|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-343 |
1.74e-176 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 493.44 E-value: 1.74e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 4 TAILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkhLSLE 83
Cdd:COG3839 2 ASLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV------TDLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 84 PFERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRT 163
Cdd:COG3839 72 PKDRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 164 PQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVA 243
Cdd:COG3839 152 PKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 244 GFIGTPSMNFLSAEIIK--------SIKKP---------NITIGIRPQDIEIRPPNKGIINAFVKLVEKIGDKYLVHVDY 306
Cdd:COG3839 232 GFIGSPPMNLLPGTVEGggvrlggvRLPLPaalaaaaggEVTLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVRL 311
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2500156532 307 RKQKIIIET---SNFSKEKEVSLFWPKEKMHFFDKN-GERI 343
Cdd:COG3839 312 GGQELVARVpgdTRLRPGDTVRLAFDPERLHLFDAEtGRRL 352
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-338 |
1.03e-139 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 400.24 E-value: 1.03e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkhL 80
Cdd:COG3842 1 MAMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV------T 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 SLEPFERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRAL 160
Cdd:COG3842 71 GLPPEKRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 161 VRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNT 240
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 241 FVAGFIGTpsMNFLSAEIIKSIKKP--------------------NITIGIRPQDIEIRPPNK-GIINAFVKLVEKIGDK 299
Cdd:COG3842 231 FVADFIGE--ANLLPGTVLGDEGGGvrtggrtlevpadaglaaggPVTVAIRPEDIRLSPEGPeNGLPGTVEDVVFLGSH 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2500156532 300 YLVHVDYRK-QKIIIETSN-----FSKEKEVSLFWPKEKMHFFDK 338
Cdd:COG3842 309 VRYRVRLGDgQELVVRVPNraalpLEPGDRVGLSWDPEDVVVLPA 353
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-344 |
6.23e-137 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 393.44 E-value: 6.23e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVKKifsTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfSDkkhlsLEP 84
Cdd:PRK11650 3 GLKLQAVRK---SYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-NE-----LEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 FERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTP 164
Cdd:PRK11650 74 ADRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 165 QVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVAG 244
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVAS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 245 FIGTPSMNFLSAEI--------------------IKSIKKPNITIGIRPQDIEIrPPNKGIINAFVKLVEKIGDKYLVHV 304
Cdd:PRK11650 234 FIGSPAMNLLDGRVsadgaafelaggialplgggYRQYAGRKLTLGIRPEHIAL-SSAEGGVPLTVDTVELLGADNLAHG 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2500156532 305 DYRKQKIIIETSNFSKEKE---VSLFWPKEKMHFFDKN-GERIE 344
Cdd:PRK11650 313 RWGGQPLVVRLPHQERPAAgstLWLHLPANQLHLFDADtGRRIE 356
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-228 |
9.39e-115 |
|
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: 331.53 E-value: 9.39e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfSDkkhlsLEPF 85
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TD-----LPPK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQ 165
Cdd:cd03301 71 DRDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTG 228
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-341 |
4.03e-112 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 330.84 E-value: 4.03e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 4 TAILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfSDkkhlsLE 83
Cdd:PRK11000 2 ASVTLRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-ND-----VP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 84 PFERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRT 163
Cdd:PRK11000 72 PAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 164 PQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVA 243
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 244 GFIGTPSMNFLSAEIIKS------IKKPN------------------ITIGIRPQdiEIRPPNKG--IINAFVKLVEKIG 297
Cdd:PRK11000 232 GFIGSPKMNFLPVKVTATaieqvqVELPNrqqvwlpvegrgvqvganMSLGIRPE--HLLPSDIAdvTLEGEVQVVEQLG 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2500156532 298 DKYLVHVDYR--KQKIIIETSNFSKEKEVSLF---WPKEKMHFFDKNGE 341
Cdd:PRK11000 310 NETQIHIQIPaiRQNLVYRQNDVVLVEEGATFaigLPPERCHLFREDGT 358
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-304 |
1.19e-109 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 323.64 E-value: 1.19e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDkkhlsLEPF 85
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN-----LPPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQ 165
Cdd:COG1118 74 ERRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVAGF 245
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARF 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 246 IGtpSMNFLSAEII--------------KSIKKPNITIGIRPQDIEI--RPPNKGIINAFVKLVEKIGDKYLVHV 304
Cdd:COG1118 234 LG--CVNVLRGRVIggqleadgltlpvaEPLPDGPAVAGVRPHDIEVsrEPEGENTFPATVARVSELGPEVRVEL 306
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-228 |
1.86e-109 |
|
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: 318.31 E-value: 1.86e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSdkkhlsLEPF 85
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG------VPPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQ 165
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTG 228
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
6-336 |
4.76e-109 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 322.72 E-value: 4.76e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKhLSLEPF 85
Cdd:NF040933 3 VRVENVTKIFKKGKKEVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASPGK-IIVPPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQ 165
Cdd:NF040933 82 DRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVAGF 245
Cdd:NF040933 162 VLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVARL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 246 IGtpSMNFLSAEII----------------KSIKKPNITIGIRPQDIEIRP----PNKGIIN---AFVKLVEKIGDKYLV 302
Cdd:NF040933 242 IG--DINLLEGKVEeeglvdgndlkiplpnPKLEAGEVIIGIRPEDIDISEsdmrLPPGFVEvgkGRVKVSSYAGGVFRV 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 2500156532 303 HVDY--RKQKIIIETSNFSKE--KEVSLFWPKEKMHFF 336
Cdd:NF040933 320 VVSPidDDSIEIIVNSDRPIEegEEVNLYVRPDKIKIF 357
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-247 |
2.14e-106 |
|
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: 311.09 E-value: 2.14e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkhLSLEPF 85
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI------TNLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQ 165
Cdd:cd03300 71 KRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVAGF 245
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADF 230
|
..
gi 2500156532 246 IG 247
Cdd:cd03300 231 IG 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-314 |
2.16e-97 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 293.39 E-value: 2.16e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVKKIFSTAKgrvlALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkKHL 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI----THV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 SLEpfERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRAL 160
Cdd:PRK09452 82 PAE--NRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 161 VRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNT 240
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 241 FVAGFIGtpSMNFLSAEIIKSIKKPNITIGIRPQDIEIRppnkgiinafVKLVEKIGDKylVHVDYRKQKIIIE 314
Cdd:PRK09452 240 FVARFIG--EINIFDATVIERLDEQRVRANVEGRECNIY----------VNFAVEPGQK--LHVLLRPEDLRVE 299
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-247 |
1.17e-91 |
|
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: 273.83 E-value: 1.17e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEp 84
Cdd:cd03296 2 SIEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE----DATDVPVQ- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 fERDVAMVFQSYALYPHMTVYQNMAF----PLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRAL 160
Cdd:cd03296 73 -ERNVGFVFQHYALFRHMTVFDNVAFglrvKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 161 VRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNT 240
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASP 231
|
....*..
gi 2500156532 241 FVAGFIG 247
Cdd:cd03296 232 FVYSFLG 238
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
8-300 |
6.66e-90 |
|
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: 273.45 E-value: 6.66e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSlePFER 87
Cdd:TIGR03265 7 IDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGR----DITRLP--PQKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 88 DVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVL 167
Cdd:TIGR03265 77 DYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 168 LMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVAGFIG 247
Cdd:TIGR03265 157 LLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 248 tpSMNFLSAEIIK----------------SIKKPN-ITIGIRPQDIEIRP--PNKGIINAFVKLVEKIGDKY 300
Cdd:TIGR03265 237 --EVNWLPGTRGGgsrarvggltlacapgLAQPGAsVRLAVRPEDIRVSPagNAANLLLARVEDMEFLGAFY 306
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-222 |
2.33e-88 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 266.18 E-value: 2.33e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkhl 80
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 slEPFERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRAL 160
Cdd:COG1116 76 --TGPGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 161 VRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-219 |
2.55e-84 |
|
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: 254.70 E-value: 2.55e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkhlslEPF 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV---------TGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQ 165
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALL 219
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-304 |
2.65e-82 |
|
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: 253.18 E-value: 2.65e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 40 ILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkhLSLEPFERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKK 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV------TNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 120 KKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITT 199
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 200 IYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVAGFIGTPSM-NFLSAE--------------------I 258
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVfEATVIErkseqvvlagvegrrcdiytD 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 259 IKSIKKPNITIGIRPQDIEIR--PPNKGiINAFVKLVEKI---GDKYLVHV 304
Cdd:TIGR01187 235 VPVEKDQPLHVVLRPEKIVIEeeDEANS-SNAIIGHVIDItylGMTLEVHV 284
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-247 |
4.69e-82 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 249.33 E-value: 4.69e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEpf 85
Cdd:TIGR00968 1 IEIANISKRF----GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQ----DATRVHAR-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQ 165
Cdd:TIGR00968 71 DRKIGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVAGF 245
Cdd:TIGR00968 151 VLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSF 230
|
..
