|
Name |
Accession |
Description |
Interval |
E-value |
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
47-421 |
0e+00 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 793.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 47 SQKLNIQPRSRSPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITH 126
Cdd:PRK09452 1 SKKLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 127 VPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVV 206
Cdd:PRK09452 81 VPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 207 NKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLF 286
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 287 VASFIGEINIFDATVIERLDEQRVRANVEGRECNITVNFAVEAGQRLHVLLRPEDLRVDEIHHNSDADGLIGYVRERNYK 366
Cdd:PRK09452 241 VARFIGEINIFDATVIERLDEQRVRANVEGRECNIYVNFAVEPGQKLHVLLRPEDLRVEEINDDEHAEGLIGYVRERNYK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1460644645 367 GMTLESVVELENGKMVMVSEFFNEDDPDFDHSLDQKMSINWVESWEVVLADEELQ 421
Cdd:PRK09452 321 GMTLDSVVELENGKMVMVSEFFNEDDPDFDHSLGQKVAVTWVEGWEVVLADEEHK 375
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
91-415 |
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: 554.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 91 LLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPR 170
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 171 VLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHD 250
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 251 QEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINIFDATVIERLDEQRVRANVEGRECNITVNFAVEAG 330
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAGVEGRRCDIYTDVPVEKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 331 QRLHVLLRPEDLRVDEIHHNSDADGLIGYVRERNYKGMTLESVVELENGKMVMVSEFFNEDDPDFDHSLDQKMSINWVES 410
Cdd:TIGR01187 241 QPLHVVLRPEKIVIEEEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQKVLVSEFFNEDDPHMSPSIGDRVGLTWHPG 320
|
....*
gi 1460644645 411 WEVVL 415
Cdd:TIGR01187 321 SEVVL 325
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
57-417 |
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: 537.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 57 RSPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNT 136
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 137 VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 216
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 217 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINI 296
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 297 FDATVIERlDEQRVRanVEGRECNITVNFAVEAGQRLHVLLRPEDLRVDEihhNSDADGLIGYVRERNYKGMTLESVVEL 376
Cdd:COG3842 242 LPGTVLGD-EGGGVR--TGGRTLEVPADAGLAAGGPVTVAIRPEDIRLSP---EGPENGLPGTVEDVVFLGSHVRYRVRL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1460644645 377 ENGKMVMVSEFFNEDDPdfdHSLDQKMSINWVESWEVVLAD 417
Cdd:COG3842 316 GDGQELVVRVPNRAALP---LEPGDRVGLSWDPEDVVVLPA 353
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
61-346 |
4.06e-154 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 439.51 E-value: 4.06e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNTVFQS 140
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 141 YALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 220
Cdd:COG3839 84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 221 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGE--INIFD 298
Cdd:COG3839 164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppMNLLP 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1460644645 299 ATVIERldeqrvRANVEGRECNITVNFAVEAGQRLHVLLRPEDLRVDE 346
Cdd:COG3839 244 GTVEGG------GVRLGGVRLPLPAALAAAAGGEVTLGIRPEHLRLAD 285
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
61-292 |
5.83e-149 |
|
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: 422.03 E-value: 5.83e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNTVFQS 140
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 141 YALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 220
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 221 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIG 292
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
61-353 |
5.68e-134 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 388.35 E-value: 5.68e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDI-THVPAENRHVNTVFQ 139
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 140 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 219
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 220 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINIFDA 299
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 300 TVIErldeqrvrANVEGRECNITVNFAVEAGQRlHVLLRPEDLRVDEIHHNSDA 353
Cdd:COG1118 243 RVIG--------GQLEADGLTLPVAEPLPDGPA-VAGVRPHDIEVSREPEGENT 287
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
58-378 |
5.57e-122 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 358.19 E-value: 5.57e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 58 SPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNTV 137
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 138 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 218 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINIF 297
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 298 DAtviERLDEQRVRANVEGRECNITVnfaVEAGQRLHVLLRPEDLRVdeiHHNSDADGLI-GYVRERNYKGMTLESVVEL 376
Cdd:TIGR03265 242 PG---TRGGGSRARVGGLTLACAPGL---AQPGASVRLAVRPEDIRV---SPAGNAANLLlARVEDMEFLGAFYRLRLRL 312
|
..
gi 1460644645 377 EN 378
Cdd:TIGR03265 313 EG 314
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
61-273 |
2.55e-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: 343.35 E-value: 2.55e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNTVFQS 140
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 141 YALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 220
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 221 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 273
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
61-300 |
4.44e-111 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 330.14 E-value: 4.44e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNTVFQS 140
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 141 YALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 220
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 221 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINIFDAT 300
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPAT 246
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
61-343 |
2.23e-110 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 328.34 E-value: 2.23e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKT-VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHV-PAEnRHVNTVF 138
Cdd:PRK11650 4 LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELePAD-RDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 139 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 218
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 219 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGE--INI 296
Cdd:PRK11650 163 SNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpaMNL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1460644645 297 FDATVierLDEQRVRANVEGRECNITVNFAVEAGQRLHVLLRPEDLR 343
Cdd:PRK11650 243 LDGRV---SADGAAFELAGGIALPLGGGYRQYAGRKLTLGIRPEHIA 286
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
61-293 |
4.21e-110 |
|
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: 323.52 E-value: 4.21e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNTVFQS 140
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 141 YALFPHMTVFENVAFGLRMQK----TPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 216
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKPrserPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1460644645 217 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGE 293
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
61-273 |
1.02e-109 |
|
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: 321.51 E-value: 1.02e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNTVFQS 140
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 141 YALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 220
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 221 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 273
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
53-382 |
1.68e-109 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 327.18 E-value: 1.68e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 53 QPRSR---SPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPA 129
Cdd:PRK11607 9 QAKTRkalTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 130 ENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKP 209
Cdd:PRK11607 89 YQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 210 RLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVAS 289
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 290 FIGEINIFDATVIERLDEQRVrANVEGRECNITVN--FAVEAGQRLHVLLRPEDLRVDEihhNSDADGL---IGYVRERN 364
Cdd:PRK11607 249 FIGSVNVFEGVLKERQEDGLV-IDSPGLVHPLKVDadASVVDNVPVHVALRPEKIMLCE---EPPADGCnfaVGEVIHIA 324
|
330
....*....|....*...
gi 1460644645 365 YKGMTLESVVELENGKMV 382
Cdd:PRK11607 325 YLGDLSIYHVRLKSGQMI 342
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
56-272 |
1.57e-100 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 299.70 E-value: 1.57e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 56 SRSPLVQLAGIRKSF----DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIThvpAEN 131
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT---GPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 132 RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRL 211
Cdd:COG1116 80 PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 212 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGKIEQD 272
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEE 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
61-301 |
2.64e-100 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 302.77 E-value: 2.64e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNTVFQS 140
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 141 YALFPHMTVFENVAFGLRM----QKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 216
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 217 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINI 296
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNR 242
|
....*
gi 1460644645 297 FDATV 301
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 ... |
61-269 |
9.00e-96 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 286.29 E-value: 9.00e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGK----TVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDhdiTHVPAENRHVNT 136
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG---EPVTGPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 137 VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 216
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1460644645 217 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGKI 269
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRI 212
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
61-342 |
1.09e-93 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 286.54 E-value: 1.09e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNTVFQS 140
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 141 YALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 220
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 221 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIG--EINIFD 298
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGspKMNFLP 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 299 ATV---------IERLDEQRVRANVEGRecnitvnfAVEAGQRLHVLLRPEDL 342
Cdd:PRK11000 244 VKVtataieqvqVELPNRQQVWLPVEGR--------GVQVGANMSLGIRPEHL 288
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
75-296 |
1.99e-89 |
|
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: 270.75 E-value: 1.99e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 75 VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNTVFQSYALFPHMTVFENVA 154
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 155 FGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELK 234
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 235 ALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINI 296
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
72-343 |
5.17e-87 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 269.67 E-value: 5.17e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 72 GKTV-IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE------NRHVNTVFQSYALF 144
Cdd:COG4175 38 GQTVgVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKelrelrRKKMSMVFQHFALL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 145 PHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 224
Cdd:COG4175 118 PHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 225 LRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEIN---IFDA-- 299
Cdd:COG4175 198 IRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDVDrskVLTAgs 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1460644645 300 ------TVIERLDEQRVrANVEGRECNITVNFAVEAGQRLHVLLRPEDLR 343
Cdd:COG4175 278 vmrppeAVVSEKDGPRV-ALRRMREEGISSLYVVDRDRRLLGVVTADDAL 326
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
58-272 |
1.17e-84 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 258.05 E-value: 1.17e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 58 SPLVQLAGIRKSF-DGK---TVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE--- 130
Cdd:COG1136 2 SPLLELRNLTKSYgTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 131 ---NRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVN 207
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460644645 208 KPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqEEALTMSDRIVVMRDGKIEQD 272
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
61-293 |
1.74e-84 |
|
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: 1.74e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSF-DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTV 137
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 138 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLED--FAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 215
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644645 216 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGE 293
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
54-283 |
9.93e-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: 262.92 E-value: 9.93e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 54 PRSRSPLVQLAGIRKSFDGK-----TVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVP 128
Cdd:COG1123 254 AAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 129 AEN-----RHVNTVFQ--SYALFPHMTVFENVAFGLRMQKT-PAAEITPRVLDALKMVQL-EDFAQRKPHQLSGGQQQRV 199
Cdd:COG1123 334 RRSlrelrRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 200 AIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIY 279
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
....
gi 1460644645 280 EEPK 283
Cdd:COG1123 494 ANPQ 497
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
66-291 |
2.33e-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: 251.02 E-value: 2.33e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 66 IRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN------RHVNTVFQ 139
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 140 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 219
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 220 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFI 291
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
56-291 |
7.68e-81 |
|
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: 248.74 E-value: 7.68e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 56 SRSPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE----- 130
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 131 NRHVNTVFQSYALFPHMTVFENVAFGLRMQKT-PAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKP 209
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 210 RLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIyEEPKNLFVAS 289
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL-LASDDPWVRQ 239
|
..
gi 1460644645 290 FI 291
Cdd:COG1127 240 FL 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
61-269 |
1.38e-78 |
|
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: 242.01 E-value: 1.38e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDG----KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE------ 130
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 131 NRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPR 210
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 211 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALtMSDRIVVMRDGKI 269
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
60-284 |
1.68e-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: 242.59 E-value: 1.68e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 60 LVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE----NRHVN 135
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinklRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 136 TVFQSYALFPHMTVFENVAFGLRM-QKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 214
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 215 DESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKN 284
Cdd:COG1126 161 DEPTSALD----PELVGEVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
68-360 |
1.43e-76 |
|
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: 242.07 E-value: 1.43e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 68 KSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHV-PAENRHVN-----TVFQSY 141
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQsPVELREVRrkkigMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 142 ALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 221
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 222 DYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINIFDATV 301
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 302 IERLDEqrvRANvegrecniTVNFAVEAGQRLHVLLR-PEDLRVDEIHHNSDADGLIGYV 360
Cdd:TIGR01186 241 AERIAQ---RMN--------TGPITKTADKGPRSALQlMRDERVDSLYVVDRQNKLVGVV 289
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
71-285 |
2.73e-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: 231.45 E-value: 2.73e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQS--YALFpH 146
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQNpdDQLF-A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 147 MTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 226
Cdd:COG1122 91 PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 227 KQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 285
Cdd:COG1122 171 RELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
61-278 |
1.66e-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: 229.70 E-value: 1.66e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHV-PAENRHVNT--- 136
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLsEAELYRLRRrmg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 137 -VFQSYALFPHMTVFENVAFGLRMQ-KTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 214
Cdd:cd03261 81 mLFQSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 215 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
61-268 |
7.22e-72 |
|
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: 223.60 E-value: 7.22e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIT----HVPAENRHVNT 136
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 137 VFQSYALFPHMTVFENVAFGLrmqktpaaeitprvldalkmvqledfaqrkphqlSGGQQQRVAIARAVVNKPRLLLLDE 216
Cdd:cd03229 81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 217 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGK 268
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
60-291 |
2.44e-71 |
|
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: 224.68 E-value: 2.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 60 LVQLAGIRKSF----DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVP--AENRH 133
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRrkAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 134 VNTVFQSY--ALFPHMTVFENVAFGLRMQKTPaaEITPRVLDALKMVQL-EDFAQRKPHQLSGGQQQRVAIARAVVNKPR 210
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 211 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKN-----L 285
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHpytreL 238
|
....*.
gi 1460644645 286 FVASFI 291
Cdd:COG1124 239 LAASLA 244
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
63-273 |
1.91e-70 |
|
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: 221.01 E-value: 1.91e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 63 LAGIRKSFDGKTVidNLNLTINnGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLED------HDITHVPAENRHVNT 136
Cdd:cd03297 3 CVDIEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 137 VFQSYALFPHMTVFENVAFGLRmqKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 216
Cdd:cd03297 80 VFQQYALFPHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1460644645 217 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 273
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
78-293 |
2.08e-70 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 221.55 E-value: 2.08e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 78 NLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNTVFQSYALFPHMTVFENVAFGL 157
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFPHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 158 RmqktPAAEITP----RVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVV-NKPrLLLLDESLSALDYKLRKQMQNE 232
Cdd:COG3840 97 R----PGLKLTAeqraQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDEPFSALDPALRQEMLDL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460644645 233 LKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGE 293
Cdd:COG3840 172 VDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
73-269 |
6.19e-70 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 221.66 E-value: 6.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHvPAENRHVntVFQSYALFPHMTVFEN 152
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV--VFQKDALLPWLNVLDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 153 VAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 232
Cdd:COG4525 97 VAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQEL 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1460644645 233 LKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGKI 269
Cdd:COG4525 177 LLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRI 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
61-273 |
1.35e-69 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 219.15 E-value: 1.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSF-DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN-----RHV 134
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 135 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 214
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 215 DESLSALDYKLRKQMQNELKALQRkLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 273
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
61-281 |
4.33e-68 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 215.70 E-value: 4.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE-NRHVNTVFQ 139
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 140 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 219
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 220 ALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 281
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
60-273 |
1.36e-67 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 214.29 E-value: 1.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 60 LVQLAGIRKSFDGK----TVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENR--- 132
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 133 --HVNTVFQSY--ALFPHMTVFENVAFGLRMQK--TPAAEITPRVLDALKMVQL-EDFAQRKPHQLSGGQQQRVAIARAV 205
Cdd:cd03257 81 rkEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGklSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644645 206 VNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 273
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
59-281 |
2.09e-67 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 214.54 E-value: 2.09e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 59 PLVQLAGIRKSF-DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN-----R 132
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 133 HVNTVFQSYALFPHMTVFENVAFG-----------LRMQktPAAEItPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAI 201
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGrlgrtstwrslLGLF--PPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 202 ARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 281
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDA 237
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
80-307 |
4.25e-67 |
|
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: 217.28 E-value: 4.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 80 NLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHD------ITHVPAENRHVNTVFQSYALFPHMTVFENV 153
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsarGIFLPPHRRRIGYVFQEARLFPHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 154 AFGLRmqKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNEL 233
Cdd:COG4148 99 LYGRK--RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 234 KALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINIFDATVIERLDE 307
Cdd:COG4148 177 ERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVAAHDPD 250
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
61-371 |
1.52e-66 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 215.33 E-value: 1.52e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGK----TVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVP-----AEN 131
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSerelrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 132 RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRL 211
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 212 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeealtMS------DRIVVMRDGKIEQDGTPREIYEEPKNL 285
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE------MDvvrricDRVAVLENGRIVEQGPVLDVFANPQSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 286 FVASFIGEINIFD--ATVIERLDEQrvranvEGRECNITVNFAVEAGQR--LHVLLRPEDLRVDEIHhnsdadGLIGYVR 361
Cdd:COG1135 236 LTRRFLPTVLNDElpEELLARLREA------AGGGRLVRLTFVGESADEplLSELARRFGVDVNILS------GGIEEIQ 303
|
330
....*....|
gi 1460644645 362 ERNYKGMTLE 371
Cdd:COG1135 304 GTPVGRLIVE 313
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
61-269 |
2.16e-66 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 210.85 E-value: 2.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITH----VPAENRHVNT 136
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkknINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 137 VFQSYALFPHMTVFENVAFGLR-MQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 215
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 216 ESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
62-268 |
7.63e-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: 209.25 E-value: 7.63e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 62 QLAGIRKSFDGKT--VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTV 137
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 138 FQsyalFP-HM----TVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLL 212
Cdd:cd03225 81 FQ----NPdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1460644645 213 LLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGK 268
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
58-285 |
1.02e-64 |
|
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: 1.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 58 SPLVQLAGIRKSFDG--KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGL---ENVDSGRIHLEDHDITHVPAENR 132
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 133 --HVNTVFQS--YALFPhMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNK 208
Cdd:COG1123 82 grRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1460644645 209 PRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 285
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
60-278 |
2.18e-63 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 204.51 E-value: 2.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 60 LVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTV 137
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 138 FQSYALFPHMTVFENVAFG----LRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 213
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460644645 214 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
60-283 |
4.74e-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: 202.81 E-value: 4.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 60 LVQLAGIRKSFDGK----TVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVP-----AE 130
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 131 NRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPR 210
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 211 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 283
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
54-283 |
3.00e-62 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 203.81 E-value: 3.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 54 PRSRSPLVQLAGIRKSFD------GKTV-----IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDH 122
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPvrgglfGRTVgvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 123 DITHVPAEN-----RHVNTVFQ-SYA-LFPHMTVFENVAFGLRMQK-TPAAEITPRVLDALKMVQL-EDFAQRKPHQLSG 193
Cdd:COG4608 81 DITGLSGRElrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLrPEHADRYPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 194 GQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLTM----SDRIVVMRDGKI 269
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKI 236
|
250
....*....|....
gi 1460644645 270 EQDGTPREIYEEPK 283
Cdd:COG4608 237 VEIAPRDELYARPL 250
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
62-281 |
1.01e-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: 197.02 E-value: 1.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 62 QLAGIRKSF-DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN-----RHVN 135
Cdd:cd03256 2 EVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 136 TVFQSYALFPHMTVFENVAFGLRMQKT---------PAAEItPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVV 206
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGRLGRRStwrslfglfPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460644645 207 NKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 281
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
71-285 |
3.62e-60 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 196.50 E-value: 3.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDI---THVPAENRHVNTVFQSyalfPH- 146
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeENLWEIRKKVGMVFQN----PDn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 147 ----MTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 222
Cdd:TIGR04520 89 qfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 223 YKLRKQMQNELKALQRKLGITFVFVTHDQEEALtMSDRIVVMRDGKIEQDGTPREIYEEPKNL 285
Cdd:TIGR04520 169 PKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQVELL 230
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
60-281 |
3.47e-58 |
|
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: 190.45 E-value: 3.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 60 LVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE-NRHVNTVF 138
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 139 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 218
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 219 SALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 281
Cdd:COG4555 161 NGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
60-291 |
4.11e-57 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 187.61 E-value: 4.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 60 LVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHV----N 135
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 136 TVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 214
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1460644645 215 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFI 291
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
60-283 |
6.04e-57 |
|
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: 189.88 E-value: 6.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 60 LVQLAGIRKSFDGK----TVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLE---NVDSGRIHLEDHDITHVPAEN- 131
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 132 -----RHVNTVFQ-SY-ALFPHMTVFENVAFGLRM-QKTPAAEITPRVLDALKMVQL---EDFAQRKPHQLSGGQQQRVA 200
Cdd:COG0444 81 rkirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 201 IARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKI-EQdGTPREIY 279
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIvEE-GPVEELF 239
|
....
