|
Name |
Accession |
Description |
Interval |
E-value |
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
24-397 |
0e+00 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 767.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 24 IQTLNAKQQAGKPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQ 103
Cdd:PRK09452 1 SKKLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 104 VPAEQRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVV 183
Cdd:PRK09452 81 VPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 184 NKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLF 263
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 264 VARFIGEINVFNATMLERIDEKRIRAEIEGVESVVYYDREAQPGDKLQVLLRPEDLR-IEEIKESEEKGIVGHVTERTYK 342
Cdd:PRK09452 241 VARFIGEINIFDATVIERLDEQRVRANVEGRECNIYVNFAVEPGQKLHVLLRPEDLRvEEINDDEHAEGLIGYVRERNYK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2127793354 343 GMTLDSVIQLDSGMRVMVSEFFNEDDPDVDHSLGQKVAITWVESWEVVLNDKQEA 397
Cdd:PRK09452 321 GMTLDSVVELENGKMVMVSEFFNEDDPDFDHSLGQKVAVTWVEGWEVVLADEEHK 375
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
35-393 |
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: 529.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 35 KPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTV 114
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 115 FQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 195 LSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGEINVF 274
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 275 NATMLERIDEkriRAEIEGVESVVYYDREAQPGDKLQVLLRPEDLRieEIKESEEKGIVGHVTERTYKGMTLDSVIQLDS 354
Cdd:COG3842 243 PGTVLGDEGG---GVRTGGRTLEVPADAGLAAGGPVTVAIRPEDIR--LSPEGPENGLPGTVEDVVFLGSHVRYRVRLGD 317
|
330 340 350
....*....|....*....|....*....|....*....
gi 2127793354 355 GMRVMVSEFFNEDDPdvdHSLGQKVAITWVESWEVVLND 393
Cdd:COG3842 318 GQELVVRVPNRAALP---LEPGDRVGLSWDPEDVVVLPA 353
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
68-391 |
8.40e-179 |
|
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: 500.10 E-value: 8.40e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 68 ILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPR 147
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 148 VMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHD 227
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 228 QEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGEINVFNATMLERIDEKRIRAEIEGVESVVYYDREAQPG 307
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAGVEGRRCDIYTDVPVEKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 308 DKLQVLLRPEDLR-IEEIKESEEKGIVGHVTERTYKGMTLDSVIQLDSGMRVMVSEFFNEDDPDVDHSLGQKVAITWVES 386
Cdd:TIGR01187 241 QPLHVVLRPEKIViEEEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQKVLVSEFFNEDDPHMSPSIGDRVGLTWHPG 320
|
....*
gi 2127793354 387 WEVVL 391
Cdd:TIGR01187 321 SEVVL 325
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
38-383 |
1.48e-151 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 432.19 E-value: 1.48e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTVFQS 117
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 YALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSA 197
Cdd:COG3839 84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 198 LDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGE--INVFN 275
Cdd:COG3839 164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppMNLLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 276 ATMLERidekriRAEIEGVESVVYYDREAQPGDKLQVLLRPEDLRieeIKESEEKGIVGHVTERTYKGMtlDSVIQLDSG 355
Cdd:COG3839 244 GTVEGG------GVRLGGVRLPLPAALAAAAGGEVTLGIRPEHLR---LADEGDGGLEATVEVVEPLGS--ETLVHVRLG 312
|
330 340
....*....|....*....|....*...
gi 2127793354 356 MRVMVSEFfnedDPDVDHSLGQKVAITW 383
Cdd:COG3839 313 GQELVARV----PGDTRLRPGDTVRLAF 336
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
38-269 |
6.61e-150 |
|
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: 423.19 E-value: 6.61e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTVFQS 117
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 YALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSA 197
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 198 LDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIG 269
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
38-320 |
8.39e-131 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 379.49 E-value: 8.39e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDV-TQVPAEQRHVNTVFQ 116
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 117 SYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLS 196
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 197 ALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGEINVFNA 276
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2127793354 277 tmlERIDEkriRAEIEGVESVVYydrEAQPGDKLQVLLRPEDLR 320
Cdd:COG1118 243 ---RVIGG---QLEADGLTLPVA---EPLPDGPAVAGVRPHDIE 277
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
38-250 |
4.55e-119 |
|
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: 344.50 E-value: 4.55e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTVFQS 117
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 YALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSA 197
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2127793354 198 LDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDG 250
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
36-354 |
5.77e-114 |
|
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: 336.62 E-value: 5.77e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLS--GISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNT 113
Cdd:TIGR03265 1 SSPYLSidNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 114 VFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDE 193
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 194 SLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGEINV 273
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 274 FNATMleridEKRIRAEIEGVESVVYYDReAQPGDKLQVLLRPEDLRiEEIKESEEKGIVGHVTERTYKGMTLDSVIQLD 353
Cdd:TIGR03265 241 LPGTR-----GGGSRARVGGLTLACAPGL-AQPGASVRLAVRPEDIR-VSPAGNAANLLLARVEDMEFLGAFYRLRLRLE 313
|
.
gi 2127793354 354 S 354
Cdd:TIGR03265 314 G 314
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
38-320 |
3.33e-108 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 322.18 E-value: 3.33e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGK-EIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQV-PAEqRHVNTVF 115
Cdd:PRK11650 4 LKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELePAD-RDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 116 QSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESL 195
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 196 SALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGE--INV 273
Cdd:PRK11650 163 SNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpaMNL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2127793354 274 FNAtmleRIDEKRIRAEI-EGVESVVYYDREAQPGDKLQVLLRPEDLR 320
Cdd:PRK11650 243 LDG----RVSADGAAFELaGGIALPLGGGYRQYAGRKLTLGIRPEHIA 286
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
38-270 |
7.39e-108 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 316.97 E-value: 7.39e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTVFQS 117
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 YALFPHMTVFENVAFGLRMQK----TPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDE 193
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKPrserPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 194 SLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGE 270
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
38-250 |
8.04e-108 |
|
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: 315.73 E-value: 8.04e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTVFQS 117
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 YALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSA 197
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2127793354 198 LDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDG 250
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
38-278 |
1.05e-104 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 313.19 E-value: 1.05e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTVFQS 117
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 YALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSA 197
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 198 LDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGEINVFNAT 277
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPAT 246
|
.
gi 2127793354 278 M 278
Cdd:PRK11432 247 L 247
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
31-317 |
1.40e-103 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 311.00 E-value: 1.40e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 31 QQAGKPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRH 110
Cdd:PRK11607 13 RKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 111 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLL 190
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 191 LDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGE 270
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2127793354 271 INVFNATMLERIDEKRIrAEIEGVESVVYYDREAQPGD--KLQVLLRPE 317
Cdd:PRK11607 253 VNVFEGVLKERQEDGLV-IDSPGLVHPLKVDADASVVDnvPVHVALRPE 300
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
33-244 |
2.34e-98 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 293.53 E-value: 2.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 33 AGKPVVRLSGISKSF----DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEq 108
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 109 rhVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKV 188
Cdd:COG1116 82 --RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 189 LLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDG 244
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
38-278 |
6.71e-96 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 290.45 E-value: 6.71e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTVFQS 117
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 YALFPHMTVFENVAFGLRM----QKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDE 193
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 194 SLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGEINV 273
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNR 242
|
....*
gi 2127793354 274 FNATM 278
Cdd:PRK10851 243 LQGTI 247
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
38-319 |
2.41e-95 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 289.62 E-value: 2.41e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTVFQS 117
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 YALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSA 197
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 198 LDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIG--EINvFN 275
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGspKMN-FL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 276 ATMLERIDEKRIRAEIEG-------VESvvyydREAQPGDKLQVLLRPEDL 319
Cdd:PRK11000 243 PVKVTATAIEQVQVELPNrqqvwlpVEG-----RGVQVGANMSLGIRPEHL 288
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
38-241 |
1.92e-93 |
|
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: 279.36 E-value: 1.92e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGK----EIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPaeqRHVNT 113
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG---PDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 114 VFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDE 193
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2127793354 194 SLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVM 241
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
55-269 |
9.24e-87 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 263.04 E-value: 9.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTVFQSYALFPHMTVFENVAFGL 134
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAYGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 135 RMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQ 214
Cdd:cd03299 97 KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2127793354 215 RQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIG 269
Cdd:cd03299 177 KEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
35-249 |
2.12e-83 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 253.81 E-value: 2.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 35 KPVVRLSGISKSF-DGKE---IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQR- 109
Cdd:COG1136 2 SPLLELRNLTKSYgTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 110 -----HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVN 184
Cdd:COG1136 82 rlrrrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 185 KPKVLLLDESLSALDYKLRKQ-MQIeLKQLQRQLGITFIFVTHDqEEALSMSDRIIVMRDGVIEQD 249
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEvLEL-LRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
55-352 |
1.50e-82 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 257.34 E-value: 1.50e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ------RHVNTVFQSYALFPHMTVFE 128
Cdd:COG4175 45 DASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPHRTVLE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 129 NVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQI 208
Cdd:COG4175 125 NVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 209 ELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGEIN---VFNA--------- 276
Cdd:COG4175 205 ELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDVDrskVLTAgsvmrppea 284
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 277 --TMLERIDEKRIRAEIEGVESVVYYDREaqpgDKLQVLLRPEDLRIEEIKESEEKGIVGHVTERTYKGMTLDSVIQL 352
Cdd:COG4175 285 vvSEKDGPRVALRRMREEGISSLYVVDRD----RRLLGVVTADDALEAVKGEKDLEEILLTDVPTVSPDTPLRDLLPL 358
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
38-270 |
3.42e-81 |
|
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: 249.14 E-value: 3.42e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSF-DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNTV 114
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 115 FQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLE--KMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLD 192
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 193 ESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGE 270
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
55-268 |
6.08e-80 |
|
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: 246.79 E-value: 6.08e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ------RHVNTVFQSYALFPHMTVFE 128
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 129 NVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQI 208
Cdd:cd03294 122 NVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQD 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 209 ELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFI 268
Cdd:cd03294 202 ELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
33-268 |
3.11e-79 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 243.73 E-value: 3.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 33 AGKPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ---- 108
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 109 -RHVNTVFQSYALFPHMTVFENVAFGLRMQKT-PAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKP 186
Cdd:COG1127 81 rRRIGMLFQGGALFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 187 KVLLLDESLSALD-------YKLrkqmqieLKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIyEEP 259
Cdd:COG1127 161 EILLYDEPTAGLDpitsaviDEL-------IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL-LAS 232
|
....*....
gi 2127793354 260 KNLFVARFI 268
Cdd:COG1127 233 DDPWVRQFL 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
32-260 |
1.24e-78 |
|
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: 251.36 E-value: 1.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 32 QAGKPVVRLSGISKSFDGKE-----IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPA 106
Cdd:COG1123 255 AAAEPLLEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 107 EQ-----RHVNTVFQ--SYALFPHMTVFENVAFGLRMQKT-PAAEIEPRVMDALRMVRL-EKMAQRKPHQLSGGQQQRIA 177
Cdd:COG1123 335 RSlrelrRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 178 IARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYE 257
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
...
gi 2127793354 258 EPK 260
Cdd:COG1123 495 NPQ 497
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
37-271 |
6.89e-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: 240.28 E-value: 6.89e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE----QRHVN 112
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinklRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 113 TVFQSYALFPHMTVFENVAFGLRM-QKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLL 191
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 192 DESLSALDYKLRKqmqiE----LKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARF 267
Cdd:COG1126 161 DEPTSALDPELVG----EvldvMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAF 235
|
....
gi 2127793354 268 IGEI 271
Cdd:COG1126 236 LSKV 239
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
38-246 |
6.65e-77 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 237.00 E-value: 6.65e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDG----KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQR---- 109
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 110 --HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPK 187
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2127793354 188 VLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEAlSMSDRIIVMRDGVI 246
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
38-244 |
4.02e-74 |
|
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: 228.61 E-value: 4.02e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT----QVPAEQRHVNT 113
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 114 VFQSYALFPHMTVFENVAFGlrmqktpaaeieprvmdalrmvrlekmaqrkphqLSGGQQQRIAIARAVVNKPKVLLLDE 193
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 194 SLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDG 244
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
55-270 |
4.88e-74 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 230.41 E-value: 4.88e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTVFQSYALFPHMTVFENVAFGL 134
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFPHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 135 RmqktP-----AAEIEpRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIE 209
Cdd:COG3840 97 R----PglkltAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 210 LKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGE 270
Cdd:COG3840 172 VDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
55-250 |
3.76e-72 |
|
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: 224.87 E-value: 3.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNhGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQ---DVTQ---VPAEQRHVNTVFQSYALFPHMTVFE 128
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkinLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 129 NVAFGLRmqKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQI 208
Cdd:cd03297 95 NLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2127793354 209 ELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDG 250
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
48-262 |
1.93e-71 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 223.36 E-value: 1.93e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNTVFQS--YALFpH 123
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQNpdDQLF-A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 124 MTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLR 203
Cdd:COG1122 91 PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2127793354 204 KQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNL 262
Cdd:COG1122 171 RELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
45-285 |
3.91e-71 |
|
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: 227.43 E-value: 3.91e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 45 KSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT-QVPAEQRHVN-----TVFQSY 118
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMkQSPVELREVRrkkigMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 119 ALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSAL 198
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 199 DYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGEINVFNATM 278
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240
|
....*..
gi 2127793354 279 LERIDEK 285
Cdd:TIGR01186 241 AERIAQR 247
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
37-250 |
7.88e-71 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 221.85 E-value: 7.88e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSF-DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ-----RH 110
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 111 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLL 190
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 191 LDESLSALDYKLRKQ-MQIeLKQLQRqLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDG 250
Cdd:COG2884 161 ADEPTGNLDPETSWEiMEL-LEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
36-241 |
2.18e-68 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 216.65 E-value: 2.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDG----KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQvPAEQRHV 111
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 112 ntVFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLL 191
Cdd:COG4525 81 --VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2127793354 192 DESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVM 241
Cdd:COG4525 159 DEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
38-255 |
2.87e-68 |
|
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: 215.44 E-value: 2.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQV-PAEQRHVNT--- 113
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLsEAELYRLRRrmg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 114 -VFQSYALFPHMTVFENVAFGLRMQ-KTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLL 191
Cdd:cd03261 81 mLFQSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 192 DESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
38-246 |
3.92e-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: 209.31 E-value: 3.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT----QVPAEQRHVNT 113
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 114 VFQSYALFPHMTVFENVAFGLR-MQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLD 192
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 193 ESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVI 246
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
38-261 |
4.61e-65 |
|
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: 207.73 E-value: 4.61e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSF----DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVP--AEQRHV 111
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRrkAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 112 NTVFQSY--ALFPHMTVFENVAFGLRMQKTPaaEIEPRVMDALRMVRL-EKMAQRKPHQLSGGQQQRIAIARAVVNKPKV 188
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127793354 189 LLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKN 261
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
54-318 |
8.18e-65 |
|
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: 210.73 E-value: 8.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 54 GNLNLDVN----HGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDD---QDVTQ---VPAEQRHVNTVFQSYALFPH 123
Cdd:COG4148 12 GGFTLDVDftlpGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgifLPPHRRRIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 124 MTVFENVAFGLRmqKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLR 203
Cdd:COG4148 92 LSVRGNLLYGRK--RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 204 KQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGEINVFNATMLERID 283
Cdd:COG4148 170 AEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVAAHDP 249
|
250 260 270
....*....|....*....|....*....|....*.
gi 2127793354 284 EKRI-RAEIEGVESVVyYDREAQPGDKLQVLLRPED 318
Cdd:COG4148 250 DYGLtRLALGGGRLWV-PRLDLPPGTRVRVRIRARD 284
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
36-258 |
9.83e-65 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 206.83 E-value: 9.83e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSF-DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ-----R 109
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 110 HVNTVFQSYALFPHMTVFENVAFG-----------LRMQktPAAEIEpRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAI 178
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGrlgrtstwrslLGLF--PPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 179 ARAVVNKPKVLLLDESLSALDYKLRKQ-MQIeLKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYE 257
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQvMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTD 236
|
.
gi 2127793354 258 E 258
Cdd:COG3638 237 A 237
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
37-248 |
1.38e-64 |
|
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: 205.82 E-value: 1.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSFDGK----EIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQR--- 109
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 110 --HVNTVFQSY--ALFPHMTVFENVAFGLRMQK--TPAAEIEPRVMDALRMVRL-EKMAQRKPHQLSGGQQQRIAIARAV 182
Cdd:cd03257 81 rkEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGklSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 183 VNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDG-VIEQ 248
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGkIVEE 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
39-244 |
9.26e-64 |
|
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: 203.08 E-value: 9.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 39 RLSGISKSFDGKE--IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNTV 114
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 115 FQsyalFP-HM----TVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVL 189
Cdd:cd03225 81 FQ----NPdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2127793354 190 LLDESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDG 244
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
38-271 |
1.65e-63 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 206.85 E-value: 1.65e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGK----EIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ----- 108
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 109 RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKV 188
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 189 LLLDESLSALDYK-------LrkqmqieLKQLQRQLGITFIFVTHDqeealsMS------DRIIVMRDGVIEQDGSPREI 255
Cdd:COG1135 162 LLCDEATSALDPEttrsildL-------LKDINRELGLTIVLITHE------MDvvrricDRVAVLENGRIVEQGPVLDV 228
|
250
....*....|....*.
gi 2127793354 256 YEEPKNLFVARFIGEI 271
Cdd:COG1135 229 FANPQSELTRRFLPTV 244
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
37-255 |
3.65e-63 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 202.97 E-value: 3.65e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNTV 114
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 115 FQSYALFPHMTVFENVAFG----LRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLL 190
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 191 LDESLSALDykLRKQMQI--ELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:COG1120 161 LDEPTSHLD--LAHQLEVleLLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
35-262 |
3.68e-63 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 210.92 E-value: 3.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 35 KPVVRLSGISKSFDG--KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAG---FETADNGQIVLDDQDVTQVPAEQR 109
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 110 --HVNTVFQS--YALFPhMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNK 185
Cdd:COG1123 82 grRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 186 PKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNL 262
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
38-258 |
4.88e-63 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 202.22 E-value: 4.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE-QRHVNTVFQ 116
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 117 SYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLS 196
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 197 ALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEE 258
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
37-260 |
2.33e-61 |
|
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: 197.80 E-value: 2.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSFDGK----EIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVP-----AE 107
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 108 QRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPK 187
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127793354 188 VLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPK 260
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
48-243 |
3.32e-59 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 191.54 E-value: 3.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETAD---NGQIVLDDQDVTQVPAEQRHVNTVFQSYALFPHM 124
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 125 TVFENVAFGLRmQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRK 204
Cdd:COG4136 92 SVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2127793354 205 QM-QIELKQLqRQLGITFIFVTHDQEEALSMSdRIIVMRD 243
Cdd:COG4136 171 QFrEFVFEQI-RQRGIPALLVTHDEEDAPAAG-RVLDLGN 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
37-261 |
5.56e-58 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 189.15 E-value: 5.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHV----N 112
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 113 TVFQSYALFPHMTVFENVAFG-LRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLL 191
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 192 DESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKN 261
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
33-260 |
7.52e-58 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 191.87 E-value: 7.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 33 AGKPVVRLSGISKSFDGKeiiGNL--------------NLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDD 98
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVR---GGLfgrtvgvvkavdgvSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 99 QDVTQVPAEQ-----RHVNTVFQ-SYA-LFPHMTVFENVAFGLRMQK-TPAAEIEPRVMDALRMVRLEK-MAQRKPHQLS 169
Cdd:COG4608 80 QDITGLSGRElrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPeHADRYPHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 170 GGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDqeeaLSM----SDRIIVMRDGV 245
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGK 235
|
250
....*....|....*
gi 2127793354 246 IEQDGSPREIYEEPK 260
Cdd:COG4608 236 IVEIAPRDELYARPL 250
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
37-271 |
1.24e-57 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 191.55 E-value: 1.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSFD--GKEIIG--NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ---- 108
Cdd:PRK11153 1 MIELKNISKVFPqgGRTIHAlnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 109 -RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPK 187
Cdd:PRK11153 81 rRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 188 VLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDG-VIEQdGSPREIYEEPKNLFVAR 266
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGrLVEQ-GTVSEVFSHPKHPLTRE 239
|
....*
gi 2127793354 267 FIGEI 271
Cdd:PRK11153 240 FIQST 244
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
39-258 |
1.86e-57 |
|
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: 187.78 E-value: 1.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 39 RLSGISKSF-DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVP-----AEQRHVN 112
Cdd:cd03256 2 EVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkalrQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 113 TVFQSYALFPHMTVFENVAFGLRMQKT---------PAAEIEpRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVV 183
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGRLGRRStwrslfglfPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 184 NKPKVLLLDESLSALDYKLRKQ-MQIeLKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEE 258
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQvMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
39-246 |
6.92e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 182.71 E-value: 6.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 39 RLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNTVFQ 116
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 117 SYALFPhMTVFENVAFGLRMQKTPAAeiEPRVMDALRMVRL-EKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESL 195
Cdd:COG4619 82 EPALWG-GTVRDNLPFPFQLRERKFD--RERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 196 SALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVI 246
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
38-262 |
9.55e-56 |
|
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: 184.17 E-value: 9.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKE--IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDV---TQVPAEQRHVN 112
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 113 TVFQSyalfPH-----MTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPK 187
Cdd:TIGR04520 81 MVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 188 VLLLDESLSALDYKLRKQ-MQIeLKQLQRQLGITFIFVTHDQEEALsMSDRIIVMRDGVIEQDGSPREIYEEPKNL 262
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEvLET-IRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQVELL 230
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
37-258 |
1.02e-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: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSF-DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE-----QRH 110
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrklRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 111 VNTVFQSYALFPHMTVFENVAFG-LRMQKT--------PAAEIEpRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARA 181
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGrLGYKPTwrsllgrfSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 182 VVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEE 258
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
38-255 |
1.08e-54 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 180.07 E-value: 1.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFE-----TADNGQIVLDDQDV----TQVPAEQ 108
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIydldVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 109 RHVNTVFQSYALFPhMTVFENVAFGLRMQKT-PAAEIEPRVMDALRMVRL-EKMAQR-KPHQLSGGQQQRIAIARAVVNK 185
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 186 PKVLLLDESLSALDykLRKQMQIE--LKQLQRQlgITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:cd03260 160 PEVLLLDEPTSALD--PISTAKIEelIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
36-249 |
1.10e-54 |
|
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: 180.32 E-value: 1.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDGKE----IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQR-- 109
Cdd:COG4181 7 PIIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 110 ----HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEiePRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNK 185
Cdd:COG4181 87 lrarHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 186 PKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEAlSMSDRIIVMRDGVIEQD 249
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVED 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
38-250 |
2.02e-54 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 179.23 E-value: 2.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFdgKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTVFQS 117
Cdd:cd03298 1 VRLDKIRFSY--GEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 YALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSA 197
Cdd:cd03298 79 NNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2127793354 198 LDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDG 250
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
40-244 |
3.64e-54 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 179.90 E-value: 3.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 40 LSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQvPAEQRHVntVFQSYA 119
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 120 LFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALD 199
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2127793354 200 YKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDG 244
Cdd:PRK11248 161 AFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
39-258 |
5.49e-54 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 178.90 E-value: 5.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 39 RLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE-QRHVNTVFQS 117
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 YALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSA 197
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 198 LDYKLRKQMQIELKQLqRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEE 258
Cdd:COG4555 163 LDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
34-255 |
8.14e-54 |
|
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: 179.08 E-value: 8.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 34 GKPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRH--- 110
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 111 -VNTvFQSYALFPHMTVFENVA---------------FGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQ 174
Cdd:COG0411 81 iART-FQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 175 RIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPRE 254
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
.