gi 2500156532 246 IG 247
Cdd:TIGR00968 231 LG 232
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
25-298 |
6.13e-80 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 248.07 E-value: 6.13e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkhLSLEPFERDVAMVFQSYALYPHMTV 104
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDI------TNLPPEKRGIAYVYQNYMLFPHKTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 105 YQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEM 184
Cdd:NF040840 90 FENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 185 RVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVAGFIGTPSMNFLSAEI---IKS 261
Cdd:NF040840 170 IREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGVAEKggeGTI 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 262 IKKPNITI------------GIRPQDIEI--RPPNKGIINAFVKLVEKIGD 298
Cdd:NF040840 250 LDTGNIKIelpeekkgkvriGIRPEDITIstEKVKTSARNEFKGKVEEIED 300
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-314 |
1.77e-79 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 246.94 E-value: 1.77e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVVfsdkkH 79
Cdd:PRK11432 2 TQKNFVVLKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGEDVT-----H 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 80 LSLEpfERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRA 159
Cdd:PRK11432 73 RSIQ--QRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 160 LVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKN 239
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 240 TFVAGFIGTPSMnF---LSAEIIK----SIKKPN----------ITIGIRPQDIEIRPPNKGIINAFVKLVEKIGDKYLV 302
Cdd:PRK11432 231 RFMASFMGDANI-FpatLSGDYVDiygyRLPRPAafafnlpdgeCTVGVRPEAITLSEQGEESQRCTIKHVAYMGPQYEV 309
|
330
....*....|..
gi 2500156532 303 HVDYRKQKIIIE 314
Cdd:PRK11432 310 TVDWHGQELLLQ 321
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
8-248 |
3.12e-77 |
|
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: 237.23 E-value: 3.12e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFSTAKgrvlaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkhLSLEPFER 87
Cdd:cd03299 3 VENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI------TNLPPEKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 88 DVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVL 167
Cdd:cd03299 72 DISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 168 LMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVAGFIG 247
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
.
gi 2500156532 248 T 248
Cdd:cd03299 232 F 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-258 |
1.23e-74 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 234.59 E-value: 1.23e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEp 84
Cdd:PRK10851 2 SIEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT----DVSRLHAR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 fERDVAMVFQSYALYPHMTVYQNMAFPLKN----LKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRAL 160
Cdd:PRK10851 73 -DRKVGFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 161 VRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNT 240
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATR 231
|
250
....*....|....*...
gi 2500156532 241 FVAGFIGtpSMNFLSAEI 258
Cdd:PRK10851 232 FVLEFMG--EVNRLQGTI 247
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-222 |
2.57e-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: 227.46 E-value: 2.57e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsDKKHLSLEPF 85
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL--TDLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFPlknlkykkkkireqvikiaqmlrietllerkpaeLSGGQRQRVAIGRALVRTPQ 165
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-251 |
6.78e-72 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 228.18 E-value: 6.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFSTAkgrvLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFgdkvvfsDKKHLS-LEPFE 86
Cdd:PRK11607 22 IRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-------DGVDLShVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 87 RDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQV 166
Cdd:PRK11607 91 RPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 167 LLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVAGFI 246
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
|
....*
gi 2500156532 247 GTPSM 251
Cdd:PRK11607 251 GSVNV 255
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-234 |
2.37e-71 |
|
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: 226.14 E-value: 2.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 23 LALDrINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLEPFERDVAMVFQSYALYPHM 102
Cdd:COG4148 14 FTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQEARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 103 TVYQNMAFPLKNLKYKKKKIR-EQVIkiaQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLR 181
Cdd:COG4148 93 SVRGNLLYGRKRAPRAERRISfDEVV---ELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 182 AEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:COG4148 170 AEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
27-248 |
4.76e-71 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 221.17 E-value: 4.76e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 27 RINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsdkKHLSLEPFERDVAMVFQSYALYPHMTVYQ 106
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ------DLTALPPAERPVSMLFQENNLFPHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 107 NMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRV 186
Cdd:COG3840 91 NIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 187 ELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVAGFIGT 248
Cdd:COG3840 171 LVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-224 |
4.78e-71 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 220.69 E-value: 4.78e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 3 KTAILVRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVV--FSDKKhl 80
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIssLSERE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 sLEPFERD-VAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRA 159
Cdd:COG1136 80 -LARLRRRhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 160 LVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQtEAMTLGDRIALLKEGVL 224
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-228 |
1.26e-70 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 219.47 E-value: 1.26e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIK---PGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLEPFERDVAMVFQSYALYPH 101
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 102 MTVYQNMAFplKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLR 181
Cdd:cd03297 90 LNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2500156532 182 AEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTG 228
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-247 |
2.01e-70 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 221.89 E-value: 2.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstaKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkhLSLEPF 85
Cdd:COG1125 2 IEFENVTKRY---PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDI------RDLDPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 E--RDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQM--LRIETLLERKPAELSGGQRQRVAIGRALV 161
Cdd:COG1125 73 ElrRRIGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELvgLDPEEYRDRYPHELSGGQQQRVGVARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 162 RTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTF 241
Cdd:COG1125 153 ADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDF 232
|
....*.
gi 2500156532 242 VAGFIG 247
Cdd:COG1125 233 VADFVG 238
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-224 |
3.64e-70 |
|
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: 218.51 E-value: 3.64e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVV--FSDKKhlsLE 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIskLSEKE---LA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 84 PFERD-VAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVR 162
Cdd:cd03255 78 AFRRRhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 163 TPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMtLGDRIALLKEGVL 224
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-247 |
5.81e-70 |
|
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: 218.71 E-value: 5.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstaKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEPF 85
Cdd:cd03295 1 IEFENVTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE----DIREQDPVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIE--TLLERKPAELSGGQRQRVAIGRALVRT 163
Cdd:cd03295 74 RRKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 164 PQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVA 243
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVA 233
|
....
gi 2500156532 244 GFIG 247
Cdd:cd03295 234 EFVG 237
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
6-246 |
8.77e-70 |
|
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: 219.05 E-value: 8.77e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFSTAKGRVLALDR--------------------INLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGE 65
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAFKLLAkgkskeeilkktgqtvgvndVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 66 IFFGDKVV--FSDKKHLSLEpfERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKP 143
Cdd:cd03294 81 VLIDGQDIaaMSRKELRELR--RKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 144 AELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGV 223
Cdd:cd03294 159 DELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGR 238
|
250 260
....*....|....*....|...
gi 2500156532 224 LQQTGSPDELFYCPKNTFVAGFI 246
Cdd:cd03294 239 LVQVGTPEEILTNPANDYVREFF 261
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-239 |
1.62e-66 |
|
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: 210.04 E-value: 1.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkKHLSLEP 84
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV----TRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 FERDVAMVFQSY--ALYPHMTVYQNMAFPLKNLKykkkkIREQVIKIAQMLRI----ETLLERKPAELSGGQRQRVAIGR 158
Cdd:COG1124 77 FRRRVQMVFQDPyaSLHPRHTVDRILAEPLRIHG-----LPDREERIAELLEQvglpPSFLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 159 ALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPK 238
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
.