gi 1460644645 280 EEPK 283
Cdd:COG0444 240 ENPR 243
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
71-280 |
8.49e-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: 198.52 E-value: 8.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALFpHMT 148
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFLF-SGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 VFENVAFGlrmqktpAAEITP-RVLDALKMVQLEDFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDE 216
Cdd:COG2274 565 IRENITLG-------DPDATDeEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 217 SLSALDYKLRKQMQNELKALQRklGITFVFVTHDqEEALTMSDRIVVMRDGKIEQDGTPREIYE 280
Cdd:COG2274 638 ATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
58-278 |
1.80e-56 |
|
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: 186.40 E-value: 1.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 58 SPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRH---- 133
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 134 VNTvFQSYALFPHMTVFENVA---------------FGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQR 198
Cdd:COG0411 82 ART-FQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 199 VAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
54-277 |
2.10e-56 |
|
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: 185.72 E-value: 2.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 54 PRSRSPLVQLAGIRKSFDGK----TVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPA 129
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 130 E------NRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEitPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIAR 203
Cdd:COG4181 82 DararlrARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 204 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALtMSDRIVVMRDGKIEQDGTPRE 277
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLVEDTAATA 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
61-294 |
4.26e-56 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 188.47 E-value: 4.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGK----TVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVP-----AEN 131
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekelrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 132 RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRL 211
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 212 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFI 291
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFI 241
|
...
gi 1460644645 292 GEI 294
Cdd:PRK11153 242 QST 244
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
60-267 |
5.25e-56 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 185.29 E-value: 5.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 60 LVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEnRHVntVFQ 139
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE-RGV--VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 140 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 219
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1460644645 220 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 267
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
71-266 |
7.89e-56 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 183.45 E-value: 7.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVD---SGRIHLEDHDITHVPAENRHVNTVFQSYALFPHM 147
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 148 TVFENVAFGLRmQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRK 227
Cdd:COG4136 92 SVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1460644645 228 QMQNELKALQRKLGITFVFVTHDQEEALTMSdRIVVMRD 266
Cdd:COG4136 171 QFREFVFEQIRQRGIPALLVTHDEEDAPAAG-RVLDLGN 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
61-278 |
1.17e-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: 183.54 E-value: 1.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENV-----DSGRIHLEDHDI----THVPAEN 131
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydldVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 132 RHVNTVFQSYALFPhMTVFENVAFGLRMQKT-PAAEITPRVLDALKMVQLEDFAQRKPH--QLSGGQQQRVAIARAVVNK 208
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 209 PRLLLLDESLSALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
65-281 |
1.38e-55 |
|
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: 183.65 E-value: 1.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 65 GIRKSF-DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN-----RHVNTVF 138
Cdd:TIGR02315 6 NLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 139 QSYALFPHMTVFENVAFGlRMQKTPA---------AEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKP 209
Cdd:TIGR02315 86 QHYNLIERLTVLENVLHG-RLGYKPTwrsllgrfsEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 210 RLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 281
Cdd:TIGR02315 165 DLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
62-269 |
2.33e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 181.94 E-value: 2.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 62 QLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQ 139
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 140 SYALFPhMTVFENVAFGLRMQKTPAAEitPRVLDALKMVQL-EDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 218
Cdd:COG4619 82 EPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1460644645 219 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
59-272 |
2.38e-55 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 183.73 E-value: 2.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 59 PLVqLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRhvnTVF 138
Cdd:PRK11247 12 PLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---LMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 139 QSYALFPHMTVFENVAFGLRMQKTPAAeitprvLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 218
Cdd:PRK11247 88 QDARLLPWKKVIDNVGLGLKGQWRDAA------LQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 219 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQD 272
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
58-282 |
3.81e-54 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 180.28 E-value: 3.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 58 SPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVpaeNRHVNTV 137
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA---RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 138 FQSYAL---FPhMTVFENVAFGL----RMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPR 210
Cdd:COG1121 81 PQRAEVdwdFP-ITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 211 LLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEqDGTPREIYEEP 282
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVA-HGPPEEVLTPE 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
54-293 |
3.96e-54 |
|
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: 187.97 E-value: 3.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 54 PRSRSPLVQLAGIRKSFD------GKTV-----IDNLNLTINNGEFLTLLGPSGCGKTT----VLRLIAGlenvdSGRIH 118
Cdd:COG4172 269 PPDAPPLLEARDLKVWFPikrglfRRTVghvkaVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIPS-----EGEIR 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 119 LEDHDITHVPAEN-----RHVNTVFQS-YA-LFPHMTVFENVAFGLRMQKTP--AAEITPRVLDALKMVQL-EDFAQRKP 188
Cdd:COG4172 344 FDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRMTVGQIIAEGLRVHGPGlsAAERRARVAEALEEVGLdPAARHRYP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 189 HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGK 268
Cdd:COG4172 424 HEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
250 260 270
....*....|....*....|....*....|.
gi 1460644645 269 I-EQdGTPREIYEEPKN-----LFVASFIGE 293
Cdd:COG4172 504 VvEQ-GPTEQVFDAPQHpytraLLAAAPLLE 533
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
79-303 |
5.89e-54 |
|
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: 183.00 E-value: 5.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 79 LNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDI------THVPAENRHVNTVFQSYALFPHMTVFEN 152
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkgIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 153 VAFGLRMQKTPAAEITP-RVLDalkMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQN 231
Cdd:TIGR02142 96 LRYGMKRARPSERRISFeRVIE---LLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 232 ELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPkNLFVASFIGEINIFDATVIE 303
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP-DLPWLAREDQGSLIEGVVAE 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
65-278 |
1.59e-53 |
|
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: 178.01 E-value: 1.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 65 GIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRH---VNTVFQSY 141
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRTFQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 142 ALFPHMTVFENVAFGLRMQKTPA----------AEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRL 211
Cdd:cd03219 85 RLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1460644645 212 LLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
61-269 |
3.28e-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: 175.28 E-value: 3.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENR-HVNTVFQ 139
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 140 SYALFPHMTVFENVafglrmqktpaaeitprvldalkmvqledfaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLS 219
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1460644645 220 ALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
76-282 |
4.25e-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: 176.89 E-value: 4.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHvPAENRHVntVFQSYALFPHMTVFENVAF 155
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV--VFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 156 GLR--MQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNEL 233
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1460644645 234 KALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGtprEIYEEP 282
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG---QILEVP 203
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
76-304 |
7.22e-52 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 179.07 E-value: 7.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVP-AENRHVN-----TVFQSYALFPHMTV 149
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdAELREVRrkkiaMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 150 FENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQM 229
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644645 230 QNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINI---FDATVIER 304
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDIsqvFSAKDIAR 281
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
61-283 |
1.60e-51 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 173.28 E-value: 1.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDH--DITHVPAEN------R 132
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKairllrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 133 HVNTVFQSYALFPHMTVFEN-VAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRL 211
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 212 LLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTpREIYEEPK 283
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
62-273 |
3.48e-51 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 170.31 E-value: 3.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 62 QLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQ 139
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 140 syalfphmtvfenvafglrmqktpaaeitprvldALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 219
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 220 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 273
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
61-283 |
3.54e-51 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 172.51 E-value: 3.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDH--DITHVPAEN------R 132
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKairelrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 133 HVNTVFQSYALFPHMTVFENVAFG----LRMQKTPAAEitpRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNK 208
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEApcrvLGLSKDQALA---RAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460644645 209 PRLLLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTpREIYEEPK 283
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQ 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
79-273 |
8.93e-51 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 170.37 E-value: 8.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 79 LNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNTVFQSYALFPHMTVFENVAFGLr 158
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 159 mqkTPAAEITP----RVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELK 234
Cdd:cd03298 96 ---SPGLKLTAedrqAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1460644645 235 ALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 273
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
76-216 |
7.17e-50 |
|
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: 165.90 E-value: 7.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITH--VPAENRHVNTVFQSYALFPHMTVFENV 153
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1460644645 154 AFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRK----PHQLSGGQQQRVAIARAVVNKPRLLLLDE 216
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
71-277 |
7.58e-50 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 177.28 E-value: 7.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALFpHMT 148
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 VFENVAFGlrmqktpAAEITP-RVLDALKMVQLEDFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDE 216
Cdd:COG1132 430 IRENIRYG-------RPDATDeEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460644645 217 SLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPRE 277
Cdd:COG1132 503 ATSALDTETEALIQEALERLMK--GRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEE 560
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
72-269 |
1.02e-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: 167.58 E-value: 1.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 72 GKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITH-----VPAENRHVNTVFQSYALFPH 146
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 147 MTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 226
Cdd:cd03292 93 RNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1460644645 227 KQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:cd03292 173 WEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
59-268 |
1.31e-49 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 166.89 E-value: 1.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 59 PLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE-NRHVNTV 137
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 138 FQSYALFPHMTVFENVAFGLRMQKTPAAEItpRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 218 LSALDyklrKQMQNELKAL---QRKLGITFVFVTHDQEEALtmSDRIVVMRDGK 268
Cdd:COG4133 159 FTALD----AAGVALLAELiaaHLARGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
61-278 |
4.69e-49 |
|
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: 166.14 E-value: 4.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSF--DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDI-THVPAENRHVNTV 137
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 138 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460644645 218 LSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
73-285 |
7.85e-49 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 167.53 E-value: 7.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE----NRHVNTVFQ--SYALFPH 146
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdiRKKVGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 147 mTVFENVAFGLRMQKTPAAEITPRVLDALKMVQL--EDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 224
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460644645 225 LRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 285
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETL 239
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
53-282 |
4.63e-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: 172.26 E-value: 4.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 53 QPRSRSPLVQLAGIRKSFDG--KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE 130
Cdd:COG4987 326 APAPGGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 131 N--RHVNTVFQSYALFpHMTVFENVAFGlRMQKTPAAeitprVLDALKMVQLEDFAQRKPH-----------QLSGGQQQ 197
Cdd:COG4987 406 DlrRRIAVVPQRPHLF-DTTLRENLRLA-RPDATDEE-----LWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 198 RVAIARAVVNKPRLLLLDESLSALDYKLRKQ-MQNELKALQRKlgiTFVFVTHDQEEALTMsDRIVVMRDGKIEQDGTPR 276
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQAlLADLLEALAGR---TVLLITHRLAGLERM-DRILVLEDGRIVEQGTHE 554
|
....*.
gi 1460644645 277 EIYEEP 282
Cdd:COG4987 555 ELLAQN 560
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
61-278 |
5.59e-48 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 163.31 E-value: 5.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE-NRHVNTVFQ 139
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 140 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 219
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 220 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
62-268 |
7.11e-48 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 160.87 E-value: 7.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 62 QLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQ 139
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 140 syalfphmtvfenvafglrmqktpaaeitprvldalkmvqledfaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDESLS 219
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1460644645 220 ALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGK 268
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
69-264 |
3.46e-47 |
|
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: 160.78 E-value: 3.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 69 SFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHL-------EDHDITHVPaENRHVNTvfqsy 141
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkplekERKRIGYVP-QRRSIDR----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 142 aLFPhMTVFENVAFGL----RMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:cd03235 82 -DFP-ISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1460644645 218 LSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVM 264
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
80-278 |
3.51e-47 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 161.67 E-value: 3.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 80 NLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNTVFQSYALFPHMTVFENVAFGLRm 159
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLN- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 160 qktPAAEITP----RVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKA 235
Cdd:PRK10771 98 ---PGLKLNAaqreKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1460644645 236 LQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
57-283 |
1.24e-46 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 161.12 E-value: 1.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 57 RSPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIT--------HVP 128
Cdd:COG4598 5 APPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgeLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 129 AENRHVNT-------VFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVA 200
Cdd:COG4598 85 ADRRQLQRirtrlgmVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 201 IARAVVNKPRLLLLDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPRE 277
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALD----PELVGEVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAE 240
|
....*.
gi 1460644645 278 IYEEPK 283
Cdd:COG4598 241 VFGNPK 246
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
76-280 |
1.64e-46 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 161.34 E-value: 1.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITH--VPAENRHVNTVFQSY-ALFPHMTVFEN 152
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetVWDVRRQVGMVFQNPdNQFVGATVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 153 VAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 232
Cdd:PRK13635 103 VAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLET 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1460644645 233 LKALQRKLGITFVFVTHDQEEALTmSDRIVVMRDGKIEQDGTPREIYE 280
Cdd:PRK13635 183 VRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
61-292 |
2.77e-46 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 159.92 E-value: 2.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDI----------THVPAE 130
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqqkGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 131 NRHVNTVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKP 209
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 210 RLLLLDESLSALDYKLRKQMQNELKAL-QRKLgiTFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKN---- 284
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQprtr 241
|
....*...
gi 1460644645 285 LFVASFIG 292
Cdd:PRK11264 242 QFLEKFLL 249
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
71-268 |
3.11e-46 |
|
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: 156.77 E-value: 3.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALFpHMT 148
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAYVPQDPFLF-SGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 VFENVafglrmqktpaaeitprvldalkmvqledfaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQ 228
Cdd:cd03228 92 IRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1460644645 229 MQNELKALQRklGITFVFVTHDqEEALTMSDRIVVMRDGK 268
Cdd:cd03228 135 ILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
76-279 |
6.28e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 159.90 E-value: 6.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIT--HVPAENRHVNTVFQSY-ALFPHMTVFEN 152
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRHKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 153 VAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 232
Cdd:PRK13650 103 VAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1460644645 233 LKALQRKLGITFVFVTHDQEEaLTMSDRIVVMRDGKIEQDGTPREIY 279
Cdd:PRK13650 183 IKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
54-281 |
8.44e-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: 166.09 E-value: 8.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 54 PRSRSPLVQLAGIRKSF-DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN- 131
Cdd:COG4988 330 PAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASw 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 132 -RHVNTVFQSYALFpHMTVFENVAFGlRMQKTPAAeitprVLDALKMVQLEDFAQRKPH-----------QLSGGQQQRV 199
Cdd:COG4988 410 rRQIAWVPQNPYLF-AGTIRENLRLG-RPDASDEE-----LEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 200 AIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHDqEEALTMSDRIVVMRDGKIEQDGTPREIY 279
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELL 559
|
..
gi 1460644645 280 EE 281
Cdd:COG4988 560 AK 561
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
65-283 |
1.13e-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: 155.01 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 65 GIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRH---VNTVFQSY 141
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRArlgIGYLPQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 142 ALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 221
Cdd:cd03218 85 SIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 222 DYKLRKQMQNELKAL-QRKLGitfVFVT-HDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 283
Cdd:cd03218 165 DPIAVQDIQKIIKILkDRGIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
75-278 |
2.15e-44 |
|
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: 153.74 E-value: 2.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 75 VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE---NRHVNTVFQSYALFPHMTVFE 151
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHeraRAGIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 152 NVAFGLRMQKTPAAEITP-RVLDALKMvqLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ 230
Cdd:cd03224 95 NLLLGAYARRRAKRKARLeRVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1460644645 231 NELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:cd03224 173 EAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
69-277 |
8.97e-44 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 153.35 E-value: 8.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 69 SFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENR-HVNTVF-QSYAL-FP 145
Cdd:COG4559 10 RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELaRRRAVLpQHSSLaFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 146 hMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARA-------VVNKPRLLLLDESL 218
Cdd:COG4559 90 -FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVlaqlwepVDGGPRWLFLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460644645 219 SALDykLRKQMQ--NELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPRE 277
Cdd:COG4559 169 SALD--LAHQHAvlRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
73-274 |
1.34e-43 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 153.30 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN-----RHVNTVFQSY--ALFP 145
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrRDIQMVFQDSisAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 146 HMTVFENVAFGLR-MQKTPAAEITPRVLDALKMVQLED-FAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 223
Cdd:PRK10419 105 RKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1460644645 224 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGT 274
Cdd:PRK10419 185 VLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
73-269 |
2.07e-43 |
|
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: 152.65 E-value: 2.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN-----RHVNTVFQ-SYALF-P 145
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQdSPSAVnP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 146 HMTVFENVAFGLR-MQKTPAAEITPRVLDALKMVQLE-DFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 223
Cdd:TIGR02769 104 RMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1460644645 224 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:TIGR02769 184 VLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
58-283 |
3.95e-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: 3.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 58 SPLVQLAGIRKSFDG----KTVIDNLNLTINNGEFLTLLGPSGCGKT----TVLRLIAGLENVDSGRIHLEDHDITHVP- 128
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 129 AENRHVN-----TVFQ--SYALFPHMTVFENVAFGLRM-QKTPAAEITPRVLDALKMVQLEDFAQR---KPHQLSGGQQQ 197
Cdd:COG4172 84 RELRRIRgnriaMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 198 RVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLT----MSDRIVVMRDGKIEQDG 273
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQG 239
|
250
....*....|
gi 1460644645 274 TPREIYEEPK 283
Cdd:COG4172 240 PTAELFAAPQ 249
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
71-280 |
7.77e-43 |
|
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: 150.07 E-value: 7.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALFpHMT 148
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 VFENVAFGLRmqktpaaEITP-RVLDALKMVQLEDFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDE 216
Cdd:cd03251 92 VAENIAYGRP-------GATReEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 217 SLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREIYE 280
Cdd:cd03251 165 ATSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
61-273 |
1.02e-42 |
|
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: 149.27 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGeFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENR-HVNTVFQ 139
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 140 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 219
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 220 ALDYKLRKQMQNELKALQRklGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 273
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
65-283 |
1.48e-42 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 149.41 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 65 GIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPaenrhvntVFQ----- 139
Cdd:COG1137 8 NLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP--------MHKrarlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 140 -SY-----ALFPHMTVFENVAFGLRMQKTPAAEITPRvLDALkmvqLEDF-----AQRKPHQLSGGQQQRVAIARAVVNK 208
Cdd:COG1137 80 iGYlpqeaSIFRKLTVEDNILAVLELRKLSKKEREER-LEEL----LEEFgithlRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1460644645 209 PRLLLLDESLSALDYKLRKQMQNELKAL-QRKLGitfVFVT-HDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 283
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKIIRHLkERGIG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
73-281 |
1.69e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 150.62 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHD---ITHVPAENRHVNTVFQSyalfPH--- 146
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdEENLWDIRNKAGMVFQN----PDnqi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 147 --MTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 224
Cdd:PRK13633 99 vaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1460644645 225 LRKQMQNELKALQRKLGITFVFVTHDQEEALTmSDRIVVMRDGKIEQDGTPREIYEE 281
Cdd:PRK13633 179 GRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
58-278 |
3.07e-42 |
|
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: 149.08 E-value: 3.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 58 SPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGlEN--VDSGRIHLEDHDITHV-PAENR-- 132
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG-DLppTYGNDVRLFGERRGGEdVWELRkr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 133 --HVNTVFQSYaLFPHMTVFENVAFGL-----RMQKTPAAEITpRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAV 205
Cdd:COG1119 80 igLVSPALQLR-FPRDETVLDVVLSGFfdsigLYREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 206 VNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
61-273 |
3.15e-42 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 148.12 E-value: 3.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDG--KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHV-PAE-NRHVNT 136
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLdPADlRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 137 VFQSYALFpHMTVFENVAFGLrmqktPAAEiTPRVLDALKMVQLEDFAQRKPH-----------QLSGGQQQRVAIARAV 205
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLGA-----PLAD-DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644645 206 VNKPRLLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHDQeEALTMSDRIVVMRDGKIEQDG 273
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
70-284 |
8.64e-42 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 148.26 E-value: 8.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 70 FDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLR-------LIAGLEnVdSGRIHLEDHDI----THVPAENRHVNTVF 138
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR-V-EGEILLDGEDIydpdVDVVELRRRVGMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 139 QSYALFPhMTVFENVAFGLRMQ-KTPAAEITPRVLDALKMVQL----EDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 213
Cdd:COG1117 99 QKPNPFP-KSIYDNVAYGLRLHgIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 214 LDESLSALD-----------YKLRKQMqnelkalqrklgiTFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEP 282
Cdd:COG1117 178 MDEPTSALDpistakieeliLELKKDY-------------TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNP 244
|
..
