: 185.27 E-value: 1.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFD------GKTV-----ISDFSLTINHGEFLTLLGPSGCGKTT----VLRLIAGlenadAGRITLDAQD 84
Cdd:COG4172 274 PLLEARDLKVWFPikrglfRRTVghvkaVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIPS-----EGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 85 ITDVPAEH-----RHVNTVFQS-YA-LFPHMTVFENVAFGLRMQKTP--AAEITPRVMDALKMVQL-EEFAQRKPHQLSG 154
Cdd:COG4172 349 LDGLSRRAlrplrRRMQVVFQDpFGsLSPRMTVGQIIAEGLRVHGPGlsAAERRARVAEALEEVGLdPAARHRYPHEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 155 GQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI-EQd 233
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVvEQ- 507
|
250 260
....*....|....*....|....*.
gi 495142058 234 GTPREIYEEPKN-----LFVASFIGE 254
Cdd:COG4172 508 GPTEQVFDAPQHpytraLLAAAPLLE 533
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
37-265 |
1.49e-53 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 182.16 E-value: 1.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 37 ISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVP-AEHRHVN-----TVFQSYALFPHMTV 110
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdAELREVRrkkiaMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 111 FENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQM 190
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495142058 191 QNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGEINI---FDATVIER 265
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDIsqvFSAKDIAR 281
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-233 |
2.24e-53 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 177.56 E-value: 2.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 13 TQPRSL---SPLLqLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVP 89
Cdd:PRK11247 2 MNTARLnqgTPLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 90 AEHRhvnTVFQSYALFPHMTVFENVAFGLRMQKTPAAEitprvmDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 169
Cdd:PRK11247 81 EDTR---LMFQDARLLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142058 170 PRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQD 233
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
37-228 |
2.60e-53 |
|
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: 176.50 E-value: 2.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 37 ISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDvPAEHRHVntVFQSYALFPHMTVFENVAF 116
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV--VFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 117 GLR--MQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNEL 194
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190
....*....|....*....|....*....|....
gi 495142058 195 KALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 228
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
22-230 |
2.89e-53 |
|
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: 174.12 E-value: 2.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHR-HVNTVFQ 100
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 101 SYALFPHMTVFENVafglrmqktpaaeitprvmdalkmvqleefaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLS 180
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495142058 181 ALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
32-238 |
4.71e-52 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 182.29 E-value: 4.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE--HRHVNTVFQSYALFpHMT 109
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLEslRRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 110 VFENVAFGlrmqktpAAEITP-RVMDALKMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:COG1132 430 IRENIRYG-------RPDATDeEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495142058 178 SLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 238
Cdd:COG1132 503 ATSALDTETEALIQEALERLMK--GRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEE 560
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
23-234 |
6.75e-52 |
|
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: 171.08 E-value: 6.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 23 QLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH--RHVNTVFQ 100
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 101 syalfphmtvfenvafglrmqktpaaeitprvmdALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 180
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495142058 181 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 234
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
20-229 |
9.12e-52 |
|
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: 171.51 E-value: 9.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE-HRHVNTV 98
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 99 FQSYALFPHMTVFENVAFGLRMQKTPAAEItpRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495142058 179 LSALDyklrKQMQNELKAL---QRKLGITFVFVTHDQEEALtmSDRIVVMRDGR 229
Cdd:COG4133 159 FTALD----AAGVALLAELiaaHLARGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
22-244 |
2.24e-50 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 169.04 E-value: 2.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQ--DITDVPAE------HR 93
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEkairllRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 94 HVNTVFQSYALFPHMTVFEN-VAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRL 172
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 173 LLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTpREIYEEPK 244
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ 232
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
20-244 |
2.89e-50 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 169.21 E-value: 2.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT--------DVPAE 91
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgeLVPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 92 HRHVNT-------VFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIA 163
Cdd:COG4598 87 RRQLQRirtrlgmVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 164 RAVVNKPRLLLLDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIY 240
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALD----PELVGEVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVF 242
|
....
gi 495142058 241 EEPK 244
Cdd:COG4598 243 GNPK 246
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
40-239 |
3.31e-50 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 168.22 E-value: 3.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 40 FSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNTVFQSYALFPHMTVFENVAFGLR 119
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 120 mqktPAAEITP----RVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELK 195
Cdd:PRK10771 98 ----PGLKLNAaqreKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495142058 196 ALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
33-230 |
1.01e-49 |
|
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: 166.43 E-value: 1.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 33 GKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITD-----VPAEHRHVNTVFQSYALFPH 107
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 108 MTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 187
Cdd:cd03292 93 RNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495142058 188 KQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:cd03292 173 WEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
37-177 |
1.60e-49 |
|
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: 163.59 E-value: 1.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 37 ISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT--DVPAEHRHVNTVFQSYALFPHMTVFENV 114
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTddERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 115 AFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRK----PHQLSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
39-241 |
2.31e-49 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 167.88 E-value: 2.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 39 DFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITD--VPAEHRHVNTVFQSY-ALFPHMTVFENVA 115
Cdd:PRK13635 25 DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetVWDVRRQVGMVFQNPdNQFVGATVQDDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 116 FGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELK 195
Cdd:PRK13635 105 FGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495142058 196 ALQRKLGITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYE 241
Cdd:PRK13635 185 QLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
22-244 |
2.44e-49 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 166.34 E-value: 2.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITL--DAQDITDVPAE------HR 93
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFSKTPSDkairelRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 94 HVNTVFQSYALFPHMTVFENVAFG----LRMQKTPAAEitpRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 169
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEApcrvLGLSKDQALA---RAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495142058 170 PRLLLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTpREIYEEPK 244
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQ 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
22-229 |
3.50e-48 |
|
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: 161.01 E-value: 3.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKT--VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE--HRHVNT 97
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEslRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 98 VFQSYALFpHMTVFENVafglrmqktpaaeitprvmdalkmvqleefaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495142058 178 SLSALDYKLRKQMQNELKALQRklGITFVFVTHDqEEALTMSDRIVVMRDGR 229
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
30-225 |
4.27e-48 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 162.32 E-value: 4.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 30 SFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDvpaEHRHVNTVFQSYAL---FP 106
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---ERKRIGYVPQRRSIdrdFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 107 hMTVFENVAFGL----RMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 182
Cdd:cd03235 85 -ISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495142058 183 DYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVM 225
Cdd:cd03235 164 DPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-243 |
6.73e-48 |
|
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: 170.72 E-value: 6.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 12 NTQPRSLSPLLQLADIGKSFDG--KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVP 89
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 90 AE--HRHVNTVFQSYALFpHMTVFENVAFGlRMQKTPAAeitprVMDALKMVQLEEFAQRKPH-----------QLSGGQ 156
Cdd:COG4987 404 EDdlRRRIAVVPQRPHLF-DTTLRENLRLA-RPDATDEE-----LWAALERVGLGDWLAALPDgldtwlgeggrRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 157 QQRVAIARAVVNKPRLLLLDESLSALDYKLRKQ-MQNELKALQRKlgiTFVFVTHDQEEALTMsDRIVVMRDGRIEQDGT 235
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQAlLADLLEALAGR---TVLLITHRLAGLERM-DRILVLEDGRIVEQGT 552
|
....*...
gi 495142058 236 PREIYEEP 243
Cdd:COG4987 553 HEELLAQN 560
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
37-240 |
9.04e-48 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 163.75 E-value: 9.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 37 ISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT--DVPAEHRHVNTVFQSY-ALFPHMTVFEN 113
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRHKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 114 VAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 193
Cdd:PRK13650 103 VAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495142058 194 LKALQRKLGITFVFVTHDQEEaLTMSDRIVVMRDGRIEQDGTPREIY 240
Cdd:PRK13650 183 IKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
34-242 |
3.51e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 162.14 E-value: 3.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE----HRHVNTVFQ--SYALFPH 107
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdiRKKVGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 108 mTVFENVAFGLRMQKTPAAEITPRVMDALKMVQL--EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 185
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 186 LRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
23-229 |
1.85e-46 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 156.25 E-value: 1.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 23 QLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE--HRHVNTVFQ 100
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEelRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 101 syalfphmtvfenvafglrmqktpaaeitprvmdalkmvqleefaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDESLS 180
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495142058 181 ALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 229
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
13-242 |
9.91e-46 |
|
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: 164.93 E-value: 9.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 13 TQPRSLSPLLQLADIGKSF-DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE 91
Cdd:COG4988 328 PLPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 92 --HRHVNTVFQSYALFpHMTVFENVAFGlRMQKTPAAeitprVMDALKMVQLEEFAQRKPH-----------QLSGGQQQ 158
Cdd:COG4988 408 swRRQIAWVPQNPYLF-AGTIRENLRLG-RPDASDEE-----LEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQ 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 159 RVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHDqEEALTMSDRIVVMRDGRIEQDGTPRE 238
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEE 557
|
....
gi 495142058 239 IYEE 242
Cdd:COG4988 558 LLAK 561
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-238 |
1.50e-45 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 157.20 E-value: 1.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVP----AEHRHVn 96
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSpwelARRRAV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 97 tVFQSYAL-FPhMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARA-------VVN 168
Cdd:COG4559 80 -LPQHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVlaqlwepVDG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 169 KPRLLLLDESLSALDykLRKQMQ--NELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 238
Cdd:COG4559 158 GPRWLFLDEPTSALD--LAHQHAvlRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
22-239 |
1.83e-45 |
|
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: 155.74 E-value: 1.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSF--DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDI-TDVPAEHRHVNTV 98
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 99 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495142058 179 LSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
29-253 |
8.07e-45 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 154.91 E-value: 8.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 29 KSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRI-----TLDA-----QDITDVPAEHRHVNTV 98
Cdd:PRK11264 11 KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTarslsQQKGLIRQLRQHVGFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 99 FQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:PRK11264 91 FQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 178 SLSALDYKLRKQMQNELKAL-QRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN----LFVASFI 252
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQprtrQFLEKFL 248
|
.
gi 495142058 253 G 253
Cdd:PRK11264 249 L 249
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-235 |
1.51e-44 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 154.84 E-value: 1.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSFDG---------KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT--- 86
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAkln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 87 --DVPAEHRHVNTVFQSY--ALFPHMTVFENVAFGLR-MQKTPAAEITPRVMDALKMVQL-EEFAQRKPHQLSGGQQQRV 160
Cdd:PRK10419 81 raQRKAFRRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495142058 161 AIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 235
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
34-230 |
2.97e-44 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 153.81 E-value: 2.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE-----HRHVNTVFQ-SYALF-P 106
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKqrrafRRDVQLVFQdSPSAVnP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 107 HMTVFENVAFGLR-MQKTPAAEITPRVMDALKMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 184
Cdd:TIGR02769 104 RMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495142058 185 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:TIGR02769 184 VLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
22-244 |
4.22e-44 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 152.31 E-value: 4.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRH---VNTV 98
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRArlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 99 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495142058 179 LSALDYKLRKQMQNELKAL-QRKLGitfVFVT-HDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 244
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILkDRGIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
20-244 |
5.90e-44 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 152.11 E-value: 5.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPaehrhvntVF 99
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP--------MH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 100 Q------SY-----ALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 168
Cdd:COG1137 74 KrarlgiGYlpqeaSIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495142058 169 KPRLLLLDESLSALDYKLRKQMQNELKAL-QRKLGitfVFVT-HDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 244
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQKIIRHLkERGIG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
20-238 |
8.15e-44 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 152.62 E-value: 8.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVP----AEHRHV 95
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpaelARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 96 ntVFQSYAL-FPhMTVFENVAFGL---RMQKTPAAEITPRVMDAlkmVQLEEFAQRKPHQLSGGQQQRVAIARAVV---- 167
Cdd:PRK13548 81 --LPQHSSLsFP-FTVEEVVAMGRaphGLSRAEDDALVAAALAQ---VDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwe 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495142058 168 --NKPRLLLLDESLSALDykLRKQMQ--NELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 238
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALD--LAHQHHvlRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
26-239 |
9.64e-44 |
|
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: 150.98 E-value: 9.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 26 DIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE-HRHVNTVFQSYAL 104
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 105 FPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 184
Cdd:cd03265 85 DDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495142058 185 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:cd03265 165 QTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
22-230 |
1.22e-43 |
|
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: 150.45 E-value: 1.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNTVFQS 101
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 102 YALFPHMTVFENVAFGLRMQKTPAAeitpRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 181
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495142058 182 LDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:cd03268 157 LDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-244 |
1.74e-43 |
|
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: 158.31 E-value: 1.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSFDG----KTVISDFSLTINHGEFLTLLGPSGCGKT----TVLRLIAGLENADAGRITLDAQDITDVPA 90
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 91 EH------RHVNTVFQ--SYALFPHMTVFENVAFGLRM-QKTPAAEITPRVMDALKMVQLEEFAQR---KPHQLSGGQQQ 158
Cdd:COG4172 84 RElrrirgNRIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 159 RVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLT----MSDRIVVMRDGRIEQDG 234
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQG 239
|
250
....*....|
gi 495142058 235 TPREIYEEPK 244
Cdd:COG4172 240 PTAELFAAPQ 249
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
22-234 |
1.86e-43 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 150.04 E-value: 1.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGeFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE-HRHVNTVFQ 100
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 101 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 180
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495142058 181 ALDYKLRKQMQNELKALQRklGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 234
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-244 |
2.29e-43 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 153.32 E-value: 2.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFD-----------GKTV--ISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT 86
Cdd:PRK15079 7 VLLEVADLKVHFDikdgkqwfwqpPKTLkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 87 DVPAEHRH-----VNTVFQS--YALFPHMTVFENVAFGLRM--QKTPAAEITPRVMDALKMVQL-EEFAQRKPHQLSGGQ 156
Cdd:PRK15079 87 GMKDDEWRavrsdIQMIFQDplASLNPRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 157 QQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 236
Cdd:PRK15079 167 CQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTY 246
|
....*...
gi 495142058 237 REIYEEPK 244
Cdd:PRK15079 247 DEVYHNPL 254
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
31-245 |
5.93e-43 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 150.19 E-value: 5.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 31 FDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLR-------LIAG--LEnadaGRITLDAQDI----TDVPAEHRHVNT 97
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGarVE----GEILLDGEDIydpdVDVVELRRRVGM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 98 VFQSYALFPhMTVFENVAFGLRMQ-KTPAAEITPRVMDALKMVQL-EEFAQR--KP-HQLSGGQQQRVAIARAVVNKPRL 172
Cdd:COG1117 97 VFQKPNPFP-KSIYDNVAYGLRLHgIKSKSELDEIVEESLRKAALwDEVKDRlkKSaLGLSGGQQQRLCIARALAVEPEV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 173 LLLDESLSALD-----------YKLRKQMqnelkalqrklgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 241
Cdd:COG1117 176 LLMDEPTSALDpistakieeliLELKKDY-------------TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFT 242
|
....
gi 495142058 242 EPKN 245
Cdd:COG1117 243 NPKD 246
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
32-241 |
1.40e-42 |
|
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: 148.53 E-value: 1.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDV--PAEHRHVNTVFQSYALFpHMT 109
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYtlASLRRQIGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 110 VFENVAFGLRmqktpaaEITP-RVMDALKMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:cd03251 92 VAENIAYGRP-------GATReEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142058 178 SLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYE 241
Cdd:cd03251 165 ATSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-239 |
2.16e-42 |
|
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: 2.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE---HRHVNTV 98
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHeraRAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 99 FQSYALFPHMTVFENVAFGLRMQKtpAAEITPRVMDALKMV-QLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARR--RAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 178 SLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
19-245 |
3.44e-42 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 148.45 E-value: 3.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSFDGKT---------VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT--D 87
Cdd:COG4167 2 SALLEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEygD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 88 VPAEHRHVNTVFQ--SYALFPHMTVFENVAFGLRMQ-KTPAAEITPRVMDALKMVQL-EEFAQRKPHQLSGGQQQRVAIA 163
Cdd:COG4167 82 YKYRCKHIRMIFQdpNTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 164 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 243
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
..