gi 2500156532 239 N 239
Cdd:COG1124 232 H 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-239 |
1.18e-63 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 202.15 E-value: 1.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHlsLEPF 85
Cdd:COG1126 2 IEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKD--INKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKkkiREQVIKIAqmlriETLLER---------KPAELSGGQRQRVAI 156
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMS---KAEAEERA-----MELLERvgladkadaYPAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 157 GRALVRTPQVLLMDEPLSNLDAQLRAEMrveLKVlIKDL---GITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEV---LDV-MRDLakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
....*.
gi 2500156532 234 FYCPKN 239
Cdd:COG1126 224 FENPQH 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-234 |
2.25e-63 |
|
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: 201.75 E-value: 2.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVV--FSDKK 78
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItgLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 79 hlsLEPFERDVAMVFQSYALYPHMTVYQNMAFP-LKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIG 157
Cdd:COG1127 77 ---LYELRRRIGMLFQGGALFDSLTVFENVAFPlREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 158 RALVRTPQVLLMDEPLSNLDAQlraeMRVELKVLIKDL----GITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPI----TSAVIDELIRELrdelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
.
gi 2500156532 234 F 234
Cdd:COG1127 230 L 230
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
3-257 |
2.90e-62 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 203.41 E-value: 2.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 3 KTAILVRNVKKIFS--------------------TAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPT 62
Cdd:COG4175 1 MPKIEVRNLYKIFGkrperalklldqgkskdeilEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 63 EGEIFFGDKVVFS-DKKHLsLEPFERDVAMVFQSYALYPHMTVYQNMAFPLKnlkykkkkIR----EQVIKIAQmlriET 137
Cdd:COG4175 81 AGEVLIDGEDITKlSKKEL-RELRRKKMSMVFQHFALLPHRTVLENVAFGLE--------IQgvpkAERRERAR----EA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 138 L----LE----RKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEA 209
Cdd:COG4175 148 LelvgLAgwedSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEA 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2500156532 210 MTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVAGFI-GTPSMNFLSAE 257
Cdd:COG4175 228 LRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVeDVDRSKVLTAG 276
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-234 |
7.73e-62 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 205.91 E-value: 7.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIF-STAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfSDKKHLSLEPFE 86
Cdd:COG1123 263 VRNLSKRYpVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDL-TKLSRRSLRELR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 87 RDVAMVFQ--SYALYPHMTVYQNMAFPLKNLKYKKKKIREQviKIAQMLRI----ETLLERKPAELSGGQRQRVAIGRAL 160
Cdd:COG1123 342 RRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRE--RVAELLERvglpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 161 VRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
18-247 |
2.83e-61 |
|
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: 200.46 E-value: 2.83e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 18 AKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVVFSDKKHLSlEPFERDVAMVFQSY 96
Cdd:TIGR01186 2 KTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIdGENIMKQSPVELR-EVRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 97 ALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNL 176
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 177 DAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVAGFIG 247
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-233 |
1.23e-59 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 191.82 E-value: 1.23e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSlepf 85
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 eRDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQ 165
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMRVELKVLiKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-228 |
1.33e-59 |
|
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: 191.57 E-value: 1.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLsLEPFER 87
Cdd:cd03257 4 VKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRL-RKIRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 88 DVAMVFQSY--ALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRI---ETLLERKPAELSGGQRQRVAIGRALVR 162
Cdd:cd03257 83 EIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 163 TPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTG 228
Cdd:cd03257 163 NPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-245 |
5.66e-59 |
|
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: 190.02 E-value: 5.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFStakGRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHlSLEPF 85
Cdd:cd03261 1 IELRGLTKSFG---GRTV-LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEA-ELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFP-LKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTP 164
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENVAFPlREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 165 QVLLMDEPLSNLDAqLRAEMRVELKVLIKD-LGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPkNTFVA 243
Cdd:cd03261 156 ELLLYDEPTAGLDP-IASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVR 233
|
..
gi 2500156532 244 GF 245
Cdd:cd03261 234 QF 235
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-233 |
4.80e-58 |
|
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: 191.86 E-value: 4.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDrINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLEPFERDVAMVFQSYALYPHMT 103
Cdd:TIGR02142 13 SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 104 VYQNMAFPLKNLKYKKKKIREQviKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAE 183
Cdd:TIGR02142 92 VRGNLRYGMKRARPSERRISFE--RVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2500156532 184 MRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-234 |
3.92e-56 |
|
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: 182.53 E-value: 3.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKkiFSTAKGRVlALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkKHLSLEPF 85
Cdd:COG1122 1 IELENLS--FSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI----TKKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQsyalYP-----HMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRAL 160
Cdd:COG1122 74 RRKVGLVFQ----NPddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 161 VRTPQVLLMDEPLSNLDAQLRAEMRVELKVLiKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-222 |
5.73e-56 |
|
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: 181.51 E-value: 5.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKkiFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkKHLSLEPFER 87
Cdd:cd03225 2 LKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL----TKLSLKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 88 DVAMVFQsyalYP-HM----TVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVR 162
Cdd:cd03225 76 KVGLVFQ----NPdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 163 TPQVLLMDEPLSNLDAQLRAEMRVELKVLiKDLGITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-264 |
1.28e-55 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 184.90 E-value: 1.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVV--FSDKKhlsLE 83
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtaLSERE---LR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 84 PFERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREqvikiaqmlRIETLLE---------RKPAELSGGQRQRV 154
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRK---------RVAELLElvglsdkadAYPSQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 155 AIGRALVRTPQVLLMDEPLSNLDAQ-----LRaemrvelkvLIKD----LGITTIYVTHDqteaM----TLGDRIALLKE 221
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPEttrsiLD---------LLKDinreLGLTIVLITHE----MdvvrRICDRVAVLEN 216
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2500156532 222 GVLQQTGSPDELFYCPKNTFVAGFIGTPSMNFLSAEIIKSIKK 264
Cdd:COG1135 217 GRIVEQGPVLDVFANPQSELTRRFLPTVLNDELPEELLARLRE 259
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-238 |
1.89e-55 |
|
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: 181.24 E-value: 1.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHlSLEPF 85
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGK-ELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQ 165
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPK 238
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-224 |
7.89e-55 |
|
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: 178.88 E-value: 7.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFSTAKgrvlALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLEpf 85
Cdd:cd03262 1 IEIKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINEL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKkkiREQVIKIA-QMLRIETLLERK---PAELSGGQRQRVAIGRALV 161
Cdd:cd03262 75 RQKVGMVFQQFNLFPHLTVLENITLAPIKVKGMS---KAEAEERAlELLEKVGLADKAdayPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 162 RTPQVLLMDEPLSNLDAQLRAEMrveLKVlIKDL---GITTIYVTHDQTEAMTLGDRIALLKEGVL 224
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEV---LDV-MKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-233 |
8.31e-54 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 176.70 E-value: 8.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 27 RINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFgdkvvfSDKKHLSLEPFERDVAMVFQSYALYPHMTVYQ 106
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL------NGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 107 NMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRV 186
Cdd:PRK10771 91 NIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2500156532 187 ELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
11-224 |
1.96e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 175.00 E-value: 1.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 11 VKKIFSTAKGRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSdkkhLSLEPFERDVA 90
Cdd:COG4619 3 LEGLSFRVGGKPI-LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA----MPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 91 MVFQSYALYPhMTVYQNMAFPLKNLKYKKKkiREQVIKIAQMLRI-ETLLERKPAELSGGQRQRVAIGRALVRTPQVLLM 169
Cdd:COG4619 78 YVPQEPALWG-GTVRDNLPFPFQLRERKFD--RERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 170 DEPLSNLDAQLRAemRVE--LKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVL 224
Cdd:COG4619 155 DEPTSALDPENTR--RVEelLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-238 |
3.01e-53 |
|
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: 183.18 E-value: 3.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 3 KTAILVRNVKkiFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPT---EGEIFFGDKvvfsDKKH 79
Cdd:COG1123 2 TPLLEVRDLS--VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGR----DLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 80 LSLEPFERDVAMVFQS--YALYPhMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIG 157
Cdd:COG1123 76 LSEALRGRRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 158 RALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCP 237
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
.