gi 1460644645 283 KN 284
Cdd:COG1117 245 KD 246
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
61-310 |
9.01e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 148.31 E-value: 9.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSF-----DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENR--H 133
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 134 VNTVFQSYAL--FPHMTVFENVA--------FGLRMQKTPA--AEITPRvLDALKMvQLEDFAQRKPHQLSGGQQQRVAI 201
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGLTKKrrELFREL-LATLGL-GLENRLDTKVGLLSGGQRQALSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 202 ARAVVNKPRLLLLDESLSALDYKlRKQMQNEL-KALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQD--Gtprei 278
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDvsG----- 233
|
250 260 270
....*....|....*....|....*....|..
gi 1460644645 279 yEEPKNLFVASFIGEiniFDATVIERLDEQRV 310
Cdd:COG1101 234 -EEKKKLTVEDLLEL---FEEIRGEELADDRL 261
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
58-284 |
1.36e-41 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 147.68 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 58 SPLVQLAGIRKSFDGKT---------VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVP 128
Cdd:COG4167 2 SALLEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 129 AENR--HVNTVFQ--SYALFPHMTVFENVAFGLRMQ-KTPAAEITPRVLDALKMVQL-EDFAQRKPHQLSGGQQQRVAIA 202
Cdd:COG4167 82 YKYRckHIRMIFQdpNTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 203 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEP 282
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
..
gi 1460644645 283 KN 284
Cdd:COG4167 242 QH 243
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
61-269 |
4.68e-41 |
|
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: 144.67 E-value: 4.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNTVFQS 140
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 141 YALFPHMTVFENVAFGLRMQKTPAAEITpRVLDalkMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 220
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRID-EVLD---VVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1460644645 221 LDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:cd03268 157 LDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
59-277 |
1.62e-40 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 144.91 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 59 PLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNT 136
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 137 VFQSYAL-FPhMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVV------NKP 209
Cdd:PRK13548 81 LPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 210 RLLLLDESLSALDykLRKQMQ--NELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPRE 277
Cdd:PRK13548 160 RWLLLDEPTSALD--LAHQHHvlRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
58-283 |
1.96e-40 |
|
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: 143.97 E-value: 1.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 58 SPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPA-------- 129
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhriarlgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 130 ----ENRHVntvfqsyalFPHMTVFEN--VAFGLRMQKTPAAEITPRVLD---ALKmvqleDFAQRKPHQLSGGQQQRVA 200
Cdd:COG0410 81 gyvpEGRRI---------FPSLTVEENllLGAYARRDRAEVRADLERVYElfpRLK-----ERRRQRAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 201 IARAVVNKPRLLLLDE-SLsALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIY 279
Cdd:COG0410 147 IGRALMSRPKLLLLDEpSL-GLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
....
gi 1460644645 280 EEPK 283
Cdd:COG0410 225 ADPE 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
75-281 |
3.13e-40 |
|
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: 143.45 E-value: 3.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 75 VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIT--HVPAENRHVNTVFQSYALFPhMTVFEN 152
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRdlNLRWLRSQIGLVSQEPVLFD-GTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 153 VAFGlrmqKTPAAEITprVLDALKMVQLEDFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 221
Cdd:cd03249 97 IRYG----KPDATDEE--VEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460644645 222 DYKLRKQMQnelKALQR-KLGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 281
Cdd:cd03249 171 DAESEKLVQ---EALDRaMKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
60-273 |
3.63e-40 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 142.51 E-value: 3.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 60 LVQLAGIRKSFDGKT----VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE-NRHV 134
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEaRRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 135 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 214
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 215 DESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 273
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
76-283 |
5.43e-40 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 145.62 E-value: 5.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRH-----VNTVFQS--YALFPHMT 148
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavrsdIQMIFQDplASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 VFENVAFGLRM--QKTPAAEITPRVLDALKMVQL-EDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 225
Cdd:PRK15079 117 IGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644645 226 RKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 283
Cdd:PRK15079 197 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
71-285 |
9.55e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 143.29 E-value: 9.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLE----DHDITHVPAENRHVNTVFQSY--ALF 144
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepiKYDKKSLLEVRKTVGIVFQNPddQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 145 PHmTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 224
Cdd:PRK13639 93 AP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460644645 225 LRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 285
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
56-274 |
2.71e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 140.72 E-value: 2.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 56 SRSPLVQLAGIRKSF-DGKT---VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPA-- 129
Cdd:PRK11629 1 MNKILLQCDNLCKRYqEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 130 ----ENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAV 205
Cdd:PRK11629 81 kaelRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 206 VNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSdRIVVMRDGKIEQDGT 274
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAELS 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
73-288 |
3.20e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 141.67 E-value: 3.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIThvpAEN-----RHVNTVFQSY-ALFPH 146
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS---KENlkeirKKIGIIFQNPdNQFIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 147 MTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 226
Cdd:PRK13632 99 ATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGK 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 227 KQMQNELKALQRKLGITFVFVTHDQEEALtMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVA 288
Cdd:PRK13632 179 REIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEILEKA 239
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
61-310 |
3.56e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 142.55 E-value: 3.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHvpaenRHVNTVfqS 140
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-----EDRRRI--G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 141 Y-----ALFPHMTVFENVAF-----GLrmqktPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPR 210
Cdd:COG4152 75 YlpeerGLYPKMKVGEQLVYlarlkGL-----SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 211 LLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE-PKNLFVAS 289
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQfGRNTLRLE 228
|
250 260
....*....|....*....|....*
gi 1460644645 290 FIGEI----NIFDATVIERLDEQRV 310
Cdd:COG4152 229 ADGDAgwlrALPGVTVVEEDGDGAE 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
59-269 |
5.88e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 146.32 E-value: 5.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 59 PLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITH---VPAENRHVN 135
Cdd:COG1129 3 PLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFrspRDAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 136 TVFQSYALFPHMTVFENVAFGlRMQKTPA----AEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRL 211
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLG-REPRRGGlidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 212 LLLDESLSALDYK----LRKQMqNELKAlqrkLGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:COG1129 162 LILDEPTASLTEReverLFRII-RRLKA----QGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
61-269 |
8.43e-39 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 138.95 E-value: 8.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIThvPAENRHVNTVFQS 140
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD--IAARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 141 YALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 220
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1460644645 221 LDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:cd03269 159 LDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
61-269 |
1.36e-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: 136.79 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDhdithvpaenrhvntvfqs 140
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 141 yalfphmtvfENVAFGlrmqktpaaeiTPRvlDALK----MVqledfaqrkpHQLSGGQQQRVAIARAVVNKPRLLLLDE 216
Cdd:cd03216 62 ----------KEVSFA-----------SPR--DARRagiaMV----------YQLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 217 SLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
60-282 |
3.11e-38 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 139.13 E-value: 3.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 60 LVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIthvPAENRH------ 133
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI---PAMSRSrlytvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 134 --VNTVFQSYALFPHMTVFENVAFGLRMQ-KTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPR 210
Cdd:PRK11831 84 krMSMLFQSGALFTDMNVFDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 211 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEP 282
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
59-282 |
3.39e-38 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 138.58 E-value: 3.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 59 PLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RH--V 134
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiaRMgvV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 135 NTvFQSYALFPHMTVFEN--VAFGLRMQ--------KTPA-----AEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRV 199
Cdd:PRK11300 84 RT-FQHVRLFREMTVIENllVAQHQQLKtglfsgllKTPAfrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 200 AIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIY 279
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
...
gi 1460644645 280 EEP 282
Cdd:PRK11300 243 NNP 245
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
71-285 |
6.23e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 138.35 E-value: 6.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQS-YALFPHM 147
Cdd:PRK13648 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQNpDNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 148 TVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRK 227
Cdd:PRK13648 100 IVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644645 228 QMQNELKALQRKLGITFVFVTHDQEEALTmSDRIVVMRDGKIEQDGTPREIYEEPKNL 285
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
59-280 |
2.00e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 138.01 E-value: 2.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 59 PLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDI-THVPAENRHVNTV 137
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 138 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 218 LSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYE 280
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
78-282 |
2.13e-37 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 138.85 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 78 NLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDH---DI---THVPAENRHVNTVFQSYALFPHMTVFE 151
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAekgICLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 152 NVAFGlrMQKTPAAEItprvldaLKMVQL---EDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQ 228
Cdd:PRK11144 96 NLRYG--MAKSMVAQF-------DKIVALlgiEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 229 MQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEP 282
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
71-269 |
3.45e-37 |
|
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: 134.31 E-value: 3.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIhLEDHDITHVPAENRHVNTVFQS--YALFPHmT 148
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSI-LLNGKPIKAKERRKSIGYVMQDvdYQLFTD-S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 VFENVAFGLRmqktPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQ 228
Cdd:cd03226 89 VREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1460644645 229 MQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:cd03226 165 VGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
73-285 |
5.71e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 136.08 E-value: 5.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN-----RHVNTVFQSY-ALFPH 146
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTvwdirEKVGIVFQNPdNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 147 MTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 226
Cdd:PRK13640 100 ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 227 KQMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 285
Cdd:PRK13640 180 EQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEML 237
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
70-285 |
6.71e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 136.30 E-value: 6.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 70 FDGKTVIDnLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIT------HVPAENRHVNTVFQsyal 143
Cdd:PRK13634 18 FERRALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 144 FPHMTVFE-----NVAFGLRMQKTPAAEITPRVLDALKMVQL-EDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:PRK13634 93 FPEHQLFEetvekDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644645 218 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 285
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEL 240
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
71-277 |
9.74e-37 |
|
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: 134.28 E-value: 9.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALFpHMT 148
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrRAIGVVPQDTVLF-NDT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 VFENVAFGlrmqKTPAAEItpRVLDALKMVQLEDFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:cd03253 91 IGYNIRYG----RPDATDE--EVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 218 LSALDYKLRKQMQNELKALQRklGITFVFVTHDQEEALTmSDRIVVMRDGKIEQDGTPRE 277
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
45-342 |
1.21e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 136.88 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 45 GQSQKLNIQPRSRSPL-VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDhd 123
Cdd:PRK13536 25 GISEAKASIPGSMSTVaIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 124 iTHVPAENR----HVNTVFQSYALFPHMTVFEN-VAFG--LRMQKTPAAEITPRVLDalkMVQLEDFAQRKPHQLSGGQQ 196
Cdd:PRK13536 103 -VPVPARARlaraRIGVVPQFDNLDLEFTVRENlLVFGryFGMSTREIEAVIPSLLE---FARLESKADARVSDLSGGMK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 197 QRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPR 276
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPH 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 277 EIYEE-------------PKNL--FVASFIGEINIFDATVI-ERLDEQRVRANVEGRecnitvnfaveAGQRLhvLLRPE 340
Cdd:PRK13536 258 ALIDEhigcqvieiyggdPHELssLVKPYARRIEVSGETLFcYAPDPEQVRVQLRGR-----------AGLRL--LQRPP 324
|
..
gi 1460644645 341 DL 342
Cdd:PRK13536 325 NL 326
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
62-274 |
2.66e-36 |
|
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: 132.65 E-value: 2.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 62 QLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENR---HVNTVF 138
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 139 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDaLKMVqLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 218
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYE-LFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1460644645 219 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGT 274
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
71-278 |
6.64e-36 |
|
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: 138.70 E-value: 6.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALFPHmT 148
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVALVSQDVVLFND-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 VFENVAFGlRMQKTPAAEItprvLDALKMVQLEDFAQRKP---HQ--------LSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:TIGR02203 422 IANNIAYG-RTEQADRAEI----ERALAAAYAQDFVDKLPlglDTpigengvlLSGGQRQRLAIARALLKDAPILILDEA 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460644645 218 LSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:TIGR02203 497 TSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
60-282 |
1.00e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 132.42 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 60 LVQLAGIRKSF-DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRI---HLEDHDITHVPAENRHVN 135
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 136 TVFQS-YALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 214
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644645 215 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEaLTMSDRIVVMRDGKIEQDGTPREIYEEP 282
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
65-283 |
1.16e-35 |
|
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: 131.24 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 65 GIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRH---VNTVFQSY 141
Cdd:TIGR04406 6 NLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERArlgIGYLPQEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 142 ALFPHMTVFENVAFGL-RMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 220
Cdd:TIGR04406 86 SIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460644645 221 LDYKLRKQMQNELKAL-QRKLGitfVFVT-HDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 283
Cdd:TIGR04406 166 VDPIAVGDIKKIIKHLkERGIG---VLITdHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
66-291 |
4.29e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 130.47 E-value: 4.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 66 IRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNT--------- 136
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVadknqlrll 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 137 ------VFQSYALFPHMTVFENVAFG----LRMQKTPAAEitpRVLDALKMVQLEDFAQRK-PHQLSGGQQQRVAIARAV 205
Cdd:PRK10619 91 rtrltmVFQHFNLWSHMTVLENVMEApiqvLGLSKQEARE---RAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 206 VNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 285
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
....*.
gi 1460644645 286 FVASFI 291
Cdd:PRK10619 247 RLQQFL 252
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
72-278 |
4.98e-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: 136.03 E-value: 4.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 72 GKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALFPHmTV 149
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 150 FENVAfglRMqktpaAEITP-RVLDALKMVQLEDFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:COG4618 423 AENIA---RF-----GDADPeKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460644645 218 LSALDYKLRKQMQNELKALqRKLGITFVFVTHDQeEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:COG4618 495 NSNLDDEGEAALAAAIRAL-KARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
76-285 |
9.95e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 129.83 E-value: 9.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIThvpAEN-----RHVNTVFQSY-ALFPHMTV 149
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT---AENvwnlrRKIGMVFQNPdNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 150 FENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQM 229
Cdd:PRK13642 100 EDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1460644645 230 QNELKALQRKLGITFVFVTHDQEEALTmSDRIVVMRDGKIEQDGTPREIYEEPKNL 285
Cdd:PRK13642 180 MRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDM 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
72-269 |
1.76e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 127.68 E-value: 1.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 72 GKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIT-----HVPAENRHVNTVFQSYALFPH 146
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 147 MTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 226
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1460644645 227 KQMQNELKALQRkLGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:PRK10908 174 EGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
71-278 |
2.59e-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: 127.60 E-value: 2.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE--NRHVNTVFQSYALFpHMT 148
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 VFENVAFGlrmqkTPAAEITpRVLDALKMVQLEDFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:cd03252 92 IRDNIALA-----DPGMSME-RVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460644645 218 LSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
69-277 |
3.41e-34 |
|
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: 126.96 E-value: 3.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 69 SFD-GKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALFP 145
Cdd:cd03254 11 SYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 146 HmTVFENVAFGlrmqkTPAAEITpRVLDALKMVQLEDFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLL 214
Cdd:cd03254 91 G-TIMENIRLG-----RPNATDE-EVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 215 DESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPRE 277
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDE 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
66-285 |
4.30e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 129.05 E-value: 4.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 66 IRKSFDGKT-----VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIH--LEDHDITHVPAEN------- 131
Cdd:PRK13651 8 IVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNKKKTKEKekvlekl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 132 -----------------RHVNTVFQ--SYALFpHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQL-EDFAQRKPHQL 191
Cdd:PRK13651 88 viqktrfkkikkikeirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 192 SGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQ 271
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIK 245
|
250
....*....|....
gi 1460644645 272 DGTPREIYEEPKNL 285
Cdd:PRK13651 246 DGDTYDILSDNKFL 259
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
57-253 |
8.45e-34 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 125.98 E-value: 8.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 57 RSPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE--NRHV 134
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 135 NTVFQSYALFPHmTVFENVAFGLRM-QKTPAAEitpRVLDALKMVQLEDFAQRKP-HQLSGGQQQRVAIARAVVNKPRLL 212
Cdd:PRK10247 84 SYCAQTPTLFGD-TVYDNLIFPWQIrNQQPDPA---IFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1460644645 213 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEE 253
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
56-281 |
8.72e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 132.07 E-value: 8.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 56 SRSPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIT-HVPAE--NR 132
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDaiAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 133 HVNTVFQSYALFPHMTVFENVAFGLRmqKTPAAEITPRVLDAlkmvQLEDFAQR---------KPHQLSGGQQQRVAIAR 203
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLE--PTKGGRLDRKAARA----RIRELSERygldvdpdaKVEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 204 AVVNKPRLLLLDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYE 280
Cdd:COG3845 155 ALYRGARILILDEPTAVLT----PQEADELFEILRRLaaeGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSE 230
|
.