gi 495142058 244 KN 245
Cdd:COG4167 242 QH 243
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-234 |
9.24e-42 |
|
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: 145.97 E-value: 9.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGKT----VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE-HRHV 95
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEaRRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 96 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 175
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 176 DESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 234
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-244 |
9.33e-42 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 146.28 E-value: 9.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPA-------- 90
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhriarlgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 91 ----EHRHVntvfqsyalFPHMTVFENVAFGLRMQKTPAaeitpRVMDALKMV-----QLEEFAQRKPHQLSGGQQQRVA 161
Cdd:COG0410 81 gyvpEGRRI---------FPSLTVEENLLLGAYARRDRA-----EVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 162 IARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 241
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
...
gi 495142058 242 EPK 244
Cdd:COG0410 226 DPE 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-239 |
1.75e-41 |
|
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: 146.00 E-value: 1.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGlEN--ADAGRITLDAQDI--TDVPaEHR- 93
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG-DLppTYGNDVRLFGERRggEDVW-ELRk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 94 ---HVNTVFQSYaLFPHMTVFENVAFGL-----RMQKTPAAEITpRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARA 165
Cdd:COG1119 79 rigLVSPALQLR-FPRDETVLDVVLSGFfdsigLYREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142058 166 VVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
36-242 |
2.12e-41 |
|
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: 145.37 E-value: 2.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 36 VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH--RHVNTVFQSYALFPhMTVFEN 113
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 114 VAFGlrmqKTPAAEITprVMDALKMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 182
Cdd:cd03249 97 IRYG----KPDATDEE--VEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495142058 183 DYKLRKQMQnelKALQR-KLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:cd03249 171 DAESEKLVQ---EALDRaMKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
34-242 |
2.56e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 146.77 E-value: 2.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRI---TLDAQDITDVPAEHRHVNTVFQSyalfPH--- 107
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdGLDTSDEENLWDIRNKAGMVFQN----PDnqi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 108 --MTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 185
Cdd:PRK13633 99 vaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 186 LRKQMQNELKALQRKLGITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:PRK13633 179 GRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-230 |
7.75e-41 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 150.17 E-value: 7.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDI---TDVPAEHRHVN 96
Cdd:COG1129 3 PLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrSPRDAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 97 TVFQSYALFPHMTVFENVAFGlRMQKTPA----AEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRL 172
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLG-REPRRGGlidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 173 LLLDESLSALDYK----LRKQMqNELKAlqrkLGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:COG1129 162 LILDEPTASLTEReverLFRII-RRLKA----QGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
36-234 |
1.03e-40 |
|
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: 143.11 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 36 VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDV-PAE-HRHVNTVFQSYALFpHMTVFEN 113
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLdPADlRRNIGYVPQDVTLF-YGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 114 VAFGLrmqktPAAEiTPRVMDALKMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 182
Cdd:cd03245 98 ITLGA-----PLAD-DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495142058 183 DYKLRKQMQNELKALQRklGITFVFVTHDQeEALTMSDRIVVMRDGRIEQDG 234
Cdd:cd03245 172 DMNSEERLKERLRQLLG--DKTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-235 |
6.73e-40 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 141.49 E-value: 6.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSF-DGKT---VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPA---- 90
Cdd:PRK11629 3 KILLQCDNLCKRYqEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaaka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 91 --EHRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 168
Cdd:PRK11629 83 elRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 169 KPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSdRIVVMRDGRIEQDGT 235
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAELS 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
34-249 |
1.39e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 141.67 E-value: 1.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITD--VPAEHRHVNTVFQSY-ALFPHMTV 110
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRKKIGIIFQNPdNQFIGATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 111 FENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQM 190
Cdd:PRK13632 102 EDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 191 QNELKALQRKLGITFVFVTHDQEEALtMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVA 249
Cdd:PRK13632 182 KKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEILEKA 239
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-298 |
1.72e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 142.17 E-value: 1.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITdvpaeHRHVNTVfqS 101
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-----PEDRRRI--G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 102 Y-----ALFPHMTVFENVAF-----GLrmqktPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPR 171
Cdd:COG4152 75 YlpeerGLYPKMKVGEQLVYlarlkGL-----SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 172 LLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE-PKNLFVAS 250
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQfGRNTLRLE 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 495142058 251 FIGEI----NIFDATVIERidaqrvranvEGRECVLYVAFPVTAGQKLNVLL 298
Cdd:COG4152 229 ADGDAgwlrALPGVTVVEE----------DGDGAELKLEDGADAQELLRALL 270
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
22-244 |
7.40e-39 |
|
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: 138.95 E-value: 7.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRH---VNTV 98
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERArlgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 99 FQSYALFPHMTVFENVAFGL-RMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 178 SLSALDYKLRKQMQNELKAL-QRKLGitfVFVT-HDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 244
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLkERGIG---VLITdHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
34-246 |
1.17e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 139.55 E-value: 1.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGL---ENADAGRITLDAQDIT-----DVpaeHRHVNTVFQSY-AL 104
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTaktvwDI---REKVGIVFQNPdNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 105 FPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 184
Cdd:PRK13640 97 FVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 185 KLRKQMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGRIEQDGTPREIYEEPKNL 246
Cdd:PRK13640 177 AGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEML 237
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-243 |
1.38e-38 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 138.58 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVP----AEHRHV 95
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPghqiARMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 96 NTvFQSYALFPHMTVFEN--VAFGLRMQ--------KTPA-----AEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRV 160
Cdd:PRK11300 84 RT-FQHVRLFREMTVIENllVAQHQQLKtglfsgllKTPAfrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 161 AIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIY 240
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
...
gi 495142058 241 EEP 243
Cdd:PRK11300 243 NNP 245
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-230 |
2.18e-38 |
|
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: 135.25 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDitdvpaehrhvntvfqs 101
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 102 yalfphmtvfenVAFGlrmqktpaaeiTPRvmDALK----MVqleefaqrkpHQLSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:cd03216 64 ------------VSFA-----------SPR--DARRagiaMV----------YQLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495142058 178 SLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-246 |
4.69e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 137.90 E-value: 4.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSF-DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDI----TDVPAEHRHV 95
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 96 NTVFQSY--ALFPHmTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLL 173
Cdd:PRK13639 81 GIVFQNPddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495142058 174 LLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNL 246
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-233 |
1.30e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 136.37 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSF-----DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHR--H 94
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 95 VNTVFQSYAL--FPHMTVFENVA--------FGLRMqktpaaeitprvmdALKMVQLEEFAQR--------------KPH 150
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRR--------------GLTKKRRELFRELlatlglglenrldtKVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 151 QLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKlRKQMQNEL-KALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 229
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
....
gi 495142058 230 IEQD 233
Cdd:COG1101 227 IILD 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-242 |
1.33e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 138.43 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 9 KKLNTQPRSLSPL-LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRIT-LDAQDIT 86
Cdd:PRK13536 28 EAKASIPGSMSTVaIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvLGVPVPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 87 DVPAEHRHVNTVFQSYALFPHMTVFEN-VAFGlRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARA 165
Cdd:PRK13536 108 RARLARARIGVVPQFDNLDLEFTVRENlLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 166 VVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
32-246 |
1.42e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 136.42 E-value: 1.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRI-----TLDAQDITDVpaeHRHVNTVFQS-YALF 105
Cdd:PRK13648 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEKL---RKHIGIVFQNpDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 106 PHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 185
Cdd:PRK13648 97 VGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495142058 186 LRKQMQNELKALQRKLGITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPKNL 246
Cdd:PRK13648 177 ARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
34-243 |
1.84e-37 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 136.05 E-value: 1.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDItdvPAEHRH--------VNTVFQSYALF 105
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI---PAMSRSrlytvrkrMSMLFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 106 PHMTVFENVAFGLRMQ-KTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 184
Cdd:PRK11831 97 TDMNVFDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 185 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 243
Cdd:PRK11831 177 ITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
30-238 |
4.48e-37 |
|
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: 133.89 E-value: 4.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 30 SFD-GKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE--HRHVNTVFQSYALFP 106
Cdd:cd03254 11 SYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKslRSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 107 HmTVFENVAFGlrmqkTPAAEITpRVMDALKMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLL 175
Cdd:cd03254 91 G-TIMENIRLG-----RPNATDE-EVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495142058 176 DESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 238
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDE 223
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
22-235 |
5.04e-37 |
|
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: 133.80 E-value: 5.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHR---HVNTV 98
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 99 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDaLKMVqLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYE-LFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 179 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 235
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
22-230 |
6.10e-37 |
|
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: 132.79 E-value: 6.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITdvPAEHRHVNTVFQS 101
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD--IAARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 102 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 181
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495142058 182 LDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:cd03269 159 LDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
36-230 |
7.99e-37 |
|
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: 131.57 E-value: 7.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 36 VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDV-PAEHR-HVNTVFQSYALFPHmTVFEN 113
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWdPNELGdHVGYLPQDDELFSG-SIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 114 VafglrmqktpaaeitprvmdalkmvqleefaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 193
Cdd:cd03246 96 I-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 495142058 194 LKALqRKLGITFVFVTHdQEEALTMSDRIVVMRDGRI 230
Cdd:cd03246 139 IAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
41-244 |
1.04e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 135.86 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 41 SLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRH-----VNTVFQS-YA-LFPHMTVFEN 113
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllrqkIQIVFQNpYGsLNPRKKVGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 114 VAFGLRMQKT-PAAEITPRVMDALKMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ 191
Cdd:PRK11308 115 LEEPLLINTSlSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495142058 192 NELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 244
Cdd:PRK11308 195 NLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
52-243 |
1.13e-36 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 136.16 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 52 LLGPSGCGKTTVLRLIAGLENADAGRITL------DAQDITDVPAEHRHVNTVFQSYALFPHMTVFENVAFGLRmqktpa 125
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLngrvlfDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 126 aeitpRVMDAL--KMVQL---EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRK 200
Cdd:PRK11144 103 -----KSMVAQfdKIVALlgiEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLARE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495142058 201 LGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 243
Cdd:PRK11144 178 INIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
32-238 |
1.58e-36 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 132.74 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDV--PAEHRHVNTVFQSYALFpHMT 109
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtlDSLRRAIGVVPQDTVLF-NDT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 110 VFENVAFGlrmqKTPAAEItpRVMDALKMVQLEEFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:cd03253 91 IGYNIRYG----RPDATDE--EVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 179 LSALDYKLRKQMQNELKALQRklGITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPRE 238
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
21-243 |
2.08e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 133.57 E-value: 2.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSF-DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRIT---LDAQDITDVPAEHRHVN 96
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 97 TVFQS-YALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 175
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495142058 176 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEaLTMSDRIVVMRDGRIEQDGTPREIYEEP 243
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-241 |
3.22e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 133.78 E-value: 3.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDItdvPAEHRH----V 95
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV---PSRARHarqrV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 96 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 175
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495142058 176 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 241
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
22-252 |
9.73e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 131.24 E-value: 9.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE---------- 91
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 92 -----HRHVNTVFQSYALFPHMTVFENVAFG----LRMQKTPAAEitpRVMDALKMVQLEEFAQRK-PHQLSGGQQQRVA 161
Cdd:PRK10619 86 qlrllRTRLTMVFQHFNLWSHMTVLENVMEApiqvLGLSKQEARE---RAVKYLAKVGIDERAQGKyPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 162 IARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 241
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
250
....*....|.
gi 495142058 242 EPKNLFVASFI 252
Cdd:PRK10619 242 NPQSPRLQQFL 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-247 |
1.95e-35 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 135.99 E-value: 1.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 15 PRSLSPLLQLADIGKSF-----------DGKTVISDFSLTINHGEFLTLLGPSGCGKTT----VLRLIAGlenadAGRIT 79
Cdd:PRK15134 269 PEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 80 LDAQDITD------VPAEHRhVNTVFQ--SYALFPHMTVFENVAFGLRM-QKT-PAAEITPRVMDALKMVQLE-EFAQRK 148
Cdd:PRK15134 344 FDGQPLHNlnrrqlLPVRHR-IQVVFQdpNSSLNPRLNVLQIIEEGLRVhQPTlSAAQREQQVIAVMEEVGLDpETRHRY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 149 PHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 228
Cdd:PRK15134 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
250
....*....|....*....
gi 495142058 229 RIEQDGTPREIYEEPKNLF 247
Cdd:PRK15134 503 EVVEQGDCERVFAAPQQEY 521
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
19-214 |
2.11e-35 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 129.45 E-value: 2.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE--HRHVN 96
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 97 TVFQSYALFPHmTVFENVAFGLRM-QKTPAAEitpRVMDALKMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 174
Cdd:PRK10247 85 YCAQTPTLFGD-TVYDNLIFPWQIrNQQPDPA---IFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495142058 175 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEE 214
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
33-239 |
2.18e-35 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 136.42 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 33 GKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH--RHVNTVFQSYALFPHmTV 110
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 111 FENVAfglRMqktpaAEITP-RVMDALKMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:COG4618 423 AENIA---RF-----GDADPeKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495142058 179 LSALDYKLRKQMQNELKALqRKLGITFVFVTHDQeEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:COG4618 495 NSNLDDEGEAALAAAIRAL-KARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
32-230 |
9.70e-35 |
|
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: 126.99 E-value: 9.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDvPAEHRHVNTVFQS--YALFPHmT 109
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KERRKSIGYVMQDvdYQLFTD-S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 110 VFENVAFGLRmqktPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQ 189
Cdd:cd03226 89 VREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495142058 190 MQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:cd03226 165 VGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
41-246 |
1.12e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 129.06 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 41 SLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT--DVPAEHRHVNTVFQSY-ALFPHMTVFENVAFG 117
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIGMVFQNPdNQFVGATVEDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 118 LRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKAL 197
Cdd:PRK13642 107 MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEI 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495142058 198 QRKLGITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPKNL 246
Cdd:PRK13642 187 KEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDM 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
39-246 |
1.38e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 128.98 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 39 DFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT------DVPAEHRHVNTVFQsyalFPHMTVFE 112
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQ----FPEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 113 -----NVAFGLRMQKTPAAEITPRVMDALKMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 186
Cdd:PRK13634 101 etvekDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 187 RKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNL 246
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEL 240
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
32-239 |
2.35e-34 |
|
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: 133.30 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE--HRHVNTVFQSYALFPHmT 109
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAslRRQVALVSQDVVLFND-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 110 VFENVAFGlRMQKTPAAEItprvMDALKMVQLEEFAQRKP---HQ--------LSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:TIGR02203 422 IANNIAYG-RTEQADRAEI----ERALAAAYAQDFVDKLPlglDTpigengvlLSGGQRQRLAIARALLKDAPILILDEA 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495142058 179 LSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:TIGR02203 497 TSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
18-242 |
4.03e-34 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 127.05 E-value: 4.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 18 LSPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADA---GRITLDAQDIT-------D 87
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQregrlarD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 88 VPAEHRHVNTVFQSYALFPHMTVFENVAFGlRMQKTP---------AAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQ 158
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 159 RVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 238
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
....