gi 2500156532 238 K 238
Cdd:COG1123 235 Q 235
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-228 |
2.44e-52 |
|
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: 172.35 E-value: 2.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 27 RINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFgdkvvfSDKKHLSLEPFERDVAMVFQSYALYPHMTVYQ 106
Cdd:TIGR01277 16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKV------NDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 107 NMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRV 186
Cdd:TIGR01277 90 NIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2500156532 187 ELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTG 228
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-225 |
7.55e-52 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 171.39 E-value: 7.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstaKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfSDKKHLSLEPF 85
Cdd:COG2884 2 IRFENVSKRY---PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL-SRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQ 165
Cdd:COG2884 78 RRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMrveLKVL--IKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQ 225
Cdd:COG2884 158 LLLADEPTGNLDPETSWEI---MELLeeINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-233 |
1.06e-51 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 171.78 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 4 TAILVRNVKKIFStakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHlSLE 83
Cdd:COG3638 1 PMLELRNLSKRYP---GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGR-ALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 84 PFERDVAMVFQSYALYPHMTVYQN--------MAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVA 155
Cdd:COG3638 77 RLRRRIGMIFQQFNLVPRLSVLTNvlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 156 IGRALVRTPQVLLMDEPLSNLDAQLrAE--MRVeLKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKT-ARqvMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
20-234 |
8.72e-51 |
|
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: 169.84 E-value: 8.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEPFERDVAMVFQSYALY 99
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGR----DLASLSRRELARRIAYVPQEPPAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 100 PHMTVYQNMA---FPLKNLKYKKKKI-REQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSN 175
Cdd:COG1120 88 FGLTVRELVAlgrYPHLGLFGRPSAEdREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSH 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 176 LD--AQLRAeMRVeLKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:COG1120 168 LDlaHQLEV-LEL-LRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-219 |
1.35e-50 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 169.66 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 4 TAILVRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSdkkhlsle 83
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 84 P-FERDVamVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVR 162
Cdd:COG4525 74 PgADRGV--VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 163 TPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALL 219
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
9-239 |
1.55e-49 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 166.04 E-value: 1.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 9 RNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLepFERD 88
Cdd:PRK09493 5 KNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL--IRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 89 VAMVFQSYALYPHMTVYQNMAF-PLKNLKYKKKKIREQVikiAQMLRIETLLERK---PAELSGGQRQRVAIGRALVRTP 164
Cdd:PRK09493 79 AGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQA---RELLAKVGLAERAhhyPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500156532 165 QVLLMDEPLSNLDAQLRAEMrveLKVLiKDL---GITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKN 239
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEV---LKVM-QDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-228 |
3.95e-49 |
|
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: 164.20 E-value: 3.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 27 RINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGeiffgdKVVFSDKKHLSLEPFERDVAMVFQSYALYPHMTVYQ 106
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSG------RVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 107 NMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRV 186
Cdd:cd03298 90 NVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2500156532 187 ELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTG 228
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-224 |
2.40e-48 |
|
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: 160.64 E-value: 2.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSlepf 85
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 eRDVAMVFQSYALYPHMTVYQNMafplknlkykkkkireqvikiaqmlrietllerkpaELSGGQRQRVAIGRALVRTPQ 165
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMRVELKVLIKDlGITTIYVTHDQTEAMTLGDRIALLKEGVL 224
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
6-216 |
1.69e-47 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 161.06 E-value: 1.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKhlslepf 85
Cdd:NF040729 2 LKIQNISKTFINNKKENEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGP------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 erDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKkkiREQVIKIAQMLRIETLLERK---PAELSGGQRQRVAIGRALVR 162
Cdd:NF040729 75 --DRGFVFQNYALFPWMTVKENIEYPMKQQKMPK---QEREKRLNELLEMAQLTGKEnlyPHQISGGMKQRTAVIRALAC 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 163 TPQVLLMDEPLSNLDAQLRAEMRVELK-VLIKDlGITTIYVTHDQTEAMTLGDRI 216
Cdd:NF040729 150 KPEVLLMDEPLGAVDFQMRQILQEELEsIWLKD-KTTVLMVTHDVDEAVYLSDRV 203
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
24-233 |
1.90e-47 |
|
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: 160.04 E-value: 1.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEE-----PTEGEIFFGDKVVFSDKKHLSLepFERDVAMVFQSYAL 98
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLE--LRRRVGMVFQKPNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 99 YPhMTVYQNMAFPLKNLKYKKKKIREQVIKIAqmLRIETLLER-----KPAELSGGQRQRVAIGRALVRTPQVLLMDEPL 173
Cdd:cd03260 93 FP-GSIYDNVAYGLRLHGIKLKEELDERVEEA--LRKAALWDEvkdrlHALGLSGGQQQRLCLARALANEPEVLLLDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 174 SNLDAqlRAEMRVELkvLIKDLG--ITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:cd03260 170 SALDP--ISTAKIEE--LIAELKkeYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-205 |
2.15e-47 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 159.57 E-value: 2.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEP---TEGEIFFGDKVVfsdkkhLSLEPFERDVAMVFQSY 96
Cdd:COG4136 13 GRPL-LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL------TALPAEQRRIGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 97 ALYPHMTVYQNMAFplknlkykkkKIREQVIKIAQMLRIETLLE---------RKPAELSGGQRQRVAIGRALVRTPQVL 167
Cdd:COG4136 86 LLFPHLSVGENLAF----------ALPPTIGRAQRRARVEQALEeaglagfadRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 2500156532 168 LMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHD 205
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-233 |
3.54e-47 |
|
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: 160.02 E-value: 3.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHlslepF 85
Cdd:COG4555 2 IEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-----A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQ 165
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMRVELKVLiKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-233 |
4.13e-47 |
|
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: 159.66 E-value: 4.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFStakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHlSLEPF 85
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGK-ALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQN--------MAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIG 157
Cdd:cd03256 77 RRQIGMIFQQFNLIERLSVLENvlsgrlgrRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 158 RALVRTPQVLLMDEPLSNLDAQL-RAEMRVeLKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASsRQVMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-232 |
4.50e-47 |
|
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: 159.52 E-value: 4.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkhLSLEPFER 87
Cdd:cd03219 3 VRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI------TGLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 88 ---DVAMVFQSYALYPHMTVYQNM----------AFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRV 154
Cdd:cd03219 73 arlGIGRTFQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500156532 155 AIGRALVRTPQVLLMDEPLSNLDAQLRAEMrVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDE 232
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEEL-AELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-228 |
2.56e-46 |
|
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: 157.24 E-value: 2.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkhlsLEPFErDVAMVFQSYALYPHMTV 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI--------TEPGP-DRMVVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 105 YQNMAF------PLKNLKYKKKKIREQVikiaQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDA 178
Cdd:TIGR01184 72 RENIALavdrvlPDLSKSERRAIVEEHI----ALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2500156532 179 QLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTG 228
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
9-222 |
1.23e-45 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 155.10 E-value: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 9 RNVKKIFSTAkgrVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEI-FFGDKVvfSDKKHLSLEPFER 87
Cdd:TIGR02673 5 HNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVrIAGEDV--NRLRGRQLPLLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 88 DVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVL 167
Cdd:TIGR02673 80 RIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 168 LMDEPLSNLDAQLRAE-MRVELKVliKDLGITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:TIGR02673 160 LADEPTGNLDPDLSERiLDLLKRL--NKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
5-246 |
1.78e-45 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 156.11 E-value: 1.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVVFSDKKHLSLE 83
Cdd:COG4598 8 ALEVRDLHKSF----GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVgGEEIRLKPDRDGELV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 84 PFERD--------VAMVFQSYALYPHMTVYQN-MAFPLknlkykkkkireQVIKIAQ---MLRIETLLER---------K 142
Cdd:COG4598 84 PADRRqlqrirtrLGMVFQSFNLWSHMTVLENvIEAPV------------HVLGRPKaeaIERAEALLAKvgladkrdaY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 143 PAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMrveLKVlIKDL---GITTIYVTHDQTEAMTLGDRIALL 219
Cdd:COG4598 152 PAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEV---LKV-MRDLaeeGRTMLVVTHEMGFARDVSSHVVFL 227
|
250 260
....*....|....*....|....*..