gi 2127793354 255 I 255
Cdd:COG0411 240 V 240
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
38-257 |
1.86e-53 |
|
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: 188.50 E-value: 1.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSF--DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNT 113
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 114 VFQSYALFpHMTVFENVAFGLrmqktPAAEIEpRVMDALRMVRLEKMAQRKPH-----------QLSGGQQQRIAIARAV 182
Cdd:COG2274 554 VLQDVFLF-SGTIRENITLGD-----PDATDE-EIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127793354 183 VNKPKVLLLDESLSALDYKLRKQMQIELKQLQRqlGITFIFVTHDqEEALSMSDRIIVMRDGVIEQDGSPREIYE 257
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
53-260 |
5.30e-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: 176.12 E-value: 5.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 53 IGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQvPAEQRHVntVFQSYALFPHMTVFENVAF 132
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV--VFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 133 GLR--MQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIEL 210
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 211 KQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI-YEEPK 260
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPR 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
37-260 |
7.11e-53 |
|
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: 178.32 E-value: 7.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSFDGKE----IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFE---TADNGQIVLDDQDVTQVPAEQ- 108
Cdd:COG0444 1 LLEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 109 -----RHVNTVFQ-SY-ALFPHMTVFENVAFGLRM-QKTPAAEIEPRVMDALRMVRL---EKMAQRKPHQLSGGQQQRIA 177
Cdd:COG0444 81 rkirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 178 IARAVVNKPKVLLLDESLSALDykLRKQMQI--ELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDG-VIEQdGSPRE 254
Cdd:COG0444 161 IARALALEPKLLIADEPTTALD--VTIQAQIlnLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGrIVEE-GPVEE 237
|
....*.
gi 2127793354 255 IYEEPK 260
Cdd:COG0444 238 LFENPR 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
39-255 |
7.19e-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: 175.70 E-value: 7.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 39 RLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRH---VNTVF 115
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 116 QSYALFPHMTVFENVAFGLRMQKTPA----------AEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNK 185
Cdd:cd03219 82 QIPRLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 186 PKVLLLDESLSALDYKLRKQMQIELKQLqRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
57-255 |
1.49e-52 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 174.77 E-value: 1.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 57 NLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTVFQSYALFPHMTVFENVAFGLRM 136
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 137 QKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQ 216
Cdd:PRK10771 99 GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 2127793354 217 LGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:PRK10771 179 RQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
55-260 |
3.47e-52 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 182.19 E-value: 3.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADnGQIVLDDQDVTQVPAEQ-----RHVNTVFQS-YA-LFPHMTVF 127
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRMTVG 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 128 ENVAFGLRMQKTP--AAEIEPRVMDALRMVRL-EKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRK 204
Cdd:COG4172 383 QIIAEGLRVHGPGlsAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQA 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 205 QMqIEL-KQLQRQLGITFIFVTHDqeeaLS----MSDRIIVMRDG-VIEQdGSPREIYEEPK 260
Cdd:COG4172 463 QI-LDLlRDLQREHGLAYLFISHD----LAvvraLAHRVMVMKDGkVVEQ-GPTEQVFDAPQ 518
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
56-259 |
3.53e-52 |
|
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: 177.61 E-value: 3.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 56 LNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDD---QDVTQ---VPAEQRHVNTVFQSYALFPHMTVFEN 129
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgifLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 130 VAFGlrMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIE 209
Cdd:TIGR02142 96 LRYG--MKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2127793354 210 LKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEP 259
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
33-249 |
8.36e-52 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 173.71 E-value: 8.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 33 AGKPVVrLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRhvn 112
Cdd:PRK11247 9 QGTPLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 113 TVFQSYALFPHMTVFENVAFGLRMQKTPAAEieprvmDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLD 192
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 193 ESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQD 249
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
39-250 |
2.70e-51 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 169.92 E-value: 2.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 39 RLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNTVFQ 116
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 117 syalfphmtvfenvafglrmqktpaaeieprvmdALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLS 196
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 197 ALDYKlrkqMQIE----LKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDG 250
Cdd:cd03214 127 HLDIA----HQIEllelLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
36-259 |
2.77e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 171.81 E-value: 2.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQ-------VPaeQ 108
Cdd:COG1121 5 PAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRarrrigyVP--Q 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 109 RHvntvfQSYALFPhMTVFENVAFGL----RMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVN 184
Cdd:COG1121 83 RA-----EVDWDFP-ITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 185 KPKVLLLDESLSALDYKLRKQ-MQIeLKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEqDGSPREIYEEP 259
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEAlYEL-LRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVA-HGPPEEVLTPE 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
38-246 |
1.14e-50 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 167.96 E-value: 1.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE-QRHVNTVFQ 116
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 117 SYALFPHMTVFENVafglrmqktpaaeieprvmdalrmvrlekmaqrkphQLSGGQQQRIAIARAVVNKPKVLLLDESLS 196
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2127793354 197 ALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVI 246
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
57-250 |
2.98e-50 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 168.50 E-value: 2.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 57 NLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTVFQSYALFPHMTVFENVAFGLRM 136
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 137 QKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQ 216
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....
gi 2127793354 217 LGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDG 250
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
38-260 |
3.31e-50 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 169.04 E-value: 3.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQ--DVTQVPAEQ------R 109
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKairllrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 110 HVNTVFQSYALFPHMTVFEN-VAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKV 188
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127793354 189 LLLDESLSALDYKLRKQMQIELKQLQrQLGITFIFVTHDQEEALSMSDRIIVMRDG-VIEQDGSprEIYEEPK 260
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGrIIEQGDA--SHFTQPQ 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
53-281 |
1.12e-49 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 172.53 E-value: 1.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 53 IGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVP-AEQRHVN-----TVFQSYALFPHMTV 126
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdAELREVRrkkiaMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 127 FENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQM 206
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 207 QIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGEIN---VFNATMLER 281
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDisqVFSAKDIAR 281
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
55-246 |
5.04e-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: 165.27 E-value: 5.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT-----QVPAEQRHVNTVFQSYALFPHMTVFEN 129
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgrAIPYLRRKIGVVFQDFRLLPDRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 130 VAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIE 209
Cdd:cd03292 99 VAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNL 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 2127793354 210 LKQLQrQLGITFIFVTHDQEEALSMSDRIIVMRDGVI 246
Cdd:cd03292 179 LKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
55-193 |
7.83e-49 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 162.43 E-value: 7.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQ--VPAEQRHVNTVFQSYALFPHMTVFENVAF 132
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENLRL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127793354 133 GLRMQKTPAAEIEPRVMDALRMVRLEKMAQRK----PHQLSGGQQQRIAIARAVVNKPKVLLLDE 193
Cdd:pfam00005 83 GLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
36-243 |
3.39e-48 |
|
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: 162.65 E-value: 3.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE-QRHVNTV 114
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 115 FQSYALFPHMTVFENVAFGLRMQKTPAAEIepRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 195 LSALDyklrKQMQIELKQL---QRQLGITFIFVTHDQEEALsmSDRIIVMRD 243
Cdd:COG4133 159 FTALD----AAGVALLAELiaaHLARGGAVLLTTHQPLELA--AARVLDLGD 204
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
38-248 |
2.70e-47 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 161.72 E-value: 2.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQ--DVTQVPAEQ------R 109
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKairelrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 110 HVNTVFQSYALFPHMTVFEN-VAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKV 188
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 189 LLLDESLSALDYKLRKQMQIELKQLQrQLGITFIFVTHDQEEALSMSDRIIVMRDG-VIEQ 248
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGhIVEQ 222
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
32-268 |
4.36e-47 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 161.51 E-value: 4.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 32 QAGKPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT--------Q 103
Cdd:COG4598 3 DTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgeL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 104 VPAEQRHVNT-------VFQSYALFPHMTVFENVAFG-LRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQR 175
Cdd:COG4598 83 VPADRRQLQRirtrlgmVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 176 IAIARAVVNKPKVLLLDESLSALDyklrKQMQIELKQLQRQL---GITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSP 252
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALD----PELVGEVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPP 238
|
250
....*....|....*.
gi 2127793354 253 REIYEEPKNLFVARFI 268
Cdd:COG4598 239 AEVFGNPKSERLRQFL 254
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
35-257 |
5.67e-47 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 161.72 E-value: 5.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 35 KPVVRLSGISKSFDGKE--IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQI-----VLDDQDVTQVpae 107
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItvggmVLSEETVWDV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 108 QRHVNTVFQSY-ALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKP 186
Cdd:PRK13635 80 RRQVGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 187 KVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSmSDRIIVMRDGVIEQDGSPREIYE 257
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
28-261 |
2.28e-46 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 159.43 E-value: 2.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 28 NAKQQAGKPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLR-------MIAGFETadNGQIVLDDQD 100
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 101 V----TQVPAEQRHVNTVFQSYALFPhMTVFENVAFGLRMQ-KTPAAEIEPRVMDALRMV--------RLEKMAQRkphq 167
Cdd:COG1117 80 IydpdVDVVELRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHgIKSKSELDEIVEESLRKAalwdevkdRLKKSALG---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 168 LSGGQQQRIAIARAVVNKPKVLLLDESLSALD-----------YKLRKQMQIelkqlqrqlgitfIFVTHDQEEALSMSD 236
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistakieeliLELKKDYTI-------------VIVTHNMQQAARVSD 221
|
250 260
....*....|....*....|....*
gi 2127793354 237 RIIVMRDGVIEQDGSPREIYEEPKN 261
Cdd:COG1117 222 YTAFFYLGELVEFGPTEQIFTNPKD 246
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
38-244 |
2.77e-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: 156.39 E-value: 2.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDG--KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE--QRHVNT 113
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEslRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 114 VFQSYALFpHMTVFENVafglrmqktpaaeieprvmdalrmvrlekmaqrkphqLSGGQQQRIAIARAVVNKPKVLLLDE 193
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 194 SLSALDYKLRKQMQIELKQLQRqlGITFIFVTHDqEEALSMSDRIIVMRDG 244
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
38-269 |
6.06e-46 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 158.37 E-value: 6.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDD----------QDVTQVPAE 107
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslsQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 108 QRHVNTVFQSYALFPHMTVFENVAFG-LRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKP 186
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 187 KVLLLDESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKN----L 262
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQprtrQ 242
|
....*..
gi 2127793354 263 FVARFIG 269
Cdd:PRK11264 243 FLEKFLL 249
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
36-259 |
6.49e-46 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 165.71 E-value: 6.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDG--KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHV 111
Cdd:COG4987 332 PSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 112 NTVFQSYALFpHMTVFENvafgLRMQKtPAAEiEPRVMDALRMVRLEKMAQRKPH-----------QLSGGQQQRIAIAR 180
Cdd:COG4987 412 AVVPQRPHLF-DTTLREN----LRLAR-PDAT-DEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 181 AVVNKPKVLLLDESLSALDYKLRKQMqieLKQLQRQL-GITFIFVTHDqEEALSMSDRIIVMRDGVIEQDGSPREIYEEP 259
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQAL---LADLLEALaGRTVLLITHR-LAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
39-244 |
1.23e-45 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 154.32 E-value: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 39 RLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNTVFQ 116
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 117 syalfphmtvfenvafglrmqktpaaeieprvmdalrmvrlekmaqrkphqLSGGQQQRIAIARAVVNKPKVLLLDESLS 196
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2127793354 197 ALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDG 244
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
48-254 |
3.69e-45 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 163.80 E-value: 3.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNTVFQSYALFpHMT 125
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 126 VFENVAFGLrmqktPAAEIEpRVMDALRMVRLEKMAQRKPH-----------QLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:COG1132 430 IRENIRYGR-----PDATDE-EVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127793354 195 LSALDYKLRKQMQIELKQLQRqlGITFIFVTHDqeeaLS---MSDRIIVMRDGVIEQDGSPRE 254
Cdd:COG1132 504 TSALDTETEALIQEALERLMK--GRTTIVIAHR----LStirNADRILVLDDGRIVEQGTHEE 560
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
55-256 |
5.57e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 156.82 E-value: 5.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQ--VPAEQRHVNTVFQSY-ALFPHMTVFENVA 131
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenVWDIRHKIGMVFQNPdNQFVGATVEDDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 132 FGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELK 211
Cdd:PRK13650 105 FGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2127793354 212 QLQRQLGITFIFVTHDQEEaLSMSDRIIVMRDGVIEQDGSPREIY 256
Cdd:PRK13650 185 GIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
39-246 |
5.64e-45 |
|
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: 154.61 E-value: 5.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 39 RLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQvpaEQRHVNTVFQSY 118
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---ERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 119 AL---FPhMTVFENVAFGL----RMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLL 191
Cdd:cd03235 78 SIdrdFP-ISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2127793354 192 DESLSALDYKLRKQMQIELKQLqRQLGITFIFVTHDQEEALSMSDRIIVMRDGVI 246
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
33-258 |
2.49e-44 |
|
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: 161.46 E-value: 2.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 33 AGKPVVRLSGISKSF-DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE--QR 109
Cdd:COG4988 332 AGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 110 HVNTVFQSYALFpHMTVFENVAFGlrmqkTPAAEIEpRVMDALRMVRLEKMAQRKPH-----------QLSGGQQQRIAI 178
Cdd:COG4988 412 QIAWVPQNPYLF-AGTIRENLRLG-----RPDASDE-ELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 179 ARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRqlGITFIFVTHDQEEALSMsDRIIVMRDGVIEQDGSPREIYEE 258
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEELLAK 561
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
50-258 |
1.54e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 153.28 E-value: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE----QRHVNTVFQ--SYALFPH 123
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdiRKKVGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 124 mTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRL--EKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYK 201
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 202 LRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEE 258
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
38-260 |
1.95e-43 |
|
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: 151.16 E-value: 1.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRH---VNTV 114
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRArlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 115 FQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 195 LSALDYKLRKQMQIELKQLqRQLGITfIFVT-HDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPK 260
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKIL-KDRGIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
38-266 |
4.64e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 151.01 E-value: 4.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSF-----DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQR--H 110
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 111 VNTVFQSYAL--FPHMTVFENVA--------FGLRMQKTpAAEIEpRVMDALRMVR--LEKMAQRKPHQLSGGQQQRIAI 178
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGLT-KKRRE-LFRELLATLGlgLENRLDTKVGLLSGGQRQALSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 179 ARAVVNKPKVLLLDESLSALDYKlRKQMQIEL-KQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPreiyE 257
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVSG----E 234
|
....*....
gi 2127793354 258 EPKNLFVAR 266
Cdd:COG1101 235 EKKKLTVED 243
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
39-255 |
9.97e-43 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 148.74 E-value: 9.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 39 RLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRH---VNTVF 115
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 116 QSYALFPHMTVFENVAFGLRMQKtpAAEIEPRVMDALRMV-RLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:cd03224 82 EGRRIFPELTVEENLLLGAYARR--RAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 195 LSALDYKLRKQMQIELKQLqRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:cd03224 160 SEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
36-268 |
2.85e-42 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 149.22 E-value: 2.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDGK---------EIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPA 106
Cdd:COG4167 3 ALLEVRNLSKTFKYRtglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 107 EQR--HVNTVFQ--SYALFPHMTVFENVAFGLRMQ-KTPAAEIEPRVMDALRMVRL-EKMAQRKPHQLSGGQQQRIAIAR 180
Cdd:COG4167 83 KYRckHIRMIFQdpNTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 181 AVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDG-VIEQdGSPREIYEEP 259
Cdd:COG4167 163 ALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGeVVEY-GKTAEVFANP 241
|
....*....