gi 495142058 239 IYEE 242
Cdd:PRK09984 240 FDNE 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
21-230 |
5.49e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 125.76 E-value: 5.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSF-DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT-----DVPAEHRH 94
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 95 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 174
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495142058 175 LDESLSALDYKLRKQMQNELKALQRkLGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
32-239 |
6.18e-34 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 125.68 E-value: 6.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE--HRHVNTVFQSYALFpHMT 109
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 110 VFENVAFGlrmqkTPAAEITpRVMDALKMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:cd03252 92 IRDNIALA-----DPGMSME-RVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495142058 179 LSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-242 |
2.06e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 130.15 E-value: 2.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLD--AQDITDvPAE-HRH-V 95
Cdd:COG3845 4 PALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkPVRIRS-PRDaIALgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 96 NTVFQSYALFPHMTVFENVAFGLRmqKTPAAEITPRVMDAlkmvQLEEFAQR---------KPHQLSGGQQQRVAIARAV 166
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGLE--PTKGGRLDRKAARA----RIRELSERygldvdpdaKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 167 VNKPRLLLLDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:COG3845 157 YRGARILILDEPTAVLT----PQEADELFEILRRLaaeGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEE 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
47-271 |
2.23e-33 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 131.13 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 47 GEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE-----HRHVNTVFQS-YA-LFPHMTVFENVAFGLR 119
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqalRRDIQFIFQDpYAsLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 120 MQKT-PAAEITPRVMDALKMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKAL 197
Cdd:PRK10261 430 VHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142058 198 QRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFIGEINIFDAtviERIDAQRV 271
Cdd:PRK10261 510 QRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVADP---SRQRPQRV 580
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-245 |
3.30e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 124.25 E-value: 3.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGL-----ENADAGRITLDAQDI--TDVPAEHRH 94
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIfkMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 95 VNTVFQSYALFPHMTVFENVAFGLRMQK--TPAAEITPRVMDALKMVQL-EEFAQR---KPHQLSGGQQQRVAIARAVVN 168
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 169 KPRLLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 245
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
32-239 |
5.25e-33 |
|
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: 130.25 E-value: 5.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQD--ITDVPAEHRHVNTVFQSYALFPHmT 109
Cdd:TIGR01846 468 DSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDlaIADPAWLRRQMGVVLQENVLFSR-S 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 110 VFENVAFGlrmqkTPAAEITpRVMDALKMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:TIGR01846 547 IRDNIALC-----NPGAPFE-HVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFDEA 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495142058 179 LSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:TIGR01846 621 TSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-245 |
5.37e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 123.73 E-value: 5.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGL-----ENADAGRITLDAQDI----TDVP 89
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysprTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 90 AEHRHVNTVFQSYALFPhMTVFENVAFGLRMQKTPAAEITPRVMD-ALKMVQLEEFAQRKPHQ----LSGGQQQRVAIAR 164
Cdd:PRK14239 83 DLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEkSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 165 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 244
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
.
gi 495142058 245 N 245
Cdd:PRK14239 240 H 240
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
36-243 |
1.69e-32 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 129.07 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 36 VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE--HRHVNTVFQSYALFPHmTVFEN 113
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 114 VAFGLRmqKTPAAEItprvMDALKMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 182
Cdd:TIGR00958 575 IAYGLT--DTPDEEI----MAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495142058 183 DyklrKQMQNELKALQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 243
Cdd:TIGR00958 649 D----AECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-238 |
1.76e-32 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 128.69 E-value: 1.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 18 LSPLLQLADIGKSF---DGKT-VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE-- 91
Cdd:PRK10535 1 MTALLELKDIRRSYpsgEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 92 ----HRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 167
Cdd:PRK10535 81 aqlrREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495142058 168 NKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEAlTMSDRIVVMRDGRIEQDGTPRE 238
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEIVRNPPAQE 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-245 |
2.02e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 122.26 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 36 VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGL--ENADA---GRITLDAQDI--TDV-PAE-HRHVNTVFQSYALFP 106
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEArveGEVRLFGRNIysPDVdPIEvRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 107 HMTVFENVAFGLRMQK--TPAAEITPRVMDALKMVQL-EEFAQR---KPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 180
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495142058 181 ALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 245
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-177 |
2.49e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 121.76 E-value: 2.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 13 TQPRSLSPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPaEH 92
Cdd:COG4674 2 SLDTMHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLD-EH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 93 RHVNT----VFQSYALFPHMTVFENVAFGLRMQKTP--------AAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRV 160
Cdd:COG4674 81 EIARLgigrKFQKPTVFEELTVFENLELALKGDRGVfaslfarlTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWL 160
|
170
....*....|....*..
gi 495142058 161 AIARAVVNKPRLLLLDE 177
Cdd:COG4674 161 EIGMLLAQDPKLLLLDE 177
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
39-238 |
5.41e-32 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 126.86 E-value: 5.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 39 DFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE--HRHVNTVFQSYALFpHMTVFENVAF 116
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAAIGIVPQDTVLF-NDTIAYNIAY 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 117 GlRMQKTPAAeitprVMDALKMVQLEEFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 185
Cdd:COG5265 455 G-RPDASEEE-----VEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSR 528
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 186 LRKQMQNELKALQRklGITFVFVTH------DqeealtmSDRIVVMRDGRIEQDGTPRE 238
Cdd:COG5265 529 TERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAE 578
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
26-246 |
5.89e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 122.50 E-value: 5.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 26 DIGKSFDGKT-----VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQD---------------- 84
Cdd:PRK13651 7 NIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekekvlek 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 85 ----------ITDVPAEHRHVNTVFQ--SYALFpHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQL-EEFAQRKPHQ 151
Cdd:PRK13651 87 lviqktrfkkIKKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 152 LSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIE 231
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
250
....*....|....*
gi 495142058 232 QDGTPREIYEEPKNL 246
Cdd:PRK13651 245 KDGDTYDILSDNKFL 259
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
32-210 |
6.00e-32 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 126.46 E-value: 6.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLdaqditdvPAEHRhvnTVF---QSYalFPHM 108
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--------PAGAR---VLFlpqRPY--LPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 109 TVFENVAFGLRMQKTPAAEITprvmDALKMVQLEEFAQR------KPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 182
Cdd:COG4178 441 TLREALLYPATAEAFSDAELR----EALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
170 180
....*....|....*....|....*....
gi 495142058 183 DYKLRKQMqneLKALQRKL-GITFVFVTH 210
Cdd:COG4178 517 DEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
32-237 |
6.53e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 121.38 E-value: 6.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE--HRHVNTVFQSY--ALFPh 107
Cdd:PRK13647 16 DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvRSKVGLVFQDPddQVFS- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 108 MTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 187
Cdd:PRK13647 95 STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495142058 188 KQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPR 237
Cdd:PRK13647 175 ETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-239 |
6.75e-32 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 124.18 E-value: 6.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDI--TDVPAEHRHVNT 97
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeaLSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 98 VFQSYALFPHMTVFENVafglRMQKTP-------AAEITPRVMD-ALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 169
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVV----EMGRTPhrsrfdtWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495142058 170 PRLLLLDESLSALDykLRKQMQNelKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:PRK09536 158 TPVLLLDEPTASLD--INHQVRT--LELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
34-242 |
7.75e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 120.89 E-value: 7.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH--RHVntvfqsyALFP--HMT 109
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRL-------ALLPqhHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 110 -----VFENVAFGlrmqKTP--------AAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 176
Cdd:PRK11231 88 pegitVRELVAYG----RSPwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 177 ESLSALDYklrkQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:PRK11231 164 EPTTYLDI----NHQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
28-242 |
1.31e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 121.00 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 28 GKSFDGKTvISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT------DVPAEHRHVNTVFQs 101
Cdd:PRK13649 15 GTPFEGRA-LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQIRKKVGLVFQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 102 yalFPHMTVFE-----NVAFGLRMQKTPAAEITPRVMDALKMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 175
Cdd:PRK13649 93 ---FPESQLFEetvlkDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 176 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:PRK13649 170 DEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-242 |
2.35e-31 |
|
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: 124.53 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGK---SFDGKTV--ISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAG----RITLDAQDITDVPA 90
Cdd:TIGR03269 278 PIIKVRNVSKryiSVDRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvRVGDEWVDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 91 EHR-----HVNTVFQSYALFPHMTVFENV--AFGLRMQKTPAAEitpRVMDALKMV-----QLEEFAQRKPHQLSGGQQQ 158
Cdd:TIGR03269 358 DGRgrakrYIGILHQEYDLYPHRTVLDNLteAIGLELPDELARM---KAVITLKMVgfdeeKAEEILDKYPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 159 RVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 238
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
....
gi 495142058 239 IYEE 242
Cdd:TIGR03269 515 IVEE 518
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-242 |
2.93e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 119.95 E-value: 2.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSF-DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDItDVPAE-----H 92
Cdd:PRK13636 3 DYILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmklR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 93 RHVNTVFQS--YALFPhMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 170
Cdd:PRK13636 82 ESVGMVFQDpdNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 171 RLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
34-239 |
3.12e-31 |
|
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: 124.38 E-value: 3.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH--RHVNTVFQSYALFPHmTVF 111
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 112 ENVAfglRMQKTPAAEitpRVMDALKMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDESLS 180
Cdd:TIGR01842 410 ENIA---RFGENADPE---KIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 181 ALDYKLRKQMQNELKALQRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:TIGR01842 484 NLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
35-233 |
7.35e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 117.57 E-value: 7.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 35 TVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHR------HVNTVFQSYALFPHM 108
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 109 TVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRK 188
Cdd:PRK10584 104 NALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495142058 189 QMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGRIEQD 233
Cdd:PRK10584 184 KIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQEE 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
20-250 |
8.74e-31 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 118.10 E-value: 8.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVP------AEHR 93
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalseAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 94 HvntVFQSYALFPHmtvfENVAFGLRMQKTPAAEITPRVM---------------DALKMVQLEefAQR---KPHQLSGG 155
Cdd:PRK11701 85 R---LLRTEWGFVH----QHPRDGLRMQVSAGGNIGERLMavgarhygdiratagDWLERVEID--AARiddLPTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 156 QQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR-IEQDG 234
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRvVESGL 235
|
250 260
....*....|....*....|..
gi 495142058 235 T------PREIYEEpknLFVAS 250
Cdd:PRK11701 236 TdqvlddPQHPYTQ---LLVSS 254
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-243 |
1.35e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 117.83 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 18 LSPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADA-----GRITLDAQDI----TDV 88
Cdd:PRK14258 4 LIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 89 PAEHRHVNTVFQSYALFPhMTVFENVAFGLRMQK-TPAAEITPRVMDALKMVQLEEFAQRKPHQ----LSGGQQQRVAIA 163
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 164 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM-----RDGRIEQDGTPRE 238
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEFGLTKK 242
|
....*
gi 495142058 239 IYEEP 243
Cdd:PRK14258 243 IFNSP 247
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-230 |
1.57e-29 |
|
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: 112.53 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGksfdGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNTVF 99
Cdd:cd03215 3 PVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 100 ------QSYALFPHMTVFENVAFglrmqktpaaeitprvmdalkmvqleefaqrkPHQLSGGQQQRVAIARAVVNKPRLL 173
Cdd:cd03215 79 yvpedrKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 174 LLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-269 |
1.88e-29 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 115.98 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSF---DGK-TVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLEnADAGRIT----LDAQDITDVPA 90
Cdd:PRK09473 10 DALLDVKDLRVTFstpDGDvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIGgsatFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 91 EH------RHVNTVFQS--YALFPHMTVFENVAFGL----RMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQ 158
Cdd:PRK09473 89 KElnklraEQISMIFQDpmTSLNPYMRVGEQLMEVLmlhkGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 159 RVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 238
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
250 260 270
....*....|....*....|....*....|.
gi 495142058 239 IYEEPKNLFVasfIGEINifdatVIERIDAQ 269
Cdd:PRK09473 249 VFYQPSHPYS---IGLLN-----AVPRLDAE 271
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
36-225 |
3.60e-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: 118.16 E-value: 3.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 36 VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH--RHVNTVFQSYALFPHmTVFEN 113
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAWVPQHPFLFAG-TIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 114 VAFGLRMQktPAAEITprvmDALKMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 182
Cdd:TIGR02857 416 IRLARPDA--SDAEIR----EALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495142058 183 DYKLRKQMQNELKALQRklGITFVFVTHDQEEALTMsDRIVVM 225
Cdd:TIGR02857 490 DAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
37-240 |
7.87e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 113.56 E-value: 7.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 37 ISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGR-------ITLDAQDITDVPAEHRHVNTVFQ--SYALFPH 107
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaIPANLKKIKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 108 mTVFENVAFGLRMQKTPAAEITPRVMDALKMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 186
Cdd:PRK13645 107 -TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495142058 187 RKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIY 240
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-239 |
7.97e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 112.29 E-value: 7.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRH---VNT 97
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArrgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 98 VFQSYALFPHMTVFENVAFGLRMQKTPAAEI-TPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 176
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDDLSAEQrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495142058 177 ESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
34-234 |
1.54e-28 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 111.09 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQdITDVPAehrhVNTVFQsyalfPHMTVFEN 113
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSLLG----LGGGFN-----PELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 114 VAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 193
Cdd:cd03220 105 IYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495142058 194 LKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 234
Cdd:cd03220 185 LRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
28-242 |
1.71e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 111.33 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 28 GKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQditdVPA--EhrhVNTVFQsyalf 105
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR----VSAllE---LGAGFH----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 106 PHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 185
Cdd:COG1134 101 PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 186 LRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:COG1134 181 FQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-243 |
1.94e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 112.20 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDG-KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT--DVPAEHRHVNT 97
Cdd:PRK13652 3 LIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 98 VFQSY--ALFPhMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 175
Cdd:PRK13652 83 VFQNPddQIFS-PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495142058 176 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 243
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-256 |
2.36e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 112.11 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENA-----DAGRITLDAQDI---TDVPA 90
Cdd:PRK14271 19 APAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfnyRDVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 91 EHRHVNTVFQSYALFPhMTVFENVAFGLRMQK-TPAAEITPRVMDALKMVQLEEFAQRK----PHQLSGGQQQRVAIARA 165
Cdd:PRK14271 99 FRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 166 VVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 245
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKH 255
|
250
....*....|.