gi 1460644645 281 E 281
Cdd:COG3845 231 E 231
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
75-269 |
9.65e-34 |
|
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: 124.25 E-value: 9.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 75 VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALFPHmTVFEN 152
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYLPQDDELFSG-SIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 153 VafglrmqktpaaeitprvldalkmvqledfaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 232
Cdd:cd03246 96 I-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 1460644645 233 LKALqRKLGITFVFVTHdQEEALTMSDRIVVMRDGKI 269
Cdd:cd03246 139 IAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
61-284 |
2.23e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 125.41 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGL-----ENVDSGRIHLEDHDITHVPAE--NRH 133
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIelRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 134 VNTVFQSYALFPHMTVFENVAFGLRMQK--TPAAEITPRVLDALKMVQLEDFAQRK----PHQLSGGQQQRVAIARAVVN 207
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1460644645 208 KPRLLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKN 284
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
76-283 |
3.78e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 127.00 E-value: 3.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRH-----VNTVFQS-YA-LFPHMT 148
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllrqkIQIVFQNpYGsLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 VFENVAFGLRMQKT-PAAEITPRVLDALKMVQLE-DFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 226
Cdd:PRK11308 111 VGQILEEPLLINTSlSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1460644645 227 KQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 283
Cdd:PRK11308 191 AQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
54-286 |
6.30e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 129.83 E-value: 6.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 54 PRSRSPLVQLAGIRKSF-----------DGKTVIDNLNLTINNGEFLTLLGPSGCGKTT----VLRLIAGlenvdSGRIH 118
Cdd:PRK15134 269 PEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 119 LEDHDITH------VPAENRhVNTVFQ--SYALFPHMTVFENVAFGLRM-QKT-PAAEITPRVLDALKMVQLE-DFAQRK 187
Cdd:PRK15134 344 FDGQPLHNlnrrqlLPVRHR-IQVVFQdpNSSLNPRLNVLQIIEEGLRVhQPTlSAAQREQQVIAVMEEVGLDpETRHRY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 188 PHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 267
Cdd:PRK15134 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
250
....*....|....*....
gi 1460644645 268 KIEQDGTPREIYEEPKNLF 286
Cdd:PRK15134 503 EVVEQGDCERVFAAPQQEY 521
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
71-278 |
6.42e-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: 131.02 E-value: 6.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHV-PAE-NRHVNTVFQSYALFPHmT 148
Cdd:TIGR01846 468 DSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIAdPAWlRRQMGVVLQENVLFSR-S 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 VFENVAFGlrmqkTPAAEITpRVLDALKMVQLEDFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:TIGR01846 547 IRDNIALC-----NPGAPFE-HVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFDEA 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460644645 218 LSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:TIGR01846 621 TSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
60-281 |
1.47e-32 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 123.58 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 60 LVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDS---GRIHLEDHDITH-------VPA 129
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQRegrlardIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 130 ENRHVNTVFQSYALFPHMTVFENVAFGlRMQKTP---------AAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVA 200
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 201 IARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYE 280
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDN 242
|
.
gi 1460644645 281 E 281
Cdd:PRK09984 243 E 243
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
71-249 |
1.96e-32 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 128.77 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLedhdithvPAENRhvnTVF---QSYalFPHM 147
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--------PAGAR---VLFlpqRPY--LPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 148 TVFENVAFGLRMQKTPAAEItprvLDALKMVQLEDFAQR------KPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 221
Cdd:COG4178 441 TLREALLYPATAEAFSDAEL----REALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
170 180
....*....|....*....|....*....
gi 1460644645 222 DYKLRKQMqneLKALQRKL-GITFVFVTH 249
Cdd:COG4178 517 DEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
75-284 |
2.18e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 123.03 E-value: 2.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 75 VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVD-----------SGR-IHLEDHDITHVpaeNRHVNTVFQSYA 142
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvegevrlFGRnIYSPDVDPIEV---RREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 143 LFPHMTVFENVAFGLRMQK--TPAAEITPRVLDALKMVQL----EDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 216
Cdd:PRK14267 96 PFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644645 217 SLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKN 284
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
53-216 |
3.74e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 122.15 E-value: 3.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 53 QPRSRSPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPaENR 132
Cdd:COG4674 3 LDTMHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLD-EHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 133 HVNT----VFQSYALFPHMTVFENVAFGLRMQKTP--------AAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVA 200
Cdd:COG4674 82 IARLgigrKFQKPTVFEELTVFENLELALKGDRGVfaslfarlTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLE 161
|
170
....*....|....*.
gi 1460644645 201 IARAVVNKPRLLLLDE 216
Cdd:COG4674 162 IGMLLAQDPKLLLLDE 177
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
58-284 |
4.48e-32 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 122.19 E-value: 4.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 58 SPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVD-----SGRIHLEDHDI----THVP 128
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysprTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 129 AENRHVNTVFQSYALFPhMTVFENVAFGLRMQKTPAAEITPRVLD-ALKMVQLEDFAQRKPHQ----LSGGQQQRVAIAR 203
Cdd:PRK14239 83 DLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEkSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 204 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 283
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
.
gi 1460644645 284 N 284
Cdd:PRK14239 240 H 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
76-281 |
9.08e-32 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 126.46 E-value: 9.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSG----RIHLEDHDITHVPAENR-----HVNTVFQSYALFPH 146
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvRVGDEWVDMTKPGPDGRgrakrYIGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 147 MTVFENV--AFGLRMQKTPAAEitpRVLDALKMVQL-EDFAQ----RKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 219
Cdd:TIGR03269 380 RTVLDNLteAIGLELPDELARM---KAVITLKMVGFdEEKAEeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 220 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 281
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
71-276 |
1.22e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 121.38 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIThvpAENRH-----VNTVFQSY--AL 143
Cdd:PRK13647 16 DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN---AENEKwvrskVGLVFQDPddQV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 144 FPhMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 223
Cdd:PRK13647 93 FS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 224 KLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPR 276
Cdd:PRK13647 172 RGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
58-277 |
5.31e-31 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 125.22 E-value: 5.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 58 SPLVQLAGIRKSF---DGKT-VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE--- 130
Cdd:PRK10535 2 TALLELKDIRRSYpsgEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADala 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 131 ---NRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVN 207
Cdd:PRK10535 82 qlrREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 208 KPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEAlTMSDRIVVMRDGKIEQDGTPRE 277
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEIVRNPPAQE 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
74-272 |
7.87e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 117.96 E-value: 7.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 74 TVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENR------HVNTVFQSYALFPHM 147
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 148 TVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRK 227
Cdd:PRK10584 104 NALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1460644645 228 QMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGKIEQD 272
Cdd:PRK10584 184 KIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQEE 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
76-279 |
8.46e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 119.73 E-value: 8.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDH-------DITHVPAENRHVNTVFQ--SYALFPH 146
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipanlkKIKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 147 mTVFENVAFGLRMQKTPAAEITPRVLDALKMVQL-EDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 225
Cdd:PRK13645 107 -TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 226 RKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIY 279
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
71-281 |
1.29e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 119.18 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLE----DHDITHVPAENRHVNTVFQS--YALF 144
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkpiDYSRKGLMKLRESVGMVFQDpdNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 145 PhMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 224
Cdd:PRK13636 97 S-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1460644645 225 LRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 281
Cdd:PRK13636 176 GVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
73-281 |
1.39e-30 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 118.19 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVntvfqsyALFP--HMT 148
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRL-------ALLPqhHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 -----VFENVAFGlrmqKTP--------AAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 215
Cdd:PRK11231 88 pegitVRELVAYG----RSPwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 216 ESLSALDYklrkQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 281
Cdd:PRK11231 164 EPTTYLDI----NHQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
59-278 |
1.49e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 121.49 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 59 PLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE--NRHVNT 136
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARaaSRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 137 VFQSYALFPHMTVFENVafglRMQKTP-------AAEITPRVLD-ALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNK 208
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVV----EMGRTPhrsrfdtWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 209 PRLLLLDESLSALDykLRKQMQNelKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:PRK09536 158 TPVLLLDEPTASLD--INHQVRT--LELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
59-282 |
1.51e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 118.22 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 59 PLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDS-----GRIHLEDHDI----THVPA 129
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 130 ENRHVNTVFQSYALFPhMTVFENVAFGLRMQK-TPAAEITPRVLDALKMVQLEDFAQRKPHQ----LSGGQQQRVAIARA 204
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 205 VVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM-----RDGKIEQDGTPREIY 279
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEFGLTKKIF 244
|
...
gi 1460644645 280 EEP 282
Cdd:PRK14258 245 NSP 247
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
54-264 |
1.63e-30 |
|
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: 123.17 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 54 PRSRSPLVQLAGIRKSFDGKT-VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN- 131
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSw 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 132 -RHVNTVFQSYALFPHmTVFENVAFGLRMQktPAAEITprvlDALKMVQLEDFAQRKP-----------HQLSGGQQQRV 199
Cdd:TIGR02857 395 rDQIAWVPQHPFLFAG-TIAENIRLARPDA--SDAEIR----EALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460644645 200 AIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHDQEEALTMsDRIVVM 264
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
70-281 |
1.94e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 118.31 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 70 FDGKTVIDnLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITH------VPAENRHVNTVFQsyal 143
Cdd:PRK13649 18 FEGRALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIKQIRKKVGLVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 144 FPHMTVFE-----NVAFGLRMQKTPAAEITPRVLDALKMVQL-EDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:PRK13649 93 FPESQLFEetvlkDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 218 LSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 281
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
76-285 |
2.09e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 118.39 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIT------HVPAENRHVNTVFQsyalFPHMTV 149
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQ----FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 150 FEN-----VAFGLRMQKTPAAEITPRVLDALKMVQL-EDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 223
Cdd:PRK13641 99 FENtvlkdVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 224 KLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 285
Cdd:PRK13641 179 EGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWL 239
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
76-310 |
5.29e-30 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 122.27 E-value: 5.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN-----RHVNTVFQS-YA-LFPHMT 148
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 VFENVAFGLRMQKT-PAAEITPRVLDALKMVQLE-DFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 226
Cdd:PRK10261 420 VGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 227 KQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINIFDAtviERLD 306
Cdd:PRK10261 500 GQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVADP---SRQR 576
|
....
gi 1460644645 307 EQRV 310
Cdd:PRK10261 577 PQRV 580
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
74-277 |
1.02e-29 |
|
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: 121.47 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 74 TVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALFpHMTVFE 151
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF-NDTIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 152 NVAFGlRMQKTPAAeitprVLDALKMVQLEDFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLLDESLSA 220
Cdd:COG5265 451 NIAYG-RPDASEEE-----VEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 221 LDYKLRKQMQNELKALQRklGITFVFVTH------DqeealtmSDRIVVMRDGKIEQDGTPRE 277
Cdd:COG5265 525 LDSRTERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAE 578
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
73-278 |
1.15e-29 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 120.53 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALFPHmTVF 150
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 151 ENVAfglRMQKTPAAEitpRVLDALKMVQLEDFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDESLS 219
Cdd:TIGR01842 410 ENIA---RFGENADPE---KIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 220 ALDYKLRKQMQNELKALQRKlGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:TIGR01842 484 NLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
75-282 |
1.84e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 120.98 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 75 VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLE-------DHDITHvpaenRHVNTVFQSYALFPHm 147
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDgvplvqyDHHYLH-----RQVALVGQEPVLFSG- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 148 TVFENVAFGLRmqKTPAAEITprvlDALKMVQLEDFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDE 216
Cdd:TIGR00958 570 SVRENIAYGLT--DTPDEEIM----AAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1460644645 217 SLSALDyklrKQMQNELKALQRKLGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREIYEEP 282
Cdd:TIGR00958 644 ATSALD----AECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
54-273 |
3.93e-29 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 113.40 E-value: 3.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 54 PRSRSPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLeDHDITHVPAenrh 133
Cdd:cd03220 16 GSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-RGRVSSLLG---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 134 VNTVFQsyalfPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 213
Cdd:cd03220 91 LGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 214 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 273
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
73-285 |
4.19e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.51 E-value: 4.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIT--HVPAENRHVNTVFQSY--ALFPhMT 148
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFVGLVFQNPddQIFS-PT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 VFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQ 228
Cdd:PRK13652 96 VEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1460644645 229 MQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 285
Cdd:PRK13652 176 LIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLL 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
67-281 |
5.68e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 113.25 E-value: 5.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 67 RKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIH--------LEdhdithvpaenrhVNTVF 138
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEvngrvsalLE-------------LGAGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 139 QsyalfPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 218
Cdd:COG1134 100 H-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 219 SALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 281
Cdd:COG1134 175 AVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
55-308 |
6.82e-29 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 115.21 E-value: 6.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 55 RSRSPLVQLAGIRKSF---DGK-TVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLEnVDSGRI------------H 118
Cdd:PRK09473 7 QQADALLDVKDLRVTFstpDGDvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIggsatfngreilN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 119 LEDHDITHVPAEnrHVNTVFQS--YALFPHMTVFENVAFGL----RMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLS 192
Cdd:PRK09473 86 LPEKELNKLRAE--QISMIFQDpmTSLNPYMRVGEQLMEVLmlhkGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 193 GGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQD 272
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 243
|
250 260 270
....*....|....*....|....*....|....*.
gi 1460644645 273 GTPREIYEEPKNLFVasfIGEINifdatVIERLDEQ 308
Cdd:PRK09473 244 GNARDVFYQPSHPYS---IGLLN-----AVPRLDAE 271
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
71-295 |
1.56e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 112.83 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDH------DITHVPA--ENRHVNTVFQSYA 142
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAikLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 143 LFPHMTVFENVAFGLRMQKTPAA-EITPRVLDALKMV----QLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 218 LSALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASF-IGEIN 295
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYvIGRIS 257
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
59-269 |
3.02e-28 |
|
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: 109.44 E-value: 3.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 59 PLVQLAGIRksfdGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIT------------- 125
Cdd:cd03215 3 PVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrsprdairagia 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 126 HVPaENRHvntvfqSYALFPHMTVFENVAFglrmqktpaaeitprvldalkmvqledfaqrkPHQLSGGQQQRVAIARAV 205
Cdd:cd03215 79 YVP-EDRK------REGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 206 VNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
61-249 |
4.90e-28 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 109.51 E-value: 4.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRksfDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENR-------H 133
Cdd:PRK13538 5 RNLACER---DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHqdllylgH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 134 VNtvfqsyALFPHMTVFENVAFGLRMQKTPAAEitpRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 213
Cdd:PRK13538 82 QP------GIKTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 1460644645 214 LDESLSALDYKLRKQMQNELKALQRKLGITfVFVTH 249
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQHAEQGGMV-ILTTH 187
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
61-280 |
7.35e-28 |
|
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: 115.28 E-value: 7.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENV--DSGRI--------------------- 117
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 118 -------HLEDHDI-------THVPAENRHVNTVFQ-SYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLED 182
Cdd:TIGR03269 81 pcpvcggTLEPEEVdfwnlsdKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 183 FAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIV 262
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....*...
gi 1460644645 263 VMRDGKIEQDGTPREIYE 280
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVA 258
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
73-278 |
7.69e-28 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 110.85 E-value: 7.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALFPHMTVF 150
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 151 ENVAFGlRMQKTPA-----AEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 225
Cdd:PRK10253 100 ELVARG-RYPHQPLftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 226 RKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:PRK10253 179 QIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
50-269 |
1.04e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 114.76 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 50 LNIQPRSRSPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPA 129
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 130 ENRH---VNTVFQSYALFPHMTVFENVAFGLrmqktPAAEITPRVLDALkMVQLEdfAQRKPHQLSG----GQQQRVAIA 202
Cdd:PRK15439 81 AKAHqlgIYLVPQEPLLFPNLSVKENILFGL-----PKRQASMQKMKQL-LAALG--CQLDLDSSAGslevADRQIVEIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1460644645 203 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
45-295 |
1.06e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 110.96 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 45 GQSQKLNIQprSRSPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLED--- 121
Cdd:PRK14271 8 GQSGAADVD--AAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDvll 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 122 -----HDITHVPAENRHVNTVFQSYALFPhMTVFENVAFGLRMQK-TPAAEITPRVLDALKMVQLEDFAQRK----PHQL 191
Cdd:PRK14271 86 ggrsiFNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 192 SGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGKIEQ 271
Cdd:PRK14271 165 SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
250 260
....*....|....*....|....
gi 1460644645 272 DGTPREIYEEPKNLFVASFIGEIN 295
Cdd:PRK14271 243 EGPTEQLFSSPKHAETARYVAGLS 266
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
49-270 |
1.14e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.78 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 49 KLNIQPRSRS--PLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDhdith 126
Cdd:COG0488 302 EIRFPPPERLgkKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE----- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 127 vpaenrhvnTVFQSY------ALFPHMTVFENVAFGLRMQKtpaaEITPRVLdalkmvqLEDF-----AQRKP-HQLSGG 194
Cdd:COG0488 377 ---------TVKIGYfdqhqeELDPDKTVLDELRDGAPGGT----EQEVRGY-------LGRFlfsgdDAFKPvGVLSGG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 195 QQQRVAIARAVVNKPRLLLLDE--------SLSALdyklrkqmqneLKALQRKLGiTFVFVTHDQE--EALTmsDRIVVM 264
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEptnhldieTLEAL-----------EEALDDFPG-TVLLVSHDRYflDRVA--TRILEF 502
|
....*.
gi 1460644645 265 RDGKIE 270
Cdd:COG0488 503 EDGGVR 508
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
76-293 |
1.64e-27 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 110.26 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENR--HVNTVFQ--SYALFPHMTVFE 151
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRsqRIRMIFQdpSTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 152 NVAFGLRMQ-KTPAAEITPRVLDALKMVQL-EDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQM 229
Cdd:PRK15112 109 ILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 230 QNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEP-----KNLfVASFIGE 293
Cdd:PRK15112 189 INLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPlheltKRL-IAGHFGE 256
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
76-285 |
1.94e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 110.25 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHvPAENRHVNTVFQSYAL---FPHMTVFEN 152
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITH-KTKDKYIRPVRKRIGMvfqFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 153 -----VAFGLRMQKTPAAEITPRVLDALKMVQLE-DFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 226
Cdd:PRK13646 102 tvereIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 227 KQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 285
Cdd:PRK13646 182 RQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
60-268 |
3.96e-27 |
|
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: 113.00 E-value: 3.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 60 LVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGL--ENVDSGRIHLEDHDI--THV-PAENRHV 134
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLkaSNIrDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 135 NTVFQSYALFPHMTVFENVAFG----LRMQKTPAAEITPRVLDALKMVQLEDFAQRKP-HQLSGGQQQRVAIARAVVNKP 209
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 210 RLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGK 268
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
68-278 |
4.40e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 108.06 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 68 KSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRH---VNTVFQSYALF 144
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArrgIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 145 PHMTVFENVAFGLRMQKTPAAEI-TPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 223
Cdd:PRK10895 91 RRLSVYDNLMAVLQIRDDLSAEQrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1460644645 224 KLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:PRK10895 171 ISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
59-250 |
6.79e-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: 112.45 E-value: 6.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 59 PLVQLAGIRKSFDG-KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPA-ENRHVNT 136
Cdd:TIGR02868 333 PTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 137 VF-QSYALFpHMTVFENVAFGlRMQKTPAAeitprVLDALKMVQLEDFAQRKPH-----------QLSGGQQQRVAIARA 204
Cdd:TIGR02868 413 VCaQDAHLF-DTTVRENLRLA-RPDATDEE-----LWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1460644645 205 VVNKPRLLLLDESLSALDYKLRKQMQNEL-KALQRKlgiTFVFVTHD 250
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLlAALSGR---TVVLITHH 529
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
69-264 |
6.85e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 106.16 E-value: 6.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 69 SFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHD-ITHVPAENRHVNTvfqsyalFPhM 147
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArVAYVPQRSEVPDS-------LP-L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 148 TVFENVAFGL----RMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 223
Cdd:NF040873 73 TVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1460644645 224 KLRKQMQNELKALQRKlGITFVFVTHDQEEALTmSDRIVVM 264
Cdd:NF040873 153 ESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
59-289 |
1.81e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 106.93 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 59 PLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHL-----EDHDITHVP-AENR 132
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdgQLRDLYALSeAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 133 HVntvFQSYALFPHmtvfENVAFGLRMQKTPAAEITPRV---------------LDALKMVQLEdfAQR---KPHQLSGG 194
Cdd:PRK11701 85 RL---LRTEWGFVH----QHPRDGLRMQVSAGGNIGERLmavgarhygdirataGDWLERVEID--AARiddLPTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 195 QQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGK-IEQDG 273
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRvVESGL 235
|
250 260
....*....|....*....|..