gi 2500156532 220 KEGVLQQTGSPDELFYCPKNTFVAGFI 246
Cdd:COG4598 228 HQGRIEEQGPPAEVFGNPKSERLRQFL 254
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-238 |
2.10e-45 |
|
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: 157.52 E-value: 2.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEP---TEGEIFFGDKVVFsdkkHLSLEP 84
Cdd:COG0444 4 VRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLL----KLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 FE----RDVAMVFQ-SY-ALYPHMTVYQNMAFPLKN-LKYKKKKIREQVIKIAQMLRI---ETLLERKPAELSGGQRQRV 154
Cdd:COG0444 80 LRkirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 155 AIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDqteamtLG------DRIALLKEGVLQQTG 228
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHD------LGvvaeiaDRVAVMYAGRIVEEG 233
|
250
....*....|
gi 2500156532 229 SPDELFYCPK 238
Cdd:COG0444 234 PVEELFENPR 243
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
24-234 |
2.23e-45 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 156.46 E-value: 2.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKhLSLEPFERDVAMVFQsyalYPHM- 102
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKK-KKLKDLRKKVGLVFQ----FPEHq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 103 ----TVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRI-ETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:TIGR04521 95 lfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 178 AQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:TIGR04521 175 PKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-233 |
2.27e-45 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 154.59 E-value: 2.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFStaKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSlepf 85
Cdd:cd03263 1 LQIRNLTKTYK--KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 eRDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQ 165
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMRVELKVLIKDLGIttIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
8-234 |
2.37e-45 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 157.59 E-value: 2.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKK-------IFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfSDKKHL 80
Cdd:COG4608 10 VRDLKKhfpvrggLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI-TGLSGR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 SLEPFERDVAMVFQ-SYA-LYPHMTVYQNMAFPLKNLKYKKKKIREQviKIAQMLRIETL----LERKPAELSGGQRQRV 154
Cdd:COG4608 89 ELRPLRRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGLASKAERRE--RVAELLELVGLrpehADRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 155 AIGRALVRTPQVLLMDEPLSNLDAQLRAE---MRVELKvliKDLGITTIYVTHDqteamtLG------DRIALLKEGVLQ 225
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVSIQAQvlnLLEDLQ---DELGLTYLFISHD------LSvvrhisDRVAVMYLGKIV 237
|
....*....
gi 2500156532 226 QTGSPDELF 234
Cdd:COG4608 238 EIAPRDELY 246
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
12-245 |
5.34e-45 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 158.66 E-value: 5.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 12 KKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFgDKVVFSDKKHLSLEPFERD-VA 90
Cdd:PRK10070 31 KEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI-DGVDIAKISDAELREVRRKkIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 91 MVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMD 170
Cdd:PRK10070 110 MVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 171 EPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVAGF 245
Cdd:PRK10070 190 EAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-231 |
5.42e-45 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 154.40 E-value: 5.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVKKIFSTAKgrvlALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEI-FFGDKVVFS----DKKH 79
Cdd:PRK11124 2 SIQLNGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLnIAGNHFDFSktpsDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 80 LSLEpfeRDVAMVFQSYALYPHMTVYQNM-AFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGR 158
Cdd:PRK11124 78 RELR---RNVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 159 ALVRTPQVLLMDEPLSNLDAQLRAEMrVElkvLIKDL---GITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPD 231
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQI-VS---IIRELaetGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-222 |
5.83e-45 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 157.34 E-value: 5.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 23 LALDrINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLEPFERDVAMVFQSYALYPHM 102
Cdd:PRK11144 13 LCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 103 TVYQN----MAfplknlkykkKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDA 178
Cdd:PRK11144 92 KVRGNlrygMA----------KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2500156532 179 QLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:PRK11144 162 PRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQG 205
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-233 |
6.48e-45 |
|
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: 163.47 E-value: 6.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVKkiFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEP 84
Cdd:COG2274 473 DIELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI----DLRQIDPAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 FERDVAMVFQSYALYpHMTVYQNMAF--PLKNLkykkkkirEQVIKIAQMLRIETLLERKP-----------AELSGGQR 151
Cdd:COG2274 547 LRRQIGVVLQDVFLF-SGTIRENITLgdPDATD--------EEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQR 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 152 QRVAIGRALVRTPQVLLMDEPLSNLDAQlrAEMRVeLKVLIKDL-GITTIYVTHDqTEAMTLGDRIALLKEGVLQQTGSP 230
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAE--TEAII-LENLRRLLkGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTH 693
|
...
gi 2500156532 231 DEL 233
Cdd:COG2274 694 EEL 696
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-174 |
7.80e-45 |
|
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: 150.88 E-value: 7.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDkkhlSLEPFERDVAMVFQSYALYPHMTV 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD----ERKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 105 YQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERK----PAELSGGQRQRVAIGRALVRTPQVLLMDEPLS 174
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-238 |
2.42e-44 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 155.34 E-value: 2.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFS-DKKHLSLep 84
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlSEKELRK-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 FERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTP 164
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 165 QVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPK 238
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPK 233
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-222 |
2.76e-44 |
|
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: 149.70 E-value: 2.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEPFER 87
Cdd:cd00267 2 IENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK----DIAKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 88 DVAMVFQsyalyphmtvyqnmafplknlkykkkkireqvikiaqmlrietllerkpaeLSGGQRQRVAIGRALVRTPQVL 167
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 168 LMDEPLSNLDAQLRAEMRVELKVLIKDlGITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-246 |
3.97e-44 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 152.09 E-value: 3.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEI------F-FGDKVvfSDK 77
Cdd:COG4161 2 SIQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLniaghqFdFSQKP--SEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 78 KHLSLEpfeRDVAMVFQSYALYPHMTVYQNM-AFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAI 156
Cdd:COG4161 76 AIRLLR---QKVGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 157 GRALVRTPQVLLMDEPLSNLDAQLRAEMrVElkvLIKDL---GITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPdEL 233
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQV-VE---IIRELsqtGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SH 227
|
250
....*....|...
gi 2500156532 234 FYCPKNTFVAGFI 246
Cdd:COG4161 228 FTQPQTEAFAHYL 240
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-234 |
1.04e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 151.01 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVkkifSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHL 80
Cdd:COG1121 2 MMMPAIELENL----TVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 S----LEPFERD--------VAMvfqsyALYPHMTVYQNMAfplknlkykkkkiREQVIKIAQMLR---IETLLERKPAE 145
Cdd:COG1121 78 GyvpqRAEVDWDfpitvrdvVLM-----GRYGRRGLFRRPS-------------RADREAVDEALErvgLEDLADRPIGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 146 LSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMrveLKVL--IKDLGITTIYVTHDQTEAMTLGDRIALLKEGV 223
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEAL---YELLreLRREGKTILVVTHDLGAVREYFDRVLLLNRGL 216
|
250
....*....|.
gi 2500156532 224 LQQtGSPDELF 234
Cdd:COG1121 217 VAH-GPPEEVL 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-227 |
2.50e-43 |
|
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: 149.51 E-value: 2.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsdkkhl 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 SLEPFERD---------VAMVFQSYALYPHMTVYQNMAFPlknlkykkkkireqvIKIAQML----RIETLLER------ 141
Cdd:COG4181 75 DLFALDEDararlrarhVGFVFQSFQLLPTLTALENVMLP---------------LELAGRRdaraRARALLERvglghr 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 142 ---KPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAmTLGDRIAL 218
Cdd:COG4181 140 ldhYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLR 218
|
....*....