gi 2127793354 260 KNLFVARFI 268
Cdd:COG4167 242 QHEVTKRLI 250
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
41-254 |
3.25e-42 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 148.73 E-value: 3.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 41 SGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQR-HVNTVF-QSY 118
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELaRRRAVLpQHS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 119 AL-FPhMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARA-------VVNKPKVLL 190
Cdd:COG4559 85 SLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVlaqlwepVDGGPRWLF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 191 LDESLSALDykLRKQ---MQIeLKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPRE 254
Cdd:COG4559 164 LDEPTSALD--LAHQhavLRL-ARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
50-248 |
3.19e-41 |
|
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: 146.49 E-value: 3.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ-----RHVNTVFQ-SYALF-P 122
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQdSPSAVnP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 123 HMTVFENVAFGLR-MQKTPAAEIEPRVMDALRMVRLE-KMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDY 200
Cdd:TIGR02769 104 RMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2127793354 201 KLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDG-VIEQ 248
Cdd:TIGR02769 184 VLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGqIVEE 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
38-250 |
4.03e-41 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 144.65 E-value: 4.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEI--IGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQV-PAE-QRHVNT 113
Cdd:cd03245 3 IEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLdPADlRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 114 VFQSYALFpHMTVFENVAFGLrmqktPAAEIEpRVMDALRMVRLEKMAQRKPH-----------QLSGGQQQRIAIARAV 182
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLGA-----PLADDE-RILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 183 VNKPKVLLLDESLSALDYKLRKQMQIELKQLQRqlGITFIFVTHDQeEALSMSDRIIVMRDGVIEQDG 250
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
45-260 |
4.27e-41 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 147.93 E-value: 4.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 45 KSFDGkeiignLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRH-----VNTVFQS-- 117
Cdd:PRK15079 35 KAVDG------VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavrsdIQMIFQDpl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 YALFPHMTVFENVAFGLRM--QKTPAAEIEPRVMDALRMVRL-EKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:PRK15079 109 ASLNPRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 195 LSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPK 260
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
36-254 |
7.25e-41 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 145.30 E-value: 7.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNT 113
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 114 VFQSYAL-FPhMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVV------NKP 186
Cdd:PRK13548 81 LPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 187 KVLLLDESLSALDykLRKQ---MQIeLKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPRE 254
Cdd:PRK13548 160 RWLLLDEPTSALD--LAHQhhvLRL-ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
41-255 |
9.67e-41 |
|
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: 143.66 E-value: 9.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 41 SGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE-QRHVNTVFQSYA 119
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 120 LFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALD 199
Cdd:cd03265 84 VDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 200 YKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
39-260 |
1.74e-40 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 143.63 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 39 RLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTVfqSY 118
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGI--GY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 119 -----ALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDE 193
Cdd:COG1137 83 lpqeaSIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2127793354 194 SLSALDYKLRKQMQIELKQL-QRQLGitfIFVT-HDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPK 260
Cdd:COG1137 163 PFAGVDPIAVADIQKIIRHLkERGIG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
38-255 |
3.51e-40 |
|
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: 142.26 E-value: 3.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKE--IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDV-TQVPAEQRHVNTV 114
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 115 FQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 195 LSALDYKLRKQMQIELKQLQRQLgiTFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
50-249 |
4.79e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 143.29 E-value: 4.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ-----RHVNTVFQSY--ALFP 122
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrRDIQMVFQDSisAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 123 HMTVFENVAFGLR-MQKTPAAEIEPRVMDALRMVRL-EKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDY 200
Cdd:PRK10419 105 RKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2127793354 201 KLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQD 249
Cdd:PRK10419 185 VLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
40-250 |
6.28e-40 |
|
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: 141.18 E-value: 6.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 40 LSGISKSFDGKEIIGNLNLDVNHGeFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE-QRHVNTVFQSY 118
Cdd:cd03264 3 LENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlRRRIGYLPQEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 119 ALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSAL 198
Cdd:cd03264 82 GVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 199 DYKLRkqmqIELKQLQRQLG--ITFIFVTHDQEEALSMSDRIIVMRDGVIEQDG 250
Cdd:cd03264 162 DPEER----IRFRNLLSELGedRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
35-259 |
1.67e-39 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 141.67 E-value: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 35 KPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RH-- 110
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiaRMgv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 111 VNTvFQSYALFPHMTVFEN--VAFGLRMQ--------KTPA---AEIEP--RVMDALRMVRLEKMAQRKPHQLSGGQQQR 175
Cdd:PRK11300 83 VRT-FQHVRLFREMTVIENllVAQHQQLKtglfsgllKTPAfrrAESEAldRAATWLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 176 IAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
....
gi 2127793354 256 YEEP 259
Cdd:PRK11300 242 RNNP 245
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
36-255 |
2.10e-39 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 140.99 E-value: 2.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAG--FETADNGQIVLDDQ----DVTQVPAEQR 109
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdlPPTYGNDVRLFGERrggeDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 110 HVNTVFQSYaLFPHMTVFENVAFGL-----RMQKTPAAEIEpRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVN 184
Cdd:COG1119 82 LVSPALQLR-FPRDETVLDVVLSGFfdsigLYREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 185 KPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
38-246 |
5.90e-39 |
|
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: 137.17 E-value: 5.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTqvpaeqrhvntvfqs 117
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 yalfphmtvFENVAfglrmqktpaaeieprvmDALR----MVrlekmaqrkpHQLSGGQQQRIAIARAVVNKPKVLLLDE 193
Cdd:cd03216 66 ---------FASPR------------------DARRagiaMV----------YQLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2127793354 194 SLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVI 246
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
36-260 |
8.48e-39 |
|
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: 138.96 E-value: 8.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQR------ 109
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlgig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 110 HVNtvfQSYALFPHMTVFEN---VAFGLRMQKTPAAEIEpRVMDalRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKP 186
Cdd:COG0410 82 YVP---EGRRIFPSLTVEENlllGAYARRDRAEVRADLE-RVYE--LFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 187 KVLLLDESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPK 260
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
38-246 |
1.02e-38 |
|
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: 137.73 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTVFQS 117
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 YALFPHMTVFENVAFGLRMQKTPaaeiEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSA 197
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2127793354 198 LDYKLRKQMQiELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVI 246
Cdd:cd03268 157 LDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
38-250 |
2.13e-38 |
|
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: 137.50 E-value: 2.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKE----IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE-QRHVN 112
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEaRRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 113 TVFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLD 192
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 193 ESLSALDYkLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDG 250
Cdd:cd03266 162 EPTTGLDV-MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
33-260 |
2.27e-38 |
|
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: 144.44 E-value: 2.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 33 AGKPVVRLSGISKSFDG----KEIIGNLNLDVNHGEFLTILGPSGCGKT----TVLRMIAGFETADNGQIVLDDQDVTQV 104
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 105 PAEQ------RHVNTVFQ--SYALFPHMTVFENVAFGLRM-QKTPAAEIEPRVMDALRMVRL---EKMAQRKPHQLSGGQ 172
Cdd:COG4172 82 SERElrrirgNRIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 173 QQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDqeeaLS----MSDRIIVMRDGVIEQ 248
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVE 237
|
250
....*....|..
gi 2127793354 249 DGSPREIYEEPK 260
Cdd:COG4172 238 QGPTAELFAAPQ 249
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
35-283 |
3.44e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 138.59 E-value: 3.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 35 KPVVRLSGISKSFDGKE--IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQ--VPAEQRH 110
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 111 VNTVFQSY-ALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVL 189
Cdd:PRK13632 85 IGIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 190 LLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALsMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVAR--- 266
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEILEKAKids 243
|
250
....*....|....*...
gi 2127793354 267 -FIGEInvfnATMLERID 283
Cdd:PRK13632 244 pFIYKL----SKKLKGID 257
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
51-258 |
4.07e-38 |
|
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: 137.29 E-value: 4.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 51 EIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNTVFQSYALFPhMTVFE 128
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 129 NVAFGlrmqKTPAAEIEprVMDALRMVRLEKMAQRKPH-----------QLSGGQQQRIAIARAVVNKPKVLLLDESLSA 197
Cdd:cd03249 96 NIRYG----KPDATDEE--VEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 198 LDYKLRKQMQIELKQLQRqlGITFIFVTHdqeeALSM---SDRIIVMRDGVIEQDGSPREIYEE 258
Cdd:cd03249 170 LDAESEKLVQEALDRAMK--GRTTIVIAH----RLSTirnADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
35-244 |
4.49e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 143.24 E-value: 4.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 35 KPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQ---VPAEQRHV 111
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFrspRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 112 NTVFQSYALFPHMTVFENVAFGlRMQKTPA----AEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPK 187
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLG-REPRRGGlidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 188 VLLLDESLSALDyklrkQMQIE-----LKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDG 244
Cdd:COG1129 161 VLILDEPTASLT-----EREVErlfriIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDG 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
32-259 |
4.94e-38 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 137.97 E-value: 4.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 32 QAGKPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDV-----TQVPA 106
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 107 EQRHVNTVFQSYALFPHMTVFENVAFGLRMQ-KTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNK 185
Cdd:PRK11831 82 VRKRMSMLFQSGALFTDMNVFDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 186 PKVLLLDESLSALDyklRKQMQIELK---QLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEP 259
Cdd:PRK11831 162 PDLIMFDEPFVGQD---PITMGVLVKlisELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
48-257 |
1.12e-37 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 135.82 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNTVFQSYALFpHMT 125
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 126 VFENVAFGlrmqkTPAAEIEpRVMDALRMVRLEKMAQRKPH-----------QLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:cd03251 92 VAENIAYG-----RPGATRE-EVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 195 LSALDYKLRKQMQIELKQLQRqlGITFIFVTHdqeeALSM---SDRIIVMRDGVIEQDGSPREIYE 257
Cdd:cd03251 166 TSALDTESERLVQAALERLMK--NRTTFVIAH----RLSTienADRIVVLEDGKIVERGTHEELLA 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
35-249 |
1.63e-37 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 135.71 E-value: 1.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 35 KPVVRLSGISKSF-DGK---EIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPA---- 106
Cdd:PRK11629 3 KILLQCDNLCKRYqEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaaka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 107 --EQRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVN 184
Cdd:PRK11629 83 elRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127793354 185 KPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSdRIIVMRDGVIEQD 249
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
48-262 |
2.08e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 136.36 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLD----DQDVTQVPAEQRHVNTVFQSY--ALF 121
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepiKYDKKSLLEVRKTVGIVFQNPddQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 122 PHmTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYK 201
Cdd:PRK13639 93 AP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 202 LRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNL 262
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
36-306 |
5.55e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 136.09 E-value: 5.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDV-TQVPAEQRHVNTV 114
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 115 FQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 195 LSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGEINVF 274
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCDVIEIYGPDPVA 244
|
250 260 270
....*....|....*....|....*....|..
gi 2127793354 275 NATMLERIDEkriRAEIEGvESVVYYDREAQP 306
Cdd:PRK13537 245 LRDELAPLAE---RTEISG-ETLFCYVRDPEP 272
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
48-259 |
6.28e-37 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 142.02 E-value: 6.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT--QVPAEQRHVNTVFQSYALFPHmT 125
Cdd:TIGR03797 464 DGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAglDVQAVRRQLGVVLQNGRLMSG-S 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 126 VFENVAFGLRMqkTPaaeiePRVMDALRMVRLEKMAQRKP---H--------QLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:TIGR03797 543 IFENIAGGAPL--TL-----DEAWEAARMAGLAEDIRAMPmgmHtvisegggTLSGGQRQRLLIARALVRKPRILLFDEA 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 195 LSALDYKlrkqMQIELKQLQRQLGITFIFVTHdqeeALSM---SDRIIVMRDGVIEQDGSPREIYEEP 259
Cdd:TIGR03797 616 TSALDNR----TQAIVSESLERLKVTRIVIAH----RLSTirnADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
50-258 |
1.07e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 134.83 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT---QVPAEQRHVNTVFQSyalfPH--- 123
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeeNLWDIRNKAGMVFQN----PDnqi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 124 --MTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYK 201
Cdd:PRK13633 99 vaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 202 LRKQMQIELKQLQRQLGITFIFVTHDQEEALSmSDRIIVMRDGVIEQDGSPREIYEE 258
Cdd:PRK13633 179 GRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
43-268 |
1.41e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 133.94 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 43 ISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT---------------QVPAE 107
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadknQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 108 QRHVNTVFQSYALFPHMTVFENVAFG----LRMQKTPAAEiepRVMDALRMVRLEKMAQRK-PHQLSGGQQQRIAIARAV 182
Cdd:PRK10619 91 RTRLTMVFQHFNLWSHMTVLENVMEApiqvLGLSKQEARE---RAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 183 VNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNL 262
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
....*.
gi 2127793354 263 FVARFI 268
Cdd:PRK10619 247 RLQQFL 252
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
54-259 |
2.31e-36 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 135.77 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 54 GNLNLDVNH---GEFLT-ILGPSGCGKTTVLRMIAGFETADNGQIVLDDQ---DVTQ---VPAEQRHVNTVFQSYALFPH 123
Cdd:PRK11144 11 GDLCLTVNLtlpAQGITaIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgicLPPEKRRIGYVFQDARLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 124 MTVFENVAFGlrMQKTPAAEIEprvmDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLR 203
Cdd:PRK11144 91 YKVRGNLRYG--MAKSMVAQFD----KIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 204 KQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEP 259
Cdd:PRK11144 165 RELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
52-255 |
3.88e-36 |
|
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: 138.73 E-value: 3.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 52 IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNTVFQSYALFPHmTVFEN 129
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 130 VAfglRMQKTPAAEIEprvmDALRMVRLEKMAQRKP-----------HQLSGGQQQRIAIARAVVNKPKVLLLDESLSAL 198
Cdd:COG4618 426 IA---RFGDADPEKVV----AAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 199 DYKLRKQMQIELKQLqRQLGITFIFVTHDQeEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:COG4618 499 DDEGEAALAAAIRAL-KARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
38-258 |
4.12e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 134.96 E-value: 4.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQI-VLDDQDVTQVPAEQRHVNTVFQ 116
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 117 SYALFPHMTVFEN-VAFGlRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESL 195
Cdd:PRK13536 122 FDNLDLEFTVRENlLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127793354 196 SALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEE 258
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
48-255 |
4.63e-36 |
|
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: 139.49 E-value: 4.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQV-PAE-QRHVNTVFQSYALFPHmT 125
Cdd:TIGR01846 468 DSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIAdPAWlRRQMGVVLQENVLFSR-S 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 126 VFENVAFGlrmqkTPAAEIEpRVMDALRMVRLEKMAQRKPH-----------QLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:TIGR01846 547 IRDNIALC-----NPGAPFE-HVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFDEA 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 195 LSALDYKLRKQMQIELKQLQRqlGITFIFVTHdQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:TIGR01846 621 TSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
63-262 |
1.11e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 131.80 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 63 GEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE--QRHVNTVFQS-YALFPHMTVFENVAFGLRMQKT 139
Cdd:PRK13648 35 GQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEklRKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 140 PAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGI 219
Cdd:PRK13648 115 PYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNI 194
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2127793354 220 TFIFVTHDQEEALSmSDRIIVMRDGVIEQDGSPREIYEEPKNL 262
Cdd:PRK13648 195 TIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
39-246 |
1.42e-35 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 129.68 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 39 RLSGISKSF-DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQvPAEQRHVNTVFQS 117
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 --YALFPHmTVFENVAFGLRmqktPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESL 195
Cdd:cd03226 80 vdYQLFTD-SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 196 SALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVI 246
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
35-241 |
1.56e-35 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 130.22 E-value: 1.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 35 KPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVN 112
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 113 TVFQSYALFPHmTVFENVAFGLRM-QKTPaaeiEPRVM--DALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVL 189
Cdd:PRK10247 85 YCAQTPTLFGD-TVYDNLIFPWQIrNQQP----DPAIFldDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 190 LLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEaLSMSDRIIVM 241
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
37-259 |
1.64e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 131.65 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSF-DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIV---LDDQDVTQVPAEQRHVN 112
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 113 TVFQS-YALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLL 191
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 192 DESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEaLSMSDRIIVMRDGVIEQDGSPREIYEEP 259
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
38-254 |
1.04e-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: 128.11 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKE-IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNTV 114
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 115 FQSYALFPHmTVFENVAFGlrmqkTPAAEIEpRVMDALRMVRLEKMAQRKP-----------HQLSGGQQQRIAIARAVV 183
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLG-----RPNATDE-EVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 184 NKPKVLLLDESLSALDYKLRKQMQIELKQLQRqlGITFIFVTHdqeeALSM---SDRIIVMRDGVIEQDGSPRE 254
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH----RLSTiknADKILVLDDGKIIEEGTHDE 223
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
39-251 |
1.74e-34 |
|
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: 127.26 E-value: 1.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 39 RLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQR---HVNTVF 115
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 116 QSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDaLRMVrLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESL 195
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYE-LFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 196 SALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGS 251
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
63-260 |
2.06e-34 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 129.70 E-value: 2.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 63 GEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRH-----VNTVFQS-YA-LFPHMTVFENVAFGLR 135
Cdd:PRK11308 41 GKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllrqkIQIVFQNpYGsLNPRKKVGQILEEPLL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 136 MQKT-PAAEIEPRVMDALRMVRLE-KMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQL 213
Cdd:PRK11308 121 INTSlSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDL 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 214 QRQLGITFIFVTHDqeeaLS----MSDRIIVMRDG-VIEQdGSPREIYEEPK 260
Cdd:PRK11308 201 QQELGLSYVFISHD----LSvvehIADEVMVMYLGrCVEK-GTKEQIFNNPR 247
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
37-244 |
1.11e-33 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 124.99 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSF-DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT-----QVPAEQRH 110
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 111 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLL 190
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 191 LDESLSALDYKLRKQMQIELKQLQRqLGITFIFVTHDQEEALSMSDRIIVMRDG 244
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
37-268 |
1.45e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 125.41 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGF-----ETADNGQIVLDDQDVTQVPAEQ--R 109
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIElrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 110 HVNTVFQSYALFPHMTVFENVAFGLRMQK--TPAAEIEPRVMDALRMVRL-EKMAQR---KPHQLSGGQQQRIAIARAVV 183
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 184 NKPKVLLLDESLSALDYKlrKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLF 263
Cdd:PRK14247 163 FQPEVLLADEPTANLDPE--NTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHEL 240
|
....*
gi 2127793354 264 VARFI 268
Cdd:PRK14247 241 TEKYV 245
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
48-255 |
1.62e-33 |
|
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: 124.91 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE--QRHVNTVFQSYALFpHMT 125
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 126 VFENVAFGlrmqkTPAAEIEpRVMDALRMVRLEKMAQRKPH-----------QLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:cd03252 92 IRDNIALA-----DPGMSME-RVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 195 LSALDYKLRKQMQIELKQLQRqlGITFIFVTHdQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
37-260 |
1.71e-33 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 125.08 E-value: 1.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRH---VNT 113
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERArlgIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 114 VFQSYALFPHMTVFENVAFGL-RMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLD 192
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 193 ESLSALDYKLRKQMQIELKQLqRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPK 260
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
50-262 |
1.90e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 126.07 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGF---ETADNGQIVLDDQDVTQ--VPAEQRHVNTVFQSY-ALFPH 123
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAktVWDIREKVGIVFQNPdNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 124 MTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLR 203
Cdd:PRK13640 100 ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2127793354 204 KQMQIELKQLQRQLGITFIFVTHDQEEAlSMSDRIIVMRDGVIEQDGSPREIYEEPKNL 262
Cdd:PRK13640 180 EQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEML 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
36-263 |
2.67e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 130.60 E-value: 2.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSF-----------DGKEIIGNLNLDVNHGEFLTILGPSGCGKTT----VLRMIAGfetadNGQIVLDDQD 100
Cdd:PRK15134 274 PLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 101 VTQVPAEQ-----RHVNTVFQ--SYALFPHMTVFENVAFGLRM-QKT-PAAEIEPRVMDALRMVRLEKMA-QRKPHQLSG 170
Cdd:PRK15134 349 LHNLNRRQllpvrHRIQVVFQdpNSSLNPRLNVLQIIEEGLRVhQPTlSAAQREQQVIAVMEEVGLDPETrHRYPAEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 171 GQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDG-VIEQd 249
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGeVVEQ- 507
|
250
....*....|....
gi 2127793354 250 GSPREIYEEPKNLF 263
Cdd:PRK15134 508 GDCERVFAAPQQEY 521
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
48-255 |
2.96e-33 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 130.61 E-value: 2.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE--QRHVNTVFQSYALFPHmT 125
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAslRRQVALVSQDVVLFND-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 126 VFENVAFGlRMQKTPAAEIEprvmDALRMVRLEKMAQRKP---HQ--------LSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:TIGR02203 422 IANNIAYG-RTEQADRAEIE----RALAAAYAQDFVDKLPlglDTpigengvlLSGGQRQRLAIARALLKDAPILILDEA 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 195 LSALDYKLRKQMQIELKQLQRqlGITFIFVTHdQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:TIGR02203 497 TSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
40-314 |
3.45e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 125.61 E-value: 3.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 40 LSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPA-------EQRhvn 112
Cdd:COG4152 4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRrrigylpEER--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 113 tvfqsyALFPHMTVFENVAF-----GLrmqktPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPK 187
Cdd:COG4152 81 ------GLYPKMKVGEQLVYlarlkGL-----SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 188 VLLLDESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEE-PKNLFVAR 266
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQfGRNTLRLE 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2127793354 267 FIGeinvfNATMLERIDEKRiRAEIEGVESVVYYDREAQPGDKLQVLL 314
Cdd:COG4152 229 ADG-----DAGWLRALPGVT-VVEEDGDGAELKLEDGADAQELLRALL 270
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
33-244 |
4.69e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 129.38 E-value: 4.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 33 AGKPVVRLSGISKSFDGkeIIGN--LNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQV-PAE-- 107
Cdd:COG3845 1 MMPPALELRGITKRFGG--VVANddVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRsPRDai 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 108 QRHVNTVFQSYALFPHMTVFENVAFGLrmqktpaaeiEPRVMDALRMVRLEKMAQ-------------RKPHQLSGGQQQ 174
Cdd:COG3845 79 ALGIGMVHQHFMLVPNLTVAENIVLGL----------EPTKGGRLDRKAARARIRelserygldvdpdAKVEDLSVGEQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127793354 175 RIAIARAVVNKPKVLLLDESLSAL-----DyKLrkqMQIeLKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDG 244
Cdd:COG3845 149 RVEILKALYRGARILILDEPTAVLtpqeaD-EL---FEI-LRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
37-258 |
4.89e-33 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 124.35 E-value: 4.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADN---------GQIVLDDQDVTQVPAE 107
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 108 QR-HVNTVFQSYALFPHMTVFENVAFGlRMQKTP---------AAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIA 177
Cdd:PRK09984 84 SRaNTGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 178 IARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYE 257
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDN 242
|
.