gi 1460644645 274 T------PREIYEEpknLFVAS 289
Cdd:PRK11701 236 TdqvlddPQHPYTQ---LLVSS 254
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
72-291 |
1.84e-26 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 112.14 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 72 GKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVP--AENRHVNTVFQSYALFPHmTV 149
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDrhTLRQFINYLPQEPYIFSG-SI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 150 FENvafgLRMQKTPAAEITpRVLDALKMVQLEDFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDESL 218
Cdd:TIGR01193 565 LEN----LLLGAKENVSQD-EIWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 219 SALDYKLRKQMQNELKALQRKlgiTFVFVTHDQEEAlTMSDRIVVMRDGKIEQDGTPREIYEEpkNLFVASFI 291
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLDR--NGFYASLI 706
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
70-279 |
2.63e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 107.02 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 70 FDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLE----DHDITHVPAENRHVNTVFQSyalfP 145
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgkplDYSKRGLLALRQQVATVFQD----P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 146 HMTVF-----ENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 220
Cdd:PRK13638 87 EQQIFytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 221 LDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIY 279
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
71-222 |
3.96e-26 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 104.36 E-value: 3.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE-NRHVNTVFQSYALFPHMTV 149
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 150 FENVAFGLRMQKTPAAEItprvLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 222
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
71-249 |
6.75e-26 |
|
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: 102.62 E-value: 6.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHL-EDHDITHVPAEnrhvntvfqsyalfPHMTV 149
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLPQR--------------PYLPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 150 fenvafG-LRMQktpaaeitprVLDALKMVqledfaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDyklrKQ 228
Cdd:cd03223 78 ------GtLREQ----------LIYPWDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EE 125
|
170 180
....*....|....*....|.
gi 1460644645 229 MQNELKALQRKLGITFVFVTH 249
Cdd:cd03223 126 SEDRLYQLLKELGITVISVGH 146
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
58-267 |
6.97e-26 |
|
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: 104.44 E-value: 6.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 58 SPLVQLAGIRKSF-----DGKT--VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDH----DITH 126
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 127 vpAENRHV-----NT---VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQL-EDFAQRKPHQLSGGQQQ 197
Cdd:COG4778 82 --ASPREIlalrrRTigyVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 198 RVAIARAVVNKPRLLLLDESLSALDYKLR---KQMQNELKAlqrkLGITFVFVTHDQEEALTMSDRIVVMRDG 267
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRavvVELIEEAKA----RGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
69-286 |
9.69e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 109.55 E-value: 9.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 69 SFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGL----ENVDSGRIHLEDHDITHVpaeNRHVNTVFQSYALF 144
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpyqGSLKINGIELRELDPESW---RKHLSWVGQNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 145 pHMTVFENVAFGlrmqktpAAEITP-RVLDALKMVQLEDFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLL 212
Cdd:PRK11174 436 -HGTLRDNVLLG-------NPDASDeQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 213 LLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPkNLF 286
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG-GLF 577
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
63-222 |
1.04e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 103.42 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 63 LAGIRKsfdGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITH-VPAENRHvntvfqsY 141
Cdd:PRK13539 8 LACVRG---GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpDVAEACH-------Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 142 -----ALFPHMTVFENVAFGLRMQKTPAAEITprvlDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 216
Cdd:PRK13539 78 lghrnAMKPALTVAENLEFWAAFLGGEELDIA----AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
....*.
gi 1460644645 217 SLSALD 222
Cdd:PRK13539 154 PTAALD 159
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
68-268 |
1.21e-25 |
|
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: 103.32 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 68 KSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHdITHVPAENRHVNTvfqsyalfphm 147
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-IAYVSQEPWIQNG----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 148 TVFENVAFGLRMQKtpaaeitPRVLDALKMVQLE-DFAQRkPHQ-----------LSGGQQQRVAIARAVVNKPRLLLLD 215
Cdd:cd03250 81 TIRENILFGKPFDE-------ERYEKVIKACALEpDLEIL-PDGdlteigekginLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 216 ESLSALDYKLRKQ-MQNELKALqRKLGITFVFVTHdQEEALTMSDRIVVMRDGK 268
Cdd:cd03250 153 DPLSAVDAHVGRHiFENCILGL-LLNNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
53-274 |
2.05e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 108.37 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 53 QPRSRSPLVQLAGIRKSFDGKT--VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAE 130
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 131 N--RHVNTVFQSYALFPHmTVFENvafgLRMQKTPAAEitPRVLDALKMVQLEDFAQRKP----------HQLSGGQQQR 198
Cdd:PRK11160 411 AlrQAISVVSQRVHLFSA-TLRDN----LLLAAPNASD--EALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRR 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1460644645 199 VAIARAVVNKPRLLLLDESLSALDYKLRKQ-MQNELKALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGKIEQDGT 274
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQiLELLAEHAQNK---TVLMITH-RLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
76-283 |
3.85e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 104.82 E-value: 3.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLEN----VDSGRIHLEDHDITHVPAENRH------VNTVFQS--YAL 143
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRnlvgaeVAMIFQDpmTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 144 FPHMTVFENVAFGLRM-QKTPAAEITPRVLDALKMVQLEDFAQR---KPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 219
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 220 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 283
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPR 246
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
44-281 |
4.03e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.05 E-value: 4.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 44 MGQSQKLNIQPRSRSPLVQlagiRKSFDgktvidnLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHD 123
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFAS----RALFD-------IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 124 ITHVPAEN------RHVNTVFQsyalFPHMTVFE-----NVAFGLRMQKTPAAEITPRVLDALKMVQL-EDFAQRKPHQL 191
Cdd:PRK13643 70 VSSTSKQKeikpvrKKVGVVFQ----FPESQLFEetvlkDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 192 SGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQ 271
Cdd:PRK13643 146 SGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
250
....*....|
gi 1460644645 272 DGTPREIYEE 281
Cdd:PRK13643 225 CGTPSDVFQE 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
46-282 |
4.31e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 104.55 E-value: 4.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 46 QSQKLNIQPRSRSPLVQLAGIRKSFDGKT-----VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLE 120
Cdd:PRK13631 7 KKKLKVPNPLSDDIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 121 D----HDITHVPAENRH--------------VNTVFQ--SYALFPHmTVFENVAFG---LRMQKTPAAEITPRVLDalKM 177
Cdd:PRK13631 87 DiyigDKKNNHELITNPyskkiknfkelrrrVSMVFQfpEYQLFKD-TIEKDIMFGpvaLGVKKSEAKKLAKFYLN--KM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 178 VQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQnELKALQRKLGITFVFVTHDQEEALTM 257
Cdd:PRK13631 164 GLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMM-QLILDAKANNKTVFVITHTMEHVLEV 242
|
250 260
....*....|....*....|....*
gi 1460644645 258 SDRIVVMRDGKIEQDGTPREIYEEP 282
Cdd:PRK13631 243 ADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
58-268 |
4.52e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 106.94 E-value: 4.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 58 SPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDS--GRIHLEDHDIT--HV-PAENR 132
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQasNIrDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 133 HVNTVFQSYALFPHMTVFENVAFGlrmqktpaAEITPR-VLDALKM----------VQLEDFAQRKPHQLSGGQQQRVAI 201
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLG--------NEITPGgIMDYDAMylraqkllaqLKLDINPATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1460644645 202 ARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGK 268
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
72-269 |
4.93e-25 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 101.09 E-value: 4.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 72 GKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENV--DSGRIHLEDHDItHVPAENRHVNTVFQSYALFPHMTV 149
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL-DKRSFRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 150 FENVAFGLRMQktpaaeitprvldalkmvqledfaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQM 229
Cdd:cd03213 100 RETLMFAAKLR-----------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1460644645 230 QNELKALqRKLGITFVFVTHD-QEEALTMSDRIVVMRDGKI 269
Cdd:cd03213 151 MSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
65-274 |
7.77e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.33 E-value: 7.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 65 GIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKT----TVLRLIAGLENV-DSGRIHLEDHDITHVPAEN-RHVN--- 135
Cdd:PRK15134 14 AFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLLHASEQTlRGVRgnk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 136 --TVFQS--YALFPHMTV----FENVAFGLRMQKTPA-AEItprvLDALKMVQLEDFAQR---KPHQLSGGQQQRVAIAR 203
Cdd:PRK15134 94 iaMIFQEpmVSLNPLHTLekqlYEVLSLHRGMRREAArGEI----LNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 204 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGK-IEQDGT 274
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRcVEQNRA 241
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
61-268 |
1.64e-24 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 98.29 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGrihledhdithvpaenrhvntvfqs 140
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 141 yalfphmtvfenvafglrmqktpaaeiTPRVLDALKMVQLEdfaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 220
Cdd:cd03221 56 ---------------------------IVTWGSTVKIGYFE--------QLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1460644645 221 LDYKLRKQMQNELKALQRklgiTFVFVTHDQEEALTMSDRIVVMRDGK 268
Cdd:cd03221 101 LDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
61-222 |
1.15e-23 |
|
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: 97.56 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRksfDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHV-PAENRHVNTVFQ 139
Cdd:cd03231 4 DELTCER---DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQrDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 140 SYALFPHMTVFENVAFGLRMQKTPAaeitprVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 219
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
...
gi 1460644645 220 ALD 222
Cdd:cd03231 155 ALD 157
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
73-273 |
1.55e-23 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 96.61 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRHVNTVF-QSYALFpHMTVFE 151
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLnQRPYLF-DTTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 152 NVafGLRmqktpaaeitprvldalkmvqledfaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQN 231
Cdd:cd03247 94 NL--GRR--------------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLS 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1460644645 232 EL-KALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGKIEQDG 273
Cdd:cd03247 140 LIfEVLKDK---TLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
69-274 |
1.91e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 102.73 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 69 SFDGKT-VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALFp 145
Cdd:PRK13657 343 SYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIAVVFQDAGLF- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 146 HMTVFENvafgLRMQKTPAAEitPRVLDALKMVQLEDFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLL 214
Cdd:PRK13657 422 NRSIEDN----IRVGRPDATD--EEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 215 DESLSALDYKLRKQMQNELKALqRKLGITFVfVTHdQEEALTMSDRIVVMRDGKIEQDGT 274
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDEL-MKGRTTFI-IAH-RLSTVRNADRILVFDNGRVVESGS 552
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
67-273 |
2.09e-23 |
|
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: 97.79 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 67 RKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHdithVPAENR-----HVNTVF-QS 140
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRkkflrRIGVVFgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 141 YALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 220
Cdd:cd03267 104 TQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 221 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 273
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
75-269 |
2.30e-23 |
|
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: 97.54 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 75 VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRH--VNTVFQSYALFPHmTVFEN 152
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHskVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 153 VAFGLrmQKTPAAEITprvlDALKMVQLEDFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 221
Cdd:cd03248 108 IAYGL--QSCSFECVK----EAAQKAHAHSFISELASgydtevgekgsQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1460644645 222 DYKLRKQMQnelKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:cd03248 182 DAESEQQVQ---QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
76-294 |
2.62e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 102.24 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKT-TVLRLIAGLE----NVDSGRIHLEDHD------ITHVPAENRHVN-----TVFQ 139
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEqaggLVQCDKMLLRRRSrqvielSEQSAAQMRHVRgadmaMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 140 S--YALFPHMTVFENVAFGLRMQ----KTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 213
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLHqgasREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 214 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGE 293
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAA 271
|
.
gi 1460644645 294 I 294
Cdd:PRK10261 272 V 272
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
75-269 |
3.06e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 97.64 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 75 VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN---RHVNTVFQSYALFPHMTVFE 151
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 152 NVAF-GLRMQKTPAAEITPRVLDALKMVQlEDFAQRKpHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ 230
Cdd:PRK11614 100 NLAMgGFFAERDQFQERIKWVYELFPRLH-ERRIQRA-GTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIF 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 1460644645 231 NELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:PRK11614 178 DTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
54-222 |
5.01e-23 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 96.46 E-value: 5.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 54 PRSRSPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVpAENRH 133
Cdd:PRK13543 5 LHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG-DRSRF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 134 VNTVFQSYALFPHMTVFENVAF-----GLRMQKTPAaeitprvlDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNK 208
Cdd:PRK13543 84 MAYLGHLPGLKADLSTLENLHFlcglhGRRAKQMPG--------SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSP 155
|
170
....*....|....
gi 1460644645 209 PRLLLLDESLSALD 222
Cdd:PRK13543 156 APLWLLDEPYANLD 169
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
53-278 |
5.19e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 97.55 E-value: 5.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 53 QPRSRSPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIT--HVPAE 130
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 131 NRHVNTVFQSYALFPHMTVFENVAFGlrmqKTP--------AAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIA 202
Cdd:PRK10575 84 ARKVAYLPQQLPAAEGMTVRELVAIG----RYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1460644645 203 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
76-259 |
7.15e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.16 E-value: 7.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLR-------LIAGLEnVDsGRIHLEDHDI--THV-PAE-NRHVNTVFQSYALF 144
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR-VE-GKVTFHGKNLyaPDVdPVEvRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 145 PHmTVFENVAFGLRMQ--KTPAAEITPRvldALKMVQLEDFAQRKPHQ----LSGGQQQRVAIARAVVNKPRLLLLDESL 218
Cdd:PRK14243 104 PK-SIYDNIAYGARINgyKGDMDELVER---SLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1460644645 219 SALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSD 259
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSD 218
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
79-285 |
8.99e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 96.45 E-value: 8.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 79 LNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENvDSGRIHLEDHDITHVPA-ENRHVNTVF--QSYALFPhMTVFENVAF 155
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAaELARHRAYLsqQQSPPFA-MPVFQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 156 GLRmQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAV------VN-KPRLLLLDESLSALDYklrkQ 228
Cdd:COG4138 93 HQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLDEPMNSLDV----A 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 229 MQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYeEPKNL 285
Cdd:COG4138 168 QQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPENL 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
63-269 |
1.25e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 63 LAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLE-DHDITHVPaenrhvntvfQSY 141
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLP----------QEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 142 ALFPHMTVFENVAFGL--------RMQKTPAAEITP---------------------------RVLDALKmVQLEDFaQR 186
Cdd:COG0488 71 PLDDDLTVLDTVLDGDaelraleaELEELEAKLAEPdedlerlaelqeefealggweaearaeEILSGLG-FPEEDL-DR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 187 KPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQrklgITFVFVTHDQE--EALTmsDRIVVM 264
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP----GTVLVVSHDRYflDRVA--TRILEL 222
|
....*
gi 1460644645 265 RDGKI 269
Cdd:COG0488 223 DRGKL 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
58-290 |
1.56e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 95.95 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 58 SPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDH-DITHVPaenrhvnt 136
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlRIGYVP-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 137 vfQSYALFPHMTVfeNVAFGLRMQK-TPAAEITPrvldALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 215
Cdd:PRK09544 74 --QKLYLDTTLPL--TVNRFLRLRPgTKKEDILP----ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460644645 216 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMrDGKIEQDGTPREIYEEPKnlFVASF 290
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE--FISMF 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
71-281 |
1.79e-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: 94.13 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLEN--VDSGRIHLEDHDITHVPAENRHVNTVFqsyalfphmt 148
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERARLGIF---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 vfenvafgLRMQKTPaaEITprvldalkMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQ 228
Cdd:cd03217 81 --------LAFQYPP--EIP--------GVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 229 MQNELKALqRKLGITFVFVTHDQEEALTM-SDRIVVMRDGKIEQDGtPREIYEE 281
Cdd:cd03217 143 VAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
69-275 |
3.10e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 94.75 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 69 SFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLEN--VDSGRIHLEDHDITHVPAENRH---VNTVFQSYAL 143
Cdd:COG0396 9 SVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERAragIFLAFQYPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 144 FPHMTV--FENVAFGLRMQKT-PAAEITPRVLDALKMVQL-EDFAQRKPHQ-LSGGQQQRVAIARAVVNKPRLLLLDESL 218
Cdd:COG0396 89 IPGVSVsnFLRTALNARRGEElSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 219 SALDYKLRKQMQNELKALQRKlGITFVFVTHdQEEALTM--SDRIVVMRDGKIEQDGTP 275
Cdd:COG0396 169 SGLDIDALRIVAEGVNKLRSP-DRGILIITH-YQRILDYikPDFVHVLVDGRIVKSGGK 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
59-269 |
3.17e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.56 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 59 PLVQLAGIR-KSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIT------------ 125
Cdd:COG3845 256 VVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITglsprerrrlgv 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 126 -HVPaENRHvntvfqSYALFPHMTVFENVAFGLRMQKtpaaEITPRVLdaLKMVQLEDFAQRK----------PHQ---- 190
Cdd:COG3845 336 aYIP-EDRL------GRGLVPDMSVAENLILGRYRRP----PFSRGGF--LDRKAIRAFAEELieefdvrtpgPDTpars 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 191 LSGGQQQRVAIARAVVNKPRLLL-------LDESLSAldyklrkQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVV 263
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIaaqptrgLDVGAIE-------FIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAV 474
|
....*.