gi 2500156532 219 LKEGVLQQT 227
Cdd:COG4181 219 LRAGRLVED 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-234 |
6.62e-43 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 149.57 E-value: 6.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 4 TAILVRNVKKIFST-----AKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVVFSDK 77
Cdd:TIGR02769 1 SLLEVRDVTHTYRTgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFrGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 78 KhlSLEPFERDVAMVFQ-SY-ALYPHMTVYQNMAFPLKNLKYKKKKirEQVIKIAQMLRIETL----LERKPAELSGGQR 151
Cdd:TIGR02769 81 K--QRRAFRRDVQLVFQdSPsAVNPRMTVRQIIGEPLRHLTSLDES--EQKARIAELLDMVGLrsedADKLPRQLSGGQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 152 QRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPD 231
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVA 236
|
...
gi 2500156532 232 ELF 234
Cdd:TIGR02769 237 QLL 239
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-228 |
1.56e-42 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 147.13 E-value: 1.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGeiffgdkVVFSDKKHLSLEPF 85
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAG-------FATVDGFDVVKEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 E--RDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRT 163
Cdd:cd03266 75 EarRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 164 PQVLLMDEPLSNLDAQLRAEMRVELKVLiKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTG 228
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-232 |
3.42e-42 |
|
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: 147.49 E-value: 3.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 4 TAIL-VRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkhLSL 82
Cdd:COG0411 2 DPLLeVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI------TGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 83 EPFER---DVAMVFQSYALYPHMTVYQNMA---------------FPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPA 144
Cdd:COG0411 72 PPHRIarlGIARTFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 145 ELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVL 224
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
....*...
gi 2500156532 225 QQTGSPDE 232
Cdd:COG0411 232 IAEGTPAE 239
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
20-228 |
3.62e-42 |
|
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: 144.89 E-value: 3.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEPFERDVAMVFQsyALy 99
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK----DLASLSPKELARKIAYVPQ--AL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 100 phmtvyqnmafplknlkykkkkireqvikiaQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQ 179
Cdd:cd03214 83 -------------------------------ELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2500156532 180 LRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTG 228
Cdd:cd03214 132 HQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-222 |
4.26e-42 |
|
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: 144.45 E-value: 4.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKkiFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEPF 85
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGV----DLRDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYpHMTVYQNMafplknlkykkkkireqvikiaqmlrietllerkpaeLSGGQRQRVAIGRALVRTPQ 165
Cdd:cd03228 75 RKNIAYVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMRVELKVLIKdlGITTIYVTHDqTEAMTLGDRIALLKEG 222
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-233 |
4.77e-42 |
|
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: 146.67 E-value: 4.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFSTAKgrvLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHlSLEPF 85
Cdd:TIGR02315 2 LEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGK-KLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKI-----REQVIKIAQMLR---IETLLERKPAELSGGQRQRVAIG 157
Cdd:TIGR02315 78 RRRIGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLlgrfsEEDKERALSALErvgLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 158 RALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-224 |
2.06e-41 |
|
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: 144.09 E-value: 2.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFStakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfSDKKHLSLEPF 85
Cdd:cd03292 1 IEFINVTKTYP---NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV-SDLRGRAIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQ 165
Cdd:cd03292 77 RRKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMrVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVL 224
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEI-MNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-233 |
2.70e-41 |
|
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: 151.83 E-value: 2.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVkkIFSTAKGRVlALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEP 84
Cdd:COG4988 336 SIELEDV--SFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGV----DLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 FERDVAMVFQSYALyPHMTVYQNMAF--PLKNlkykkkkiREQVIKIAQMLRIETLLERKP-----------AELSGGQR 151
Cdd:COG4988 409 WRRQIAWVPQNPYL-FAGTIRENLRLgrPDAS--------DEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 152 QRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLgiTTIYVTHDqTEAMTLGDRIALLKEGVLQQTGSPD 231
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHR-LALLAQADRILVLDDGRIVEQGTHE 556
|
..
gi 2500156532 232 EL 233
Cdd:COG4988 557 EL 558
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
6-246 |
1.73e-40 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 143.05 E-value: 1.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GD----------KVVF 74
Cdd:TIGR03005 1 VRFSDVTKRF----GILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVeGEqlyhmpgrngPLVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 75 SDKKHLSlePFERDVAMVFQSYALYPHMTVYQNMAF-PLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQR 153
Cdd:TIGR03005 77 ADEKHLR--QMRNKIGMVFQSFNLFPHKTVLDNVTEaPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 154 VAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:TIGR03005 155 VAIARALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEI 234
|
250
....*....|...
gi 2500156532 234 FYCPKNTFVAGFI 246
Cdd:TIGR03005 235 FRQPKEERTREFL 247
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-222 |
1.78e-40 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 142.89 E-value: 1.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 4 TAILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsdkkhlSLE 83
Cdd:PRK11247 11 TPLLLNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA---------PLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 84 PFERDVAMVFQSYALYPHMTVYQNMAFplknlkYKKKKIREQVIkiaQMLRIETLLERK---PAELSGGQRQRVAIGRAL 160
Cdd:PRK11247 78 EAREDTRLMFQDARLLPWKKVIDNVGL------GLKGQWRDAAL---QALAAVGLADRAnewPAALSGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 161 VRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
24-233 |
3.29e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 149.16 E-value: 3.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEPFERDVAMVFQSYALYpHMT 103
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV----DIRDLTLESLRRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 104 VYQNMAFPLKNLKykkkkiREQVIKIAQMLRIETLLERKP-----------AELSGGQRQRVAIGRALVRTPQVLLMDEP 172
Cdd:COG1132 430 IRENIRYGRPDAT------DEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 173 LSNLDAqlRAEMRVE--LKVLIKdlGITTIYVTH--DQTEAMtlgDRIALLKEGVLQQTGSPDEL 233
Cdd:COG1132 504 TSALDT--ETEALIQeaLERLMK--GRTTIVIAHrlSTIRNA---DRILVLDDGRIVEQGTHEEL 561
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-216 |
4.00e-40 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 140.44 E-value: 4.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFstaKGRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLEPFER 87
Cdd:TIGR03608 1 LKNISKKF---GDKVI-LDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 88 DVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVL 167
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2500156532 168 LMDEPLSNLDAQLRAEMrVELKVLIKDLGITTIYVTHDqTEAMTLGDRI 216
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEV-LDLLLELNDEGKTIIIVTHD-PEVAKQADRV 203
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-233 |
4.94e-40 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 140.58 E-value: 4.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGE-IFFGDKVVFSDKKhlslep 84
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHDVVREPRE------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 FERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREqviKIAQMLRIETLLE---RKPAELSGGQRQRVAIGRALV 161
Cdd:cd03265 71 VRRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRE---RIDELLDFVGLLEaadRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 162 RTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
8-209 |
7.63e-40 |
|
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: 139.54 E-value: 7.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkHLSLEPFER 87
Cdd:COG4133 5 AENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-----RDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 88 DVAMVFQSYALYPHMTVYQNMAFplKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVL 167
Cdd:COG4133 76 RLAYLGHADGLKPELTVRENLRF--WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2500156532 168 LMDEPLSNLDAQ----LRAEMRVELkvlikDLGITTIYVTHDQTEA 209
Cdd:COG4133 154 LLDEPFTALDAAgvalLAELIAAHL-----ARGGAVLLTTHQPLEL 194
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-222 |
9.19e-40 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 140.99 E-value: 9.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKhlslepfERDVamVFQSYALYPHMT 103
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-------ERGV--VFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 104 VYQNMAFPLKNLKYKkkkiREQVIKIA-QMLR---IETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQ 179
Cdd:PRK11248 87 VQDNVAFGLQLAGVE----KMQRLEIAhQMLKkvgLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2500156532 180 LRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:PRK11248 163 TREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-233 |
4.71e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 144.78 E-value: 4.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 4 TAIL-VRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVVFSDKKhls 81
Cdd:COG1129 2 EPLLeMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPVRFRSPR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 82 lEPFERDVAMVFQSYALYPHMTVYQNMAF---PLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGR 158
Cdd:COG1129 75 -DAQAAGIAIIHQELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 159 ALVRTPQVLLMDEPLSNLDaqlRAEMRVELKVL--IKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:COG1129 154 ALSRDARVLILDEPTASLT---EREVERLFRIIrrLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-233 |
5.00e-39 |
|
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: 145.68 E-value: 5.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVkkIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEP 84
Cdd:COG4987 333 SLELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGV----DLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 FERDVAMVFQSYALYpHMTVYQNmafplknlkykkkkIR--------EQVIKIAQMLRIETLLERKP-----------AE 145
Cdd:COG4987 407 LRRRIAVVPQRPHLF-DTTLREN--------------LRlarpdatdEELWAALERVGLGDWLAALPdgldtwlgeggRR 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 146 LSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLgiTTIYVTHDQTeAMTLGDRIALLKEGVLQ 225
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLA-GLERMDRILVLEDGRIV 548
|
....*...