gi 2127793354 258 E 258
Cdd:PRK09984 243 E 243
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
55-262 |
4.99e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 125.13 E-value: 4.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT------QVPAEQRHVNTVFQsyalFPHMTVFE 128
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQ----FPEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 129 -----NVAFGLRMQKTPAAEIEPRVMDALRMVRL-EKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKL 202
Cdd:PRK13634 101 etvekDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 203 RKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNL 262
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEL 240
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
36-241 |
5.30e-33 |
|
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: 129.71 E-value: 5.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDGK-EIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE--QRHVN 112
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 113 TVFQSYALFPHmTVFENVAFGLRMQktPAAEIEPRVMDA--LRMVR-----LEKMAQRKPHQLSGGQQQRIAIARAVVNK 185
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLARPDA--SDAEIREALERAglDEFVAalpqgLDTPIGEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 186 PKVLLLDESLSALDYKLRKQMQIELKQLQRqlGITFIFVTHDQEEALSMsDRIIVM 241
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
48-244 |
9.23e-33 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 129.16 E-value: 9.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVL-DDQDVTQVPaeQRhvntvfqSYalFPHMTV 126
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLP--QR-------PY--LPLGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 127 FENVAFGLRMQKTPAAEIEprvmDALRMVRLEKMAQR------KPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDY 200
Cdd:COG4178 443 REALLYPATAEAFSDAELR----EALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2127793354 201 KLRKQMqieLKQLQRQL-GITFIFVTHdQEEALSMSDRIIVMRDG 244
Cdd:COG4178 519 ENEAAL---YQLLREELpGTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
38-246 |
1.50e-32 |
|
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: 121.62 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTqvPAEQRHVNTVFQS 117
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD--IAARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 YALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSA 197
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2127793354 198 LDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVI 246
Cdd:cd03269 159 LDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
39-246 |
1.88e-32 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 120.01 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 39 RLSGISKSFDGKE--IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNTV 114
Cdd:cd03246 2 EVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 115 FQSYALFPHmTVFENVafglrmqktpaaeieprvmdalrmvrlekmaqrkphqLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:cd03246 82 PQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 195 LSALDYKLRKQMQIELKQLQRQlGITFIFVTHdQEEALSMSDRIIVMRDGVI 246
Cdd:cd03246 124 NSHLDVEGERALNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
48-253 |
2.82e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 122.92 E-value: 2.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE--QRHVNTVFQSY--ALFPh 123
Cdd:PRK13647 16 DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvRSKVGLVFQDPddQVFS- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 124 MTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLR 203
Cdd:PRK13647 95 STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2127793354 204 KQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPR 253
Cdd:PRK13647 175 ETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
48-254 |
3.93e-32 |
|
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: 121.18 E-value: 3.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQV--PAEQRHVNTVFQSYALFpHMT 125
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtlDSLRRAIGVVPQDTVLF-NDT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 126 VFENVAFGlrmqKTPAAEIEprVMDALRMVRLEKMAQRKPHQ-----------LSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:cd03253 91 IGYNIRYG----RPDATDEE--VIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 195 LSALDYKLRKQMQIELKQLQRqlGITFIFVTHDQEEALSmSDRIIVMRDGVIEQDGSPRE 254
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
23-262 |
1.05e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 121.35 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 23 EIQTLNAKQQAGKPVVRLSGISKSfdgkeiignlnldVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT 102
Cdd:PRK13642 6 EVENLVFKYEKESDVNQLNGVSFS-------------ITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 103 --QVPAEQRHVNTVFQSY-ALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIA 179
Cdd:PRK13642 73 aeNVWNLRRKIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 180 RAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSmSDRIIVMRDGVIEQDGSPREIYEEP 259
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATS 231
|
...
gi 2127793354 260 KNL 262
Cdd:PRK13642 232 EDM 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
36-254 |
1.27e-31 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 126.38 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDGKE----IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--- 108
Cdd:PRK10535 3 ALLELKDIRRSYPSGEeqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 109 ---RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNK 185
Cdd:PRK10535 83 lrrEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2127793354 186 PKVLLLDESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEAlSMSDRIIVMRDGVIEQDGSPRE 254
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEIVRNPPAQE 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
51-268 |
3.37e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 119.18 E-value: 3.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 51 EIIGNLNLDVNHGEFLTILGPSGCGKTTVLR----MIAGFETAD-NGQIVLDDQDVTQV---PAE-QRHVNTVFQSYALF 121
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrLLELNEEARvEGEVRLFGRNIYSPdvdPIEvRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 122 PHMTVFENVAFGLRMQK--TPAAEIEPRVMDALRMVRL-EKMAQR---KPHQLSGGQQQRIAIARAVVNKPKVLLLDESL 195
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127793354 196 SALDYKLRKQMQIELKQLQRQLgiTFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFI 268
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
55-273 |
4.54e-31 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 124.97 E-value: 4.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ-----RHVNTVFQS-YA-LFPHMTVF 127
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 128 ENVAFGLRMQKT-PAAEIEPRVMDALRMVRLE-KMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQ 205
Cdd:PRK10261 422 DSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQ 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 206 MQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFIGEINV 273
Cdd:PRK10261 502 IINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPV 569
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
48-258 |
7.06e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 119.18 E-value: 7.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDV----TQVPAEQRHVNTVFQS--YALF 121
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMKLRESVGMVFQDpdNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 122 PhMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYK 201
Cdd:PRK13636 97 S-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 202 LRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEE 258
Cdd:PRK13636 176 GVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-272 |
9.08e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 118.23 E-value: 9.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 32 QAGKPVVRLSGISKSF---DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGF-ETAD-----NGQIVLDDQDVT 102
Cdd:PRK14246 2 EAGKSAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDskikvDGKVLYFGKDIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 103 QVPA--EQRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAA-EIEPRVMDALRMVRLEKMAQRK----PHQLSGGQQQR 175
Cdd:PRK14246 82 QIDAikLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 176 IAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQlgITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
250
....*....|....*...
gi 2127793354 256 YEEPKNLFVARF-IGEIN 272
Cdd:PRK14246 240 FTSPKNELTEKYvIGRIS 257
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
35-261 |
1.03e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 117.95 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 35 KPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGF-----ETADNGQIVLDDQDV----TQVP 105
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysprTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 106 AEQRHVNTVFQSYALFPhMTVFENVAFGLRMQKTPAAEI-EPRVMDALRMVRLEKMAQRKPHQ----LSGGQQQRIAIAR 180
Cdd:PRK14239 83 DLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 181 AVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLgiTFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPK 260
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
.
gi 2127793354 261 N 261
Cdd:PRK14239 240 H 240
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
33-227 |
1.92e-30 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 122.47 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 33 AGKPVVRLSGISKSFDG-KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPA-EQRH 110
Cdd:TIGR02868 330 LGKPTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 111 VNTVF-QSYALFpHMTVFENVAFGlRMQKTPAAeieprVMDALRMVRLEKMAQRKPH-----------QLSGGQQQRIAI 178
Cdd:TIGR02868 410 RVSVCaQDAHLF-DTTVRENLRLA-RPDATDEE-----LWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2127793354 179 ARAVVNKPKVLLLDESLSALDYKLRKQMQIELkqLQRQLGITFIFVTHD 227
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-258 |
2.58e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 117.54 E-value: 2.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 23 EIQTLNAKQQAGKPvvrlsgisksFDGKEIIgNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT 102
Cdd:PRK13649 4 NLQNVSYTYQAGTP----------FEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 103 ------QVPAEQRHVNTVFQsyalFPHMTVFE-----NVAFGLRMQKTPAAEIEPRVMDALRMVRL-EKMAQRKPHQLSG 170
Cdd:PRK13649 73 stsknkDIKQIRKKVGLVFQ----FPESQLFEetvlkDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 171 GQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQrQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDG 250
Cdd:PRK13649 149 GQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
....*...
gi 2127793354 251 SPREIYEE 258
Cdd:PRK13649 228 KPKDIFQD 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-236 |
3.19e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 117.06 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGF-----ETADNGQIVLDDQDVTQ----VPA 106
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYErrvnLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 107 EQRHVNTVFQSYALFPhMTVFENVAFGLRMQK-TPAAEIEPRVMDALRMVRLEKMAQRKPHQ----LSGGQQQRIAIARA 181
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2127793354 182 VVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSD 236
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
38-262 |
4.90e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 117.49 E-value: 4.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGK-----EIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQI------------------ 94
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 95 VLDD--------QDVTQVPAEQRHVNTVFQ--SYALFpHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRL-EKMAQR 163
Cdd:PRK13651 83 VLEKlviqktrfKKIKKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 164 KPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRD 243
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250
....*....|....*....
gi 2127793354 244 GVIEQDGSPREIYEEPKNL 262
Cdd:PRK13651 241 GKIIKDGDTYDILSDNKFL 259
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
34-258 |
9.54e-30 |
|
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: 120.29 E-value: 9.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 34 GKPVVRLSGISKSFDGKE-----IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQI---VLDDQ-DVTQV 104
Cdd:TIGR03269 276 GEPIIKVRNVSKRYISVDrgvvkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrVGDEWvDMTKP 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 105 PAEQR-----HVNTVFQSYALFPHMTVFENV--AFGLRMQKtpaaeiEPRVMDA---LRMV-----RLEKMAQRKPHQLS 169
Cdd:TIGR03269 356 GPDGRgrakrYIGILHQEYDLYPHRTVLDNLteAIGLELPD------ELARMKAvitLKMVgfdeeKAEEILDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 170 GGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQD 249
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
....*....
gi 2127793354 250 GSPREIYEE 258
Cdd:TIGR03269 510 GDPEEIVEE 518
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
52-244 |
1.13e-29 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 114.49 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 52 IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQR------HVNTVFQSYALFPHMT 125
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 126 VFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQ 205
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 2127793354 206 MQIELKQLQRQLGITFIFVTHDQEEAlSMSDRIIVMRDG 244
Cdd:PRK10584 185 IADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNG 222
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
53-255 |
1.84e-29 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 119.80 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 53 IGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQV-PAEQR-HVNTVFQSYALFPHmTVFENV 130
Cdd:TIGR02204 356 LDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLdPAELRaRMALVPQDPVLFAA-SVMENI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 131 AFGlrmqkTPAAEIEpRVMDALRMVRLEKMAQRKPH-----------QLSGGQQQRIAIARAVVNKPKVLLLDESLSALD 199
Cdd:TIGR02204 435 RYG-----RPDATDE-EVEAAARAAHAHEFISALPEgydtylgergvTLSGGQRQRIAIARAILKDAPILLLDEATSALD 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 200 YKLRKQMQIELKQLQRqlGITFIFVTHDQEEALSmSDRIIVMRDGVIEQDGSPREI 255
Cdd:TIGR02204 509 AESEQLVQQALETLMK--GRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAEL 561
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
32-248 |
2.69e-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: 119.54 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 32 QAGKPVVRLSGISKSFDGK-EIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE--Q 108
Cdd:COG5265 352 VVGGGEVRFENVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 109 RHVNTVFQSYALFpHMTVFENVAFGlRMQKTPAaEIEprvmDALRMVRLEKMAQRKPHQ-----------LSGGQQQRIA 177
Cdd:COG5265 432 AAIGIVPQDTVLF-NDTIAYNIAYG-RPDASEE-EVE----AAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVA 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127793354 178 IARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRqlGITFIFVTHdqeeALSM---SDRIIVMRDG-VIEQ 248
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAH----RLSTivdADEILVLEAGrIVER 573
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
36-244 |
2.77e-29 |
|
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: 113.30 E-value: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSF-----DGKEIIG--NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQ----DVTQV 104
Cdd:COG4778 3 TLLEVENLSKTFtlhlqGGKRLPVldGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 105 PAEQ------RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRL-EKMAQRKPHQLSGGQQQRIA 177
Cdd:COG4778 83 SPREilalrrRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2127793354 178 IARAVVNKPKVLLLDESLSALDYKLRkQMQIELKQLQRQLGITFIFVTHDQE--EALsmSDRIIVMRDG 244
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANR-AVVVELIEEAKARGTAIIGIFHDEEvrEAV--ADRVVDVTPF 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
50-258 |
3.20e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.96 E-value: 3.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVntvfqsyALFP--HMT 125
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRL-------ALLPqhHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 126 -----VFENVAFGlrmqKTP--------AAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLD 192
Cdd:PRK11231 88 pegitVRELVAYG----RSPwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2127793354 193 ESLSALDYklrkQMQIELKQLQRQL---GITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEE 258
Cdd:PRK11231 164 EPTTYLDI----NHQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
35-248 |
4.65e-29 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 113.48 E-value: 4.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 35 KPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVP------AEQ 108
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalseAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 109 RHVntvFQSYALFPHmtvfENVAFGLRMQKTPAAEIEPRVMDA-------LR------MVRLEKMAQR---KPHQLSGGQ 172
Cdd:PRK11701 84 RRL---LRTEWGFVH----QHPRDGLRMQVSAGGNIGERLMAVgarhygdIRatagdwLERVEIDAARiddLPTTFSGGM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 173 QQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDG-VIEQ 248
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGrVVES 233
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
50-255 |
4.79e-29 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 118.60 E-value: 4.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNTVFQSYALFPHmTVF 127
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 128 ENVAfglRMQKTPAAEiepRVMDALRMVRLEKMAQRKPH-----------QLSGGQQQRIAIARAVVNKPKVLLLDESLS 196
Cdd:TIGR01842 410 ENIA---RFGENADPE---KIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2127793354 197 ALDYKLRKQMQIELKQLQRQlGITFIFVTHdQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:TIGR01842 484 NLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
50-259 |
5.22e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 119.06 E-value: 5.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE--QRHVNTVFQSYALFPHmTVF 127
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 128 ENVAFGLRmqKTPAAEIEPRVMDALRMVRLEKMAQ-------RKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDy 200
Cdd:TIGR00958 573 ENIAYGLT--DTPDEEIMAAAKAANAHDFIMEFPNgydtevgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD- 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2127793354 201 klrKQMQIELKQLQRQLGITFIFVTHdQEEALSMSDRIIVMRDGVIEQDGSPREIYEEP 259
Cdd:TIGR00958 650 ---AECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
50-266 |
1.20e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 112.97 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQ--VPAEQRHVNTVFQSY--ALFPhMT 125
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenIREVRKFVGLVFQNPddQIFS-PT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 126 VFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQ 205
Cdd:PRK13652 96 VEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 206 MQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVAR 266
Cdd:PRK13652 176 LIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVH 236
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-193 |
1.68e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 111.75 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 35 KPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPaEQRHVNT- 113
Cdd:COG4674 8 GPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLD-EHEIARLg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 114 ---VFQSYALFPHMTVFENVAFGLRMQKTP--------AAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAV 182
Cdd:COG4674 87 igrKFQKPTVFEELTVFENLELALKGDRGVfaslfarlTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLL 166
|
170
....*....|.
gi 2127793354 183 VNKPKVLLLDE 193
Cdd:COG4674 167 AQDPKLLLLDE 177
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
51-268 |
1.80e-28 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 112.19 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 51 EIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQR--HVNTVFQ--SYALFPHMTV 126
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRsqRIRMIFQdpSTSLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 127 FENVAFGLRMQ-KTPAAEIEPRVMDALRMVRL-EKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRK 204
Cdd:PRK15112 107 SQILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 205 QMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFI 268
Cdd:PRK15112 187 QLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLI 250
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
37-255 |
2.30e-28 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 112.00 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSG--ISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVN 112
Cdd:PRK10253 5 VARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 113 TVFQSYALFPHMTVFENVAFGlRMQKTPA-----AEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPK 187
Cdd:PRK10253 85 LLAQNATTPGDITVQELVARG-RYPHQPLftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 188 VLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
36-255 |
2.31e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 114.94 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNT 113
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 114 VFQSYALFPHMTVFENVafglRMQKTP-------AAEIEPRVMD-ALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNK 185
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVV----EMGRTPhrsrfdtWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127793354 186 PKVLLLDESLSALDYklrkQMQIELKQLQRQL---GITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:PRK09536 158 TPVLLLDEPTASLDI----NHQVRTLELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
49-268 |
5.99e-28 |
|
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: 115.99 E-value: 5.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 49 GKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ--RHVNTVFQSYALFPHmTV 126
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlrQFINYLPQEPYIFSG-SI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 127 FENvafgLRMQKTPAAEIEpRVMDALRMVRL----EKMAQ-------RKPHQLSGGQQQRIAIARAVVNKPKVLLLDESL 195
Cdd:TIGR01193 565 LEN----LLLGAKENVSQD-EIWAACEIAEIkddiENMPLgyqtelsEEGSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127793354 196 SALDYKLRKQMQIELKQLQRQlgiTFIFVTHDQEEAlSMSDRIIVMRDGVIEQDGSPREIYEEpkNLFVARFI 268
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLDR--NGFYASLI 706
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
43-255 |
9.08e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 109.60 E-value: 9.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 43 ISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRH---VNTVFQSYA 119
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArrgIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 120 LFPHMTVFENVAFGLRMQKTPAAEI-EPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSAL 198
Cdd:PRK10895 89 IFRRLSVYDNLMAVLQIRDDLSAEQrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 199 DyklrKQMQIELKQLQRQL---GITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:PRK10895 169 D----PISVIDIKRIIEHLrdsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
50-246 |
2.57e-27 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 108.13 E-value: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETAD---NGQIVLDDQDVTqvPAE-QRHVNTVFQSYALFPHMT 125
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRK--PDQfQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 126 VFENVAFG--LRMQ-KTPAAEIEPRVMD-ALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYK 201
Cdd:cd03234 98 VRETLTYTaiLRLPrKSSDAIRKKRVEDvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2127793354 202 LRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVI 246
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
53-259 |
2.62e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 110.58 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 53 IGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFeTADNGQIV------------LDDQDVTQVPAEQrhVNTVFQS--Y 118
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL-LAANGRIGgsatfngreilnLPEKELNKLRAEQ--ISMIFQDpmT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 119 ALFPHMTVFENVAFGL----RMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:PRK09473 109 SLNPYMRVGEQLMEVLmlhkGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127793354 195 LSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEP 259
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
53-256 |
3.71e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 109.33 E-value: 3.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 53 IGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDD-------QDVTQVPAEQRHVNTVFQ--SYALFPH 123
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 124 mTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRL-EKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKL 202
Cdd:PRK13645 107 -TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 203 RKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIY 256
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
26-247 |
4.43e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.47 E-value: 4.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 26 TLNAKQQAGKPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDqdvtqvp 105
Cdd:COG0488 304 RFPPPERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 106 aeqrhvnTVFQSY------ALFPHMTVFENVAFGLRMQKtpaaEIEPRVMdalrmvrLEKM-----AQRKP-HQLSGGQQ 173
Cdd:COG0488 377 -------TVKIGYfdqhqeELDPDKTVLDELRDGAPGGT----EQEVRGY-------LGRFlfsgdDAFKPvGVLSGGEK 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 174 QRIAIARAVVNKPKVLLLDE--------SLSAL-----DYKlrkqmqielkqlqrqlGiTFIFVTHDQE--EALsmSDRI 238
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEptnhldieTLEALeealdDFP----------------G-TVLLVSHDRYflDRV--ATRI 499
|
....*....
gi 2127793354 239 IVMRDGVIE 247
Cdd:COG0488 500 LEFEDGGVR 508
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-272 |
7.86e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 108.26 E-value: 7.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 25 QTLNAKQQAGKPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRM-------IAGFETADN----GQ 93
Cdd:PRK14271 9 QSGAADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRYSGDvllgGR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 94 IVLDDQDVTQVpaeQRHVNTVFQSYALFPhMTVFENVAFGLRMQK-TPAAEIEPRVMDALRMVRLEKMAQRK----PHQL 168
Cdd:PRK14271 89 SIFNYRDVLEF---RRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 169 SGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLgiTFIFVTHDQEEALSMSDRIIVMRDGVIEQ 248
Cdd:PRK14271 165 SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
250 260
....*....|....*....|....