gi 1460644645 264 MRDGKI 269
Cdd:COG3845 475 MYEGRI 480
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
75-269 |
5.16e-22 |
|
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: 93.87 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 75 VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAG-LENVD--SGRIHLEDHDIThvPAE-NRHVNTVFQSYALFPHMTVF 150
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGttSGQILFNGQPRK--PDQfQKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 151 ENVAFG--LRMQ-KTPAAEITPRVLD-ALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 226
Cdd:cd03234 100 ETLTYTaiLRLPrKSSDAIRKKRVEDvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1460644645 227 KQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:cd03234 180 LNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
72-269 |
6.18e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 6.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 72 GKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITH-------------VPaENRHvntvf 138
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIrsprdairagiayVP-EDRK----- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 139 qSYALFPHMTVFENVAF--------GLRMQKTPAAEITPRVLDAL--KMVQLEDFAQrkphQLSGGQQQRVAIARAVVNK 208
Cdd:COG1129 338 -GEGLVLDLSIRENITLasldrlsrGGLLDRRRERALAEEYIKRLriKTPSPEQPVG----NLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644645 209 PRLLLLDESLSALD-------YKLrkqMqNELKAlqRKLGItfVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:COG1129 413 PKVLILDEPTRGIDvgakaeiYRL---I-RELAA--EGKAV--IVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
69-281 |
1.03e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 97.40 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 69 SFDGKTV--IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALF 144
Cdd:PRK11176 350 TYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrNQVALVSQNVHLF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 145 pHMTVFENVAFGlRMQKTPAAEITprvlDALKMVQLEDFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLL 213
Cdd:PRK11176 430 -NDTIANNIAYA-RTEQYSREQIE----EAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILI 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644645 214 LDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 281
Cdd:PRK11176 504 LDEATSALDTESERAIQAALDELQKNR--TSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
71-275 |
1.90e-21 |
|
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: 92.17 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTV----LRLIagleNVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALF 144
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 145 PHmTVFENVA-FGlrmQKTPAAeitprVLDALKMVQLEDFAQRKPHQL-----------SGGQQQRVAIARAVVNKPRLL 212
Cdd:cd03244 91 SG-TIRSNLDpFG---EYSDEE-----LWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 213 LLDESLSALDYKLRKQMQnelKALQRKL-GITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTP 275
Cdd:cd03244 162 VLDEATASVDPETDALIQ---KTIREAFkDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
59-333 |
2.20e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.01 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 59 PLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHD---ITHVPAENRHVN 135
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 136 TVFQSYALFPHMTVFENVAFGLRMQK-------TPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNK 208
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 209 PRLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDG-----KIEQDGTPREIYE--- 280
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGssvcsGMVSDVSNDDIVRlmv 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 281 --EPKNLFVA-----SFIGEINIFDATVIERLDEQRVRanvegrecniTVNFAVEAGQRL 333
Cdd:PRK09700 243 grELQNRFNAmkenvSNLAHETVFEVRNVTSRDRKKVR----------DISFSVCRGEIL 292
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
59-275 |
5.11e-21 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 96.24 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 59 PLVQLAGIRKSFD--GKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDI-THVPAENRHVN 135
Cdd:TIGR01257 927 PGVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 136 TVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 215
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 216 ESLSALDYKLRKQMQNELkaLQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTP 275
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
38-252 |
7.08e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 90.40 E-value: 7.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 38 SFRCVYMGQSQKLNIQPRSRSpLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLE--NVDSG 115
Cdd:COG2401 9 VLMRVTKVYSSVLDLSERVAI-VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 116 RIHLEDHDIThvpaenrhvntvfqsyalfPHMTVFENVAfglRMQKTPAAeitprvLDALKMVQLED--FAQRKPHQLSG 193
Cdd:COG2401 88 CVDVPDNQFG-------------------REASLIDAIG---RKGDFKDA------VELLNAVGLSDavLWLRRFKELST 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 194 GQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQE 252
Cdd:COG2401 140 GQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
48-281 |
2.68e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 93.65 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 48 QKLNIQPRSRSPLVQLA----GIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHL---- 119
Cdd:NF033858 250 QPVVIPPRPADDDDEPAiearGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqp 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 120 -EDHDIthvpAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQR 198
Cdd:NF033858 330 vDAGDI----ATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQR 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 199 VAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITfVFV-THDQEEALTmSDRIVVMRDGKIEQDGTPRE 277
Cdd:NF033858 406 LSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEAER-CDRISLMHAGRVLASDTPAA 483
|
....
gi 1460644645 278 IYEE 281
Cdd:NF033858 484 LVAA 487
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
58-375 |
4.15e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 92.37 E-value: 4.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 58 SPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIT-HVPAENRH--V 134
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEagI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 135 NTVFQSYALFPHMTVFENVAFGlRMQKTPAAEITPRVLDA-----LKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKP 209
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLG-REFVNRFGRIDWKKMYAeadklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 210 RLLLLDESLSAL-DYKLRK--QMQNELKALQRklGItfVFVTHDQEEALTMSDRIVVMRDGKieqdgtpreiyeepknlf 286
Cdd:PRK10762 161 KVIIMDEPTDALtDTETESlfRVIRELKSQGR--GI--VYISHRLKEIFEICDDVTVFRDGQ------------------ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 287 vasFIGEINIFDAT---VIE-----RLDEQRVRANVEGRECNITVN-----------FAVEAGQRLHV--LL---RPEDL 342
Cdd:PRK10762 219 ---FIAEREVADLTedsLIEmmvgrKLEDQYPRLDKAPGEVRLKVDnlsgpgvndvsFTLRKGEILGVsgLMgagRTELM 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 343 RV----------------DEIHHNSDADGL---IGYVRE-RNYKGMTLE-SVVE 375
Cdd:PRK10762 296 KVlygalprtsgyvtldgHEVVTRSPQDGLangIVYISEdRKRDGLVLGmSVKE 349
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
75-282 |
6.61e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 89.96 E-value: 6.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 75 VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLEN----VDSGRIHLEDHDITHVPAENRH------VNTVFQ--SYA 142
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERRkiigreIAMIFQepSSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 143 LFPHMTVFENVAFGL-----------RMQ--KTPAAEITPRVldALKMVQleDFAQRKPHQLSGGQQQRVAIARAVVNKP 209
Cdd:COG4170 102 LDPSAKIGDQLIEAIpswtfkgkwwqRFKwrKKRAIELLHRV--GIKDHK--DIMNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 210 RLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEP 282
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
73-318 |
1.12e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.99 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDhditHVPAENRHVN-----TVF-QSYALFPH 146
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG----YVPFKRRKEFarrigVVFgQRSQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 147 MTVFENvaFGL--RMQKTPAAEITPRvLDAL-KMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 223
Cdd:COG4586 111 LPAIDS--FRLlkAIYRIPDAEYKKR-LDELvELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 224 KLRKQMQNELKALQRKLGITFVFVTHDQE--EALtmSDRIVVMRDGKIEQDGTP---REIYEEPKNLFV--ASFIGEINI 296
Cdd:COG4586 188 VSKEAIREFLKEYNRERGTTILLTSHDMDdiEAL--CDRVIVIDHGRIIYDGSLeelKERFGPYKTIVLelAEPVPPLEL 265
|
250 260
....*....|....*....|..
gi 1460644645 297 FDATVIERLDEQRVRANVEGRE 318
Cdd:COG4586 266 PRGGEVIEREGNRVRLEVDPRE 287
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
79-277 |
1.44e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 90.80 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 79 LNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIThvpAENR-----HVNTVFQSYALFPHMTVFENv 153
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPedyrkLFSAVFTDFHLFDQLLGPEG- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 154 afglrmqKTPAAEITPRVLDALKM---VQLEDFAQRKPhQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ 230
Cdd:PRK10522 418 -------KPANPALVEKWLERLKMahkLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFY 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1460644645 231 NELKALQRKLGITFVFVTHDqEEALTMSDRIVVMRDGKI-EQDGTPRE 277
Cdd:PRK10522 490 QVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLsELTGEERD 536
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
73-282 |
1.50e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 90.93 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALFPHmTVF 150
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 151 ENVAFGlRMQKTPAaEITprvlDALKMVQLEDFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDESLS 219
Cdd:PRK10789 407 NNIALG-RPDATQQ-EIE----HVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 220 ALDYKLRKQMQNELKalQRKLGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREIYEEP 282
Cdd:PRK10789 481 AVDGRTEHQILHNLR--QWGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
66-269 |
4.01e-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: 85.01 E-value: 4.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 66 IRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGL--ENVD-SGRIHLEDH-----------DITHVPAEN 131
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRteGNVSvEGDIHYNGIpykefaekypgEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 132 RHvntvfqsyalFPHMTVFENVAFGLRMQktpaaeitprvldALKMVqledfaqRKphqLSGGQQQRVAIARAVVNKPRL 211
Cdd:cd03233 93 VH----------FPTLTVRETLDFALRCK-------------GNEFV-------RG---ISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 212 LLLDESLSALDYKLRKQMQNELKALQRKLGIT-FVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
61-283 |
2.04e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 84.37 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTViDNLNLTINNGEFLTLLGPSGCGKT-TVLRLI----AGLENVdSGRIHLEDHDITHVPAENRHVN 135
Cdd:PRK10418 5 IELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQT-AGRVLLDGKPVAPCALRGRKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 136 TVFQS--YALFPHMTVFENVAFGLRMQKTPAAEitPRVLDALKMVQLED---FAQRKPHQLSGGQQQRVAIARAVVNKPR 210
Cdd:PRK10418 83 TIMQNprSAFNPLHTMHTHARETCLALGKPADD--ATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644645 211 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 283
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
71-278 |
2.35e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 84.49 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAG--LENVDS------GRIHLEDHDITHVPAEN---RHVNTVFQ 139
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPrgarvtGDVTLNGEPLAAIDAPRlarLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 140 SYALFPhMTVFENVAFGLRMQKTPAAEITPRVLD----ALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVN-------- 207
Cdd:PRK13547 92 AQPAFA-FSAREIVLLGRYPHARRAGALTHRDGEiawqALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaa 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 208 -KPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:PRK13547 171 qPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
76-269 |
3.20e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.60 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDI-THVPAENRHVNTVFQSY-----ALFPHMTV 149
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANGIVYISEdrkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 150 FENVA------FGLRMQKTPAAEITPRVLDALKMvqledFAQRKPHQ------LSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:PRK10762 348 KENMSltalryFSRAGGSLKHADEQQAVSDFIRL-----FNIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1460644645 218 LSALDYKLRK---QMQNELKAlqrkLGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:PRK10762 423 TRGVDVGAKKeiyQLINQFKA----EGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
58-331 |
4.06e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.12 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 58 SPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHL---EDHDITHVPAENRHV 134
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdgqEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 135 NTVFQSYALFPHMTVFENV-------AFGLRMQKTPAAeitpRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVN 207
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLylgqlphKGGIVNRRLLNY----EAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 208 KPRLLLLDE---SLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQEEALTMSDRIVVMRDGKIEQdgTPREIYEEPKN 284
Cdd:PRK11288 158 NARVIAFDEptsSLSAREIEQLFRVIRELRAEGRVI----LYVSHRMEEIFALCDAITVFKDGRYVA--TFDDMAQVDRD 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1460644645 285 LFVASFIG-EI-NIFDATviER-LDEQRVRA-NVEGRECNITVNFAVEAGQ 331
Cdd:PRK11288 232 QLVQAMVGrEIgDIYGYR--PRpLGEVRLRLdGLKGPGLREPISFSVRAGE 280
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
79-282 |
4.35e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 83.06 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 79 LNLTINNGEFLTLLGPSGCGKTTVLRLIAGLeNVDSGRIHLEDHDITHVPA-ENRHVNTVF--QSYALFpHMTVFENVAF 155
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAaELARHRAYLsqQQTPPF-AMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 156 GLRmQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIArAVV------NKP--RLLLLDESLSALDYKLRK 227
Cdd:PRK03695 93 HQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLA-AVVlqvwpdINPagQLLLLDEPMNSLDVAQQA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1460644645 228 QMQNELKALQRkLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEP 282
Cdd:PRK03695 171 ALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
72-267 |
6.53e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 81.99 E-value: 6.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 72 GKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN-RHVNTVFQSYA----LFPH 146
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAtRSRNRYSVAYAaqkpWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 147 MTVFENVAFGLRMQK------TPAAEITPRVlDALKMVQLEDFAQRKPHqLSGGQQQRVAIARAVVNKPRLLLLDESLSA 220
Cdd:cd03290 93 ATVEENITFGSPFNKqrykavTDACSLQPDI-DLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1460644645 221 LDYKLRKQMQNE--LKALQRKlGITFVFVTHdQEEALTMSDRIVVMRDG 267
Cdd:cd03290 171 LDIHLSDHLMQEgiLKFLQDD-KRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
71-281 |
2.99e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 84.00 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVP--AENRHVNTVFQSYALFPHmT 148
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsVLRQGVAMVQQDPVVLAD-T 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 VFENVAFGLRMQKTpaaeitpRVLDALKMVQLEDFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:PRK10790 431 FLANVTLGRDISEE-------QVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 218 LSALDYKLRKQMQNELKALQRKlgITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 281
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREH--TTLVVIAH-RLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
54-250 |
5.28e-17 |
|
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: 83.06 E-value: 5.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 54 PRSRSPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLedhdithvpAENRH 133
Cdd:TIGR03719 316 PRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI---------GETVK 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 134 VNTVFQSY-ALFPHMTVFENVAFGLRMQKTPAAEITPRVldalkMVQLEDFA----QRKPHQLSGGQQQRVAIARAVVNK 208
Cdd:TIGR03719 387 LAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRA-----YVGRFNFKgsdqQKKVGQLSGGERNRVHLAKTLKSG 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1460644645 209 PRLLLLDESLSALDYklrkqmqNELKALQRKL----GITFVfVTHD 250
Cdd:TIGR03719 462 GNVLLLDEPTNDLDV-------ETLRALEEALlnfaGCAVV-ISHD 499
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
61-281 |
7.18e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.86 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFdGKTV-IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIthvpAENRHVNTVFQ 139
Cdd:NF033858 2 ARLEGVSHRY-GKTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM----ADARHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 140 SYA---------LFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPR 210
Cdd:NF033858 77 RIAympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 211 LLLLDESLSALDYKLRKQ---MQNELKAlqRKLGITFVFVTHDQEEALTMsDRIVVMRDGKIEQDGTPREIYEE 281
Cdd:NF033858 157 LLILDEPTTGVDPLSRRQfweLIDRIRA--ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLAR 227
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
66-259 |
2.76e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 76.91 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 66 IRKSFD--GKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITH-VPAENRHVNTVFQSYA 142
Cdd:PRK13540 5 IELDFDyhDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 143 LFPHMTVFENVAFGLRMQKTpAAEITprvlDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 222
Cdd:PRK13540 85 INPYLTLRENCLYDIHFSPG-AVGIT----ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1460644645 223 YKLRKQMQNELKALQRKLGItfVFVTHDQEEALTMSD 259
Cdd:PRK13540 160 ELSLLTIITKIQEHRAKGGA--VLLTSHQDLPLNKAD 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
56-274 |
3.63e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 81.21 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 56 SRSPLVQLAGIRKSFDGKT--VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDI-THVPAENR 132
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQ 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 133 HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLL 212
Cdd:TIGR01257 2013 NMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 213 LLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGT 274
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
82-316 |
4.22e-16 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 77.45 E-value: 4.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 82 TINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPaenRHVNTVFQsyalfphMTVFEnvafgLRMQK 161
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP---QYIKADYE-------GTVRD-----LLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 162 TPAAEITPRV-LDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKL 240
Cdd:cd03237 86 TKDFYTHPYFkTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 241 GITFVFVTHDQEEALTMSDRIVVMrDGKIEQDGT--PREIYEEPKNLFVAsfigeinIFDATVieRLDEQ--RVRANVEG 316
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGVanPPQSLRSGMNRFLK-------NLDITF--RRDPEtgRPRINKLG 235
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
75-275 |
4.64e-16 |
|
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: 76.30 E-value: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 75 VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEnrhvnTVFQSYALFPH-MTVFENV 153
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE-----DLRSSLTIIPQdPTLFSGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 154 afgLRMQKTPAAEITPR-VLDALKMVQLEDfaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY----KLRKQ 228
Cdd:cd03369 98 ---IRSNLDPFDEYSDEeIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYatdaLIQKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1460644645 229 MQNELKalqrklGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTP 275
Cdd:cd03369 168 IREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
78-269 |
5.26e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.71 E-value: 5.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 78 NLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENR-HVNTVF-----QSYALFPHMTVFE 151
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 152 NVA------FGLRMQKTPAAEITPRVLDALKmVQLEDfAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 225
Cdd:PRK15439 361 NVCalthnrRGFWIKPARENAVLERYRRALN-IKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1460644645 226 RKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:PRK15439 439 RNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
73-273 |
6.09e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 80.21 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEdHDITHVPAENRHVNTVFQSYALFphmtvFEN 152
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSIAYVPQQAWIMNATVRGNILF-----FDE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 153 vafglrmqktpaaEITPRVLDALKMVQLE-DFAQ----------RKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 221
Cdd:PTZ00243 747 -------------EDAARLADAVRVSQLEaDLAQlgggleteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 222 DYKLRKQMQNELkALQRKLGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDG 273
Cdd:PTZ00243 814 DAHVGERVVEEC-FLGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSG 863
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
68-268 |
9.50e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.15 E-value: 9.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 68 KSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGL--ENVDSGRIHLEDHDITHVPAenRHVNTVFQSYALFP 145
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPTKQIL--KRTGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 146 HMTVFENVAFG--LRMQKTPAAEITPRVLDA----LKMVQLED--FAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:PLN03211 154 HLTVRETLVFCslLRLPKSLTKQEKILVAESviseLGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 218 LSALDYKLRKQMQNELKALQRKlGITFVFVTHD-QEEALTMSDRIVVMRDGK 268
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
76-278 |
1.66e-15 |
|
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: 78.83 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLR-LIAGLENVDsGRIHLEDhDITHVPAEnrhvntvfqsyALFPHMTVFENVA 154
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVE-GHVHMKG-SVAYVPQQ-----------AWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 155 FGLRMQKTPAAEITPR--VLDALKMVQLEDFAQ--RKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ 230
Cdd:TIGR00957 721 FGKALNEKYYQQVLEAcaLLPDLEILPSGDRTEigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1460644645 231 NELKALQRKL-GITFVFVTHDQeEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:TIGR00957 801 EHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
113-278 |
1.71e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.92 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 113 DSGRIHLEDHDITHVPAEN-RHVNTVFQSYALFPHMTVFENVAFGlrmQKTPAAEITPRvldALKMVQLEDFAQRKPHQ- 190
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG---KEDATREDVKR---ACKFAAIDEFIESLPNKy 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 191 ----------LSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHdQEEALTMSDR 260
Cdd:PTZ00265 1349 dtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427
|
170 180
....*....|....*....|...