gi 2500156532 226 QTGSPDEL 233
Cdd:COG4987 549 EQGTHEEL 556
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-232 |
6.19e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 144.40 E-value: 6.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIF-FGDKVVFSDkkh 79
Cdd:COG3845 1 MMPPALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILiDGKPVRIRS--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 80 lslePfeRD-----VAMVFQSYALYPHMTVYQNMAF---PLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQR 151
Cdd:COG3845 74 ----P--RDaialgIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 152 QRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLiKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPD 231
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
.
gi 2500156532 232 E 232
Cdd:COG3845 227 E 227
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
9-224 |
1.19e-38 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 137.10 E-value: 1.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 9 RNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVV--FSDKKHLSLEpfE 86
Cdd:TIGR02211 5 ENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLskLSSNERAKLR--N 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 87 RDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQV 166
Cdd:TIGR02211 83 KKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 167 LLMDEPLSNLD---AQLRAEMRVELKvliKDLGITTIYVTHDQTEAMTLgDRIALLKEGVL 224
Cdd:TIGR02211 163 VLADEPTGNLDnnnAKIIFDLMLELN---RELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-222 |
1.25e-38 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 138.28 E-value: 1.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFST-----AKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfSDKKHLSL 82
Cdd:PRK10419 6 VSGLSHHYAHgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL-AKLNRAQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 83 EPFERDVAMVFQSY--ALYPHMTVYQNMAFPLKNLKYKKKkiREQVIKIAQMLRI----ETLLERKPAELSGGQRQRVAI 156
Cdd:PRK10419 85 KAFRRDIQMVFQDSisAVNPRKTVREIIREPLRHLLSLDK--AERLARASEMLRAvdldDSVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 157 GRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNG 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-224 |
1.84e-38 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 134.48 E-value: 1.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVVFSDKKhlslEPFE 86
Cdd:cd03216 3 LRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVdGKEVSFASPR----DARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 87 RDVAMVFQsyalyphmtvyqnmafplknlkykkkkireqvikiaqmlrietllerkpaeLSGGQRQRVAIGRALVRTPQV 166
Cdd:cd03216 75 AGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2500156532 167 LLMDEPLSNLDAQLRAEMRVELKVLiKDLGITTIYVTHDQTEAMTLGDRIALLKEGVL 224
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-238 |
2.70e-38 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 137.19 E-value: 2.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 4 TAILVRNVKKIFstaKGRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKkHLS-- 81
Cdd:PRK11264 2 SAIEVKNLVKKF---HGQTV-LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTAR-SLSqq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 82 ---LEPFERDVAMVFQSYALYPHMTVYQNMafpLKNLKYKKKKIREQVIKIAQMLRIETLLERK----PAELSGGQRQRV 154
Cdd:PRK11264 77 kglIRQLRQHVGFVFQNFNLFPHRTVLENI---IEGPVIVKGEPKEEATARARELLAKVGLAGKetsyPRRLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 155 AIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDlGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
....
gi 2500156532 235 YCPK 238
Cdd:PRK11264 233 ADPQ 236
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-224 |
1.06e-37 |
|
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: 134.20 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLEP----FERD------- 88
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPqrrsIDRDfpisvrd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 89 -VAMvfqsyALYPHMtvyqnmafplKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVL 167
Cdd:cd03235 90 vVLM-----GLYGHK----------GLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 168 LMDEPLSNLDAQlraeMRVELKVLIKDL---GITTIYVTHDQTEAMTLGDRIALLKEGVL 224
Cdd:cd03235 155 LLDEPFAGVDPK----TQEDIYELLRELrreGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
25-246 |
2.01e-37 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 135.10 E-value: 2.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVV-----------FSDKKHLSLepFERDVAMVF 93
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkVADKNQLRL--LRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 94 QSYALYPHMTVYQN-MAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERK-PAELSGGQRQRVAIGRALVRTPQVLLMDE 171
Cdd:PRK10619 99 QHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 172 PLSNLDAQLRAEMRVELKVLIKDlGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVAGFI 246
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-234 |
2.28e-37 |
|
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: 135.25 E-value: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKkiFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfSDKKHLslepF 85
Cdd:TIGR04520 1 IEVENVS--FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT-LDEENL----W 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 E--RDVAMVFQSyalyPH-----MTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGR 158
Cdd:TIGR04520 74 EirKKVGMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 159 ALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAmTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-208 |
4.40e-37 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 133.30 E-value: 4.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRnVKKIFSTAKGRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHL 80
Cdd:PRK10247 1 MQENSPLLQ-LQNVGYLAGDAKI-LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE----DISTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 SLEPFERDVAMVFQSYALYPHmTVYQNMAFPlknlkykkKKIREQVIKIAQMLR-------IETLLERKPAELSGGQRQR 153
Cdd:PRK10247 75 KPEIYRQQVSYCAQTPTLFGD-TVYDNLIFP--------WQIRNQQPDPAIFLDdlerfalPDTILTKNIAELSGGEKQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 154 VAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTE 208
Cdd:PRK10247 146 ISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-234 |
7.44e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 134.38 E-value: 7.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 23 LALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLEPFERDVAMVFQsyalYPHM 102
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQ----FPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 103 -----TVYQNMAFPLKNLKYKKKKIREqviKIAQMLRI----ETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPL 173
Cdd:PRK13634 97 qlfeeTVEKDICFGPMNFGVSEEDAKQ---KAREMIELvglpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 174 SNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIF 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-233 |
1.66e-35 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 135.32 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVKKIF-STAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF--GDKVV-FSD 76
Cdd:TIGR03269 275 VGEPIIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvGDEWVdMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 77 KKHLSLEPFERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQM----LRIETLLERKPAELSGGQRQ 152
Cdd:TIGR03269 355 PGPDGRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVITLKMVgfdeEKAEEILDKYPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 153 RVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDE 232
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
.