gi 2127793354 249 DGSPREIYEEPKNLFVARFIGEIN 272
Cdd:PRK14271 243 EGPTEQLFSSPKHAETARYVAGLS 266
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-248 |
1.14e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.84 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 28 NAKQQAGKPVVRLSGISKSFDGKE--IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVP 105
Cdd:PRK11160 329 TSTAAADQVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 106 AEQ--RHVNTVFQSYALFPHmTVFENVAFGLrmqktPAAEIEpRVMDALRMVRLEKMAQRKP----------HQLSGGQQ 173
Cdd:PRK11160 409 EAAlrQAISVVSQRVHLFSA-TLRDNLLLAA-----PNASDE-ALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 174 QRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRqlGITFIFVTHdQEEALSMSDRIIVMRDG-VIEQ 248
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH-RLTGLEQFDRICVMDNGqIIEQ 554
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
34-244 |
2.52e-26 |
|
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: 104.05 E-value: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 34 GKPVVRLSGISksfdGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNT 113
Cdd:cd03215 1 GEPVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 114 VF------QSYALFPHMTVFENVAFglrmqktpaaeieprvmdalrmvrlekmaqrkPHQLSGGQQQRIAIARAVVNKPK 187
Cdd:cd03215 77 IAyvpedrKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 188 VLLLDESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDG 244
Cdd:cd03215 125 VLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
50-262 |
3.20e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.40 E-value: 3.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQV-------PAEQRhVNTVFQsyalFP 122
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkyirPVRKR-IGMVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 123 HMTVFEN-----VAFGLRMQKTPAAEIEPRVMDALRMVRLEK-MAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLS 196
Cdd:PRK13646 95 ESQLFEDtvereIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 197 ALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNL 262
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
55-262 |
3.82e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.45 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT------QVPAEQRHVNTVFQsyalFPHMTVFE 128
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQ----FPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 129 N-----VAFGLRMQKTPAAEIEPRVMDALRMVRL-EKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKL 202
Cdd:PRK13641 101 NtvlkdVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 203 RKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNL 262
Cdd:PRK13641 181 RKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWL 239
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
48-226 |
4.63e-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: 103.98 E-value: 4.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDV-TQVPAEQRHVNTVFQSYALFPHMTV 126
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 127 FENVAFGLRMQKTPAAEIEprvmDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYK-LRKQ 205
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIE----DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAgVALL 166
|
170 180
....*....|....*....|.
gi 2127793354 206 MQIELKQLQRQlGITfIFVTH 226
Cdd:TIGR01189 167 AGLLRAHLARG-GIV-LLTTH 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
55-226 |
6.64e-26 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 103.35 E-value: 6.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQR-------HVNtvfqsyALFPHMTVF 127
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHqdllylgHQP------GIKTELTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 128 ENVAFGLRMQKTPAAEiepRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQ 207
Cdd:PRK13538 93 ENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLE 169
|
170
....*....|....*....
gi 2127793354 208 IELKQLQRQLGITfIFVTH 226
Cdd:PRK13538 170 ALLAQHAEQGGMV-ILTTH 187
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
27-250 |
6.74e-26 |
|
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: 104.15 E-value: 6.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 27 LNAKQQAGKPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQdVTQVPA 106
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSLLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 107 eqrhVNTVFQsyalfPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKP 186
Cdd:cd03220 91 ----LGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 187 KVLLLDESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDG 250
Cdd:cd03220 162 DILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
35-251 |
7.94e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 104.19 E-value: 7.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 35 KPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ---RHV 111
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 112 NTVFQSYALFPHMTVFENVAF-GLRMQKTPAAEIEPRVMDALRmvRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLL 190
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMgGFFAERDQFQERIKWVYELFP--RLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127793354 191 LDESLSALDYKLRKQMQIELKQLqRQLGITFIFVTHDQEEALSMSDRIIVMRDG--VIEQDGS 251
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGhvVLEDTGD 222
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
41-256 |
2.21e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 103.93 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 41 SGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLD----DQDVTQVPAEQRHVNTVFQ 116
Cdd:PRK13638 5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgkplDYSKRGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 117 SyalfPHMTVF-----ENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLL 191
Cdd:PRK13638 85 D----PEQQIFytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127793354 192 DESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIY 256
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
44-244 |
2.82e-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: 101.47 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 44 SKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAG--FETADNGQIVLDDQDVTQvPAEQRHVNTVFQSYALF 121
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDK-RSFRKIIGYVPQDDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 122 PHMTVFENVAFglrmqktpAAEieprvmdaLRmvrlekmaqrkphQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYK 201
Cdd:cd03213 95 PTLTVRETLMF--------AAK--------LR-------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2127793354 202 LRKQMQIELKQLqRQLGITFIFVTHD-QEEALSMSDRIIVMRDG 244
Cdd:cd03213 146 SALQVMSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQG 188
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
46-263 |
3.06e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 107.62 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 46 SFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFeTADNGQIVLDDQDVTQVPAEQ--RHVNTVFQSYALFpH 123
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESwrKHLSWVGQNPQLP-H 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 124 MTVFENVAFGlrmqkTPAAEiEPRVMDALRMVRLEKMAQRKPH-----------QLSGGQQQRIAIARAVVNKPKVLLLD 192
Cdd:PRK11174 437 GTLRDNVLLG-----NPDAS-DEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 193 ESLSALDYKLRKQMQIELKQLQRQLgiTFIFVTHdQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPkNLF 263
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNAASRRQ--TTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG-GLF 577
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
37-258 |
4.40e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 102.47 E-value: 4.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSF--------DGKEIIG--------------NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQI 94
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrSLKELLLrrrrtrreefwalkDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 95 VLDDqdvtQVPA--EqrhVNTVFQsyalfPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQ 172
Cdd:COG1134 84 EVNG----RVSAllE---LGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 173 QQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSP 252
Cdd:COG1134 152 RARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
....*.
gi 2127793354 253 REIYEE 258
Cdd:COG1134 231 EEVIAA 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
33-255 |
4.93e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 106.67 E-value: 4.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 33 AGKPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQ---DVTQVPAEQR 109
Cdd:PRK15439 7 TAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcaRLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 110 HVNTVFQSYALFPHMTVFENVAFGLrmQKTPAAEiepRVMDALrmvrLEKM-AQRKPHQLSG----GQQQRIAIARAVVN 184
Cdd:PRK15439 87 GIYLVPQEPLLFPNLSVKENILFGL--PKRQASM---QKMKQL----LAALgCQLDLDSSAGslevADRQIVEILRGLMR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127793354 185 KPKVLLLDESLSALD----YKLRKQMQiELkqlqRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:PRK15439 158 DSRILILDEPTASLTpaetERLFSRIR-EL----LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
48-226 |
5.96e-25 |
|
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: 99.92 E-value: 5.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVL-DDQDVTQVPaeQRhvntvfqsyalfPHMTV 126
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLP--QR------------PYLPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 127 fenvafG-LRmqktpaaeieprvmDALRmvrlekmaqrKP--HQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDyklr 203
Cdd:cd03223 78 ------GtLR--------------EQLI----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD---- 123
|
170 180
....*....|....*....|...
gi 2127793354 204 KQMQIELKQLQRQLGITFIFVTH 226
Cdd:cd03223 124 EESEDRLYQLLKELGITVISVGH 146
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
44-244 |
8.58e-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: 100.62 E-value: 8.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 44 SKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQD--VTQVPAEQrhvntvfqsyalf 121
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIayVSQEPWIQ------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 122 pHMTVFENVAFGLRMQktpaaeiEPRVMDALRMVRLEKMAQRKPHQ-----------LSGGQQQRIAIARAVVNKPKVLL 190
Cdd:cd03250 79 -NGTIRENILFGKPFD-------EERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 191 LDESLSALDYKLRKQMqieLKQLQRQLGI---TFIFVTHdQEEALSMSDRIIVMRDG 244
Cdd:cd03250 151 LDDPLSAVDAHVGRHI---FENCILGLLLnnkTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
55-258 |
1.37e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.12 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ------RHVNTVFQsyalFPHMTVFE 128
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvrKKVGVVFQ----FPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 129 -----NVAFGLRMQKTPAAEIEPRVMDALRMVRLEK-MAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKL 202
Cdd:PRK13643 100 etvlkDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 203 RKQMqIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEE 258
Cdd:PRK13643 180 RIEM-MQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
38-297 |
1.43e-24 |
|
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: 105.27 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFET--ADNGQIV-------------------- 95
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 96 --------LDDQDV-------TQVPAEQRHVNTVFQ-SYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEK 159
Cdd:TIGR03269 81 pcpvcggtLEPEEVdfwnlsdKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 160 MAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRII 239
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 240 VMRDGVIEQDGSPREIyeepknlfVARFIGeinvfNATMLERIDEKRIRAEIEGVESV 297
Cdd:TIGR03269 241 WLENGEIKEEGTPDEV--------VAVFME-----GVSEVEKECEVEVGEPIIKVRNV 285
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
53-236 |
2.37e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 101.01 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 53 IGNLNLDVNHGEFLTILGPSGCGKTTVLR-------MIAGFETadNGQIVLDDQDV--TQV-PAE-QRHVNTVFQSYALF 121
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLyaPDVdPVEvRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 122 PHmTVFENVAFGLRMQKTpAAEIEPRVMDALRMVRLEKMAQRKPHQ----LSGGQQQRIAIARAVVNKPKVLLLDESLSA 197
Cdd:PRK14243 104 PK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 2127793354 198 LDYKLRKQMQIELKQLQRQLgiTFIFVTHDQEEALSMSD 236
Cdd:PRK14243 182 LDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSD 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
39-255 |
3.56e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 100.63 E-value: 3.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 39 RLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQ--VPAEQRHVNTVFQ 116
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 117 SYALFPHMTVFENVAFGlrmqKTP--------AAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKV 188
Cdd:PRK10575 93 QLPAAEGMTVRELVAIG----RYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 189 LLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
54-262 |
4.42e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 99.53 E-value: 4.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 54 GNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFeTADNGQIVLDDQDVTQVPA-EQRHVNTVF--QSYALFPhMTVFENV 130
Cdd:COG4138 13 GPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAaELARHRAYLsqQQSPPFA-MPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 131 AFGLRmQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAV------VN-KPKVLLLDESLSALDYklr 203
Cdd:COG4138 91 ALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLDEPMNSLDV--- 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 204 kQMQIELKQLQRQL---GITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYeEPKNL 262
Cdd:COG4138 167 -AQQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPENL 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
38-244 |
6.76e-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: 96.36 E-value: 6.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGqivlddqdvtqvpaeqrhvntvfqs 117
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 yalfphmtvfenvafglrmqktpaaeiEPRVMDALRMVRLEkmaqrkphQLSGGQQQRIAIARAVVNKPKVLLLDESLSA 197
Cdd:cd03221 56 ---------------------------IVTWGSTVKIGYFE--------QLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2127793354 198 LDYKLRKQMQIELKQLQRqlgiTFIFVTHDQEEALSMSDRIIVMRDG 244
Cdd:cd03221 101 LDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
38-250 |
7.38e-24 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 97.38 E-value: 7.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKE--IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVNTVF 115
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 116 -QSYALFpHMTVFENVafGLRmqktpaaeieprvmdalrmvrlekmaqrkphqLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:cd03247 81 nQRPYLF-DTTLRNNL--GRR--------------------------------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 195 LSALDYKLRKQMqieLKQLQRQL-GITFIFVTHdQEEALSMSDRIIVMRDGVIEQDG 250
Cdd:cd03247 126 TVGLDPITERQL---LSLIFEVLkDKTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
55-261 |
1.71e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 102.63 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKT-TVLRMIAGFETA----DNGQIVLDDQD------VTQVPAEQRHVN-----TVFQS- 117
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLRRRSrqvielSEQSAAQMRHVRgadmaMIFQEp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 -YALFPHMTVFENVAFGLRMQKTPAAEIE----PRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLD 192
Cdd:PRK10261 114 mTSLNPVFTVGEQIAESIRLHQGASREEAmveaKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIAD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2127793354 193 ESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKN 261
Cdd:PRK10261 194 EPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQH 262
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
49-199 |
6.36e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 95.33 E-value: 6.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 49 GKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT-QVPAEQRHvntvfqsY-----ALFP 122
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEACH-------YlghrnAMKP 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 123 HMTVFENVAFGLRMQKTPaaeiEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIAR-AVVNKPkVLLLDESLSALD 199
Cdd:PRK13539 87 ALTVAENLEFWAAFLGGE----ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARlLVSNRP-IWILDEPTAALD 159
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
30-246 |
7.02e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.09 E-value: 7.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 30 KQQAGKPVVRLSGISksfdGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQ------ 103
Cdd:COG1129 249 AAAPGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIrsprda 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 104 -------VPaEQRHvntvfqSYALFPHMTVFENVA---------FGLRMQKTPAAEIEpRVMDAL--RMVRLEKMAQrkp 165
Cdd:COG1129 325 iragiayVP-EDRK------GEGLVLDLSIRENITlasldrlsrGGLLDRRRERALAE-EYIKRLriKTPSPEQPVG--- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 166 hQLSGGQQQRIAIARAVVNKPKVLLLDESLSALD-------YKLrkqmqieLKQLQRQlGITFIFVTHDQEEALSMSDRI 238
Cdd:COG1129 394 -NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgakaeiYRL-------IRELAAE-GKAVIVISSELPELLGLSDRI 464
|
....*...
gi 2127793354 239 IVMRDGVI 246
Cdd:COG1129 465 LVMREGRI 472
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
60-260 |
9.81e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 97.50 E-value: 9.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 60 VNHGEFLTILGPSGCGKTTVLRMIAGF------ETADngQIVLDDQDVTQVPAEQRH------VNTVFQS--YALFPHMT 125
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSVSSLAIMGLidypgrVMAE--KLEFNGQDLQRISEKERRnlvgaeVAMIFQDpmTSLNPCYT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 126 VFENVAFGLRM-QKTPAAEIEPRVMDALRMVRLEKMAQR---KPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYK 201
Cdd:PRK11022 108 VGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVT 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2127793354 202 LRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPK 260
Cdd:PRK11022 188 IQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPR 246
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
52-246 |
4.86e-22 |
|
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: 93.69 E-value: 4.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 52 IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRH--VNTVFQSYALFPHmTVFEN 129
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHskVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 130 VAFGLrmQKTPAAEIEPRVMDALRMVRLEKMAQ-------RKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKL 202
Cdd:cd03248 108 IAYGL--QSCSFECVKEAAQKAHAHSFISELASgydtevgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2127793354 203 RKQMQIELKQ-LQRQlgiTFIFVTHdQEEALSMSDRIIVMRDGVI 246
Cdd:cd03248 186 EQQVQQALYDwPERR---TVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
37-244 |
4.93e-22 |
|
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: 97.59 E-value: 4.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETAD--NGQIVLDDQDVTQV---PAEQRHV 111
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASnirDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 112 NTVFQSYALFPHMTVFENVAFG----LRMQKTPAAEIEPRVMDALRMVRLEKMAQRKP-HQLSGGQQQRIAIARAVVNKP 186
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 187 KVLLLDESLSALDyklRKQMQIEL---KQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDG 244
Cdd:TIGR02633 161 RLLILDEPSSSLT---EKETEILLdiiRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
43-258 |
7.88e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 97.40 E-value: 7.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 43 ISKSFDGKEI--IGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT--QVPAEQRHVNTVFQSY 118
Cdd:PRK11176 347 VTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLRNQVALVSQNV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 119 ALFpHMTVFENVAFGlRMQKTPAAEIEPRVMDALRMVRLEKMAQ-------RKPHQLSGGQQQRIAIARAVVNKPKVLLL 191
Cdd:PRK11176 427 HLF-NDTIANNIAYA-RTEQYSREQIEEAARMAYAMDFINKMDNgldtvigENGVLLSGGQRQRIAIARALLRDSPILIL 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 192 DESLSALDYKLRKQMQIELKQLQRQLgiTFIFVTHdqeeALSM---SDRIIVMRDGVIEQDGSPREIYEE 258
Cdd:PRK11176 505 DEATSALDTESERAIQAALDELQKNR--TSLVIAH----RLSTiekADEILVVEDGEIVERGTHAELLAQ 568
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
40-227 |
1.96e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 40 LSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLD-DQDVTQVPaeqrhvntvfQSY 118
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLP----------QEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 119 ALFPHMTVFENVAFGLR------------MQKTPAAEIEPRVMDAL--RMVRL-------------------EKMAQRKP 165
Cdd:COG0488 71 PLDDDLTVLDTVLDGDAelraleaeleelEAKLAEPDEDLERLAELqeEFEALggweaearaeeilsglgfpEEDLDRPV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 166 HQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDyklrkqmqIE----LKQLQRQLGITFIFVTHD 227
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--------LEsiewLEEFLKNYPGTVLVVSHD 208
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
35-248 |
3.22e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 95.41 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 35 KPVVRLSG------ISKSFDGK-EIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE 107
Cdd:PRK13657 326 IDLGRVKGavefddVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 108 --QRHVNTVFQSYALFpHMTVFENvafgLRMQKTPAAEIEprVMDALRMVRLEKMAQRKPH-----------QLSGGQQQ 174
Cdd:PRK13657 406 slRRNIAVVFQDAGLF-NRSIEDN----IRVGRPDATDEE--MRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQ 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 175 RIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLqRQLGITFIfVTHdqeeALSM---SDRIIVMRDG-VIEQ 248
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFI-IAH----RLSTvrnADRILVFDNGrVVES 550
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
48-258 |
3.61e-21 |
|
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: 90.28 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFE--TADNGQIVLDDQDVTQVPAEQRHVNTVFqsyalfphmt 125
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIF---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 126 vfenvafgLRMQKTPaaEIEP-RVMDALRMVRLekmaqrkphQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRK 204
Cdd:cd03217 81 --------LAFQYPP--EIPGvKNADFLRYVNE---------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2127793354 205 QMQIELKQLqRQLGITFIFVTHDQEEALSM-SDRIIVMRDGVIEQDGsPREIYEE 258
Cdd:cd03217 142 LVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
46-239 |
5.22e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.60 E-value: 5.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 46 SFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGqivlddqDVTQVPAeqRHVNTVFQSYAL---FP 122
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG-------TVRRAGG--ARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 123 hMTVFENVAFGL----RMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSAL 198
Cdd:NF040873 72 -LTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2127793354 199 DYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRII 239
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVL 190
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
36-244 |
5.63e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 94.61 E-value: 5.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAG---FETADnGQIVLDDQDVTQV---PAEQR 109
Cdd:PRK13549 4 YLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvypHGTYE-GEIIFEGEELQASnirDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 110 HVNTVFQSYALFPHMTVFENVAFGlrmqktpaAEIEPR-VMDALRMV-RLEKMAQR---------KPHQLSGGQQQRIAI 178
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLG--------NEITPGgIMDYDAMYlRAQKLLAQlkldinpatPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 179 ARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDG 244
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
50-249 |
1.28e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.62 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKT----TVLRMI----AGFETAD---NGQIVL--DDQDVTQVPAEQrhVNTVFQ 116
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppVVYPSGDirfHGESLLhaSEQTLRGVRGNK--IAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 117 S--YALFPHMTV----FENVAFGLRMQKTPA-AEIeprvMDALRMVRLEKMAQRK---PHQLSGGQQQRIAIARAVVNKP 186
Cdd:PRK15134 100 EpmVSLNPLHTLekqlYEVLSLHRGMRREAArGEI----LNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 187 KVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDG-VIEQD 249
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGrCVEQN 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
29-246 |
1.35e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.17 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 29 AKQQAGKPVVRLSGIS-KSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE 107
Cdd:COG3845 249 APAEPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 108 QRHVNTVF------QSYALFPHMTVFENVAFGLRMQKtpaaEIEPRVMdaLRMVRLEKMAQRK----------PHQ---- 167
Cdd:COG3845 329 ERRRLGVAyipedrLGRGLVPDMSVAENLILGRYRRP----PFSRGGF--LDRKAIRAFAEELieefdvrtpgPDTpars 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 168 LSGGQQQRIAIARAVVNKPKVLL-------LDesLSALDYkLRKQMqIELkqlqRQLGITFIFVTHDQEEALSMSDRIIV 240
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIaaqptrgLD--VGAIEF-IHQRL-LEL----RDAGAAVLLISEDLDEILALSDRIAV 474
|
....*.