gi 495142058 246 LFVASFIGEIN 256
Cdd:PRK14271 256 AETARYVAGLS 266
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-229 |
4.11e-28 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 109.83 E-value: 4.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSF-----DGKT--VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQ----DITD 87
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 88 vpAEHRHV-----NT---VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQL-EEFAQRKPHQLSGGQQQ 158
Cdd:COG4778 82 --ASPREIlalrrRTigyVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142058 159 RVAIARAVVNKPRLLLLDESLSALDYKLR---KQMQNELKAlqrkLGITFVFVTHDQEEALTMSDRIVVMRDGR 229
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRavvVELIEEAKA----RGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-256 |
5.99e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 110.52 E-value: 5.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQ------DITDVPA--EHRHVNTVFQSYA 103
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAikLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 104 LFPHMTVFENVAFGLRMQKTPAA-EITPRVMDALKMVQL-EEFAQR---KPHQLSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 179 LSALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASF-IGEIN 256
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYvIGRIS 257
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
28-246 |
9.05e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 110.69 E-value: 9.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 28 GKSFDGKTVIsDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT------DVPAEHRHVNTVFQs 101
Cdd:PRK13641 15 GTPMEKKGLD-NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 102 yalFPHMTVFEN-----VAFGLRMQKTPAAEITPRVMDALKMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 175
Cdd:PRK13641 93 ---FPEAQLFENtvlkdVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495142058 176 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNL 246
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWL 239
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-211 |
1.62e-27 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 113.61 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFDG-KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPA-EHRHVNT 97
Cdd:TIGR02868 333 PTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 98 VF-QSYALFpHMTVFENVAFGlRMQKTPAAeitprVMDALKMVQLEEFAQRKPH-----------QLSGGQQQRVAIARA 165
Cdd:TIGR02868 413 VCaQDAHLF-DTTVRENLRLA-RPDATDEE-----LWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495142058 166 VVNKPRLLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHD 211
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
36-230 |
1.75e-27 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 108.33 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 36 VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE--HRHVNTVFQSYALFPHmTVFEN 113
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 114 VAFGLR---MQKTPAAEITPRVMDALKMVQLE--EFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRK 188
Cdd:cd03248 108 IAYGLQscsFECVKEAAQKAHAHSFISELASGydTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495142058 189 QMQnelKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:cd03248 188 QVQ---QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
14-235 |
1.88e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 113.90 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 14 QPRSLSPLLQLADIGKSFDGKT-VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE- 91
Cdd:PRK13657 327 DLGRVKGAVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAs 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 92 -HRHVNTVFQSYALFpHMTVFENvafgLRMQKTPAAEitPRVMDALKMVQLEEFAQRKPH-----------QLSGGQQQR 159
Cdd:PRK13657 407 lRRNIAVVFQDAGLF-NRSIEDN----IRVGRPDATD--EEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495142058 160 VAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVfVTHdQEEALTMSDRIVVMRDGRIEQDGT 235
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFI-IAH-RLSTVRNADRILVFDNGRVVESGS 552
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-241 |
1.89e-27 |
|
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: 113.36 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLEN--ADAGRI--------------------- 78
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 79 -------TLDAQDI-------TDVPAEHRHVNTVFQ-SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEE 143
Cdd:TIGR03269 81 pcpvcggTLEPEEVdfwnlsdKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 144 FAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIV 223
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....*...
gi 495142058 224 VMRDGRIEQDGTPREIYE 241
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVA 258
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-210 |
1.95e-27 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 107.58 E-value: 1.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE-HR------ 93
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyHQdllylg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 94 HVNtvfqsyALFPHMTVFENVAFGLRMQKTPAAEitpRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLL 173
Cdd:PRK13538 81 HQP------GIKTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 495142058 174 LLDESLSALDYKLRKQMQNELKALQRKLGITfVFVTH 210
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQHAEQGGMV-ILTTH 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
11-230 |
2.04e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 113.22 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 11 LNTQPRSLSPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPA 90
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 91 EHRH---VNTVFQSYALFPHMTVFENVAFGLrmqktPAAEITPRVMDALkMVQLEefAQRKPHQLSG----GQQQRVAIA 163
Cdd:PRK15439 81 AKAHqlgIYLVPQEPLLFPNLSVKENILFGL-----PKRQASMQKMKQL-LAALG--CQLDLDSSAGslevADRQIVEIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 164 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-230 |
2.32e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 108.04 E-value: 2.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 18 LSPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH---RH 94
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 95 VNTVFQSYALFPHMTVFENVAF-GLRMQKTPAAEITPRVMDALKMVQlEEFAQRKpHQLSGGQQQRVAIARAVVNKPRLL 173
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMgGFFAERDQFQERIKWVYELFPRLH-ERRIQRA-GTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 174 LLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
9-252 |
2.59e-27 |
|
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: 113.68 E-value: 2.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 9 KKLNTQPRSLSPLLQLADIGKSFD-GKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITD 87
Cdd:TIGR01193 461 KKKRTELNNLNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 88 VP--AEHRHVNTVFQSYALFPHmTVFENvafgLRMQKTPAAEITpRVMDALKMVQLEEFAQRKPH-----------QLSG 154
Cdd:TIGR01193 541 IDrhTLRQFINYLPQEPYIFSG-SILEN----LLLGAKENVSQD-EIWAACEIAEIKDDIENMPLgyqtelseegsSISG 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 155 GQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlgiTFVFVTHDQEEAlTMSDRIVVMRDGRIEQDG 234
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQG 690
|
250
....*....|....*...
gi 495142058 235 TPREIYEEpkNLFVASFI 252
Cdd:TIGR01193 691 SHDELLDR--NGFYASLI 706
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-254 |
2.89e-27 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 108.72 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGKT---------VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT--DVP 89
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 90 AEHRHVNTVFQ--SYALFPHMTVFENVAFGLRMQ-KTPAAEITPRVMDALKMVQL-EEFAQRKPHQLSGGQQQRVAIARA 165
Cdd:PRK15112 84 YRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 166 VVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP-- 243
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPlh 243
|
250
....*....|....
gi 495142058 244 ---KNLfVASFIGE 254
Cdd:PRK15112 244 eltKRL-IAGHFGE 256
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-231 |
4.06e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.47 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 15 PRSLSPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAqditdvpaehrh 94
Cdd:COG0488 309 ERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE------------ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 95 vnTVFQSY------ALFPHMTVFENVAFGLRMQKtpaaEITPRVMdalkmvqLEEF-----AQRKP-HQLSGGQQQRVAI 162
Cdd:COG0488 377 --TVKIGYfdqhqeELDPDKTVLDELRDGAPGGT----EQEVRGY-------LGRFlfsgdDAFKPvGVLSGGEKARLAL 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 163 ARAVVNKPRLLLLDE--------SLSALdyklrkqmqneLKALQRKLGiTFVFVTHDQE--EALTmsDRIVVMRDGRIE 231
Cdd:COG0488 444 AKLLLSPPNVLLLDEptnhldieTLEAL-----------EEALDDFPG-TVLLVSHDRYflDRVA--TRILEFEDGGVR 508
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-240 |
4.78e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 108.17 E-value: 4.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT----DVPAEHRHVN 96
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 97 TVFQSyalfPHMTVF-----ENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPR 171
Cdd:PRK13638 81 TVFQD----PEQQIFytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 172 LLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIY 240
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
32-183 |
1.13e-26 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 105.13 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE-HRHVNTVFQSYALFPHMTV 110
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495142058 111 FENVAFGLRMQKTPAAEItprvMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 183
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-235 |
1.37e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.07 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 12 NTQPRSLSPLLQLADIGKSFDGKT--VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVP 89
Cdd:PRK11160 329 TSTAAADQVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 90 --AEHRHVNTVFQSYALFPHmTVFENvafgLRMQKTPAAEitPRVMDALKMVQLEEFAQRKP----------HQLSGGQQ 157
Cdd:PRK11160 409 eaALRQAISVVSQRVHLFSA-TLRDN----LLLAAPNASD--EALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 158 QRVAIARAVVNKPRLLLLDESLSALDYKLRKQ-MQNELKALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 235
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQiLELLAEHAQNK---TVLMITH-RLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-239 |
2.65e-26 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 106.03 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 14 QPRSLSPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT--DVPAE 91
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 92 HRHVNTVFQSYALFPHMTVFENVAFGlrmqKTP--------AAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIA 163
Cdd:PRK10575 84 ARKVAYLPQQLPAAEGMTVRELVAIG----RYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495142058 164 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
30-247 |
2.99e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 110.32 E-value: 2.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 30 SFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADaGRITLDAQDITDVPAEH--RHVNTVFQSYALFpH 107
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESwrKHLSWVGQNPQLP-H 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 108 MTVFENVAFGlrmqktpAAEITP-RVMDALKMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLL 175
Cdd:PRK11174 437 GTLRDNVLLG-------NPDASDeQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 176 DESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPkNLF 247
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAASR--RQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG-GLF 577
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-229 |
4.37e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 109.25 E-value: 4.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGL--ENADAGRI-----TLDAQDITDvpAE 91
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIifegeELQASNIRD--TE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 92 HRHVNTVFQSYALFPHMTVFENVAFGlrmqktpaAEITPR-VMDALKM----------VQLEEFAQRKPHQLSGGQQQRV 160
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLG--------NEITPGgIMDYDAMylraqkllaqLKLDINPATPVGNLGLGQQQLV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 161 AIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 229
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
22-229 |
1.18e-25 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 100.60 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITldaqditdvpaehrhvntvfqs 101
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 102 yalfphmtvfenvafglrmqktpaaeitprVMDALKMVQLEefaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 181
Cdd:cd03221 59 ------------------------------WGSTVKIGYFE--------QLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495142058 182 LDYKLRKQMQNELKALQRklgiTFVFVTHDQEEALTMSDRIVVMRDGR 229
Cdd:cd03221 101 LDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-235 |
1.23e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 108.25 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSF----DGKTVISDFSLTINHGEFLTLLGPSGCGKT----TVLRLIAGLENA-DAGRITLDAQDITDVP 89
Cdd:PRK15134 3 QPLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 90 -AEHRHVN-----TVFQS--YALFPHMTV----FENVAFGLRMQKTPA-AEItprvMDALKMVQLEEFAQRK---PHQLS 153
Cdd:PRK15134 83 eQTLRGVRgnkiaMIFQEpmVSLNPLHTLekqlYEVLSLHRGMRREAArGEI----LNCLDRVGIRQAAKRLtdyPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 154 GGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR-IEQ 232
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRcVEQ 238
|
...
gi 495142058 233 DGT 235
Cdd:PRK15134 239 NRA 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-229 |
1.39e-25 |
|
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: 107.60 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGL--ENADAGRI-----TLDAQDITDvpAEHR 93
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIywsgsPLKASNIRD--TERA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 94 HVNTVFQSYALFPHMTVFENVAFG----LRMQKTPAAEITPRVMDALKMVQLEEFAQRKP-HQLSGGQQQRVAIARAVVN 168
Cdd:TIGR02633 79 GIVIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495142058 169 KPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 229
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
30-225 |
1.52e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.93 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 30 SFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAqditdvpaeHRHVNTVFQSYAL---FP 106
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 107 hMTVFENVAFGL----RMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 182
Cdd:NF040873 72 -LTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495142058 183 DYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTmSDRIVVM 225
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
34-239 |
2.69e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 103.14 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH--RHVNTVFQSYALFPHMTVF 111
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 112 ENVAFGlRMQKTPA-----AEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 186
Cdd:PRK10253 100 ELVARG-RYPHQPLftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495142058 187 RKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:PRK10253 179 QIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
18-251 |
2.72e-25 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 102.88 E-value: 2.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 18 LSPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQ-DITDVPaehrhvn 96
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlRIGYVP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 97 tvfQSYALFPHMTVfeNVAFGLRMQK-TPAAEITPrvmdALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 175
Cdd:PRK09544 74 ---QKLYLDTTLPL--TVNRFLRLRPgTKKEDILP----ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495142058 176 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMrDGRIEQDGTPREIYEEPKnlFVASF 251
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE--FISMF 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
37-246 |
4.23e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 103.32 E-value: 4.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 37 ISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE------HRHVNTVFQsyalFPHMTV 110
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyirpvRKRIGMVFQ----FPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 111 FEN-----VAFGLRMQKTPAAEITPRVMDALKMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 184
Cdd:PRK13646 99 FEDtvereIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 185 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNL 246
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
40-246 |
5.45e-25 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 101.84 E-value: 5.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 40 FSLTINHGEFLTLLGPSGCGKTTVLRLIAGLEnADAGRITLDAQDITDVPAEH-RHVNTVF--QSYALFPhMTVFENVAF 116
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAElARHRAYLsqQQSPPFA-MPVFQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 117 GLRmQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAV------VN-KPRLLLLDESLSALDYklrkQ 189
Cdd:COG4138 93 HQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLDEPMNSLDV----A 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 190 MQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYeEPKNL 246
Cdd:COG4138 168 QQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPENL 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
32-183 |
8.47e-25 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 100.26 E-value: 8.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDV-PAEHRHVNTVFQSYALFPHMTV 110
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQrDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495142058 111 FENVAFGLRMQKTPAaeitprVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 183
Cdd:cd03231 91 LENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
33-183 |
9.04e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 100.33 E-value: 9.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 33 GKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITD-VPAEHRHvntvfqsY-----ALFP 106
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpDVAEACH-------YlghrnAMKP 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 107 HMTVFENVAFGLRMQKTPAAEItprvMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 183
Cdd:PRK13539 87 ALTVAENLEFWAAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
22-234 |
1.20e-24 |
|
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: 99.31 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDG--KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRHVNTVF 99
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 100 -QSYALFpHMTVFENVafGLRmqktpaaeitprvmdalkmvqleefaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:cd03247 81 nQRPYLF-DTTLRNNL--GRR--------------------------------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 179 LSALDYKLRKQMQNEL-KALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 234
Cdd:cd03247 126 TVGLDPITERQLLSLIfEVLKDK---TLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
41-244 |
1.29e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 102.90 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 41 SLTINHGEFLTLLGPSGCGKTTVLRLIAGLEN----ADAGRITLDAQDITDVPAEHRH------VNTVFQS--YALFPHM 108
Cdd:PRK11022 27 SYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRnlvgaeVAMIFQDpmTSLNPCY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 109 TVFENVAFGLRM-QKTPAAEITPRVMDALKMVQLEEFAQR---KPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 184
Cdd:PRK11022 107 TVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDV 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 185 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 244
Cdd:PRK11022 187 TIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPR 246
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
26-230 |
2.95e-24 |
|
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: 98.39 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 26 DIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLEN--ADAGRITLDAQDITDvPAEHRHVNTVFQSYA 103
Cdd:cd03213 14 KSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDK-RSFRKIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 104 LFPHMTVFENVAFGLRMQktpaaeitprvmdalkmvqleefaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 183
Cdd:cd03213 93 LHPTLTVRETLMFAAKLR-----------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495142058 184 YKLRKQMQNELKALqRKLGITFVFVTHD-QEEALTMSDRIVVMRDGRI 230
Cdd:cd03213 144 SSSALQVMSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
39-242 |
3.05e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 100.96 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 39 DFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE------HRHVNTVFQsyalFPHMTVFE 112
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpvRKKVGVVFQ----FPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 113 -----NVAFGLRMQKTPAAEITPRVMDALKMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 186
Cdd:PRK13643 100 etvlkDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495142058 187 RKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:PRK13643 180 RIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
32-210 |
7.22e-24 |
|
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: 96.45 E-value: 7.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLdaqditdvpaeHRHVNTVF---QSYalFPHM 108
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGEDLLFlpqRPY--LPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 109 TvfenvafgLRmqktpaaeitprvmDALkmvqleefaqRKP--HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDykl 186
Cdd:cd03223 79 T--------LR--------------EQL----------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD--- 123
|
170 180
....*....|....*....|....
gi 495142058 187 rKQMQNELKALQRKLGITFVFVTH 210
Cdd:cd03223 124 -EESEDRLYQLLKELGITVISVGH 146
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
36-230 |
1.77e-23 |
|
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: 97.34 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 36 VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAG-LENADA--GRITLDAQDITdvPAE-HRHVNTVFQSYALFPHMTVF 111
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGTtsGQILFNGQPRK--PDQfQKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 112 ENVAFG--LRMQ-KTPAAEITPRVMD-ALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 187
Cdd:cd03234 100 ETLTYTaiLRLPrKSSDAIRKKRVEDvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495142058 188 KQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:cd03234 180 LNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
37-255 |
1.86e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 102.24 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 37 ISDFSLTINHGEFLTLLGPSGCGKT-TVLRLIAGLENADA------------GRITLDAQDITDvpAEHRHVN-----TV 98
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGlvqcdkmllrrrSRQVIELSEQSA--AQMRHVRgadmaMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 99 FQS--YALFPHMTVFENVAFGLRMQ----KTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRL 172
Cdd:PRK10261 110 FQEpmTSLNPVFTVGEQIAESIRLHqgasREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 173 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVASFI 252
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALL 269
|
...