gi 1460644645 261 IVVM----RDGK-IEQDGTPREI 278
Cdd:PTZ00265 1428 IVVFnnpdRTGSfVQAHGTHEEL 1450
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
73-277 |
2.53e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.78 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAG--LENVD-SGRIHLEDHDIThvpAENRHVNTVF--QSYALFPHM 147
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrsPKGVKgSGSVLLNGMPID---AKEMRAISAYvqQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 148 TVFENVAFG--LRMQK-TPAAEITPRVLDALKMVQLEDFAQRK---PHQ---LSGGQQQRVAIARAVVNKPRLLLLDESL 218
Cdd:TIGR00955 115 TVREHLMFQahLRMPRrVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 219 SALDYKLRKQMQNELKALQRKlGITFVFVTHD-QEEALTMSDRIVVMRDGKIEQDGTPRE 277
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
61-281 |
3.54e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 77.24 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLedhdithvpAENRHVNTVFQ- 139
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW---------SENANIGYYAQd 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 140 SYALFPH-MTVFENVAfglrmQKTPAAEITPRVLDAL-KMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:PRK15064 391 HAYDFENdLTLFDWMS-----QWRQEGDDEQAVRGTLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460644645 218 LSALDYKLRKQMQNELKALQrklGiTFVFVTHDQEEALTMSDRIVVMRDGKIEQ-DGTpreiYEE 281
Cdd:PRK15064 466 TNHMDMESIESLNMALEKYE---G-TLIFVSHDREFVSSLATRIIEITPDGVVDfSGT----YEE 522
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
56-274 |
5.99e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 74.29 E-value: 5.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 56 SRSPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLE--NVDSGRIHLEDHDITHVPAENRH 133
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 134 ---VNTVFQSYALFPHMTV--FENVAFGLRMQKTPAAEITPR-----VLDALKMVQLED-FAQRKPHQ-LSGGQQQRVAI 201
Cdd:CHL00131 83 hlgIFLAFQYPIEIPGVSNadFLRLAYNSKRKFQGLPELDPLefleiINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644645 202 ARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEealtMSDRIV-----VMRDGKIEQDGT 274
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQR----LLDYIKpdyvhVMQNGKIIKTGD 235
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
47-249 |
7.23e-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: 76.71 E-value: 7.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 47 SQKLNIQPRSRSPLVQLAGIRksFD--------GKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIH 118
Cdd:TIGR00954 433 GRNSNLVPGRGIVEYQDNGIK--FEniplvtpnGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLT 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 119 L-EDHDITHVPAENRHVNTVFQSYALFPhMTVFENVAFGLRMQktpaaeitprVLDA-LKMVQLEDFAQRK--------- 187
Cdd:TIGR00954 511 KpAKGKLFYVPQRPYMTLGTLRDQIIYP-DSSEDMKRRGLSDK----------DLEQiLDNVQLTHILEREggwsavqdw 579
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 188 PHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNelkaLQRKLGITFVFVTH 249
Cdd:TIGR00954 580 MDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYR----LCREFGITLFSVSH 637
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
65-270 |
1.58e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.21 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 65 GIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDS--GRIHLED-----HDITHvpAENRHVNTV 137
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevcrfKDIRD--SEALGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 138 FQSYALFPHMTVFENVAFGLRMQKTPA---AEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 214
Cdd:NF040905 84 HQELALIPYLSIAENIFLGNERAKRGVidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1460644645 215 DESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGK-IE 270
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRtIE 219
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
73-281 |
2.76e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.16 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAG-LENVDSGRIHLEDhDITHVPaenrHVNTVFQSyalfphmTVFE 151
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRG-TVAYVP----QVSWIFNA-------TVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 152 NVAFGL-----RMQKTPAAEITPRVLDALKMVQLEDFAQRKPHqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 226
Cdd:PLN03130 698 NILFGSpfdpeRYERAIDVTALQHDLDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVG 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1460644645 227 KQMQNelKALQRKL-GITFVFVThDQEEALTMSDRIVVMRDGKIEQDGTpreiYEE 281
Cdd:PLN03130 777 RQVFD--KCIKDELrGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGT----YEE 825
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
69-280 |
3.95e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.63 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 69 SFDGKT---VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAG-LENVDSGRIHLEDhDITHVPaenrHVNTVFQSyalf 144
Cdd:PLN03232 623 SWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRG-SVAYVP----QVSWIFNA---- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 145 phmTVFENVAFGLRMQKT---PAAEITP--RVLDALKMVQLEDFAQRKPHqLSGGQQQRVAIARAVVNKPRLLLLDESLS 219
Cdd:PLN03232 694 ---TVRENILFGSDFESErywRAIDVTAlqHDLDLLPGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1460644645 220 ALDYKLRKQ-----MQNELKalqrklGITFVFVThDQEEALTMSDRIVVMRDGKIEQDGTPREIYE 280
Cdd:PLN03232 770 ALDAHVAHQvfdscMKDELK------GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
75-297 |
3.96e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.91 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 75 VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLEN----VDSGRIHLEDHDITHVPAENRH------VNTVFQ--SYA 142
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERRklvghnVSMIFQepQSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 143 LFPHMTVFENVA---------------FGLRmqKTPAAEITPRVldALKmvQLEDFAQRKPHQLSGGQQQRVAIARAVVN 207
Cdd:PRK15093 102 LDPSERVGRQLMqnipgwtykgrwwqrFGWR--KRRAIELLHRV--GIK--DHKDAMRSFPYELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 208 KPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFV 287
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYT 255
|
250
....*....|
gi 1460644645 288 ASFIGEINIF 297
Cdd:PRK15093 256 QALIRAIPDF 265
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
73-231 |
5.17e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 70.29 E-value: 5.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEnrHVNTVFQSYALFPHMTVFEN 152
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP--YCTYIGHNLGLKLEMTVFEN 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 153 VAFGLRMQKTpaAEITPRvldALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQN 231
Cdd:PRK13541 91 LKFWSEIYNS--AETLYA---AIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN 164
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
63-268 |
8.73e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.84 E-value: 8.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 63 LAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDI---THVPAENRHVNTVFQ 139
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 140 SYALFPHMTVFENVAFGLRMQKTPAAEI------TPRVLDALKMvqleDFAQR-KPHQLSGGQQQRVAIARAVVNKPRLL 212
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGMFVDQdkmyrdTKAIFDELDI----DIDPRaKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1460644645 213 LLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGK 268
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
61-242 |
1.12e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.14 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVID---NLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLED-HDITHVPAE--NRHV 134
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKwwRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 135 NTVFQSYALFPHmTVFENVAFGLR----------------------------------------MQKTPAAEIT------ 168
Cdd:PTZ00265 463 GVVSQDPLLFSN-SIKNNIKYSLYslkdlealsnyynedgndsqenknkrnscrakcagdlndmSNTTDSNELIemrkny 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 169 -----PRVLDALKMVQLEDFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK---LRKQM 229
Cdd:PTZ00265 542 qtikdSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLVQKT 621
|
250
....*....|...
gi 1460644645 230 QNELKALQRKLGI 242
Cdd:PTZ00265 622 INNLKGNENRITI 634
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
79-276 |
1.60e-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: 72.14 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 79 LNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIThvpAENR-----HVNTVFQSYALFPHMtvfenv 153
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNReayrqLFSAVFSDFHLFDRL------ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 154 afgLRMQKTPAAEITPRVLDALKM---VQLED--FAQRKphqLSGGQQQRVAIARAVV-NKPrLLLLDEslSALD----- 222
Cdd:COG4615 422 ---LGLDGEADPARARELLERLELdhkVSVEDgrFSTTD---LSQGQRKRLALLVALLeDRP-ILVFDE--WAADqdpef 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644645 223 ----YklrKQMQNELKAlqrkLGITFVFVTHDqEEALTMSDRIVVMRDGKIEQDGTPR 276
Cdd:COG4615 493 rrvfY---TELLPELKA----RGKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPA 542
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
63-269 |
1.70e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.83 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 63 LAGIRKSFDGKTV--IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIA----GLENVDSGRIH---LEDHDIT-HVPAEnr 132
Cdd:TIGR00956 62 FRKLKKFRDTKTFdiLKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITydgITPEEIKkHYRGD-- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 133 hVNTVFQSYALFPHMTVFENVAFGLRMqKTPAAEItprvldalKMVQLEDFAQRKPH----------------------Q 190
Cdd:TIGR00956 140 -VVYNAETDVHFPHLTVGETLDFAARC-KTPQNRP--------DGVSREEYAKHIADvymatyglshtrntkvgndfvrG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 191 LSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITfVFVTHDQ--EEALTMSDRIVVMRDGK 268
Cdd:TIGR00956 210 VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTT-PLVAIYQcsQDAYELFDKVIVLYEGY 288
|
.
gi 1460644645 269 I 269
Cdd:TIGR00956 289 Q 289
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
60-273 |
3.47e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 69.05 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 60 LVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLEN--VDSGRIHLEDHDITHVPAENRHVNTV 137
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 138 FQSyalFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQL---------------SGGQQQRVAIA 202
Cdd:PRK09580 81 FMA---FQYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDIL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 203 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQE-EALTMSDRIVVMRDGKIEQDG 273
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRiLDYIKPDYVHVLYQGRIVKSG 228
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
65-222 |
6.16e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 65 GIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDhdithvpaenrhvnTVFQSY--- 141
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE--------------TVKLAYvdq 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 142 ---ALFPHMTVFENVAFGLRMQKTPAAEITPRVldalkMVQLEDFA----QRKPHQLSGGQQQRVAIARAVVNKPRLLLL 214
Cdd:PRK11819 395 srdALDPNKTVWEEISGGLDIIKVGNREIPSRA-----YVGRFNFKggdqQKKVGVLSGGERNRLHLAKTLKQGGNVLLL 469
|
....*...
gi 1460644645 215 DESLSALD 222
Cdd:PRK11819 470 DEPTNDLD 477
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
71-265 |
7.59e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.37 E-value: 7.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAENRhVNTVFQSYAL---FPhm 147
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-VAYVPQSEEVdwsFP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 148 TVFENVAFGLR-----MQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 222
Cdd:PRK15056 95 VLVEDVVMMGRyghmgWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1460644645 223 YKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMR 265
Cdd:PRK15056 175 VKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
72-304 |
2.23e-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: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 72 GKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIhledhdithvpaenRH---VNTVFQSYALFPHmT 148
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--------------KHsgrISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 VFENVAFGLRMQKTpaaeitpRVLDALKMVQLEDFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:cd03291 114 IKENIIFGVSYDEY-------RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 218 LSALDYKLRKQMQNE--LKALQRKlgiTFVFVTHDQEEaLTMSDRIVVMRDGKIEQDGTPREIYEEPKNlFVASFIGeIN 295
Cdd:cd03291 187 FGYLDVFTEKEIFEScvCKLMANK---TRILVTSKMEH-LKKADKILILHEGSSYFYGTFSELQSLRPD-FSSKLMG-YD 260
|
....*....
gi 1460644645 296 IFDATVIER 304
Cdd:cd03291 261 TFDQFSAER 269
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
44-222 |
2.33e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.82 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 44 MGqSQKLNIQPRSRS-PLV-QLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLED 121
Cdd:PRK11147 302 MG-TAKMQVEEASRSgKIVfEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 122 H-DITHvpaenrhvntvFQSY--ALFPHMTVFENVAFGLRmqktpaaEIT----PR-VLDalkmvQLEDF------AQRK 187
Cdd:PRK11147 381 KlEVAY-----------FDQHraELDPEKTVMDNLAEGKQ-------EVMvngrPRhVLG-----YLQDFlfhpkrAMTP 437
|
170 180 190
....*....|....*....|....*....|....*
gi 1460644645 188 PHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 222
Cdd:PRK11147 438 VKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
62-250 |
2.66e-12 |
|
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: 68.42 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 62 QLAGIRKSFD-GKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIhledhdithVPAENRHVNTVFQS 140
Cdd:TIGR03719 6 TMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA---------RPQPGIKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 141 YALFPHMTVFENVAFGLRMQK--------------TPAAEitprvLDAL--KMVQLEDF------------------AQR 186
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGVAEIKdaldrfneisakyaEPDAD-----FDKLaaEQAELQEIidaadawdldsqleiamdALR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 187 KP------HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNelkALQRKLGiTFVFVTHD 250
Cdd:TIGR03719 152 CPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLER---HLQEYPG-TVVAVTHD 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
72-272 |
3.15e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 72 GKTVIDNLNLTINNGEFLTLLGPSGCGKT-TVLRLIAGLENVDSGRIHLE-------------DHDITHVPaENRhvntv 137
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDgkpvkirnpqqaiAQGIAMVP-EDR----- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 138 fQSYALFPHMTVFENVAFGLRMQKTPAAeitpRVLDALKMVQLEDFAQR------KPHQ----LSGGQQQRVAIARAVVN 207
Cdd:PRK13549 348 -KRDGIVPVMGVGKNITLAALDRFTGGS----RIDDAAELKTILESIQRlkvktaSPELaiarLSGGNQQKAVLAKCLLL 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 208 KPRLLLLDESLSALD----YKLRKQMqNELKalqrKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQD 272
Cdd:PRK13549 423 NPKILILDEPTRGIDvgakYEIYKLI-NQLV----QQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
60-269 |
3.60e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.05 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 60 LVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEdHDITHVPAEN---RHVNT 136
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVARLQQdppRNVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 137 vfqsyalfphmTVFENVAFGL---------------RMQKTPAAEITPR------VLDALKMVQLEDF-----------A 184
Cdd:PRK11147 82 -----------TVYDFVAEGIeeqaeylkryhdishLVETDPSEKNLNElaklqeQLDHHNLWQLENRinevlaqlgldP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 185 QRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRklgiTFVFVTHDQEEALTMSDRIVVM 264
Cdd:PRK11147 151 DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDL 226
|
....*
gi 1460644645 265 RDGKI 269
Cdd:PRK11147 227 DRGKL 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
76-272 |
5.32e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.16 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGL-ENVDSGRIHLEDHDI-THVPAENRHVNTVF-----QSYALFPHMT 148
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdIRNPAQAIRAGIAMvpedrKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 VFENV------AFGLRMQKTPAAEITPrVLDALKMVQLEDFAQRKP-HQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 221
Cdd:TIGR02633 356 VGKNItlsvlkSFCFKMRIDAAAELQI-IGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1460644645 222 DYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQD 272
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
69-283 |
7.28e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 69 SFDGKTViDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIT-HVP-----------AENRHVNT 136
Cdd:PRK09700 273 SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPldavkkgmayiTESRRDNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 137 VFQSYALFPHMTVFENV-------AFGL---RMQKTPAAEitPRVLDALKMVQLEdfaqRKPHQLSGGQQQRVAIARAVV 206
Cdd:PRK09700 352 FFPNFSIAQNMAISRSLkdggykgAMGLfheVDEQRTAEN--QRELLALKCHSVN----QNITELSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 207 NKPRLLLLDESLSALD-------YKLRKQMQNElkalqrklGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIY 279
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDvgakaeiYKVMRQLADD--------GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDM 497
|
....
gi 1460644645 280 EEPK 283
Cdd:PRK09700 498 SEEE 501
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
80-269 |
2.36e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 80 NLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDIT-HVPAENRHVNTVF-----QSYALFPHMTVFENV 153
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLcpedrKAEGIIPVHSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 154 AFGLRMQKTPAAE-ITPRVLDALKMVQLEDFAQRKPH------QLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 226
Cdd:PRK11288 353 NISARRHHLRAGClINNRWEAENADRFIRSLNIKTPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAK 432
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1460644645 227 KQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:PRK11288 433 HEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
86-267 |
2.69e-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: 61.24 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 86 GEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLedhdithvpaenrhVNtvfqsyalfphmtvfenvafglrmqktpaa 165
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------ID------------------------------ 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 166 eiTPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ-----NELKALQRKL 240
Cdd:smart00382 38 --GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLLKSEK 115
|
170 180 190
....*....|....*....|....*....|..
gi 1460644645 241 GITFVFVTHDQEEALTM-----SDRIVVMRDG 267
Cdd:smart00382 116 NLTVILTTNDEKDLGPAllrrrFDRRIVLLLI 147
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
72-269 |
3.24e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 65.27 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 72 GKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGrihledhdithvpaenrhvnTVFQSYALfpHMTVF- 150
Cdd:PLN03073 521 GPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG--------------------TVFRSAKV--RMAVFs 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 151 ENVAFGLRMQKTP---AAEITPRVLDALKMVQLEDF------AQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 221
Cdd:PLN03073 579 QHHVDGLDLSSNPllyMMRCFPGVPEQKLRAHLGSFgvtgnlALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1460644645 222 DYKLRKQMQNELKALQRklGItfVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:PLN03073 659 DLDAVEALIQGLVLFQG--GV--LMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
59-254 |
5.92e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 59 PLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGlenvdsgrihleDH---------------- 122
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG------------DHpqgysndltlfgrrrg 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 123 ------DIthvpaeNRHVNTVfqSYALfpHM-----TVFENV-------AFGLrMQKTPAAEitpRVLDA--LKMVQLED 182
Cdd:PRK10938 327 sgetiwDI------KKHIGYV--SSSL--HLdyrvsTSVRNVilsgffdSIGI-YQAVSDRQ---QKLAQqwLDILGIDK 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 183 FAQRKP-HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDyklrkqmqnelkALQRKLGITFV------------FVTH 249
Cdd:PRK10938 393 RTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD------------PLNRQLVRRFVdvlisegetqllFVSH 460
|
....*
gi 1460644645 250 DQEEA 254
Cdd:PRK10938 461 HAEDA 465
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
75-286 |
6.50e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.61 E-value: 6.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 75 VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALFPHMtvfen 152
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFSGT----- 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 153 vafgLRMQKTPAAEITPRVL-DALKMVQLEDFAQRKPHQL-----------SGGQQQRVAIARAVVNKPRLLLLDESLSA 220
Cdd:PLN03232 1326 ----VRFNIDPFSEHNDADLwEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1460644645 221 LDYKLRKQMQNELKALQRKlgITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLF 286
Cdd:PLN03232 1402 VDVRTDSLIQRTIREEFKS--CTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
56-316 |
1.09e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.26 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 56 SRSPLVQLAGIRKSFDGKTvidnLNL---TINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHlEDHDITHVPaenR 132
Cdd:COG1245 337 EEETLVEYPDLTKSYGGFS----LEVeggEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKISYKP---Q 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 133 HVNTVFqsyalfpHMTVFENvafgLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLL 212
Cdd:COG1245 409 YISPDY-------DGTVEEF----LRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLY 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 213 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLTM----SDRIVVMrdgkieqDGTP--REIYEEPKNLF 286
Cdd:COG1245 478 LLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLidyiSDRLMVF-------EGEPgvHGHASGPMDMR 546
|
250 260 270
....*....|....*....|....*....|....