gi 2127793354 241 MRDGVI 246
Cdd:COG3845 475 MYEGRI 480
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
36-199 |
2.89e-20 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 88.37 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQvpAEQ-RHVNTV 114
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR--GDRsRFMAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 115 FQSYALFPHMTVFENVAF-----GLRMQKTPAaeieprvmDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVL 189
Cdd:PRK13543 88 GHLPGLKADLSTLENLHFlcglhGRRAKQMPG--------SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLW 159
|
170
....*....|
gi 2127793354 190 LLDESLSALD 199
Cdd:PRK13543 160 LLDEPYANLD 169
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
55-252 |
2.92e-20 |
|
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: 88.32 E-value: 2.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKTTV----LRMIagfeTADNGQIVLDDQDVTQVPAEQ--RHVNTVFQSYALFPHmTVFE 128
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLFSG-TIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 129 NVA-FGlrmQKTPAAeieprVMDALRMVRLEKMAQRKPHQL-----------SGGQQQRIAIARAVVNKPKVLLLDESLS 196
Cdd:cd03244 97 NLDpFG---EYSDEE-----LWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 197 ALDYKLRKQMQielKQLQRQL-GITFIFVTHDQEEALSmSDRIIVMRDGVIEQDGSP 252
Cdd:cd03244 169 SVDPETDALIQ---KTIREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
36-244 |
3.60e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.90 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQdvtqvpaEQRHVNT-- 113
Cdd:PRK11288 3 PYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-------EMRFASTta 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 114 --------VFQSYALFPHMTVFENVAFGLRMQKtpAAEIEPRVMDALRMVRLEKMA-----QRKPHQLSGGQQQRIAIAR 180
Cdd:PRK11288 76 alaagvaiIYQELHLVPEMTVAENLYLGQLPHK--GGIVNRRLLNYEAREQLEHLGvdidpDTPLKYLSIGQRQMVEIAK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 181 AVVNKPKVLLLDE---SLSAldyklrkqMQIE-LKQLQRQL---GITFIFVTHDQEEALSMSDRIIVMRDG 244
Cdd:PRK11288 154 ALARNARVIAFDEptsSLSA--------REIEqLFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
37-259 |
6.24e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.52 E-value: 6.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSFDGKE-----IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDD----QDVTQVPAE 107
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 108 QRH--------------VNTVFQ--SYALFPHmTVFENVAFG---LRMQKTPAAEIEPRVMDalRMVRLEKMAQRKPHQL 168
Cdd:PRK13631 101 TNPyskkiknfkelrrrVSMVFQfpEYQLFKD-TIEKDIMFGpvaLGVKKSEAKKLAKFYLN--KMGLDDSYLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 169 SGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMqIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQ 248
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
250
....*....|.
gi 2127793354 249 DGSPREIYEEP 259
Cdd:PRK13631 257 TGTPYEIFTDQ 267
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
35-288 |
1.16e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 90.61 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 35 KPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVP---AEQRHV 111
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 112 NTVFQSYALFPHMTVFENVAFGLRMQK-------TPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVN 184
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 185 KPKVLLLDESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGV-----IEQDGSPREIY--- 256
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSsvcsgMVSDVSNDDIVrlm 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 2127793354 257 --EEPKNLFVARFIGEINVFNATMLE-----RIDEKRIR 288
Cdd:PRK09700 242 vgRELQNRFNAMKENVSNLAHETVFEvrnvtSRDRKKVR 280
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
50-250 |
1.30e-19 |
|
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: 87.00 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQI-VLDDQDVTQVPAEQRHVNTVF-QSYALFPHMTVF 127
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAGLVPWKRRKKFLRRIGVVFgQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 128 ENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQ 207
Cdd:cd03267 114 DSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2127793354 208 IELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDG 250
Cdd:cd03267 194 NFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
37-240 |
2.31e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 85.78 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFE--TADNGQIVLDDQDVTQVpaeqrhvntv 114
Cdd:COG2401 30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGRE---------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 115 fqsyalfphMTVFENVAfglRMQKTPAAeieprvMDALRMVRLEKMA--QRKPHQLSGGQQQRIAIARAVVNKPKVLLLD 192
Cdd:COG2401 100 ---------ASLIDAIG---RKGDFKDA------VELLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2127793354 193 ESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQE--EALSmSDRIIV 240
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDviDDLQ-PDLLIF 210
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
36-267 |
2.64e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 86.32 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQ-DVTQVPaEQRHVNTv 114
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlRIGYVP-QKLYLDT- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 115 fqsyalfphmTVFENVAFGLRMQK-TPAAEIEPrvmdALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDE 193
Cdd:PRK09544 81 ----------TLPLTVNRFLRLRPgTKKEDILP----ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 194 SLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMrDGVIEQDGSPREIYEEPKnlFVARF 267
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE--FISMF 217
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
46-252 |
2.87e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 86.27 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 46 SFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFE--TADNGQIVLDDQDVTQVPAEQRH---VNTVFQSYAL 120
Cdd:COG0396 9 SVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERAragIFLAFQYPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 121 FPHMTV--FENVAFGLRMQKT-PAAEIEPRVMDALRMVRL-EKMAQRKPHQ-LSGGQQQRIAIARAVVNKPKVLLLDESL 195
Cdd:COG0396 89 IPGVSVsnFLRTALNARRGEElSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 196 SALDY-----------KLRKQmqielkqlqrqlGITFIFVTHdQEEALSM--SDRIIVMRDGVIEQDGSP 252
Cdd:COG0396 169 SGLDIdalrivaegvnKLRSP------------DRGILIITH-YQRILDYikPDFVHVLVDGRIVKSGGK 225
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
48-199 |
3.13e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 85.24 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQV-PAEQRHVNTVFQSYALFPHMTV 126
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQrDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127793354 127 FENVAFGLRMQKTPAaeieprVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALD 199
Cdd:cd03231 91 LENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
56-259 |
6.79e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 85.37 E-value: 6.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 56 LNLDVNHGEFLTILGPSGCGKTTVLRMIAGFeTADNGQIVLDDQDVTQVPA-EQRHVNTVF--QSYALFpHMTVFENVAF 132
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAaELARHRAYLsqQQTPPF-AMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 133 GLRmQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIArAVV------NKP--KVLLLDESLSALDYKLRK 204
Cdd:PRK03695 93 HQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLA-AVVlqvwpdINPagQLLLLDEPMNSLDVAQQA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2127793354 205 QMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEP 259
Cdd:PRK03695 171 ALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
36-297 |
6.87e-19 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 89.30 E-value: 6.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFD--GKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDV-TQVPAEQRHVN 112
Cdd:TIGR01257 927 PGVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 113 TVFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLD 192
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 193 ESLSALDYKLRKQMQIELkqLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPreiyeepknLFVARFIGeiN 272
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP---------LFLKNCFG--T 1153
|
250 260
....*....|....*....|....*
gi 2127793354 273 VFNATMLERIdeKRIRAEIEGVESV 297
Cdd:TIGR01257 1154 GFYLTLVRKM--KNIQSQRGGCEGT 1176
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
50-254 |
1.07e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.80 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETAD---NGQIVLDDQDVTqvpAEQRHVNTVF--QSYALFPHM 124
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID---AKEMRAISAYvqQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 125 TVFENVAFG--LRMQK-TPAAEIEPRVMDALRMVRLEKMAQRK---PHQ---LSGGQQQRIAIARAVVNKPKVLLLDESL 195
Cdd:TIGR00955 115 TVREHLMFQahLRMPRrVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 196 SALDYKLRKQMQIELKQLQrQLGITFIFVTHD-QEEALSMSDRIIVMRDGVIEQDGSPRE 254
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
38-258 |
1.81e-18 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 86.87 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLddqdvtqvpAEQRHVNTVFQ- 116
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW---------SENANIGYYAQd 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 117 SYALFPH-MTVFENVAfglrmQKTPAAEIEPRVMDAL-RMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:PRK15064 391 HAYDFENdLTLFDWMS-----QWRQEGDDEQAVRGTLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127793354 195 LSALDYKLRKQMQIELKQLQrqlGiTFIFVTHDQEEALSMSDRIIVMR-DGVIEQDGSpreiYEE 258
Cdd:PRK15064 466 TNHMDMESIESLNMALEKYE---G-TLIFVSHDREFVSSLATRIIEITpDGVVDFSGT----YEE 522
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
50-259 |
2.36e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 86.69 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE--QRHVNTVFQSYALFPHmTVF 127
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 128 ENVAFGlRMQKTPAaEIEprvmDALRMVRLEKMAQRKPH-----------QLSGGQQQRIAIARAVVNKPKVLLLDESLS 196
Cdd:PRK10789 407 NNIALG-RPDATQQ-EIE----HVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127793354 197 ALDYKLRKQMQIELKQLQRQLgiTFIFVTHdQEEALSMSDRIIVMRDGVIEQDGSPREIYEEP 259
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGEGR--TVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
53-246 |
3.76e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 53 IGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDV-TQVPAEQRHVNTVFQSY-----ALFPHMTV 126
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANGIVYISEdrkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 127 FENVA------FGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKP-HQLSGGQQQRIAIARAVVNKPKVLLLDESLSALD 199
Cdd:PRK10762 348 KENMSltalryFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2127793354 200 YKLRKqmqiELKQLQRQL---GITFIFVTHDQEEALSMSDRIIVMRDGVI 246
Cdd:PRK10762 428 VGAKK----EIYQLINQFkaeGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
37-260 |
7.22e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.44 E-value: 7.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSFDGkEIIGNLNLDVNHGEFLTILGPSGCGKT----TVLRMIAGFETADNGQIVLDDQDVTQVPAEQRHVN 112
Cdd:PRK10418 4 QIELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 113 TVFQS--YALFPHMTVFENVAFGLRMQKTPAAEiePRVMDALRMVRLE---KMAQRKPHQLSGGQQQRIAIARAVVNKPK 187
Cdd:PRK10418 83 TIMQNprSAFNPLHTMHTHARETCLALGKPADD--ATLTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127793354 188 VLLLDESLSALDykLRKQMQI--ELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPK 260
Cdd:PRK10418 161 FIIADEPTTDLD--VVAQARIldLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
53-254 |
2.58e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 83.48 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 53 IGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT--QVPAEQRHVNTVFQSYALFPHMTVFENv 130
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaeQPEDYRKLFSAVFTDFHLFDQLLGPEG- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 131 afglrmqKTPAAEIEPRVMDALRM---VRLEKMAQRKPhQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQ 207
Cdd:PRK10522 418 -------KPANPALVEKWLERLKMahkLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFY 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2127793354 208 IELKQLQRQLGITFIFVTHDqEEALSMSDRIIVMRDGVI-EQDGSPRE 254
Cdd:PRK10522 490 QVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLsELTGEERD 536
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
53-244 |
5.75e-17 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 79.30 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 53 IGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE-QRHVNTVFQSYA----LFPHMTVF 127
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEaTRSRNRYSVAYAaqkpWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 128 ENVAFGLRMQK------TPAAEIEPRVmDALRMVRLEKMAQRKPHqLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYK 201
Cdd:cd03290 97 ENITFGSPFNKqrykavTDACSLQPDI-DLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2127793354 202 LRKQ-MQIELKQLQRQLGITFIFVTHdQEEALSMSDRIIVMRDG 244
Cdd:cd03290 175 LSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
35-244 |
5.87e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 82.36 E-value: 5.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 35 KPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT-QVP--AEQRHV 111
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPksSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 112 NTVFQSYALFPHMTVFENVAFGlRMQKTPAAEIEPRVM----DALrMVRLEkmAQRKPHQLSG----GQQQRIAIARAVV 183
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLG-REFVNRFGRIDWKKMyaeaDKL-LARLN--LRFSSDKLVGelsiGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 184 NKPKVLLLDESLSALDYKLRKQMQIELKQLQRQ-LGITFIfvTHDQEEALSMSDRIIVMRDG 244
Cdd:PRK10762 158 FESKVIIMDEPTDALTDTETESLFRVIRELKSQgRGIVYI--SHRLKEIFEICDDVTVFRDG 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
43-244 |
6.94e-17 |
|
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: 78.46 E-value: 6.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 43 ISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAG---FETADNGQIVLDDQDVTQVpAEQRHVNTVF--QS 117
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrteGNVSVEGDIHYNGIPYKEF-AEKYPGEIIYvsEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 118 YALFPHMTVFENVAFGLRMQktpaaeieprvmdALRMVRlekmaqrkphQLSGGQQQRIAIARAVVNKPKVLLLDESLSA 197
Cdd:cd03233 92 DVHFPTLTVRETLDFALRCK-------------GNEFVR----------GISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2127793354 198 LDYKLRKQMQIELKQLQRQLGITfIFVTHDQ--EEALSMSDRIIVMRDG 244
Cdd:cd03233 149 LDSSTALEILKCIRTMADVLKTT-TFVSLYQasDEIYDLFDKVLVLYEG 196
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
52-259 |
1.57e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.95 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 52 IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFeTADNGQI-----VLDDQDVTQVPAEQRH------VNTVFQ--SY 118
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVtadrfRWNGIDLLKLSPRERRkiigreIAMIFQepSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 119 ALFPHMTVFENVafglrMQKTPAAEIEPRVMD-----ALRMVRL---------EKMAQRKPHQLSGGQQQRIAIARAVVN 184
Cdd:COG4170 101 CLDPSAKIGDQL-----IEAIPSWTFKGKWWQrfkwrKKRAIELlhrvgikdhKDIMNSYPHELTEGECQKVMIAMAIAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 185 KPKVLLLDESLSALDykLRKQMQIeLKQLQR--QL-GITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEP 259
Cdd:COG4170 176 QPRLLIADEPTNAME--STTQAQI-FRLLARlnQLqGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
31-246 |
1.62e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 31 QQAGKPVVRLSGISKsfdgkEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQR- 109
Cdd:PRK15439 262 QAAGAPVLTVEDLTG-----EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRl 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 110 HVNTVF-----QSYALFPHMTVFENVA------FGLRMQKTPAAEIEPRVMDALRmVRLEKmAQRKPHQLSGGQQQRIAI 178
Cdd:PRK15439 337 ARGLVYlpedrQSSGLYLDAPLAWNVCalthnrRGFWIKPARENAVLERYRRALN-IKFNH-AEQAARTLSGGNQQKVLI 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 179 ARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVI 246
Cdd:PRK15439 415 AKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
48-255 |
2.33e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 78.33 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETAD--------NGQIVLDDQDVTQVPAEQ---RHVNTVFQ 116
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRlarLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 117 SYALFPhMTVFENVAFGLRMQKTPAAEIEPRVMD----ALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVN-------- 184
Cdd:PRK13547 92 AQPAFA-FSAREIVLLGRYPHARRAGALTHRDGEiawqALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaa 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 185 -KPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:PRK13547 171 qPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
55-258 |
3.33e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.55 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVL-----DDQDVtqvpAEQRHVNTVFQSYALFPHMTVFEN 129
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDI----ATRRRVGYMSQAFSLYGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 130 VAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIE 209
Cdd:NF033858 360 LELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 210 LKQLQRQLGITfIFV-THDQEEALSmSDRIIVMRDG-VIEQDgSPREIYEE 258
Cdd:NF033858 440 LIELSREDGVT-IFIsTHFMNEAER-CDRISLMHAGrVLASD-TPAALVAA 487
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
51-252 |
6.13e-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: 75.91 E-value: 6.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 51 EIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE--QRHVNTVFQSYALFphmtvfe 128
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEdlRSSLTIIPQDPTLF------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 129 nvAFGLRMQKTPAAEI-EPRVMDALRMvrlekmaQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDY----KLR 203
Cdd:cd03369 95 --SGTIRSNLDPFDEYsDEEIYGALRV-------SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYatdaLIQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2127793354 204 KQMQIELKqlqrqlGITFIFVTHdQEEALSMSDRIIVMRDGVIEQDGSP 252
Cdd:cd03369 166 KTIREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-199 |
7.57e-16 |
|
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: 79.21 E-value: 7.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 34 GKPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLddqdvtqvpAEQRHVNT 113
Cdd:TIGR03719 319 GDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI---------GETVKLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 114 VFQSY-ALFPHMTVFENVAFGLRMQKTPAAEIEPRVM---------DalrmvrlekmAQRKPHQLSGGQQQRIAIARAVV 183
Cdd:TIGR03719 390 VDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAYvgrfnfkgsD----------QQKKVGQLSGGERNRVHLAKTLK 459
|
170
....*....|....*.
gi 2127793354 184 NKPKVLLLDESLSALD 199
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLD 475
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-258 |
8.48e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 79.78 E-value: 8.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 27 LNAKQQAGKPVVRLSGISKSFDGK---EIIGNLNLDVNHGEFLTILGPSGCGKTTVLR-MIAGFETADNGQIVLDDQdVT 102
Cdd:PLN03130 604 PNPPLEPGLPAISIKNGYFSWDSKaerPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-VA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 103 QVPaeqrHVNTVFQSyalfphmTVFENVAFGL-----RMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHqLSGGQQQRIA 177
Cdd:PLN03130 683 YVP----QVSWIFNA-------TVRDNILFGSpfdpeRYERAIDVTALQHDLDLLPGGDLTEIGERGVN-ISGGQKQRVS 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 178 IARAVVNKPKVLLLDESLSALDYKLRKqmQIELKQLQRQL-GITFIFVThDQEEALSMSDRIIVMRDGVIEQDGSpreiY 256
Cdd:PLN03130 751 MARAVYSNSDVYIFDDPLSALDAHVGR--QVFDKCIKDELrGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGT----Y 823
|
..
gi 2127793354 257 EE 258
Cdd:PLN03130 824 EE 825
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
5-244 |
6.15e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.46 E-value: 6.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 5 KVNDLCHINWIHPNLNVGEiqtlNAKQQAGKPVvRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIA 84
Cdd:PLN03211 41 KFMDVCYRVKFENMKNKGS----NIKRILGHKP-KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 85 GFETADN--GQIVLDDQDVTQvpAEQRHVNTVFQSYALFPHMTVFENVAFG--LRMQKTPAAEIEPRVMDA----LRMVR 156
Cdd:PLN03211 116 GRIQGNNftGTILANNRKPTK--QILKRTGFVTQDDILYPHLTVRETLVFCslLRLPKSLTKQEKILVAESviseLGLTK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 157 LEK--MAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQrQLGITFIFVTHD-QEEALS 233
Cdd:PLN03211 194 CENtiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLA-QKGKTIVTSMHQpSSRVYQ 272
|
250
....*....|.
gi 2127793354 234 MSDRIIVMRDG 244
Cdd:PLN03211 273 MFDSVLVLSEG 283
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
39-249 |
6.17e-15 |
|
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: 76.38 E-value: 6.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 39 RLSGISKSFDGKE-----IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT--QVPAEQRHV 111
Cdd:COG4615 329 ELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTadNREAYRQLF 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 112 NTVFQSYALFPHMtvfenvaFGlrmqktPAAEIEPRVMDALrmvrLEKMA-QRKPH---------QLSGGQQQRIAIARA 181
Cdd:COG4615 409 SAVFSDFHLFDRL-------LG------LDGEADPARAREL----LERLElDHKVSvedgrfsttDLSQGQRKRLALLVA 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 182 VV-NKPkVLLLDEslSALD---------YKlrkqmqiELKQLQRQLGITFIFVTHDqEEALSMSDRIIVMRDGVIEQD 249
Cdd:COG4615 472 LLeDRP-ILVFDE--WAADqdpefrrvfYT-------ELLPELKARGKTVIAISHD-DRYFDLADRVLKMDYGKLVEL 538
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
55-297 |
1.20e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.97 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQI-VLDdqdvtQVPAEQRHVN-----TVF-QSYALFPHMTVF 127
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrVLG-----YVPFKRRKEFarrigVVFgQRSQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 128 ENvaFGL--RMQKTPAAEIEPRvMDALR-MVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRK 204
Cdd:COG4586 115 DS--FRLlkAIYRIPDAEYKKR-LDELVeLLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 205 QMQIELKQLQRQLGITFIFVTHDQE--EALsmSDRIIVMRDGVIEQDGSP---REIYEEPKNLFV--ARFIGEINVFNAT 277
Cdd:COG4586 192 AIREFLKEYNRERGTTILLTSHDMDdiEAL--CDRVIVIDHGRIIYDGSLeelKERFGPYKTIVLelAEPVPPLELPRGG 269
|
250 260
....*....|....*....|
gi 2127793354 278 MLERIDEKRIRAEIEGVESV 297
Cdd:COG4586 270 EVIEREGNRVRLEVDPRESL 289
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
48-248 |
1.22e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.52 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVP--AEQRHVNTVFQSYALFPHmT 125
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsVLRQGVAMVQQDPVVLAD-T 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 126 VFENVAFGLRMQktpaaeiEPRVMDALRMVRLEKMAQRKP-----------HQLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:PRK10790 431 FLANVTLGRDIS-------EEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 195 LSALDYKLRKQMQIELKQLQRQlgITFIFVTHdqeeALSM---SDRIIVMRDG-VIEQ 248
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREH--TTLVVIAH----RLSTiveADTILVLHRGqAVEQ 555
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
49-226 |
1.23e-14 |
|
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: 75.56 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 49 GKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLD-DQDVTQVPAEQRHVNTVFQSYALFPhMTVF 127
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPaKGKLFYVPQRPYMTLGTLRDQIIYP-DSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 128 ENVAFGLRMQKtpaaeieprVMDALRMVRLEKMAQRK---------PHQLSGGQQQRIAIARAVVNKPKVLLLDESLSAL 198
Cdd:TIGR00954 543 DMKRRGLSDKD---------LEQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170 180
....*....|....*....|....*...