gi 495142058 253 GEI 255
Cdd:PRK10261 270 AAV 272
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
29-229 |
2.84e-23 |
|
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: 96.00 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 29 KSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLdaqditdvpaeHRHVNTVFQSYALFPhM 108
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-----------PGSIAYVSQEPWIQN-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 109 TVFENVAFGLRMQKtpaaeitPRVMDALKMVQLEEFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:cd03250 81 TIRENILFGKPFDE-------ERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495142058 178 SLSALDYKLRKQ-MQNELKALqRKLGITFVFVTHdQEEALTMSDRIVVMRDGR 229
Cdd:cd03250 154 PLSAVDAHVGRHiFENCILGL-LLNNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-230 |
4.13e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.48 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGksfdGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT-----D------- 87
Cdd:COG1129 255 VVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprDairagia 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 88 -VPaEHRHvntvfqSYALFPHMTVFENVAF--------GLRMQKTPAAEITPRVMDAL--KMVQLEEFAQrkphQLSGGQ 156
Cdd:COG1129 331 yVP-EDRK------GEGLVLDLSIRENITLasldrlsrGGLLDRRRERALAEEYIKRLriKTPSPEQPVG----NLSGGN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 157 QQRVAIARAVVNKPRLLLLDESLSALD-------YKLrkqMqNELKAlqRKLGItfVFVTHDQEEALTMSDRIVVMRDGR 229
Cdd:COG1129 400 QQKVVLAKWLATDPKVLILDEPTRGIDvgakaeiYRL---I-RELAA--EGKAV--IVISSELPELLGLSDRILVMREGR 471
|
.
gi 495142058 230 I 230
Cdd:COG1129 472 I 472
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
34-234 |
1.33e-22 |
|
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: 95.09 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHRH-VNTVF-QSYALFPHMTVF 111
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRrIGVVFgQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 112 ENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ 191
Cdd:cd03267 114 DSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495142058 192 NELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 234
Cdd:cd03267 194 NFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
37-220 |
1.93e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 95.23 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 37 ISDFSLTINHGEFLTLLGPSGCGKTTVLR-------LIAGLEnADaGRITLDAQDITDV---PAE-HRHVNTVFQSYALF 105
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR-VE-GKVTFHGKNLYAPdvdPVEvRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 106 PHmTVFENVAFGLRMQ--KTPAAEITPRvmdALKMVQLEEFAQRKPHQ----LSGGQQQRVAIARAVVNKPRLLLLDESL 179
Cdd:PRK14243 104 PK-SIYDNIAYGARINgyKGDMDELVER---SLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495142058 180 SALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSD 220
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
9-243 |
4.09e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.69 E-value: 4.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 9 KKLNTQPRSLSP--LLQLADIGKSFDGKT-----VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITL- 80
Cdd:PRK13631 7 KKKLKVPNPLSDdiILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 81 -----------------DAQDITDVPAEHRHVNTVFQ--SYALFPHmTVFENVAFG---LRMQKTPAAEITPRVMDalKM 138
Cdd:PRK13631 87 diyigdkknnhelitnpYSKKIKNFKELRRRVSMVFQfpEYQLFKD-TIEKDIMFGpvaLGVKKSEAKKLAKFYLN--KM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 139 VQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQnELKALQRKLGITFVFVTHDQEEALTM 218
Cdd:PRK13631 164 GLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMM-QLILDAKANNKTVFVITHTMEHVLEV 242
|
250 260
....*....|....*....|....*
gi 495142058 219 SDRIVVMRDGRIEQDGTPREIYEEP 243
Cdd:PRK13631 243 ADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
32-236 |
5.86e-22 |
|
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: 92.94 E-value: 5.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTV----LRLIagleNADAGRITLDAQDITDVPAE--HRHVNTVFQSYALF 105
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHdlRSRISIIPQDPVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 106 PHmTVFENVA-FGlrmQKTPAAeitprVMDALKMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKPRLL 173
Cdd:cd03244 91 SG-TIRSNLDpFG---EYSDEE-----LWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142058 174 LLDESLSALDYKLRKQMQnelKALQRKL-GITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTP 236
Cdd:cd03244 162 VLDEATASVDPETDALIQ---KTIREAFkDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-242 |
7.40e-22 |
|
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: 92.20 E-value: 7.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLEN--ADAGRITLDAQDITDVPAEHRHVNTVF 99
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 100 qsyalfphmtvfenvafgLRMQKTPaaEITprvmdalkMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 179
Cdd:cd03217 81 ------------------LAFQYPP--EIP--------GVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142058 180 SALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTM-SDRIVVMRDGRIEQDGtPREIYEE 242
Cdd:cd03217 133 SGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-211 |
7.55e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 7.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 24 LADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLdAQDITdvpaehrhVNTVFQSYA 103
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGLR--------IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 104 LFPHMTVFENVAFGLR------------MQKTPAAEITPRVMDAL--KMVQL-------------------EEFAQRKPH 150
Cdd:COG0488 72 LDDDLTVLDTVLDGDAelraleaeleelEAKLAEPDEDLERLAELqeEFEALggweaearaeeilsglgfpEEDLDRPVS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495142058 151 QLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQrklgITFVFVTHD 211
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP----GTVLVVSHD 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-229 |
1.04e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.52 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQditdvpaEHRHVNT- 97
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-------EMRFASTt 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 98 ---------VFQSYALFPHMTVFENV-------AFGLRMQKTPAAeitpRVMDALKMVQLEEFAQRKPHQLSGGQQQRVA 161
Cdd:PRK11288 75 aalaagvaiIYQELHLVPEMTVAENLylgqlphKGGIVNRRLLNY----EAREQLEHLGVDIDPDTPLKYLSIGQRQMVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495142058 162 IARAVVNKPRLLLLDE---SLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQEEALTMSDRIVVMRDGR 229
Cdd:PRK11288 151 IAKALARNARVIAFDEptsSLSAREIEQLFRVIRELRAEGRVI----LYVSHRMEEIFALCDAITVFKDGR 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-230 |
1.45e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.86 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIG-KSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITD----------- 87
Cdd:COG3845 256 VVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGlsprerrrlgv 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 88 --VPAEhRHvntvfqSYALFPHMTVFENVAFGLRMQKtpaaEITPRVMdaLKMVQLEEFAQRK----------PHQ---- 151
Cdd:COG3845 336 ayIPED-RL------GRGLVPDMSVAENLILGRYRRP----PFSRGGF--LDRKAIRAFAEELieefdvrtpgPDTpars 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 152 LSGGQQQRVAIARAVVNKPRLLL-------LDESLSAldyklrkQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVV 224
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIaaqptrgLDVGAIE-------FIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAV 474
|
....*.
gi 495142058 225 MRDGRI 230
Cdd:COG3845 475 MYEGRI 480
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
30-242 |
1.57e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 96.24 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 30 SFDGKTV--ISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITD--VPAEHRHVNTVFQSYALF 105
Cdd:PRK11176 350 TYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLASLRNQVALVSQNVHLF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 106 pHMTVFENVAFGlRMQKTPAAEITprvmDALKMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLL 174
Cdd:PRK11176 430 -NDTIANNIAYA-RTEQYSREQIE----EAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILI 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495142058 175 LDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:PRK11176 504 LDEATSALDTESERAIQAALDELQKNR--TSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-183 |
2.43e-21 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 91.06 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 15 PRSLSPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDvpAEH-R 93
Cdd:PRK13543 5 LHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR--GDRsR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 94 HVNTVFQSYALFPHMTVFENVAF-----GLRMQKTPAaeitprvmDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 168
Cdd:PRK13543 83 FMAYLGHLPGLKADLSTLENLHFlcglhGRRAKQMPG--------SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLS 154
|
170
....*....|....*
gi 495142058 169 KPRLLLLDESLSALD 183
Cdd:PRK13543 155 PAPLWLLDEPYANLD 169
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
32-239 |
1.86e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 89.89 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADA--------GRITLDAQDITDVPAEH---RHVNTVFQ 100
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRlarLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 101 SYALFPhMTVFENVAFGLRMQKTPAAEITPRVMD----ALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN-------- 168
Cdd:PRK13547 92 AQPAFA-FSAREIVLLGRYPHARRAGALTHRDGEiawqALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaa 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 169 -KPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:PRK13547 171 qPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-236 |
2.99e-20 |
|
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: 93.15 E-value: 2.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 18 LSPLLQLADIGKSFD--GKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDI-TDVPAEHRH 94
Cdd:TIGR01257 925 LVPGVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 95 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 174
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 175 LDESLSALDYKLRKQMQNELkaLQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 236
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
35-242 |
3.07e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 92.49 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 35 TVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITL-----DAQDItdvpAEHRHVNTVFQSYALFPHMT 109
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDI----ATRRRVGYMSQAFSLYGELT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 110 VFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQ 189
Cdd:NF033858 356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495142058 190 MQNELKALQRKLGITfVFV-THDQEEALTmSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:NF033858 436 FWRLLIELSREDGVT-IFIsTHFMNEAER-CDRISLMHAGRVLASDTPAALVAA 487
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-236 |
3.19e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.59 E-value: 3.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 22 LQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLEN--ADAGRITLDAQDITDVPAEHRH---VN 96
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERAragIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 97 TVFQSYALFPHMTV--FENVAFGLRMQKT-PAAEITPRVMDALKMVQL-EEFAQRKPHQ-LSGGQQQRVAIARAVVNKPR 171
Cdd:COG0396 81 LAFQYPVEIPGVSVsnFLRTALNARRGEElSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 172 LLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHdQEEALTM--SDRIVVMRDGRIEQDGTP 236
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITH-YQRILDYikPDFVHVLVDGRIVKSGGK 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-272 |
7.10e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 7.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQD---ITDVPAEHRHVN 96
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 97 TVFQSYALFPHMTVFENVAFG--------------LRMQKTPAAEITPRVmdALKmVQLEEFAQrkphQLSGGQQQRVAI 162
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGrhltkkvcgvniidWREMRVRAAMMLLRV--GLK-VDLDEKVA----NLSISHKQMLEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 163 ARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDG-----RIEQDGTPR 237
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGssvcsGMVSDVSND 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 495142058 238 EIY-----EEPKNLFVA-----SFIGEINIFDATVIERIDAQRVR 272
Cdd:PRK09700 236 DIVrlmvgRELQNRFNAmkenvSNLAHETVFEVRNVTSRDRKKVR 280
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-284 |
1.58e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 90.06 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT-DVPAEHRH--V 95
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEagI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 96 NTVFQSYALFPHMTVFENVAFGlRMQKTPAAEITPRVMDA-----LKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 170
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLG-REFVNRFGRIDWKKMYAeadklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 171 RLLLLDESLSAL-DYKLRK--QMQNELKALQRklGItfVFVTHDQEEALTMSDRIVVMRDGRieqdgtpreiyeepknlf 247
Cdd:PRK10762 161 KVIIMDEPTDALtDTETESlfRVIRELKSQGR--GI--VYISHRLKEIFEICDDVTVFRDGQ------------------ 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 495142058 248 vasFIGEINIFDAT---VIE-----RIDAQRVRANVEGRECVLYV 284
Cdd:PRK10762 219 ---FIAEREVADLTedsLIEmmvgrKLEDQYPRLDKAPGEVRLKV 260
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
32-243 |
1.70e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 88.42 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISD-FSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENAD----AGRITLDAQDITDVPAEHRH------VNTVFQ 100
Cdd:COG4170 17 QGRVKAVDrVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRERRkiigreIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 101 --SYALFPHMTVFENVafglrMQKTPAAEITPRVMDalkmvqleEFAQRK----------------------PHQLSGGQ 156
Cdd:COG4170 97 epSSCLDPSAKIGDQL-----IEAIPSWTFKGKWWQ--------RFKWRKkraiellhrvgikdhkdimnsyPHELTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 157 QQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 236
Cdd:COG4170 164 CQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPT 243
|
....*..
gi 495142058 237 REIYEEP 243
Cdd:COG4170 244 EQILKSP 250
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
37-230 |
2.29e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.29 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 37 ISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDI-TDVPAEHRHVNTVFQSY-----ALFPHMTV 110
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANGIVYISEdrkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 111 FENVA------FGLRMQKTPAAEITPRVMDALKMvqleeFAQRKPHQ------LSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:PRK10762 348 KENMSltalryFSRAGGSLKHADEQQAVSDFIRL-----FNIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495142058 179 LSALDYKLRK---QMQNELKAlqrkLGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:PRK10762 423 TRGVDVGAKKeiyQLINQFKA----EGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-213 |
2.47e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 85.78 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 3 FLRDRVKKLNTQPRSLSP----LLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLEnadAGRI 78
Cdd:COG2401 8 FVLMRVTKVYSSVLDLSErvaiVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL---KGTP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 79 TLDAQDITDVPaehrhvntvfqsyaLFPHMTVFENVAfglRMQKTPAAeitprvMDALKMVQLEE--FAQRKPHQLSGGQ 156
Cdd:COG2401 85 VAGCVDVPDNQ--------------FGREASLIDAIG---RKGDFKDA------VELLNAVGLSDavLWLRRFKELSTGQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495142058 157 QQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQE 213
Cdd:COG2401 142 KFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
40-243 |
3.51e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 85.75 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 40 FSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENAdAGRITLDAQDITDVP----AEHR-----HVNTVFQsyalfphMTV 110
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSaaelARHRaylsqQQTPPFA-------MPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 111 FENVAFGLRmQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIArAVV------NKP--RLLLLDESLSAL 182
Cdd:PRK03695 87 FQYLTLHQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLA-AVVlqvwpdINPagQLLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495142058 183 DYKLRKQMQNELKALQRkLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 243
Cdd:PRK03695 165 DVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
27-230 |
4.00e-19 |
|
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: 84.62 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 27 IGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADA---GRITLDAQDITDVPAEHRHvNTVF--QS 101
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPG-EIIYvsEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 102 YALFPHMTVFENVAFGLRMQktpaaeitprvmdALKMVqleefaqRKphqLSGGQQQRVAIARAVVNKPRLLLLDESLSA 181
Cdd:cd03233 92 DVHFPTLTVRETLDFALRCK-------------GNEFV-------RG---ISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495142058 182 LDYKLRKQMQNELKALQRKLGIT-FVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:cd03233 149 LDSSTALEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
37-244 |
4.19e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.91 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 37 ISDFSLTINHGEFLTLLGPSGCGKT-TVLRLI----AGLeNADAGRITLDAQDITDVPAEHRHVNTVFQS--YALFPHMT 109
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAGV-RQTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 110 VFENVAFGLRMQKTPAAEitPRVMDALKMVQLEE---FAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 186
Cdd:PRK10418 98 MHTHARETCLALGKPADD--ATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495142058 187 RKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 244
Cdd:PRK10418 176 QARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
34-243 |
1.29e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 87.46 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH--RHVNTVFQSYALFPHmTVF 111
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 112 ENVAFGlRMQKTP-----AAEITPRVMDALKMVQ--LEEFAQRKPhQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 184
Cdd:PRK10789 407 NNIALG-RPDATQqeiehVARLASVHDDILRLPQgyDTEVGERGV-MLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 185 KLRKQMQNELKalQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 243
Cdd:PRK10789 485 RTEHQILHNLR--QWGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
41-238 |
1.35e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 87.33 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 41 SLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDV-PAEHR-HVNTVFQSYALFPHMTVFENvafgl 118
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEqPEDYRkLFSAVFTDFHLFDQLLGPEG----- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 119 rmqKTPAAEITPRVMDALKM---VQLEEFAQRKPhQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELK 195
Cdd:PRK10522 418 ---KPANPALVEKWLERLKMahkLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLL 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495142058 196 ALQRKLGITFVFVTHDqEEALTMSDRIVVMRDGRI-EQDGTPRE 238
Cdd:PRK10522 494 PLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLsELTGEERD 536
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
34-309 |
4.95e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.98 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQditdVPAEHRHVN-----TVF-QSYALFPH 107
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY----VPFKRRKEFarrigVVFgQRSQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 108 MTVFENvaFGL--RMQKTPAAEITPRvMDAL-KMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 184
Cdd:COG4586 111 LPAIDS--FRLlkAIYRIPDAEYKKR-LDELvELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 185 KLRKQMQNELKALQRKLGITFVFVTHDQE--EALtmSDRIVVMRDGRIEQDGTPREIYE--EPKNLFVASFIGEINIFD- 259
Cdd:COG4586 188 VSKEAIREFLKEYNRERGTTILLTSHDMDdiEAL--CDRVIVIDHGRIIYDGSLEELKErfGPYKTIVLELAEPVPPLEl 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 495142058 260 ---ATVIERidaqrvranvEGRECVLYVAFPVTAGQKLNVLLR---PEDLRVEEIN 309
Cdd:COG4586 266 prgGEVIER----------EGNRVRLEVDPRESLAEVLARLLArypVRDLTIEEPP 311
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-220 |
9.51e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 80.76 E-value: 9.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDI-TDVPAEHRHVNTVF 99
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 100 QSYALFPHMTVFENVAFGLRMQKTpAAEITprvmDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 179
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDIHFSPG-AVGIT----ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495142058 180 SALDYKLRKQMQNELKALQRKLGItfVFVTHDQEEALTMSD 220
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKGGA--VLLTSHQDLPLNKAD 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
34-238 |
1.70e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.94 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENAD---AGRITLDAQDItDVPAEHRHVNTVFQSYALFPHMTV 110
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI-DAKEMRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 111 FENVAFG--LRMQK-TPAAEITPRVMDALKMVQLEEFAQRK---PHQ---LSGGQQQRVAIARAVVNKPRLLLLDESLSA 181
Cdd:TIGR00955 117 REHLMFQahLRMPRrVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495142058 182 LDYKLRKQMQNELKALQRKlGITFVFVTHD-QEEALTMSDRIVVMRDGRIEQDGTPRE 238
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
32-242 |
3.43e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 83.23 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVP--AEHRHVNTVFQSYALFPHmT 109
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsVLRQGVAMVQQDPVVLAD-T 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 110 VFENVAFGLRMQKTpaaeitpRVMDALKMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:PRK10790 431 FLANVTLGRDISEE-------QVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142058 179 LSALDYKLRKQMQNELKALQRKlgITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREH--TTLVVIAH-RLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-235 |
3.63e-17 |
|
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: 83.52 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGKT--VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDI-TDVPAEHRHVNT 97
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 98 VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 177
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495142058 178 SLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 235
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
7-229 |
4.73e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 82.62 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 7 RVKKLNTQPRS--LSPLL----QLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITL 80
Cdd:PLN03211 48 RVKFENMKNKGsnIKRILghkpKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 81 DAQDITDVPAEHRHVNTVFQSYALFPHMTVFENVAFG--LRMQKTPAAEITPRVMDALkmvqLEEFAQRKPHQ------- 151
Cdd:PLN03211 128 LANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCslLRLPKSLTKQEKILVAESV----ISELGLTKCENtiignsf 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 152 ---LSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHD-QEEALTMSDRIVVMRD 227
Cdd:PLN03211 204 irgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSE 282
|
..