gi 1460644645 287 VA--SFIGEINIfdaTVieRLDEQ--RVRANVEG 316
Cdd:COG1245 547 EGmnRFLKELGI---TF--RRDEEtgRPRINKPG 575
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
56-263 |
2.52e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 56 SRSPLVQLAGIRKSFDGKTvidnLNL---TINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIhLEDHDITHVPaenr 132
Cdd:PRK13409 336 ERETLVEYPDLTKKLGDFS----LEVeggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-DPELKISYKP---- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 133 hvntvfQSYALFPHMTVFENvafgLRMQKTPAA------EItprvldaLKMVQLEDFAQRKPHQLSGGQQQRVAIARAVV 206
Cdd:PRK13409 407 ------QYIKPDYDGTVEDL----LRSITDDLGssyyksEI-------IKPLQLERLLDKNVKDLSGGELQRVAIAACLS 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 207 NKPRLLLLDESLSALDYK--------LRKQMQNELKAlqrklgiTFVfVTHDqeeaLTM----SDRIVV 263
Cdd:PRK13409 470 RDADLYLLDEPSAHLDVEqrlavakaIRRIAEEREAT-------ALV-VDHD----IYMidyiSDRLMV 526
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
69-316 |
2.78e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.62 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 69 SFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHlEDHDITHVPaenrhvntvfQSYALFPHmT 148
Cdd:TIGR01271 435 SLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-HSGRISFSP----------QTSWIMPG-T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 149 VFENVAFGLRMQKTpaaeitpRVLDALKMVQLEDFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:TIGR01271 503 IKDNIIFGLSYDEY-------RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 218 LSALDYKLRKQMQNE--LKALQRKlgiTFVFVTHDQEEaLTMSDRIVVMRDGKIEQDGTPREIYEEPKNlFVASFIGEIN 295
Cdd:TIGR01271 576 FTHLDVVTEKEIFESclCKLMSNK---TRILVTSKLEH-LKKADKILLLHEGVCYFYGTFSELQAKRPD-FSSLLLGLEA 650
|
250 260
....*....|....*....|....*
gi 1460644645 296 iFDATVIER----LDEQRVRANVEG 316
Cdd:TIGR01271 651 -FDNFSAERrnsiLTETLRRVSIDG 674
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
61-271 |
3.92e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.90 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 61 VQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVlRLIAGLENVDSGRihlEDHDITHVPAENRHVNTVFQS 140
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR---RPWRF*TWCANRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 141 Y-----ALFPHMTVFENVAFGLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 215
Cdd:NF000106 90 Hrpvr*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 216 ESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEA------LTMSDRIVVMRDGKIEQ 271
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAeqlaheLTVIDRGRVIADGKVDE 230
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
75-281 |
4.98e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.89 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 75 VIDNLNLTINNGEFLTLLGPSGCGKTTV-LRLIAGLENVDsGRIHLEDHDITHVPAEN--RHVNTVFQSYALFphmtvfe 151
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINESAE-GEIIIDGLNIAKIGLHDlrFKITIIPQDPVLF------- 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 152 nvAFGLRMQKTPAAEITPR-VLDALKMVQLEDFAQRKP----HQ-------LSGGQQQRVAIARAVVNKPRLLLLDESLS 219
Cdd:TIGR00957 1373 --SGSLRMNLDPFSQYSDEeVWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 220 ALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALTMSdRIVVMRDGKIEQDGTPREIYEE 281
Cdd:TIGR00957 1451 AVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
58-270 |
6.69e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.95 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 58 SPLVQLAGIRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLedhdithvpAENRHVNTV 137
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGIKLGYF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 138 FQsyalfpHMTVFenvafgLRMQKTP---AAEITPRVLDAlkmvQLEDF----------AQRKPHQLSGGQQQRVAIARA 204
Cdd:PRK10636 381 AQ------HQLEF------LRADESPlqhLARLAPQELEQ----KLRDYlggfgfqgdkVTEETRRFSGGEKARLVLALI 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1460644645 205 VVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQEEALTMSDRIVVMRDGKIE 270
Cdd:PRK10636 445 VWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
62-250 |
2.40e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 62 QLAGIRKSFDG-KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIhledhdithVPAENRHVNTVFQS 140
Cdd:PRK11819 8 TMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA---------RPAPGIKVGYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 141 YALFPHMTVFENVAFGLRMQK--------------TPAAEitprvLDAL--KMVQLEDF------------------AQR 186
Cdd:PRK11819 79 PQLDPEKTVRENVEEGVAEVKaaldrfneiyaayaEPDAD-----FDALaaEQGELQEIidaadawdldsqleiamdALR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 187 KPH------QLSGGQQQRVAIARAVVNKPRLLLLDESlsaldyklrkqmQNELKA---------LQRKLGiTFVFVTHD 250
Cdd:PRK11819 154 CPPwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEP------------TNHLDAesvawleqfLHDYPG-TVVAVTHD 219
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
52-291 |
1.59e-08 |
|
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: 55.30 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 52 IQPRSRSPLVQLAG--------IRKSFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHD 123
Cdd:cd03288 5 ISGSSNSGLVGLGGeikihdlcVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 124 ITHVPAEN--RHVNTVFQSYALFphmtvfenvAFGLRMQKTPAAEIT-PRVLDALKMVQLEDFAQRKPHQL--------- 191
Cdd:cd03288 85 ISKLPLHTlrSRLSIILQDPILF---------SGSIRFNLDPECKCTdDRLWEALEIAQLKNMVKSLPGGLdavvtegge 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 192 --SGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQN-ELKALQRKlgiTFVFVTHDQEEALTmSDRIVVMRDGK 268
Cdd:cd03288 156 nfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKvVMTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGI 231
|
250 260
....*....|....*....|...
gi 1460644645 269 IEQDGTPREIYEEPKNLFvASFI 291
Cdd:cd03288 232 LVECDTPENLLAQEDGVF-ASLV 253
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
76-278 |
1.07e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.74 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIhledhDITHVPAenrhvnTVFQSYALFPHMTVFENVAF 155
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAA------LIAISSGLNGQLTGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 156 -GLRM--QKTPAAEITPRVLDalkMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 232
Cdd:PRK13545 109 kGLMMglTKEKIKEIIPEIIE---FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1460644645 233 LKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:PRK13545 186 MNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
73-222 |
3.22e-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: 50.32 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLEN--VDSGRIHLEDHDIThvPAENRHVNTVFQSYALFPHMTVF 150
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLD--KNFQRSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 151 ENVAFG--LRmqktpaaeitprvldalkmvqledfaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 222
Cdd:cd03232 98 EALRFSalLR-------------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
71-271 |
3.58e-07 |
|
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: 52.61 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDsGRIHledhdITHVPAENRHVNTVFQSYALFPHMTVF 150
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQ-----IDGVSWNSVTLQTWRKAFGVIPQKVFI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 151 ENVAFglRMQKTPAAEITP----RVLD--ALKMVqLEDFAQRKPHQ-------LSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:TIGR01271 1304 FSGTF--RKNLDPYEQWSDeeiwKVAEevGLKSV-IEQFPDKLDFVlvdggyvLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644645 218 LSALDyklrkqmQNELKALQRKLGITF----VFVTHDQEEALTMSDRIVVMRDGKIEQ 271
Cdd:TIGR01271 1381 SAHLD-------PVTLQIIRKTLKQSFsnctVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
76-286 |
7.62e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIhlEDHDITHVPAENRHVNTvfqsyalfpHMTVFENVAF 155
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV--DRNGEVSVIAISAGLSG---------QLTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 156 GLRMQKTPAAEITPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKA 235
Cdd:PRK13546 109 KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYE 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 236 LQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI---YEEPKNLF 286
Cdd:PRK13546 189 FKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVlpkYEAFLNDF 241
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
71-271 |
9.30e-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: 50.24 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 71 DGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDsGRIHLEDHDITHVPAENRHvntvfQSYALFPHMTVF 150
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWR-----KAFGVIPQKVFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 151 ENVAFglRMQKTP----AAEITPRVLD--ALKMVqLEDFAQRKPHQL-------SGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:cd03289 89 FSGTF--RKNLDPygkwSDEEIWKVAEevGLKSV-IEQFPGQLDFVLvdggcvlSHGHKQLMCLARSVLSKAKILLLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1460644645 218 LSALDYKLRKQMQNELKalQRKLGITFVFVTHdQEEALTMSDRIVVMRDGKIEQ 271
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 ... |
83-263 |
1.37e-06 |
|
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: 48.34 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 83 INNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPaenrhvntvfqsyalfphmtvfenvafglrmQKT 162
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP-------------------------------QYI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 163 paaeitprvldalkmvqledfaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGI 242
Cdd:cd03222 71 ---------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180
....*....|....*....|.
gi 1460644645 243 TFVFVTHDQEEALTMSDRIVV 263
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHV 144
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
75-278 |
1.69e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 75 VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVP-AENRHVNTVF-QSYALFPHmtvfeN 152
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGlMDLRKVLGIIpQAPVLFSG-----T 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 153 VAFGLrmqkTPAAEITPRVL-DALKMVQLEDFAQRKPHQL-----------SGGQQQRVAIARAVVNKPRLLLLDESLSA 220
Cdd:PLN03130 1329 VRFNL----DPFNEHNDADLwESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460644645 221 LDYK----LRKQMQNELKAlqrklgITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREI 278
Cdd:PLN03130 1405 VDVRtdalIQKTIREEFKS------CTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
86-264 |
1.91e-06 |
|
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: 48.90 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 86 GEFLTLLGPSGCGKTTVLRLIAGLENVDSGRiHLEDHDITHVPAENRhvNTVFQSYalfphmtvFENVAFG-LRMQKTPA 164
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEILDEFR--GSELQNY--------FTKLLEGdVKVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 165 -AEITPRVLDA------------------LKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 225
Cdd:cd03236 95 yVDLIPKAVKGkvgellkkkdergkldelVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1460644645 226 RKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVM 264
Cdd:cd03236 175 RLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
80-281 |
2.75e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 80 NLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITH---------VPAENRHVNTVFQSyalfphmtVF 150
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRlsfeqlqklVSDEWQRNNTDMLS--------PG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 151 ENvAFGlrmqKTpAAEI-------TPRVLDALKMVQLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 223
Cdd:PRK10938 95 ED-DTG----RT-TAEIiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644645 224 KLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 281
Cdd:PRK10938 169 ASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
73-265 |
3.00e-06 |
|
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: 46.97 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAglenvdsgrihledhdithvpaenrhvntvfqsYALFPHMTVFEN 152
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LALGGAQSATRR 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 153 VAFGLRMQKTPAAEITPRVLDalkmvqledfaqrkpHQLSGGQQQRVAIARAVVN---KPR-LLLLDESLSALDyklrkq 228
Cdd:cd03227 55 RSGVKAGCIVAAVSAELIFTR---------------LQLSGGEKELSALALILALaslKPRpLYILDEIDRGLD------ 113
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1460644645 229 MQNELKAL-----QRKLGITFVFVTHDQEEALtMSDRIVVMR 265
Cdd:cd03227 114 PRDGQALAeaileHLVKGAQVIVITHLPELAE-LADKLIHIK 154
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
191-269 |
3.04e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 191 LSGGQQQRVAIARAVVNKPRLLLLDESLSALD-------YKLRKQMQNELKalqrklGItfVFVTHDQEEALTMSDRIVV 263
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgakfeiYQLIAELAKKDK------GI--IIISSEMPELLGITDRILV 463
|
....*.
gi 1460644645 264 MRDGKI 269
Cdd:PRK10982 464 MSNGLV 469
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
86-267 |
1.22e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 86 GEFLTLLGPSGCGKTTVLRLIAglENVDSGRIHLEDHDITHVPAEN---RHVNTVFQSYALFPHMTVFENVAFGLRM--- 159
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGRPLDSsfqRSIGYVQQQDLHLPTSTVRESLRFSAYLrqp 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 160 QKTPAAEITPRVLDALKMVQLEDFAQR---KPHQ-LSGGQQQRVAIARAVVNKPRLLL-LDESLSALDyklrKQMQNELK 234
Cdd:TIGR00956 867 KSVSKSEKMEYVEEVIKLLEMESYADAvvgVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD----SQTAWSIC 942
|
170 180 190
....*....|....*....|....*....|....*...
gi 1460644645 235 ALQRKL---GITFVFVTHdQEEALTMS--DRIVVMRDG 267
Cdd:TIGR00956 943 KLMRKLadhGQAILCTIH-QPSAILFEefDRLLLLQKG 979
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
86-264 |
2.05e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 86 GEFLTLLGPSGCGKTTVLRLIAG-----LENVDSGrihledhdithVPAEN---RHVNTVFQSYalfphmtvFENVAFG- 156
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGelipnLGDYEEE-----------PSWDEvlkRFRGTELQNY--------FKKLYNGe 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 157 LR-MQKTPAAEITPRVL-----DALKMV-------------QLEDFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 217
Cdd:PRK13409 160 IKvVHKPQYVDLIPKVFkgkvrELLKKVdergkldevverlGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1460644645 218 LSALDYKLRKQMQNELKALQRklGITFVFVTHDqeeaLT----MSDRIVVM 264
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAE--GKYVLVVEHD----LAvldyLADNVHIA 284
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
75-286 |
2.34e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 75 VIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDHDITHVPAEN--RHVNTVFQSYALFPHmTVFEN 152
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 153 VafglrmqkTPAAEITP-RVLDALKMVQL-----------EDFAQRKPHQLSGGQQQRVAIARAVVNKPR-LLLLDESLS 219
Cdd:PTZ00243 1404 V--------DPFLEASSaEVWAALELVGLrervasesegiDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEATA 1475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644645 220 ALDYKLRKQMQNE-LKALQRKLGITFVFVTHdqeeALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLF 286
Cdd:PTZ00243 1476 NIDPALDRQIQATvMSAFSAYTVITIAHRLH----TVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
86-264 |
2.85e-05 |
|
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: 46.32 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 86 GEFLTLLGPSGCGKTTVLRLIAG-----LENVDSgrihledhdithvPAENRHVNTVFQSYALFPHmtvFENVAFG-LRM 159
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGelkpnLGDYDE-------------EPSWDEVLKRFRGTELQDY---FKKLANGeIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 160 -QKTPAAEITPRVL-----DALKMV----QLEDFAQ---------RKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 220
Cdd:COG1245 163 aHKPQYVDLIPKVFkgtvrELLEKVdergKLDELAEklglenildRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1460644645 221 LDYKLRKQMQNELKALQRKlGITFVFVTHDqeeaLT----MSDRIVVM 264
Cdd:COG1245 243 LDIYQRLNVARLIRELAEE-GKYVLVVEHD----LAildyLADYVHIL 285
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
93-121 |
3.37e-05 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 43.63 E-value: 3.37e-05
10 20 30
....*....|....*....|....*....|..
gi 1460644645 93 GPSGCGKTTVLRLIA---GLENVDSGRIHLED 121
Cdd:cd02020 6 GPAGSGKSTVAKLLAkklGLPYLDTGGIRTEE 37
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
76-264 |
4.99e-05 |
|
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: 43.85 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 76 IDNLNLTINNGEFLTLLGPSGCGKTTVLRliaglenvdsgrihledhDITHVPAENRHVNTVfqsYALFPHMTVFenvaf 155
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN------------------EGLYASGKARLISFL---PKFSRNKLIF----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 156 glrmqktpaaeitprvLDALKMV--------QLEdfaqRKPHQLSGGQQQRVAIAR--AVVNKPRLLLLDESLSALDYKL 225
Cdd:cd03238 65 ----------------IDQLQFLidvglgylTLG----QKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQD 124
|
170 180 190
....*....|....*....|....*....|....*....
gi 1460644645 226 RKQMQNELKALqRKLGITFVFVTHDqEEALTMSDRIVVM 264
Cdd:cd03238 125 INQLLEVIKGL-IDLGNTVILIEHN-LDVLSSADWIIDF 161
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
131-296 |
5.23e-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: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 131 NRHVNTVF---QSYALFPHMTVFENVAF----GLRMQKTPAA-----EITPRvLDALKMVQLEDFA-QRKPHQLSGGQQQ 197
Cdd:TIGR00630 417 KPEALAVTvggKSIADVSELSIREAHEFfnqlTLTPEEKKIAeevlkEIRER-LGFLIDVGLDYLSlSRAAGTLSGGEAQ 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 198 RVAIARAV------VnkprLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDqEEALTMSDRIVVM------R 265
Cdd:TIGR00630 496 RIRLATQIgsgltgV----LYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD-EDTIRAADYVIDIgpgageH 569
|
170 180 190
....*....|....*....|....*....|.
gi 1460644645 266 DGKIEQDGTPREIYEEPKNLFVASFIGEINI 296
Cdd:TIGR00630 570 GGEVVASGTPEEILANPDSLTGQYLSGRKKI 600
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
335-393 |
2.08e-04 |
|
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: 39.53 E-value: 2.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644645 335 VLLRPEDLRVDEihhnsDADGLIGYVRERNYKGMTLESVVELENGKMVMVSEFFNEDDP 393
Cdd:pfam08402 1 LAIRPEKIRLAA-----AANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHARP 54
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
69-309 |
2.23e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 69 SFDGKTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAgLENVDS-----GRIHLE---------------DHDITHVP 128
Cdd:PLN03073 186 SVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA-MHAIDGipkncQILHVEqevvgddttalqcvlNTDIERTQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 129 AENRHVNTVFQSYAL-FPHMTVFENVAFGLRMQKTPA----AEITPRvLDALKMVQLE--------------DFAQRKPH 189
Cdd:PLN03073 265 LLEEEAQLVAQQRELeFETETGKGKGANKDGVDKDAVsqrlEEIYKR-LELIDAYTAEaraasilaglsftpEMQVKATK 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 190 QLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKalqrKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 269
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLL----KWPKTFIVVSHAREFLNTVVTDILHLHGQKL 419
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1460644645 270 eqdgtpreiyeepknlfvASFIGEINIFDATVIERLDEQR 309
Cdd:PLN03073 420 ------------------VTYKGDYDTFERTREEQLKNQQ 441
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
191-269 |
3.26e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 191 LSGGQQQRVAIARAVVNKPRLLLLDESLSALD-------YKLRKQMQNELKALqrklgitfVFVTHDQEEALTMSDRIVV 263
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgakyeiYTIINELAAEGKGV--------IVISSELPELLGMCDRIYV 476
|
....*.
gi 1460644645 264 MRDGKI 269
Cdd:NF040905 477 MNEGRI 482
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
73-271 |
1.06e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 73 KTVIDNLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLE--------------------------DHDITH 126
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPgnwqlawvnqetpalpqpaleyvidgDREYRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644645 127 VPAENRHVNTVFQSYALfphmtvfenVAFGLRMQKTPAAEITPR---VLDALKMVQleDFAQRKPHQLSGGQQQRVAIAR 203
Cdd:PRK10636 94 LEAQLHDANERNDGHAI---------ATIHGKLDAIDAWTIRSRaasLLHGLGFSN--EQLERPVSDFSGGWRMRLNLAQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644645 204 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRklgiTFVFVTHDQEEALTMSDRIVvmrdgKIEQ 271
Cdd:PRK10636 163 ALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPIVDKII-----HIEQ 221
|
|
| |