gi 2127793354 199 DYklrkQMQIELKQLQRQLGITFIFVTH 226
Cdd:TIGR00954 614 SV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
62-244 |
1.24e-14 |
|
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: 70.87 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 62 HGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDvtqvpaeqrhvntvfqsyalfphmtvfenvafglrmqktpa 141
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 142 aeiepRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIE-----LKQLQRQ 216
Cdd:smart00382 40 -----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSE 114
|
170 180 190
....*....|....*....|....*....|...
gi 2127793354 217 LGITFIFVTHDQEEALSM-----SDRIIVMRDG 244
Cdd:smart00382 115 KNLTVILTTNDEKDLGPAllrrrFDRRIVLLLI 147
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-257 |
1.64e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.78 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 28 NAKQQAGKPVVRLSGISKSFDGK---EIIGNLNLDVNHGEFLTILGPSGCGKTTVLR-MIAGFETADNGQIVLDDQdVTQ 103
Cdd:PLN03232 605 NPPLQPGAPAISIKNGYFSWDSKtskPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-VAY 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 104 VPaeqrHVNTVFQSyalfphmTVFENVAFGL-----RMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHqLSGGQQQRIAI 178
Cdd:PLN03232 684 VP----QVSWIFNA-------TVRENILFGSdfeseRYWRAIDVTALQHDLDLLPGRDLTEIGERGVN-ISGGQKQRVSM 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 179 ARAVVNKPKVLLLDESLSALDYKLRKQ-----MQIELKqlqrqlGITFIFVThDQEEALSMSDRIIVMRDGVIEQDGSPR 253
Cdd:PLN03232 752 ARAVYSNSDIYIFDDPLSALDAHVAHQvfdscMKDELK------GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFA 824
|
....
gi 2127793354 254 EIYE 257
Cdd:PLN03232 825 ELSK 828
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
90-243 |
2.09e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.45 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 90 DNGQIVLDDQDVTQVPAEQ-RHVNTVFQSYALFPHMTVFENVAFGlrmqKTPAAEIEprVMDALRMVRLEKMAQRKPHQ- 167
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG----KEDATRED--VKRACKFAAIDEFIESLPNKy 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 168 ----------LSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHdQEEALSMSDR 237
Cdd:PTZ00265 1349 dtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427
|
....*.
gi 2127793354 238 IIVMRD 243
Cdd:PTZ00265 1428 IVVFNN 1433
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
40-236 |
3.12e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.75 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 40 LSGISKSFDGKE--IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQ-VPAEQRHVNTVFQ 116
Cdd:PRK13540 2 LDVIELDFDYHDqpLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 117 SYALFPHMTVFENVAFGLRMQKTpAAEIEprvmDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLS 196
Cdd:PRK13540 82 RSGINPYLTLRENCLYDIHFSPG-AVGIT----ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2127793354 197 ALDYKLRKQMQIELKQLQRQLGItfIFVTHDQEEALSMSD 236
Cdd:PRK13540 157 ALDELSLLTIITKIQEHRAKGGA--VLLTSHQDLPLNKAD 194
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
40-244 |
3.20e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.00 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 40 LSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDV---TQVPAEQRHVNTVFQ 116
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 117 SYALFPHMTVFENVAFGLRMQKTPaaeieprVMDALRMVRLEKM----------AQRKPHQLSGGQQQRIAIARAVVNKP 186
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGM-------FVDQDKMYRDTKAifdeldididPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 187 KVLLLDESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDG 244
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-251 |
3.25e-14 |
|
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: 74.66 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSFDGKE--IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDV-TQVPAEQRHVNT 113
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 114 VFQSYALFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDE 193
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 194 SLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGS 251
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
59-303 |
4.04e-14 |
|
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: 71.67 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 59 DVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPaeqRHVNTVFQsyalfphMTVFEnvafgLRMQK 138
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP---QYIKADYE-------GTVRD-----LLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 139 TPAAEIEP----RVMDALrmvRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQ 214
Cdd:cd03237 86 TKDFYTHPyfktEIAKPL---QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 215 RQLGITFIFVTHDQEEALSMSDRIIVMrDGVIEQDG--SPREIYEEPKNlfvaRFIGEINV-FnatmleRIDEKRIRAEI 291
Cdd:cd03237 163 ENNEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGvaNPPQSLRSGMN----RFLKNLDItF------RRDPETGRPRI 231
|
250
....*....|..
gi 2127793354 292 EGVESVVyyDRE 303
Cdd:cd03237 232 NKLGSVK--DRE 241
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
35-251 |
1.17e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.06 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 35 KPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFE--TADNGQIVLDDQDVTQVPAEQRH-- 110
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 111 -VNTVFQSYALFPHMTV--FENVAFGLRMQKTPAAEIEP-----RVMDALRMVRLEkmaqrkPHQL--------SGGQQQ 174
Cdd:CHL00131 85 gIFLAFQYPIEIPGVSNadFLRLAYNSKRKFQGLPELDPlefleIINEKLKLVGMD------PSFLsrnvnegfSGGEKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 175 RIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEealsMSDRII-----VMRDGVIEQD 249
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQR----LLDYIKpdyvhVMQNGKIIKT 233
|
..
gi 2127793354 250 GS 251
Cdd:CHL00131 234 GD 235
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
37-244 |
2.85e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.97 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAG------FEtadnGQIVLDDQ-----DVTQvp 105
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphgsYE----GEILFDGEvcrfkDIRD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 106 AEQRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPA---AEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAV 182
Cdd:NF040905 75 SEALGIVIIHQELALIPYLSIAENIFLGNERAKRGVidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 183 VNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDG 244
Cdd:NF040905 155 SKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
50-251 |
3.05e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 71.73 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAG-FETADnGQiVLDDQDVTQVPAEQRHVNTVFQSYALFphmtvFE 128
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSqFEISE-GR-VWAERSIAYVPQQAWIMNATVRGNILF-----FD 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 129 NvafglrmqktpaaEIEPRVMDALRMVRLE-KMAQ----------RKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSA 197
Cdd:PTZ00243 746 E-------------EDAARLADAVRVSQLEaDLAQlgggleteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 198 LDYKLRKQMQIELKqLQRQLGITFIFVTHdQEEALSMSDRIIVMRDGVIEQDGS 251
Cdd:PTZ00243 813 LDAHVGERVVEECF-LGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGS 864
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-199 |
3.89e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.92 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 34 GKPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDqdvtqvpaeqrhvnT 113
Cdd:PRK11819 321 GDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE--------------T 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 114 VFQSY------ALFPHMTVFENVAFGLRMQKTPAAEIEPRvmdalrmvrlekmA------------QRKPHQLSGGQQQR 175
Cdd:PRK11819 387 VKLAYvdqsrdALDPNKTVWEEISGGLDIIKVGNREIPSR-------------AyvgrfnfkggdqQKKVGVLSGGERNR 453
|
170 180
....*....|....*....|....
gi 2127793354 176 IAIARAVVNKPKVLLLDESLSALD 199
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-240 |
5.15e-13 |
|
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: 70.58 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 29 AKQQAGKPVVRLSGISKSFDGkeiignLNLDV-----NHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIvldDQDVT- 102
Cdd:COG1245 333 RREKEEETLVEYPDLTKSYGG------FSLEVeggeiREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLKi 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 103 ----Q-VPAEQrhvntvfqsyalfpHMTVFENvafgLRMQKTPAAE---IEPRVMDALrmvRLEKMAQRKPHQLSGGQQQ 174
Cdd:COG1245 404 sykpQyISPDY--------------DGTVEEF----LRSANTDDFGssyYKTEIIKPL---GLEKLLDKNVKDLSGGELQ 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 175 RIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDqeeaLSM----SDRIIV 240
Cdd:COG1245 463 RVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLidyiSDRLMV 528
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
40-227 |
5.61e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 70.35 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 40 LSGISKSFD-GKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIvlddqdvtqVPAEQRHVNTVFQSY 118
Cdd:TIGR03719 7 MNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA---------RPQPGIKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 119 ALFPHMTVFENVAFGLRMQKTPAAEI---------EPRVMDAL--RMVRL-EKMAQRKPHQ------------------- 167
Cdd:TIGR03719 78 QLDPTKTVRENVEEGVAEIKDALDRFneisakyaePDADFDKLaaEQAELqEIIDAADAWDldsqleiamdalrcppwda 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 168 ----LSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQielKQLQRQLGiTFIFVTHD 227
Cdd:TIGR03719 158 dvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLE---RHLQEYPG-TVVAVTHD 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
56-306 |
6.18e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 70.74 E-value: 6.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 56 LNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQdVTQVPAEqrhvntvfqsyALFPHMTVFENVAFGLR 135
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVPQQ-----------AWIQNDSLRENILFGKA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 136 MQktpaaeiEPR---VMDALRMV-RLEKMAQ-------RKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRK 204
Cdd:TIGR00957 725 LN-------EKYyqqVLEACALLpDLEILPSgdrteigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 205 QMQIELKQLQRQL-GITFIFVTHDQeEALSMSDRIIVMRDGVIEQDGSPREIYEepKNLFVARFIgeINVFNatmleriD 283
Cdd:TIGR00957 798 HIFEHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELLQ--RDGAFAEFL--RTYAP-------D 865
|
250 260
....*....|....*....|...
gi 2127793354 284 EKRIRAEIEGVESVVYYDREAQP 306
Cdd:TIGR00957 866 EQQGHLEDSWTALVSGEGKEAKL 888
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
57-246 |
8.50e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 8.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 57 NLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVT-QVPAEQRHVNTVF-----QSYALFPHMTVFENV 130
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLcpedrKAEGIIPVHSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 131 AFGLRMQKTPAAE-IEPRVMDALRMVRLEKMAQRKPH------QLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLR 203
Cdd:PRK11288 353 NISARRHHLRAGClINNRWEAENADRFIRSLNIKTPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAK 432
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2127793354 204 KQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVI 246
Cdd:PRK11288 433 HEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
49-249 |
8.78e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 8.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 49 GKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAG-FETADNGQIVLDDQDVT-------------QVPAEQRHvntv 114
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKPVKirnpqqaiaqgiaMVPEDRKR---- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 115 fqsYALFPHMTVFENVA------FGLRMQKTPAAEIeprvMDALRMVRLEKMAQRKPHQ----LSGGQQQRIAIARAVVN 184
Cdd:PRK13549 350 ---DGIVPVMGVGKNITlaaldrFTGGSRIDDAAEL----KTILESIQRLKVKTASPELaiarLSGGNQQKAVLAKCLLL 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 185 KPKVLLLDESLSALD-------YKLrkqmqieLKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQD 249
Cdd:PRK13549 423 NPKILILDEPTRGIDvgakyeiYKL-------INQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
44-244 |
1.10e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.75 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 44 SKSFDgkeIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIA----GFETADNGQIVLD----DQDVTQVPAEqrhVNTVF 115
Cdd:TIGR00956 71 TKTFD---ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDgitpEEIKKHYRGD---VVYNA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 116 QSYALFPHMTVFENVAFGLRMqKTPAAeiepRVMDALRMVRLEKMAQ---------------------RKphqLSGGQQQ 174
Cdd:TIGR00956 145 ETDVHFPHLTVGETLDFAARC-KTPQN----RPDGVSREEYAKHIADvymatyglshtrntkvgndfvRG---VSGGERK 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 175 RIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGIT-FIFVTHDQEEALSMSDRIIVMRDG 244
Cdd:TIGR00956 217 RVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTpLVAIYQCSQDAYELFDKVIVLYEG 287
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-240 |
1.49e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 30 KQQAGKPVVRLSGISKSFdgkeiiGNLNLDV-----NHGEFLTILGPSGCGKTTVLRMIAGFETADNGQiVLDDQDVTQV 104
Cdd:PRK13409 333 DESERETLVEYPDLTKKL------GDFSLEVeggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE-VDPELKISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 105 PaeqrhvntvfQSYALFPHMTVFENvafgLRMQKTPAAE--IEPRVMDALrmvRLEKMAQRKPHQLSGGQQQRIAIARAV 182
Cdd:PRK13409 406 P----------QYIKPDYDGTVEDL----LRSITDDLGSsyYKSEIIKPL---QLERLLDKNVKDLSGGELQRVAIAACL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 183 VNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDqeeaLSM----SDRIIV 240
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD----IYMidyiSDRLMV 526
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
48-246 |
3.37e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.44 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVpAEQRHVNTVFQSYAL---FPhm 124
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA-LQKNLVAYVPQSEEVdwsFP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 125 TVFENVAFGLR-----MQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALD 199
Cdd:PRK15056 95 VLVEDVVMMGRyghmgWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2127793354 200 YKLRKQMQIELKQLqRQLGITFIFVTHDQEEALSMSDRIIVMRDGVI 246
Cdd:PRK15056 175 VKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVL 220
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
38-239 |
4.42e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDdQDVTQVPAEQ---RHVNTv 114
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVARLQQdppRNVEG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 115 fqsyalfphmTVFENVAFGLRMQktpaAEIEPRVMDALRMV----------RLEKMAQRKPHQ----------------- 167
Cdd:PRK11147 82 ----------TVYDFVAEGIEEQ----AEYLKRYHDISHLVetdpseknlnELAKLQEQLDHHnlwqlenrinevlaqlg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 168 ---------LSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKlrkqmQIE-LKQLQRQLGITFIFVTHDQEEALSMSDR 237
Cdd:PRK11147 148 ldpdaalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE-----TIEwLEGFLKTFQGSIIFISHDRSFIRNMATR 222
|
..
gi 2127793354 238 II 239
Cdd:PRK11147 223 IV 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
37-258 |
9.82e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.69 E-value: 9.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 37 VVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQI-VLDdQDVtqvpAEQRHVNTVF 115
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLG-GDM----ADARHRRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 116 QSYA---------LFPHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKP 186
Cdd:NF033858 76 PRIAympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 187 KVLLLDESLSALDYKLRKQMQ--IELKQLQRQlGITFIFVTHDQEEALSMsDRIIVMRDGVIEQDGSPREIYEE 258
Cdd:NF033858 156 DLLILDEPTTGVDPLSRRQFWelIDRIRAERP-GMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLAR 227
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
68-204 |
1.31e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 63.35 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 68 ILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPaeQRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAeiepr 147
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--KPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAET----- 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 148 VMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRK 204
Cdd:PRK13541 104 LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
53-249 |
1.60e-11 |
|
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: 65.62 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 53 IGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAG-FETADNGQIVLDDQDV-TQVPAEQRHVNTVF-----QSYALFPHMT 125
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVdIRNPAQAIRAGIAMvpedrKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 126 VFENV------AFGLRMQKTPAAEiEPRVMDALRMVRLEKMAQRKP-HQLSGGQQQRIAIARAVVNKPKVLLLDESLSAL 198
Cdd:TIGR02633 356 VGKNItlsvlkSFCFKMRIDAAAE-LQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 199 DYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQD 249
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
33-231 |
2.74e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.04 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 33 AGKPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIagfeTADNGQIVLDD-------------- 98
Cdd:PRK10938 256 ANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI----TGDHPQGYSNDltlfgrrrgsgeti 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 99 QDVtqvpaeQRHVNTVFQSYalfpHM-----TVFENV-------AFGLRMQktpaaeieprVMDALRMVRLE-------- 158
Cdd:PRK10938 332 WDI------KKHIGYVSSSL----HLdyrvsTSVRNVilsgffdSIGIYQA----------VSDRQQKLAQQwldilgid 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 159 -KMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEA 231
Cdd:PRK10938 392 kRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
51-226 |
3.70e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.05 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 51 EIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQD----------------VTQVP---AEQRHV 111
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnlkdinlkwwrskigvVSQDPllfSNSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 112 NTVFQSYAL--FPHMTVFEN---------------------VAFGLRMQKTPAAEI-----------EPRVMDALRMV-- 155
Cdd:PTZ00265 479 NIKYSLYSLkdLEALSNYYNedgndsqenknkrnscrakcaGDLNDMSNTTDSNELiemrknyqtikDSEVVDVSKKVli 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 156 ---------RLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTH 226
Cdd:PTZ00265 559 hdfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
46-228 |
8.70e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 61.73 E-value: 8.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 46 SFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFE--TADNGQIVLDDQDVTQVPAEQRHVNTVFQSyalFPH 123
Cdd:PRK09580 10 SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFMA---FQY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 124 MTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQL---------------SGGQQQRIAIARAVVNKPKV 188
Cdd:PRK09580 87 PVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPEL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2127793354 189 LLLDESLSALDYKLRKQMQIELKQLqRQLGITFIFVTHDQ 228
Cdd:PRK09580 167 CILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQ 205
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
49-244 |
1.17e-10 |
|
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: 61.80 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 49 GKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIvlddqdvtqvpaeqRH---VNTVFQSYALFPHmT 125
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--------------KHsgrISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 126 VFENVAFGLRMQktpaaeiEPRVMDALRMVRLEKMAQRKPHQ-----------LSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:cd03291 114 IKENIIFGVSYD-------EYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2127793354 195 LSALDYKLRKQMqIELKQLQRQLGITFIFVTHDQEEaLSMSDRIIVMRDG 244
Cdd:cd03291 187 FGYLDVFTEKEI-FESCVCKLMANKTRILVTSKMEH-LKKADKILILHEG 234
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
52-263 |
2.42e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.69 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 52 IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQ--VPAEQRHVNTVFQSYALFPHMtvfen 129
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFSGT----- 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 130 vafgLRMQKTPAAE-IEPRVMDALRMVRLEKMAQRKPHQL-----------SGGQQQRIAIARAVVNKPKVLLLDESLSA 197
Cdd:PLN03232 1326 ----VRFNIDPFSEhNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 198 LDYKLRKQMQIELKQLQRQlgITFIFVTHDQEEALSmSDRIIVMRDGVIEQDGSPREIYEEPKNLF 263
Cdd:PLN03232 1402 VDVRTDSLIQRTIREEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
56-278 |
2.65e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.36 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 56 LNLDVNHGEFLTILGPSGCGKTTVLRMIAGFeTADNGQIV-----LDDQDVTQVPAEQRH------VNTVFQ--SYALFP 122
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTadrmrFDDIDLLRLSPRERRklvghnVSMIFQepQSCLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 123 HmtvfENVAFGLrMQKTPAAEIEPRVMDAL-----RMVRL---------EKMAQRKPHQLSGGQQQRIAIARAVVNKPKV 188
Cdd:PRK15093 105 S----ERVGRQL-MQNIPGWTYKGRWWQRFgwrkrRAIELlhrvgikdhKDAMRSFPYELTEGECQKVMIAIALANQPRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 189 LLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLFVARFI 268
Cdd:PRK15093 180 LIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQALI 259
|
250
....*....|
gi 2127793354 269 GEINVFNATM 278
Cdd:PRK15093 260 RAIPDFGSAM 269
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
52-258 |
3.23e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 62.27 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 52 IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAE--QRHVNTVFQSYALFphmtvfen 129
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHdlRFKITIIPQDPVLF-------- 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 130 vAFGLRMQKTPAAEI-EPRVMDALRMVRLEKMAQRKP----HQ-------LSGGQQQRIAIARAVVNKPKVLLLDESLSA 197
Cdd:TIGR00957 1373 -SGSLRMNLDPFSQYsDEEVWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 198 LDYKLRKQMQIELK-QLQrqlGITFIFVTHDQEEALSMSdRIIVMRDGVIEQDGSPREIYEE 258
Cdd:TIGR00957 1452 VDLETDNLIQSTIRtQFE---DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
46-245 |
7.14e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.08 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 46 SFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIvlddqdvtqvpaeqRHVNTVF---QSYALFP 122
Cdd:TIGR01271 435 SLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--------------KHSGRISfspQTSWIMP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 123 HmTVFENVAFGLRMQktpaaeiEPRVMDALRMVRLEKMAQRKPHQ-----------LSGGQQQRIAIARAVVNKPKVLLL 191
Cdd:TIGR01271 501 G-TIKDNIIFGLSYD-------EYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2127793354 192 DESLSALDYKLRKQMqIELKQLQRQLGITFIFVTHDQEEaLSMSDRIIVMRDGV 245
Cdd:TIGR01271 573 DSPFTHLDVVTEKEI-FESCLCKLMSNKTRILVTSKLEH-LKKADKILLLHEGV 624
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-248 |
7.60e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.57 E-value: 7.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 27 LNAKQQAGKPVVRLSGISKSFDGKEIIG-------NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQ 99
Cdd:PRK09700 246 LQNRFNAMKENVSNLAHETVFEVRNVTSrdrkkvrDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 100 DVT-QVP-----------AEQRHVNTVFQSYALFPHMTVFENV-------AFGLRMQKTpaaeiEPRVMDALRmvrleKM 160
Cdd:PRK09700 326 DISpRSPldavkkgmayiTESRRDNGFFPNFSIAQNMAISRSLkdggykgAMGLFHEVD-----EQRTAENQR-----EL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 161 AQRKPH-------QLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKqmqiELKQLQRQL---GITFIFVTHDQEE 230
Cdd:PRK09700 396 LALKCHsvnqnitELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKA----EIYKVMRQLaddGKVILMVSSELPE 471
|
250
....*....|....*...