gi 495142058 228 GR 229
Cdd:PLN03211 283 GR 284
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
33-228 |
6.38e-17 |
|
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: 78.91 E-value: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 33 GKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRI-----TLDAQDITDVPAEHRHVNTVFQSYALFPH 107
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 108 MTVFENVAFGLRMQK------TPAAEITPRVmDALKMVQLEEFAQRKPHqLSGGQQQRVAIARAVVNKPRLLLLDESLSA 181
Cdd:cd03290 93 ATVEENITFGSPFNKqrykavTDACSLQPDI-DLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495142058 182 LDYKLRKQMQNE--LKALQRKlGITFVFVTHdQEEALTMSDRIVVMRDG 228
Cdd:cd03290 171 LDIHLSDHLMQEgiLKFLQDD-KRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
74-239 |
8.17e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 82.38 E-value: 8.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 74 DAGRITLDAQDITDVPAEH-RHVNTVFQSYALFPHMTVFENVAFGlrmQKTPAAEITPRvmdALKMVQLEEFAQRKPHQ- 151
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG---KEDATREDVKR---ACKFAAIDEFIESLPNKy 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 152 ----------LSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHdQEEALTMSDR 221
Cdd:PTZ00265 1349 dtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427
|
170 180
....*....|....*....|...
gi 495142058 222 IVVM----RDGR-IEQDGTPREI 239
Cdd:PTZ00265 1428 IVVFnnpdRTGSfVQAHGTHEEL 1450
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-230 |
1.28e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 81.25 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADI-GKSFdgktviSDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDV-PAEHRHVNT 97
Cdd:PRK15439 267 PVLTVEDLtGEGF------RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALsTAQRLARGL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 98 VF-----QSYALFPHMTVFENVA------FGLRMQKTPAAEITPRVMDAL--KMVQLEEFAQRkphqLSGGQQQRVAIAR 164
Cdd:PRK15439 341 VYlpedrQSSGLYLDAPLAWNVCalthnrRGFWIKPARENAVLERYRRALniKFNHAEQAART----LSGGNQQKVLIAK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495142058 165 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:PRK15439 417 CLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-231 |
1.61e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 80.99 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENAD--AGRITLDAQ-----DITDvpAEHR 93
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEvcrfkDIRD--SEAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 94 HVNTVFQSYALFPHMTVFENVAFGLRMQKTPA---AEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 170
Cdd:NF040905 79 GIVIIHQELALIPYLSIAENIFLGNERAKRGVidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 171 RLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGR-IE 231
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRtIE 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
36-236 |
1.09e-15 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 75.14 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 36 VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEhrhvnTVFQSYALFPH-MTVFENV 114
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE-----DLRSSLTIIPQdPTLFSGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 115 afgLRMQKTPAAEITPR-VMDALKMVQLEEfaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY----KLRKQ 189
Cdd:cd03369 98 ---IRSNLDPFDEYSDEeIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYatdaLIQKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495142058 190 MQNELKalqrklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTP 236
Cdd:cd03369 168 IREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-230 |
1.25e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.03 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 14 QPRSLSP-LLQLADIgksfDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDIT-DVPAE 91
Cdd:PRK11288 249 RPRPLGEvRLRLDGL----KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRD 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 92 HRHVNTVF-----QSYALFPHMTVFENVAFGLRMQKTPAAE-ITPRVMDALKMVQLEEFAQRKPH------QLSGGQQQR 159
Cdd:PRK11288 325 AIRAGIMLcpedrKAEGIIPVHSVADNINISARRHHLRAGClINNRWEAENADRFIRSLNIKTPSreqlimNLSGGNQQK 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495142058 160 VAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:PRK11288 405 AILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-211 |
1.62e-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: 78.05 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 15 PRSLSPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLdaqditdvpAEHRH 94
Cdd:TIGR03719 316 PRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI---------GETVK 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 95 VNTVFQSY-ALFPHMTVFENVAFGLRMQKTPAAEITPRVMdalkmvqLEEFA------QRKPHQLSGGQQQRVAIARAVV 167
Cdd:TIGR03719 387 LAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAY-------VGRFNfkgsdqQKKVGQLSGGERNRVHLAKTLK 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495142058 168 NKPRLLLLDESLSALDYklrkqmqNELKALQRKL----GITFVfVTHD 211
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDV-------ETLRALEEALlnfaGCAVV-ISHD 499
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
34-279 |
2.70e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.90 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRItLDAQDITDVPAEHRHVNTVFQSYALFphmtvFEN 113
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSIAYVPQQAWIMNATVRGNILF-----FDE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 114 vafglrmqktpaaEITPRVMDALKMVQLE-EFAQ----------RKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 182
Cdd:PTZ00243 747 -------------EDAARLADAVRVSQLEaDLAQlgggleteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 183 DYKLRKQMQNELkALQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEqdgtpreiyeepknlfvasFIGEINIFDATV 262
Cdd:PTZ00243 814 DAHVGERVVEEC-FLGALAGKTRVLATH-QVHVVPRADYVVALGDGRVE-------------------FSGSSADFMRTS 872
|
250
....*....|....*..
gi 495142058 263 IERIDAQRVRANVEGRE 279
Cdd:PTZ00243 873 LYATLAAELKENKDSKE 889
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-224 |
3.85e-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: 74.37 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 39 DFSL-----TINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPaehRHVNTVFQsyalfphMTVFEn 113
Cdd:cd03237 12 EFTLeveggSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP---QYIKADYE-------GTVRD- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 114 vafgLRMQKTPAAEITPRV-MDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQN 192
Cdd:cd03237 81 ----LLSSITKDFYTHPYFkTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|..
gi 495142058 193 ELKALQRKLGITFVFVTHDQEEALTMSDRIVV 224
Cdd:cd03237 157 VIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-235 |
5.01e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 74.29 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 19 SPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLE--NADAGRITLDAQDITDVPAE---HR 93
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEeraHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 94 HVNTVFQSYALFPHMTV--FENVAFGLRMQKTPAAEITPR-----VMDALKMVQLEE-FAQRKPHQ-LSGGQQQRVAIAR 164
Cdd:CHL00131 85 GIFLAFQYPIEIPGVSNadFLRLAYNSKRKFQGLPELDPLefleiINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495142058 165 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEealtMSDRIV-----VMRDGRIEQDGT 235
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQR----LLDYIKpdyvhVMQNGKIIKTGD 235
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
33-210 |
5.58e-15 |
|
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: 76.33 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 33 GKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDA-QDITDVPAEHRHVNTVFQSYALFPhMTVF 111
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAkGKLFYVPQRPYMTLGTLRDQIIYP-DSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 112 ENVAFGLRMQKtpaaeitprVMDALKMVQLEEFAQRK---------PHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 182
Cdd:TIGR00954 543 DMKRRGLSDKD---------LEQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170 180
....*....|....*....|....*...
gi 495142058 183 DYKLRKQMQNelkaLQRKLGITFVFVTH 210
Cdd:TIGR00954 614 SVDVEGYMYR----LCREFGITLFSVSH 637
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-230 |
7.37e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 76.30 E-value: 7.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDgktVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIA----GLENADAGRITLDAQDITDVpAEHRHVN 96
Cdd:TIGR00956 64 KLKKFRDTKTFD---ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEI-KKHYRGD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 97 TVFQSYA--LFPHMTVFENVAFGLRMqKTPAAEItprvmdalKMVQLEEFAQRKPH----------------------QL 152
Cdd:TIGR00956 140 VVYNAETdvHFPHLTVGETLDFAARC-KTPQNRP--------DGVSREEYAKHIADvymatyglshtrntkvgndfvrGV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 153 SGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITfVFVTHDQ--EEALTMSDRIVVMRDGRI 230
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTT-PLVAIYQcsQDAYELFDKVIVLYEGYQ 289
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-242 |
1.79e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.16 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 33 GKTV-ISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDItdvpAEHRHVNTVFQSYA-------- 103
Cdd:NF033858 12 GKTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM----ADARHRRAVCPRIAympqglgk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 104 -LFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 182
Cdd:NF033858 88 nLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495142058 183 DYKLRKQ---MQNELKAlqRKLGITFVFVTHDQEEALTMsDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:NF033858 168 DPLSRRQfweLIDRIRA--ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLAR 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-241 |
3.10e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.63 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 30 SFDGKT---VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAG-LENADAGRItldaqDITDVPAEHRHVNTVFQSyalf 105
Cdd:PLN03232 623 SWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSV-----VIRGSVAYVPQVSWIFNA---- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 106 phmTVFENVAFGLRMQKT---PAAEITP--RVMDALKMVQLEEFAQRKPHqLSGGQQQRVAIARAVVNKPRLLLLDESLS 180
Cdd:PLN03232 694 ---TVRENILFGSDFESErywRAIDVTAlqHDLDLLPGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495142058 181 ALDYKLRKQ-----MQNELKalqrklGITFVFVThDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 241
Cdd:PLN03232 770 ALDAHVAHQvfdscMKDELK------GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-242 |
1.18e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 72.23 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 3 FLR-DRVKKLNTQPrslsplLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLd 81
Cdd:PRK15064 306 FIRfEQDKKLHRNA------LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 82 aqditdvpAEHRHVNTVFQ-SYALFPH-MTVFENVAfglrmQKTPAAEITPRVMDAL-KMVQLEEFAQRKPHQLSGGQQQ 158
Cdd:PRK15064 379 --------SENANIGYYAQdHAYDFENdLTLFDWMS-----QWRQEGDDEQAVRGTLgRLLFSQDDIKKSVKVLSGGEKG 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 159 RVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQrklGiTFVFVTHDQEEALTMSDRIVVMRDGRIEQ-DGTpr 237
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYE---G-TLIFVSHDREFVSSLATRIIEITPDGVVDfSGT-- 519
|
....*
gi 495142058 238 eiYEE 242
Cdd:PRK15064 520 --YEE 522
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
40-237 |
1.57e-13 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 71.75 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 40 FSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH--RHVNTVFQSYALFPHMtvfenvaFG 117
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyrQLFSAVFSDFHLFDRL-------LG 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 118 LRMQKTPAaeitpRVMDALKMVQLEE--------FAQRKphqLSGGQQQRVAIARAVV-NKPrLLLLDESLSALDYKLRK 188
Cdd:COG4615 424 LDGEADPA-----RARELLERLELDHkvsvedgrFSTTD---LSQGQRKRLALLVALLeDRP-ILVFDEWAADQDPEFRR 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495142058 189 ----QMQNELKAlqrkLGITFVFVTHDqEEALTMSDRIVVMRDGRIEQDGTPR 237
Cdd:COG4615 495 vfytELLPELKA----RGKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPA 542
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
32-226 |
1.86e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.91 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDiTDVPAEHRHVNTVFQSYAL---FPhm 108
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-TRQALQKNLVAYVPQSEEVdwsFP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 109 TVFENVAFGLR-----MQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 183
Cdd:PRK15056 95 VLVEDVVMMGRyghmgWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495142058 184 YKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMR 226
Cdd:PRK15056 175 VKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-224 |
2.85e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.99 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 1 MRFLRDRVKKLNTQPRSLS---PLLQLADIGKSFDgktvisDFSL-----TINHGEFLTLLGPSGCGKTTVLRLIAGLEN 72
Cdd:PRK13409 317 MRIRPEPIEFEERPPRDESereTLVEYPDLTKKLG------DFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 73 ADAGRITLDaQDITDVPaehrhvntvfQSYALFPHMTVFENvafgLRMqktpaaeITPRVMDA------LKMVQLEEFAQ 146
Cdd:PRK13409 391 PDEGEVDPE-LKISYKP----------QYIKPDYDGTVEDL----LRS-------ITDDLGSSyykseiIKPLQLERLLD 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 147 RKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLTM----SDRI 222
Cdd:PRK13409 449 KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD----IYMidyiSDRL 524
|
..