gi 2127793354 231 ALSMSDRIIVMRDGVIEQ 248
Cdd:PRK09700 472 IITVCDRIAVFCEGRLTQ 489
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
40-227 |
1.30e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 40 LSGISKSFDG-KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIvlddqdvtqVPAEQRHVNTVFQSY 118
Cdd:PRK11819 9 MNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA---------RPAPGIKVGYLPQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 119 ALFPHMTVFENVAFGlrMQKTPAA-----EI-----EPRV-MDAL--RMVRLEK-----------------M-AQRKPH- 166
Cdd:PRK11819 80 QLDPEKTVRENVEEG--VAEVKAAldrfnEIyaayaEPDAdFDALaaEQGELQEiidaadawdldsqleiaMdALRCPPw 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 167 -----QLSGGQQQRIAIARAVVNKPKVLLLDESLSALDyklrkqmqIE----LKQ-LQRQLGiTFIFVTHD 227
Cdd:PRK11819 158 dakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD--------AEsvawLEQfLHDYPG-TVVAVTHD 219
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
50-263 |
4.01e-09 |
|
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: 56.84 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKTTV----LRMIAGFEtadnGQIVLDDQDVTQVPAE--QRHVNTVFQSYALFPH 123
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRSRLSIILQDPILFSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 124 mtvfeNVAFGLRMQKTPAaeiEPRVMDALRMVRLEKMAQRKPHQL-----------SGGQQQRIAIARAVVNKPKVLLLD 192
Cdd:cd03288 110 -----SIRFNLDPECKCT---DDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 193 ESLSALDyklrkqMQIElKQLQRQLGITF-----IFVTHDQEEALSmSDRIIVMRDGVIEQDGSPREIYEEPKNLF 263
Cdd:cd03288 182 EATASID------MATE-NILQKVVMTAFadrtvVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
33-255 |
4.11e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.82 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 33 AGKPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGK------TTVLRMIAGFETADNGQIVLDDQDVTQVPA 106
Cdd:NF000106 9 GARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**rgalpAHV*GPDAGRRPWRF*TWCANRRALRRTIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 107 EQRHVNTVFQSyalfpHMTVFENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKP 186
Cdd:NF000106 89 *HRPVR*GRRE-----SFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2127793354 187 KVLLLDESLSALDYKLRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI 255
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-229 |
4.34e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 28 NAKQQ------AGKPVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIvlddqdv 101
Cdd:PRK11147 304 TAKMQveeasrSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 102 tqvpaeqrHVNT-----VFQSY--ALFPHMTVFENVAFGlrmQKTPAAEIEPR-VMDALRMVRLEKMAQRKP-HQLSGGQ 172
Cdd:PRK11147 377 --------HCGTklevaYFDQHraELDPEKTVMDNLAEG---KQEVMVNGRPRhVLGYLQDFLFHPKRAMTPvKALSGGE 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 173 QQRIAIARAVVNKPKVLLLDESLSALDyklrkqmqIELKQLQRQL-----GiTFIFVTHDQE 229
Cdd:PRK11147 446 RNRLLLARLFLKPSNLLILDEPTNDLD--------VETLELLEELldsyqG-TVLLVSHDRQ 498
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
63-290 |
1.60e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.07 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 63 GEFLTILGPSGCGKTTVLRMIAG--------FETADNGQIVLDD------QD-VTQVPAEQRHVNTVFQSYALFPHmTVF 127
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGklkpnlgkFDDPPDWDEILDEfrgselQNyFTKLLEGDVKVIVKPQYVDLIPK-AVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 128 ENVafGLRMQKTPAAEIEPRVMDALRmvrLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQ 207
Cdd:cd03236 105 GKV--GELLKKKDERGKLDELVDQLE---LRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 208 IELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRD-----GVIEQDGSPRE-IyeepkNLFVARFIGEINVfnatmleR 281
Cdd:cd03236 180 RLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLYGepgayGVVTLPKSVREgI-----NEFLDGYLPTENM-------R 246
|
....*....
gi 2127793354 282 IDEKRIRAE 290
Cdd:cd03236 247 FREESIEFE 255
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-199 |
2.06e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.02 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 34 GKPVVRLSGISKSFDGKEII-GNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGfETADNGQIVLDDQDVTQVPAEQRHVN 112
Cdd:PLN03073 505 GPPIISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISG-ELQPSSGTVFRSAKVRMAVFSQHHVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 113 TV-FQSYALFPHMTVFEnvafGLRMQKTPAAEIEPRVMDALRmvrLEKMaqrkpHQLSGGQQQRIAIARAVVNKPKVLLL 191
Cdd:PLN03073 584 GLdLSSNPLLYMMRCFP----GVPEQKLRAHLGSFGVTGNLA---LQPM-----YTLSGGQKSRVAFAKITFKKPHILLL 651
|
....*...
gi 2127793354 192 DESLSALD 199
Cdd:PLN03073 652 DEPSNHLD 659
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
53-244 |
6.88e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 53 IGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQRhVNTVF-------QSYALFPHMT 125
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEA-INHGFalvteerRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 126 V-FENVAFGLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQ------LSGGQQQRIAIARAVVNKPKVLLLDESLSAL 198
Cdd:PRK10982 343 IgFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2127793354 199 DYKLRKQM-QIELKQLQRQLGItfIFVTHDQEEALSMSDRIIVMRDG 244
Cdd:PRK10982 423 DVGAKFEIyQLIAELAKKDKGI--IIISSEMPELLGITDRILVMSNG 467
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
59-240 |
8.76e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.80 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 59 DVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDdqdvtqvpaeqrhvntvfqsyalfphmtvfenvafglrmQK 138
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD---------------------------------------GI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 139 TPAaeIEPRVMDalrmvrlekmaqrkphqLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLG 218
Cdd:cd03222 62 TPV--YKPQYID-----------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|..
gi 2127793354 219 ITFIFVTHDQEEALSMSDRIIV 240
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHV 144
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
53-287 |
1.61e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.36 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 53 IGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIvlddqDVTQVPAeqrhvnTVFQSYALFPHMTVFENVAF 132
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAA------LIAISSGLNGQLTGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 133 -GLRM--QKTPAAEIEPRVMDalrMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIE 209
Cdd:PRK13545 109 kGLMMglTKEKIKEIIPEIIE---FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127793354 210 LKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEEpknlfVARFIGEINVFNATMLERIDEKRI 287
Cdd:PRK13545 186 MNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH-----YDEFLKKYNQMSVEERKDFREEQI 257
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
50-199 |
5.27e-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: 49.55 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 50 KEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETAD--NGQIVLDDQDVTqvPAEQRHVNTVFQSYALFPHMTVF 127
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLD--KNFQRSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 128 ENVAFglrmqktpAAeieprvmdALRMVRLEkmaQRKphqlsggqqqRIAIARAVVNKPKVLLLDESLSALD 199
Cdd:cd03232 98 EALRF--------SA--------LLRGLSVE---QRK----------RLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
60-263 |
6.16e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.70 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 60 VNHGEFLTILGPSGCGKTTVL----RMIagfETAdNGQIVLDDQDVTQVPAEQ--RHVNTVFQSYALFPHmTVFENV-AF 132
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLltfmRMV---EVC-GGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVRQNVdPF 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 133 glrMQKTPAaeiepRVMDALRMVRL-EKMA----------QRKPHQLSGGQQQRIAIARAVVNK-PKVLLLDESLSALDY 200
Cdd:PTZ00243 1408 ---LEASSA-----EVWAALELVGLrERVAsesegidsrvLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDP 1479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127793354 201 KLRKQMQIELkqLQRQLGITFIFVTHdQEEALSMSDRIIVMRDGVIEQDGSPREIYEEPKNLF 263
Cdd:PTZ00243 1480 ALDRQIQATV--MSAFSAYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
312-391 |
9.16e-07 |
|
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: 46.07 E-value: 9.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 312 VLLRPEDLRIEEIKEseekGIVGHVTERTYKGMTLDSVIQLDSGMRVMVSEFFNEDDPdvdHSLGQKVAITWVESWEVVL 391
Cdd:pfam08402 1 LAIRPEKIRLAAAAN----GLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHARP---PAPGDRVGLGWDPEDAHVL 73
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
38-229 |
3.98e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIA-----GFETadNGQIVLDDQDVT--QVPAEQRH 110
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGIPK--NCQILHVEQEVVgdDTTALQCV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 111 VNTVFQSYALFP--------HMTVFENVAFGLRMQKTPAAEIEPRVMDALRMV--RLE---------------------- 158
Cdd:PLN03073 256 LNTDIERTQLLEeeaqlvaqQRELEFETETGKGKGANKDGVDKDAVSQRLEEIykRLElidaytaearaasilaglsftp 335
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127793354 159 KMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRqlgiTFIFVTHDQE 229
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSHARE 402
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-244 |
4.68e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.83 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 38 VRLSGIsKSFDGKEIIgnlnlDVNHGEFLtILGPSGCGKTTVLRMI--AGF-ETADNGQIVLDDQDVTQVPAEQRHVNTV 114
Cdd:cd03240 4 LSIRNI-RSFHERSEI-----EFFSPLTL-IVGQNGAGKTTIIEALkyALTgELPPNSKGGAHDPKLIREGEVRAQVKLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 115 FQS-----YALFPHMTVFENVAFglrmqkTPAAEIeprvmDALrmvrLEKMAQRkphqLSGGQQQ------RIAIARAVV 183
Cdd:cd03240 77 FENangkkYTITRSLAILENVIF------CHQGES-----NWP----LLDMRGR----CSGGEKVlasliiRLALAETFG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 184 NKPKVLLLDESLSALD-----YKLRKQMQIELKQLQRQLGItfifVTHDQEEALSMSDRIIVMRDG 244
Cdd:cd03240 138 SNCGILALDEPTTNLDeenieESLAEIIEERKSQKNFQLIV----ITHDEELVDAADHIYRVEKDG 199
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
48-212 |
8.38e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.98 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADnGQIVLDDQDVTQVPAEQRHvntvfQSYALFPHMTVF 127
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWR-----KAFGVIPQKVFI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 128 ENVAFglRMQKTPAAEIEP----RVMDAlrmVRLEKMAQRKPHQ-----------LSGGQQQRIAIARAVVNKPKVLLLD 192
Cdd:TIGR01271 1304 FSGTF--RKNLDPYEQWSDeeiwKVAEE---VGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLD 1378
|
170 180
....*....|....*....|
gi 2127793354 193 ESLSALDYKLRKQMQIELKQ 212
Cdd:TIGR01271 1379 EPSAHLDPVTLQIIRKTLKQ 1398
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
63-244 |
8.59e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 63 GEFLTILGPSGCGKTTVLRMIAgfETADNGQIVLDDQDVTQVPAE---QRHVNTVFQSYALFPHMTVFENVAFGLRM--- 136
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGRPLDssfQRSIGYVQQQDLHLPTSTVRESLRFSAYLrqp 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 137 QKTPAAEIEPRVMDALRMVRLEKMAQR---KPHQ-LSGGQQQRIAIARAVVNKPKVLL-LDESLSALDyklrKQMQIELK 211
Cdd:TIGR00956 867 KSVSKSEKMEYVEEVIKLLEMESYADAvvgVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD----SQTAWSIC 942
|
170 180 190
....*....|....*....|....*....|....*..
gi 2127793354 212 QLQRQLGIT--FIFVTHDQEEALSMS--DRIIVMRDG 244
Cdd:TIGR00956 943 KLMRKLADHgqAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
52-242 |
1.31e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.04 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 52 IIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAgfetadngqivlddqdvtqvpaeqrhvntvfqsYALFPHMTVFENVA 131
Cdd:cd03227 10 YFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LALGGAQSATRRRS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 132 FGLRMQKTPAAEIEPRVMDalrmvrlekmaqrkpHQLSGGQQQRIAIARAVVN---KPKVL-LLDESLSALD-YKLRKQM 206
Cdd:cd03227 57 GVKAGCIVAAVSAELIFTR---------------LQLSGGEKELSALALILALaslKPRPLyILDEIDRGLDpRDGQALA 121
|
170 180 190
....*....|....*....|....*....|....*.
gi 2127793354 207 QIELKQLQRQLgiTFIFVTHDQEEALsMSDRIIVMR 242
Cdd:cd03227 122 EAILEHLVKGA--QVIVITHLPELAE-LADKLIHIK 154
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
53-241 |
2.48e-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: 44.62 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 53 IGNLNLDVNHGEFLTILGPSGCGKTTVLRmiAGFETADNGQIVLDDQdvtqvpaeqrhvntvfqsyALFPHMTVFenvaf 132
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARLISFLP-------------------KFSRNKLIF----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 133 glrmqktpaaeieprvMDALRmvRLEKMA------QRKPHQLSGGQQQRIAIAR--AVVNKPKVLLLDESLSALDYKLRK 204
Cdd:cd03238 65 ----------------IDQLQ--FLIDVGlgyltlGQKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|....*..
gi 2127793354 205 QMQIELKQLqRQLGITFIFVTHDqEEALSMSDRIIVM 241
Cdd:cd03238 127 QLLEVIKGL-IDLGNTVILIEHN-LDVLSSADWIIDF 161
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
63-227 |
3.81e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 63 GEFLTILGPSGCGKTTVLRMIAG--------FETADNGQIVLDdqdvtqvpaeqRHVNTVFQSYalfphmtvFENVAFG- 133
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVLK-----------RFRGTELQNY--------FKKLYNGe 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 134 LR-MQKTPAAEIEPRVM-----DALRMV-------------RLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDES 194
Cdd:PRK13409 160 IKvVHKPQYVDLIPKVFkgkvrELLKKVdergkldevverlGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|...
gi 2127793354 195 LSALDYKLRKQMQIELKQLQRqlGITFIFVTHD 227
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAE--GKYVLVVEHD 270
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
36-247 |
4.33e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 36 PVVRLSGISKSFDGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLddqdvtqvpAEQRHVNTVF 115
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGIKLGYFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 116 QsyalfpHMTVFenvafgLRMQKTP---AAEIEPRVMD-ALR------MVRLEKMAQrKPHQLSGGQQQRIAIARAVVNK 185
Cdd:PRK10636 382 Q------HQLEF------LRADESPlqhLARLAPQELEqKLRdylggfGFQGDKVTE-ETRRFSGGEKARLVLALIVWQR 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127793354 186 PKVLLLDESLSALDYKLRKQMQIELKQLQRQLgitfIFVTHDQEEALSMSDRIIVMRDGVIE 247
Cdd:PRK10636 449 PNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
63-227 |
6.55e-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: 45.16 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 63 GEFLTILGPSGCGKTTVLRMIAGFETADNGQIvlddqdvtQVPAEQRHVNTVFQSYALFPHmtvFENVAFG-LRM-QKTP 140
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEVLKRFRGTELQDY---FKKLANGeIKVaHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 141 AAEIEPRVMD--------------ALRMVR----LEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKL 202
Cdd:COG1245 168 YVDLIPKVFKgtvrellekvdergKLDELAeklgLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180
....*....|....*....|....*
gi 2127793354 203 RKQMQIELKQLQRQlGITFIFVTHD 227
Cdd:COG1245 248 RLNVARLIRELAEE-GKYVLVVEHD 271
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
56-290 |
7.42e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 56 LNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVP-AEQRHVNTVF-QSYALFPHmtvfeNVAFG 133
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGlMDLRKVLGIIpQAPVLFSG-----TVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 134 LrmqkTPAAE-IEPRVMDALRMVRLEKMAQRKPHQL-----------SGGQQQRIAIARAVVNKPKVLLLDESLSALDYK 201
Cdd:PLN03130 1333 L----DPFNEhNDADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVDVR 1408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 202 ----LRKQMQIELKqlqrqlGITFIFVTHDQEEALSmSDRIIVMRDGVIEQDGSPREIYEEPKNLFvARFIGEINVFNAT 277
Cdd:PLN03130 1409 tdalIQKTIREEFK------SCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEGSAF-SKMVQSTGAANAQ 1480
|
250
....*....|....*..
gi 2127793354 278 MLERI----DEKRIRAE 290
Cdd:PLN03130 1481 YLRSLvfggDEDRLARE 1497
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
57-258 |
9.77e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.24 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 57 NLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIVLDDQDVTQVPAEQ---------RHVNTVFQSyalfphmtVF 127
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQlqklvsdewQRNNTDMLS--------PG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 128 ENvAFGlrmqKTPAAEIEPRVMDALRMVRLEK------MAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYK 201
Cdd:PRK10938 95 ED-DTG----RTTAEIIQDEVKDPARCEQLAQqfgitaLLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 202 LRKQMQIELKQLQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEE 258
Cdd:PRK10938 170 SRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
48-258 |
1.56e-04 |
|
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: 42.92 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 48 DGKEIIGNLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADnGQIVLDDQDVTQVPAEQRHvntvfQSYALFPHMTVF 127
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWR-----KAFGVIPQKVFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 128 ENVAFglRMQKTPAAE-IEPRVMDALRMVRLEKMAQRKPHQL-----------SGGQQQRIAIARAVVNKPKVLLLDESL 195
Cdd:cd03289 89 FSGTF--RKNLDPYGKwSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127793354 196 SALDyklRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREIYEE 258
Cdd:cd03289 167 AHLD---PITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
168-262 |
1.91e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.85 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 168 LSGGQQQRIAIARAVVNK-PKVL-LLDESLSALDYKLRKQMQIELKQLqRQLGITFIFVTHDqEEALSMSDRIIVMRDG- 244
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD-EDTIRAADYVIDIGPGa 566
|
90 100
....*....|....*....|....
gi 2127793354 245 ------VIEQdGSPREIYEEPKNL 262
Cdd:TIGR00630 567 gehggeVVAS-GTPEEILANPDSL 589
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
63-199 |
2.64e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.30 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 63 GEFLTILGPSGCGKTTVLRMIAGFETadnGQIVLDDQDVTQVPAEQ----RHVNTVFQSYALFPHMTVFENVAFG--LRM 136
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKT---GGYIEGDIRISGFPKKQetfaRISGYCEQNDIHSPQVTVRESLIYSafLRL 982
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2127793354 137 QKTPAAEIEPR----VMDALRMVRLEKMAQRKP--HQLSGGQQQRIAIARAVVNKPKVLLLDESLSALD 199
Cdd:PLN03140 983 PKEVSKEEKMMfvdeVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
55-286 |
6.74e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 55 NLNLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADNGQIvlddqdvtqvpaeQRH--VNTVFQSYALFPHMTVFENVAF 132
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-------------DRNgeVSVIAISAGLSGQLTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127793354 133 GLRMQKTPAAEIEPRVMDALRMVRLEKMAQRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQ 212
Cdd:PRK13546 109 KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYE 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2127793354 213 LQRQlGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGSPREI---YEEPKNLFVARFIGEINVFNatmlERIDEKR 286
Cdd:PRK13546 189 FKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVlpkYEAFLNDFKKKSKAEQKEFR----NKLDESR 260
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
168-241 |
2.08e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.16 E-value: 2.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2127793354 168 LSGGQQQRIAIARAVVNKPKVLL--LDESLSALDYKLRKQMQIELKQLqRQLGITFIFVTHDqEEALSMSDRIIVM 241
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHD-EDTIRAADHVIDI 211
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
67-104 |
5.17e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 37.08 E-value: 5.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2127793354 67 TILGPSGCGKTTVLRMIA---GFETADNGQIvlDDQDVTQV 104
Cdd:cd02020 3 AIDGPAGSGKSTVAKLLAkklGLPYLDTGGI--RTEEVGKL 41
|
|
| |