gi 495142058 223 VV 224
Cdd:PRK13409 525 MV 526
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
34-242 |
4.83e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.92 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPaehrHVNTVFQSyalfphmTVFEN 113
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVP----QVSWIFNA-------TVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 114 VAFGL-----RMQKTPAAEITPRVMDALKMVQLEEFAQRKPHqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRK 188
Cdd:PLN03130 699 ILFGSpfdpeRYERAIDVTALQHDLDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGR 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495142058 189 QMQNelKALQRKL-GITFVFVThDQEEALTMSDRIVVMRDGRIEQDGTpreiYEE 242
Cdd:PLN03130 778 QVFD--KCIKDELrGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGT----YEE 825
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-258 |
4.89e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 69.45 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSF---DGKTVISD-FSLTINHGEFLTLLGPSGCGKTTVLRLIAGLeNADAGRITLDAQDITDV------P 89
Cdd:PRK15093 2 PLLDIRNLTIEFktsDGWVKAVDrVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFDDIdllrlsP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 90 AEHR-----HVNTVFQ--SYALFPHMTVFENVA---------------FGLRmqKTPAAEITPRV-----MDALKMVqle 142
Cdd:PRK15093 81 RERRklvghNVSMIFQepQSCLDPSERVGRQLMqnipgwtykgrwwqrFGWR--KRRAIELLHRVgikdhKDAMRSF--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 143 efaqrkPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRI 222
Cdd:PRK15093 156 ------PYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 495142058 223 VVMRDGRIEQDGTPREIYEEPKNLFVASFIGEINIF 258
Cdd:PRK15093 230 NVLYCGQTVETAPSKELVTTPHHPYTQALIRAIPDF 265
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-183 |
5.12e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 16 RSLSPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRItldaqditdvpaehrHV 95
Cdd:PRK11147 314 RSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI---------------HC 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 96 NT-----VFQSY--ALFPHMTVFENVAFGlrmQKTpaAEITPRVMDALKMVQLEEFAQRKPHQ----LSGGQQQRVAIAR 164
Cdd:PRK11147 379 GTklevaYFDQHraELDPEKTVMDNLAEG---KQE--VMVNGRPRHVLGYLQDFLFHPKRAMTpvkaLSGGERNRLLLAR 453
|
170
....*....|....*....
gi 495142058 165 AVVNKPRLLLLDESLSALD 183
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLD 472
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
36-203 |
6.98e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.44 E-value: 6.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 36 VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITL-DAQDITDVPAE--HRHVNTVFQSYALFPHmTVFE 112
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKwwRSKIGVVSQDPLLFSN-SIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 113 NVAFGLR----------------------------------------MQKTPAAEIT-----------PRVMDALKMVQL 141
Cdd:PTZ00265 479 NIKYSLYslkdlealsnyynedgndsqenknkrnscrakcagdlndmSNTTDSNELIemrknyqtikdSEVVDVSKKVLI 558
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495142058 142 EEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK---LRKQMQNELKALQRKLGI 203
Cdd:PTZ00265 559 HDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLVQKTINNLKGNENRITI 634
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-192 |
8.42e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 66.43 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEHrhVNTVFQSYALFPHMTVFEN 113
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY--CTYIGHNLGLKLEMTVFEN 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 114 VAFGLRMQKTpaAEITPRvmdALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQN 192
Cdd:PRK13541 91 LKFWSEIYNS--AETLYA---AIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN 164
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
41-239 |
1.77e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.20 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 41 SLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQdITDVPAEhrhvntvfqsyALFPHMTVFENVAFGLRM 120
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVPQQ-----------AWIQNDSLRENILFGKAL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 121 QKtpaaEITPRVMDALKMV-QLE--------EFAQrKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ 191
Cdd:TIGR00957 726 NE----KYYQQVLEACALLpDLEilpsgdrtEIGE-KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495142058 192 NELKALQRKL-GITFVFVTHDQeEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:TIGR00957 801 EHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
33-265 |
1.86e-12 |
|
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: 67.19 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 33 GKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAG-LENAD-----AGRITLDAQDITDVPAehrhvntvfqsyalfp 106
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEPSEgkikhSGRISFSSQFSWIMPG---------------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 107 hmTVFENVAFGLRMQKTpaaeitpRVMDALKMVQLEEFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLL 175
Cdd:cd03291 113 --TIKENIIFGVSYDEY-------RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 176 DESLSALDYKLRKQMQNE--LKALQRKlgiTFVFVTHDQEEaLTMSDRIVVMRDGRIEQDGTPREIYEEPKNlFVASFIG 253
Cdd:cd03291 184 DSPFGYLDVFTEKEIFEScvCKLMANK---TRILVTSKMEH-LKKADKILILHEGSSYFYGTFSELQSLRPD-FSSKLMG 258
|
250
....*....|..
gi 495142058 254 eINIFDATVIER 265
Cdd:cd03291 259 -YDTFDQFSAER 269
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
37-233 |
2.49e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.93 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 37 ISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGL-ENADAGRITLD-------------AQDITDVPAEHRHvntvfqsY 102
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINgkpvdirnpaqaiRAGIAMVPEDRKR-------H 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 103 ALFPHMTVFENV------AFGLRMQKTPAAEITPrVMDALKMVQLEEFAQRKP-HQLSGGQQQRVAIARAVVNKPRLLLL 175
Cdd:TIGR02633 349 GIVPILGVGKNItlsvlkSFCFKMRIDAAAELQI-IGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495142058 176 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQD 233
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-224 |
2.61e-12 |
|
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: 68.27 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 1 MRFLRDRVKKLNTQPRSLS---PLLQLADIGKSFDGktvisdFSLT-----INHGEFLTLLGPSGCGKTTVLRLIAGLEN 72
Cdd:COG1245 318 VRIRDEPIEFEVHAPRREKeeeTLVEYPDLTKSYGG------FSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 73 ADAGRITLDAqDItdvpaehrhvntvfqSYAlfP-------HMTVFENvafgLRMQKTPAAEITPRVMDALKMVQLEEFA 145
Cdd:COG1245 392 PDEGEVDEDL-KI---------------SYK--PqyispdyDGTVEEF----LRSANTDDFGSSYYKTEIIKPLGLEKLL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 146 QRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLTM----SDR 221
Cdd:COG1245 450 DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLidyiSDR 525
|
...
gi 495142058 222 IVV 224
Cdd:COG1245 526 LMV 528
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
33-233 |
3.94e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 33 GKTVISDFSLTINHGEFLTLLGPSGCGKT-TVLRLIAGLENADAGRITLD-------------AQDITDVPAEHRHvntv 98
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDgkpvkirnpqqaiAQGIAMVPEDRKR---- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 99 fqsYALFPHMTVFENVA------FGLRMQKTPAAEITP--RVMDALKMvqleefaqRKPH------QLSGGQQQRVAIAR 164
Cdd:PRK13549 350 ---DGIVPVMGVGKNITlaaldrFTGGSRIDDAAELKTilESIQRLKV--------KTASpelaiaRLSGGNQQKAVLAK 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495142058 165 AVVNKPRLLLLDESLSALD----YKLRKQMqNELKalqrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQD 233
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDvgakYEIYKLI-NQLV----QQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-229 |
5.14e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 5.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 24 LADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDI---TDVPAEHRHVNTVFQ 100
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 101 SYALFPHMTVFENVAFGLRMQKTPaaeitprVMDALKMVQ-----LEEF-----AQRKPHQLSGGQQQRVAIARAVVNKP 170
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGM-------FVDQDKMYRdtkaiFDELdididPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 171 RLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 229
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-234 |
6.74e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.81 E-value: 6.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 21 LLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLEN--ADAGRITLDAQDITDVPAEHRHVNTV 98
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 99 FQSyalFPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQL---------------SGGQQQRVAIA 163
Cdd:PRK09580 81 FMA---FQYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDIL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 164 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQE-EALTMSDRIVVMRDGRIEQDG 234
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRiLDYIKPDYVHVLYQGRIVKSG 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
30-244 |
7.31e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.73 E-value: 7.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 30 SFDGKTViSDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVP------------AEHRHVNT 97
Cdd:PRK09700 273 SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavkkgmayiTESRRDNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 98 VFQSYALFPHMTVFENV-------AFGL---RMQKTPAAEitPRVMDALKMVQLEEfaqrKPHQLSGGQQQRVAIARAVV 167
Cdd:PRK09700 352 FFPNFSIAQNMAISRSLkdggykgAMGLfheVDEQRTAEN--QRELLALKCHSVNQ----NITELSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 168 NKPRLLLLDESLSALD-------YKLRKQMQNElkalqrklGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIY 240
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDvgakaeiYKVMRQLADD--------GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDM 497
|
....
gi 495142058 241 EEPK 244
Cdd:PRK09700 498 SEEE 501
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
46-229 |
1.19e-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: 62.01 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 46 HGEFLTLLGPSGCGKTTVLRLIAGLENADAGR-ITLDAQDITDVPAEHRHVNTVFqsyalfphmtvfenvafglrmqktp 124
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLIIVG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 125 aaeitprvmdalkmvqleefaqRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ-----NELKALQR 199
Cdd:smart00382 56 ----------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLLKS 113
|
170 180 190
....*....|....*....|....*....|....*
gi 495142058 200 KLGITFVFVTHDQEEALTM-----SDRIVVMRDGR 229
Cdd:smart00382 114 EKNLTVILTTNDEKDLGPAllrrrFDRRIVLLLIL 148
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
27-211 |
1.56e-11 |
|
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: 65.73 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 27 IGKSFD-GKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRItldaqditdVPAEHRHVNTVFQSYALF 105
Cdd:TIGR03719 10 VSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA---------RPQPGIKVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 106 PHMTVFENVAFGLRMQK--------------TPAAEitprvMDAL--KMVQLEEF------------------AQRKP-- 149
Cdd:TIGR03719 81 PTKTVRENVEEGVAEIKdaldrfneisakyaEPDAD-----FDKLaaEQAELQEIidaadawdldsqleiamdALRCPpw 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495142058 150 ----HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNelkALQRKLGiTFVFVTHD 211
Cdd:TIGR03719 156 dadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLER---HLQEYPG-TVVAVTHD 217
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-223 |
2.37e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADigksfdgktvisdfsLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLdAQDIT------DVPaehR 93
Cdd:PRK11147 17 PLLDNAE---------------LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-EQDLIvarlqqDPP---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 94 HVNTvfqsyalfphmTVFENVAFGLRMQktpaAEITPRVMDALKMV----------QLEEFAQRKPHQ------------ 151
Cdd:PRK11147 78 NVEG-----------TVYDFVAEGIEEQ----AEYLKRYHDISHLVetdpseknlnELAKLQEQLDHHnlwqlenrinev 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 152 --------------LSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRklgiTFVFVTHDQEEALT 217
Cdd:PRK11147 143 laqlgldpdaalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRN 218
|
....*.
gi 495142058 218 MSDRIV 223
Cdd:PRK11147 219 MATRIV 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-265 |
3.85e-11 |
|
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: 64.93 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 30 SFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAG-LENAD-----AGRITLDAQDITDVPAehrhvntvfqsya 103
Cdd:TIGR01271 435 SLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEgkikhSGRISFSPQTSWIMPG------------- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 104 lfphmTVFENVAFGLRMQKTpaaeitpRVMDALKMVQLEEFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRL 172
Cdd:TIGR01271 502 -----TIKDNIIFGLSYDEY-------RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADL 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 173 LLLDESLSALDYKLRKQMQNE--LKALQRKlgiTFVFVThDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNlFVAS 250
Cdd:TIGR01271 570 YLLDSPFTHLDVVTEKEIFESclCKLMSNK---TRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPD-FSSL 644
|
250
....*....|....*
gi 495142058 251 FIGEINiFDATVIER 265
Cdd:TIGR01271 645 LLGLEA-FDNFSAER 658
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-215 |
4.27e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.27 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 20 PLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGlenaD-----AGRITL------DAQDITDV 88
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DhpqgySNDLTLfgrrrgSGETIWDI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 89 paeHRHVNTVFQSYalfpHM-----TVFENV-------AFGLRMQKTPAAEItpRVMDALKMVQLEEFAQRKP-HQLSGG 155
Cdd:PRK10938 335 ---KKHIGYVSSSL----HLdyrvsTSVRNVilsgffdSIGIYQAVSDRQQK--LAQQWLDILGIDKRTADAPfHSLSWG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 156 QQQRVAIARAVVNKPRLLLLDESLSALDyklrkqmqnelkALQRKLGITFV------------FVTHDQEEA 215
Cdd:PRK10938 406 QQRLALIVRALVKHPTLLILDEPLQGLD------------PLNRQLVRRFVdvlisegetqllFVSHHAEDA 465
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
36-242 |
5.14e-11 |
|
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: 64.58 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 36 VISDFSLTINHGEFLTLLGPSGCGKTTV-LRLIAGLENADaGRITLDAQDITDVPAE--HRHVNTVFQSYALFphmtvfe 112
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINESAE-GEIIIDGLNIAKIGLHdlRFKITIIPQDPVLF------- 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 113 nvAFGLRMQKTPAAEITPR-VMDALKMVQLEEFAQRKP----HQ-------LSGGQQQRVAIARAVVNKPRLLLLDESLS 180
Cdd:TIGR00957 1373 --SGSLRMNLDPFSQYSDEeVWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 181 ALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALTMSdRIVVMRDGRIEQDGTPREIYEE 242
Cdd:TIGR00957 1451 AVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
131-239 |
2.60e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 61.29 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 131 RVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTH 210
Cdd:NF000106 124 RADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQ 202
|
90 100
....*....|....*....|....*....
gi 495142058 211 DQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:NF000106 203 YMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
26-183 |
3.15e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 26 DIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDaqditdvpaehrhvNTVFQSY--- 102
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG--------------ETVKLAYvdq 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 103 ---ALFPHMTVFENVAFGLRMQKTPAAEITPRvmdalkmvqleefA------------QRKPHQLSGGQQQRVAIARAVV 167
Cdd:PRK11819 395 srdALDPNKTVWEEISGGLDIIKVGNREIPSR-------------AyvgrfnfkggdqQKKVGVLSGGERNRLHLAKTLK 461
|
170
....*....|....*.
gi 495142058 168 NKPRLLLLDESLSALD 183
Cdd:PRK11819 462 QGGNVLLLDEPTNDLD 477
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
36-247 |
9.55e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 9.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 36 VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDI-----TDVpaeHRHVNTVFQSYALFPHMtv 110
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVakfglTDL---RRVLSIIPQSPVLFSGT-- 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 111 fenvafgLRMQKTPAAEIT-PRVMDALKMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:PLN03232 1326 -------VRFNIDPFSEHNdADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 179 LSALDYKLRKQMQNELKALQRKlgITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLF 247
Cdd:PLN03232 1399 TASVDVRTDSLIQRTIREEFKS--CTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-231 |
2.48e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.03 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 14 QPRSL-SPLLQLADIGKSFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH 92
Cdd:PRK10636 304 APESLpNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQH 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 93 RhvntvfqsyalfphmtvfenVAFgLRMQKTP---AAEITPRVMDAlkmvQLEEF----------AQRKPHQLSGGQQQR 159
Cdd:PRK10636 384 Q--------------------LEF-LRADESPlqhLARLAPQELEQ----KLRDYlggfgfqgdkVTEETRRFSGGEKAR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 160 VAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQEEALTMSDRIVVMRDGRIE 231
Cdd:PRK10636 439 LVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-230 |
1.20e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.79 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 33 GKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGlenadagritlDAQDITdvpaehrhvNTVFQSYALfpHMTVF- 111
Cdd:PLN03073 521 GPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISG-----------ELQPSS---------GTVFRSAKV--RMAVFs 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 112 ENVAFGLRMQKTP---AAEITPRVMDALKMVQLEEF------AQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 182
Cdd:PLN03073 579 QHHVDGLDLSSNPllyMMRCFPGVPEQKLRAHLGSFgvtgnlALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495142058 183 DYKLRKQMQNELKALQRklGItfVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:PLN03073 659 DLDAVEALIQGLVLFQG--GV--LMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-211 |
1.65e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 23 QLADIGKSFDG-KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLdAQDITdvpaehrhVNTVFQS 101
Cdd:PRK11819 8 TMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP-APGIK--------VGYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 102 YALFPHMTVFENVAFGLRMQK--------------TPAAEitprvMDAL--KMVQLEEF------------------AQR 147
Cdd:PRK11819 79 PQLDPEKTVRENVEEGVAEVKaaldrfneiyaayaEPDAD-----FDALaaEQGELQEIidaadawdldsqleiamdALR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 148 KPH------QLSGGQQQRVAIARAVVNKPRLLLLDESlsaldyklrkqmQNELKA---------LQRKLGiTFVFVTHD 211
Cdd:PRK11819 154 CPPwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEP------------TNHLDAesvawleqfLHDYPG-TVVAVTHD 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
37-230 |
2.04e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 37 ISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAeHRHVNTVF-------QSYALFPHMT 109
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNA-NEAINHGFalvteerRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 110 V-FENVAFGLRMQKTPAAEITPRVMDALKMVQLEEFAQRKP-HQ-----LSGGQQQRVAIARAVVNKPRLLLLDESLSAL 182
Cdd:PRK10982 343 IgFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPgHRtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495142058 183 D-------YKLRKQMQNELKalqrklGItfVFVTHDQEEALTMSDRIVVMRDGRI 230
Cdd:PRK10982 423 DvgakfeiYQLIAELAKKDK------GI--IIISSEMPELLGITDRILVMSNGLV 469
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
32-183 |
3.09e-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: 55.69 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADaGRITLDAQDITDVPaehrhVNTVFQSYALFPHMTVF 111
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVT-----LQTWRKAFGVIPQKVFI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 112 ENVAFglRMQKTPAAEITP----RVMD--ALKMVqLEEFAQRKPHQ-------LSGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:TIGR01271 1304 FSGTF--RKNLDPYEQWSDeeiwKVAEevGLKSV-IEQFPDKLDFVlvdggyvLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
....*
gi 495142058 179 LSALD 183
Cdd:TIGR01271 1381 SAHLD 1385
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
47-225 |
4.06e-08 |
|
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: 53.91 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 47 GEFLTLLGPSGCGKTTVLRLIAGLENADAGRITlDAQDITDVPAEHRhvNTVFQSYalfphmtvFENVAFG-LRMQKTPA 125
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEILDEFR--GSELQNY--------FTKLLEGdVKVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 126 -AEITPRVMDA------------------LKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 186
Cdd:cd03236 95 yVDLIPKAVKGkvgellkkkdergkldelVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 495142058 187 RKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVM 225
Cdd:cd03236 175 RLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
37-239 |
4.74e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.90 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 37 ISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRItldaqDITDVPAehrhvnTVFQSYALFPHMTVFENVAF 116
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAA------LIAISSGLNGQLTGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 117 -GLRM--QKTPAAEITPRVMDalkMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 193
Cdd:PRK13545 109 kGLMMglTKEKIKEIIPEIIE---FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495142058 194 LKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:PRK13545 186 MNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
34-252 |
1.63e-07 |
|
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: 51.83 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAE--HRHVNTVFQSYALFphmtvf 111
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHtlRSRLSIILQDPILF------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 112 envAFGLRMQKTPAAEIT-PRVMDALKMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKPRLLLLDESL 179
Cdd:cd03288 108 ---SGSIRFNLDPECKCTdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142058 180 SALDYKLRKQMQN-ELKALQRKlgiTFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPKNLFvASFI 252
Cdd:cd03288 185 ASIDMATENILQKvVMTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVF-ASLV 253
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
34-183 |
2.20e-07 |
|
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: 50.70 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 34 KTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENAD--AGRITLDAQDITdvPAEHRHVNTVFQSYALFPHMTVF 111
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLD--KNFQRSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142058 112 ENVAFG--LRmqktpaaeitprvmdalkmvqleefaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 183
Cdd:cd03232 98 EALRFSalLR-------------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
37-247 |
3.54e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.97 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 37 ISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITldaqditdvpaEHRHVNTVFQSYALFPHMTVFENVAF 116
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------RNGEVSVIAISAGLSGQLTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 117 GLRMQKTPAAEITPRVMDALKMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKA 196
Cdd:PRK13546 109 KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYE 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495142058 197 LQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI---YEEPKNLF 247
Cdd:PRK13546 189 FKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVlpkYEAFLNDF 241
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
32-232 |
5.57e-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: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADaGRITLDAQDITDVPAEHRHvntvfQSYALFPHMTVF 111
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWR-----KAFGVIPQKVFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 112 ENVAFglRMQKTP----AAEITPRVMD--ALKMVqLEEFAQRKPHQL-------SGGQQQRVAIARAVVNKPRLLLLDES 178
Cdd:cd03289 89 FSGTF--RKNLDPygkwSDEEIWKVAEevGLKSV-IEQFPGQLDFVLvdggcvlSHGHKQLMCLARSVLSKAKILLLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495142058 179 LSALDYKLRKQMQNELKalQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQ 232
Cdd:cd03289 166 SAHLDPITYQVIRKTLK--QAFADCTVILSEH-RIEAMLECQRFLVIEENKVRQ 216
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
44-224 |
5.59e-07 |
|
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: 49.11 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 44 INHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAqditdvpaehrhvntvfqsyalfphmtvfenvafglrmqkt 123
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG----------------------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 124 paaeITPRVmdalkmvqleefaqrKPH--QLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKL 201
Cdd:cd03222 61 ----ITPVY---------------KPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
170 180
....*....|....*....|...
gi 495142058 202 GITFVFVTHDQEEALTMSDRIVV 224
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-242 |
3.19e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 32 DGKTVISDfSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITD---------VPAEHRHVNTVFQSy 102
Cdd:PRK10938 15 DTKTLQLP-SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRlsfeqlqklVSDEWQRNNTDMLS- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 103 alfphmtVFENvAFGlrmqKTpAAEItprVMDALKMVQL-EEFAQ---------RKPHQLSGGQQQRVAIARAVVNKPRL 172
Cdd:PRK10938 93 -------PGED-DTG----RT-TAEI---IQDEVKDPARcEQLAQqfgitalldRRFKYLSTGETRKTLLCQALMSEPDL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 173 LLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 242
Cdd:PRK10938 157 LILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
47-225 |
4.09e-06 |
|
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: 48.63 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 47 GEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAqDITDVPAEHRhvNTVFQSYalfphmtvFENVAFG-LRM-QKTP 124
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEP-SWDEVLKRFR--GTELQDY--------FKKLANGeIKVaHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 125 AAEITPR-----VMDALKMV----QLEEFAQ---------RKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 186
Cdd:COG1245 168 YVDLIPKvfkgtVRELLEKVdergKLDELAEklglenildRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495142058 187 RKQMQNELKALQRKlGITFVFVTHDqeeaLT----MSDRIVVM 225
Cdd:COG1245 248 RLNVARLIRELAEE-GKYVLVVEHD----LAildyLADYVHIL 285
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
36-247 |
4.62e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.01 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 36 VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDITDVPAEH--RHVNTVFQSYALFPHmTVFEN 113
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 114 VafglrmqkTPAAEITP-RVMDALKMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKPR-LLLLDESLS 180
Cdd:PTZ00243 1404 V--------DPFLEASSaEVWAALELVGLRERVASESEGIdsrvleggsnySVGQRQLMCMARALLKKGSgFILMDEATA 1475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495142058 181 ALDYKLRKQMQNE-LKALQRKLGITFVFVTHdqeeALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLF 247
Cdd:PTZ00243 1476 NIDPALDRQIQATvMSAFSAYTVITIAHRLH----TVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
47-228 |
6.14e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 47 GEFLTLLGPSGCGKTTVLRLIAglENADAGRITLDAQDITDVPAE---HRHVNTVFQSYALFPHMTVFENVAFGLRM--- 120
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGRPLDssfQRSIGYVQQQDLHLPTSTVRESLRFSAYLrqp 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 121 QKTPAAEITPRVMDALKMVQLEEFAQR---KPHQ-LSGGQQQRVAIARAVVNKPRLLL-LDESLSALDyklrKQMQNELK 195
Cdd:TIGR00956 867 KSVSKSEKMEYVEEVIKLLEMESYADAvvgVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD----SQTAWSIC 942
|
170 180 190
....*....|....*....|....*....|....*...
gi 495142058 196 ALQRKL---GITFVFVTHdQEEALTMS--DRIVVMRDG 228
Cdd:TIGR00956 943 KLMRKLadhGQAILCTIH-QPSAILFEefDRLLLLQKG 979
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
36-239 |
8.55e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 36 VISDFSLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAQDI-----TDVpaeHRHVNTVFQSYALFPHMTV 110
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIskfglMDL---RKVLGIIPQAPVLFSGTVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 111 FENVAFGlrmqKTPAAEItprvMDALKMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKPRLLLLDESL 179
Cdd:PLN03130 1331 FNLDPFN----EHNDADL----WESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495142058 180 SALDYK----LRKQMQNELKAlqrklgITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 239
Cdd:PLN03130 1403 AAVDVRtdalIQKTIREEFKS------CTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
41-226 |
1.27e-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: 45.04 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 41 SLTINHGEFLTLLGPSGCGKTTVLRLIAglenadagritldaqditdvpaehrhvntvfqsYALFPHMTVFENVAFGLRM 120
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LALGGAQSATRRRSGVKAG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 121 QKTPAAEITPRVMDalkmvqleefaqrkpHQLSGGQQQRVAIARAVVN---KPR-LLLLDESLSALDyklrkqMQNELKA 196
Cdd:cd03227 62 CIVAAVSAELIFTR---------------LQLSGGEKELSALALILALaslKPRpLYILDEIDRGLD------PRDGQAL 120
|
170 180 190
....*....|....*....|....*....|....*
gi 495142058 197 L-----QRKLGITFVFVTHDQEEALtMSDRIVVMR 226
Cdd:cd03227 121 AeaileHLVKGAQVIVITHLPELAE-LADKLIHIK 154
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
47-225 |
1.80e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 47 GEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDAqDITDVPAEHRhvNTVFQSYalfphmtvFENVAFG-LR-MQKTP 124
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEP-SWDEVLKRFR--GTELQNY--------FKKLYNGeIKvVHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 125 AAEITPRVM-----DALKMV-------------QLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 186
Cdd:PRK13409 168 YVDLIPKVFkgkvrELLKKVdergkldevverlGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495142058 187 RKQMQNELKALQRklGITFVFVTHDqeeaLT----MSDRIVVM 225
Cdd:PRK13409 248 RLNVARLIRELAE--GKYVLVVEHD----LAvldyLADNVHIA 284
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
152-282 |
3.60e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.77 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 152 LSGGQQQRVAIARAV------VnkprLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDqEEALTMSDRIVVM 225
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD-EDTIRAADYVIDI 562
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495142058 226 ------RDGRIEQDGTPREIYEEPKNLFVASFIGEinifdatviERIDAQRVRANVEGRECVL 282
Cdd:TIGR00630 563 gpgageHGGEVVASGTPEEILANPDSLTGQYLSGR---------KKIEVPAERRPGNGKFLTL 616
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
152-230 |
8.37e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 152 LSGGQQQRVAIARAVVNKPRLLLLDESLSALD-------YKLRKQMQNELKALqrklgitfVFVTHDQEEALTMSDRIVV 224
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgakyeiYTIINELAAEGKGV--------IVISSELPELLGMCDRIYV 476
|
....*.
gi 495142058 225 MRDGRI 230
Cdd:NF040905 477 MNEGRI 482
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
296-376 |
8.56e-05 |
|
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: 40.30 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 296 VLLRPEDLRVEEIngdgeADGLIGFVRERNYKGMTLESVVELENGKIVLVSEFFNEDDPdfdHSLDQKMAVTWVESWEVV 375
Cdd:pfam08402 1 LAIRPEKIRLAAA-----ANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHARP---PAPGDRVGLGWDPEDAHV 72
|
.
gi 495142058 376 L 376
Cdd:pfam08402 73 L 73
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
147-225 |
1.88e-04 |
|
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: 41.92 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 147 RKPHQLSGGQQQRVAIAR--AVVNKPRLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDqEEALTMSDRIVV 224
Cdd:cd03238 83 QKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHN-LDVLSSADWIID 160
|
.
gi 495142058 225 M 225
Cdd:cd03238 161 F 161
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-213 |
1.96e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 30 SFDGKTVISDFSLTINHGEFLTLLGPSGCGKTTVLRLIA-----GL---------------ENADAGRITLDAqDITDVP 89
Cdd:PLN03073 186 SVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGIpkncqilhveqevvgDDTTALQCVLNT-DIERTQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 90 AEHRHVNTVFQSYAL-FPHMTVFENVAFGLRMQKTPAAEITPRVMDALKMVQL-----------------EEFAQRKPHQ 151
Cdd:PLN03073 265 LLEEEAQLVAQQRELeFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAytaearaasilaglsftPEMQVKATKT 344
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 152 LSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKalqrKLGITFVFVTHDQE 213
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLL----KWPKTFIVVSHARE 402
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
41-232 |
2.23e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 41 SLTINHGEFLTLLGPSGCGKTTVLRLIAGLENADAGRITLDA--------QDIT--DVPA---------EHR-------H 94
Cdd:PRK10636 21 TATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPalPQPAleyvidgdrEYRqleaqlhD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 95 VNTVFQSYALfphmtvfenVAFGLRMQKTPAAEITPRVMDALKMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLL 173
Cdd:PRK10636 101 ANERNDGHAI---------ATIHGKLDAIDAWTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 174 LLDESLSALDYKLRKQMQNELKALQRklgiTFVFVTHDQEEALTMSDRIVvmrdgRIEQ 232
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPIVDKII-----HIEQ 221
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
47-183 |
2.15e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.21 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 47 GEFLTLLGPSGCGKTTVLRLIAGLENadAGRITLDAQdITDVPAEH----RHVNTVFQSYALFPHMTVFENVAFG--LRM 120
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKT--GGYIEGDIR-ISGFPKKQetfaRISGYCEQNDIHSPQVTVRESLIYSafLRL 982
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495142058 121 QKTPAAE----ITPRVMDALKMVQLEEFAQRKP--HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 183
Cdd:PLN03140 983 PKEVSKEekmmFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
29-235 |
2.91e-03 |
|
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: 38.74 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 29 KSFDGKTVISDFSLtinhgefLTLL-GPSGCGKTTVL-------------RLIAGLENADAGRITldaQDITDVPAEHRH 94
Cdd:cd03240 10 RSFHERSEIEFFSP-------LTLIvGQNGAGKTTIIealkyaltgelppNSKGGAHDPKLIREG---EVRAQVKLAFEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495142058 95 VN----TVFQSYAlfphmtVFENVAFglrmqkTPAAEITPRVMDALKmvqleefaqrkphQLSGGQQQ------RVAIAR 164
Cdd:cd03240 80 ANgkkyTITRSLA------ILENVIF------CHQGESNWPLLDMRG-------------RCSGGEKVlasliiRLALAE 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495142058 165 AVVNKPRLLLLDESLSALD-YKLRKQMQNELKALQRKLGITFVFVTHDqEEALTMSDRIVvmrdgRIEQDGT 235
Cdd:cd03240 135 TFGSNCGILALDEPTTNLDeENIEESLAEIIEERKSQKNFQLIVITHD-EELVDAADHIY-----RVEKDGR 200
|
|
| |