gi 2500156532 233 L 233
Cdd:TIGR03269 515 I 515
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-234 |
2.51e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 130.17 E-value: 2.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDkVVFSDKKhLSLEPFERDVAMVFQ--SYALYPH 101
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG-VDITDKK-VKLSDIRKKVGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 102 mTVYQNMAFPLKNLKYKKKKIREQVIKIAQM--LRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQ 179
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 180 LRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-219 |
9.25e-35 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 133.18 E-value: 9.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEPFERDVAMVFQSYALY 99
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV----PLADADADSWRDQIAWVPQHPFLF 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 100 PHmTVYQNMAFplKNLKYKKKKIREQVIK--IAQMLR-----IETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEP 172
Cdd:TIGR02857 409 AG-TIAENIRL--ARPDASDAEIREALERagLDEFVAalpqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEP 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2500156532 173 LSNLDAQLRAEMRVELKVLIKdlGITTIYVTHDqTEAMTLGDRIALL 219
Cdd:TIGR02857 486 TAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-239 |
9.37e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 127.85 E-value: 9.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 3 KTAILVRNvkkiFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLL---N----IIAGLEepTEGEIFFGDKVVFS 75
Cdd:COG1117 9 EPKIEVRN----LNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclNrmndLIPGAR--VEGEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 76 DKkhlsLEPFE--RDVAMVFQSYALYPhMTVYQNMAFPlknlkykkkkIREQVIKIAQML--RIETLLER---------- 141
Cdd:COG1117 83 PD----VDVVElrRRVGMVFQKPNPFP-KSIYDNVAYG----------LRLHGIKSKSELdeIVEESLRKaalwdevkdr 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 142 --KPA-ELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQlrAEMRVELkvLIKDLG--ITTIYVTHDQTEAMTLGDRI 216
Cdd:COG1117 148 lkKSAlGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPI--STAKIEE--LILELKkdYTIVIVTHNMQQAARVSDYT 223
|
250 260
....*....|....*....|...
gi 2500156532 217 ALLKEGVLQQTGSPDELFYCPKN 239
Cdd:COG1117 224 AFFYLGELVEFGPTEQIFTNPKD 246
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-233 |
1.23e-34 |
|
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: 126.39 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVkkifSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkhLSLEPFER 87
Cdd:cd03224 3 VENL----NAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI------TGLPPHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 88 ---DVAMVFQSYALYPHMTVYQN--MAfplkNLKYKKKKIREQVIKIAQML-RIETLLERKPAELSGGQRQRVAIGRALV 161
Cdd:cd03224 73 araGIGYVPEGRRIFPELTVEENllLG----AYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 162 RTPQVLLMDEPLSNLDAQLRAEMrveLKVL--IKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEI---FEAIreLRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-238 |
2.21e-34 |
|
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: 132.50 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 12 KKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEePTEGEIFFGDKVVfSDKKHLSLEPFERDVAM 91
Cdd:COG4172 289 RGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDL-DGLSRRALRPLRRRMQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 92 VFQS-YA-LYPHMTVYQNMAFPLKNLKYKKKKiREQVIKIAQMLR----IETLLERKPAELSGGQRQRVAIGRALVRTPQ 165
Cdd:COG4172 367 VFQDpFGsLSPRMTVGQIIAEGLRVHGPGLSA-AERRARVAEALEevglDPAARHRYPHEFSGGQRQRIAIARALILEPK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMrVEL-KVLIKDLGITTIYVTHDQT--EAMTlgDRIALLKEGVLQQTGSPDELFYCPK 238
Cdd:COG4172 446 LLVLDEPTSALDVSVQAQI-LDLlRDLQREHGLAYLFISHDLAvvRALA--HRVMVMKDGKVVEQGPTEQVFDAPQ 518
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
20-234 |
3.40e-34 |
|
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: 125.97 E-value: 3.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEG---EIF---FGDKVVFSDKKHLSL------EPFER 87
Cdd:COG1119 15 GKTI-LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVWELRKRIGLvspalqLRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 88 DV---AMV----FQSYALYPHMTVYQnmafplknlkykkkkiREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRAL 160
Cdd:COG1119 94 DEtvlDVVlsgfFDSIGLYREPTDEQ----------------RERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 161 VRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-228 |
1.20e-33 |
|
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: 123.46 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstakGRVLALDRINLEIKPGeLFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDK----KHLS 81
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPqklrRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 82 LEPferdvamvfQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALV 161
Cdd:cd03264 76 YLP---------QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 162 RTPQVLLMDEPLSNLDaqlrAEMRVELKVLIKDLGITTIYV--THDQTEAMTLGDRIALLKEGVLQQTG 228
Cdd:cd03264 147 GDPSILIVDEPTAGLD----PEERIRFRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-222 |
4.61e-33 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 129.46 E-value: 4.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 4 TAIL-VRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfSDKKHLSL 82
Cdd:PRK10535 2 TALLeLKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDV-ATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 83 EPFERD-VAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALV 161
Cdd:PRK10535 81 AQLRREhFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 162 RTPQVLLMDEPLSNLDAQLRAEMRVELKVLiKDLGITTIYVTHDQTEAMTlGDRIALLKEG 222
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDG 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-222 |
1.11e-32 |
|
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: 121.16 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVKkiFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDkvvfSDKKHLSLEP 84
Cdd:cd03245 2 RIEFRNVS--FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG----TDIRQLDPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 FERDVAMVFQSYALYpHMTVYQNMAFPLKNLKYkkkkirEQVIKIAQMLRIETLLERKP-----------AELSGGQRQR 153
Cdd:cd03245 76 LRRNIGYVPQDVTLF-YGTLRDNITLGAPLADD------ERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 154 VAIGRALVRTPQVLLMDEPLSNLDaqLRAEMRV--ELKVLIKDlgITTIYVTHdQTEAMTLGDRIALLKEG 222
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMD--MNSEERLkeRLRQLLGD--KTLIIITH-RPSLLDLVDRIIVMDSG 214
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
24-224 |
1.24e-32 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 121.14 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKhlSLEPF-ERDVAMVFQSYALYPHM 102
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKN--REVPFlRRQIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 103 TVYQNMAFPLKNLKYKKKKIREQVikIAQMLRIETLLERK--PAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQL 180
Cdd:PRK10908 95 TVYDNVAIPLIIAGASGDDIRRRV--SAALDKVGLLDKAKnfPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2500156532 181 rAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVL 224
Cdd:PRK10908 173 -SEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
8-225 |
1.53e-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: 120.85 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVVFSDKKHLSLEPFE 86
Cdd:cd03269 3 VENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdGKPLDIAARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 87 RdvamvfqsyALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQV 166
Cdd:cd03269 79 R---------GLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 167 LLMDEPLSNLDAQLRAEMRVELKVLiKDLGITTIYVTHDQTEAMTLGDRIALLKEG--VLQ 225
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGraVLY 209
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-226 |
1.66e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 121.46 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHL 80
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 SLEPFERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRAL 160
Cdd:PRK11629 81 KAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 161 VRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLgDRIALLKEGVLQQ 226
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-224 |
4.14e-32 |
|
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: 119.63 E-value: 4.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLslepf 85
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 eRDVAMVFQSYALYPHMTVYQNMafplkNLKYKKKKIREQVIKiaQMLRIETLLE---RKPAELSGGQRQRVAIGRALVR 162
Cdd:cd03268 72 -RRIGALIEAPGFYPNLTARENL-----RLLARLLGIRKKRID--EVLDVVGLKDsakKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 163 TPQVLLMDEPLSNLDAQLRAEMRvELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVL 224
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
8-226 |
4.51e-32 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 119.88 E-value: 4.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLEPFER 87
Cdd:PRK10584 9 VHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 88 DVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVL 167
Cdd:PRK10584 89 HVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 168 LMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIAlLKEGVLQQ 226
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLR-LVNGQLQE 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
2-238 |
7.15e-32 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 122.12 E-value: 7.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 2 KKTAIL-VRNVKKIFSTAKGRVL---------ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEI-FFGD 70
Cdd:PRK15079 4 GKKVLLeVADLKVHFDIKDGKQWfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 71 KVVFSDKKHLSLEpfERDVAMVFQS--YALYPHMTVYQNMAFPLKNL--KYKKKKIREQVIkiAQMLRI---ETLLERKP 143
Cdd:PRK15079 84 DLLGMKDDEWRAV--RSDIQMIFQDplASLNPRMTIGEIIAEPLRTYhpKLSRQEVKDRVK--AMMLKVgllPNLINRYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 144 AELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGV 223
Cdd:PRK15079 160 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
250
....*....|....*
gi 2500156532 224 LQQTGSPDELFYCPK 238
Cdd:PRK15079 240 AVELGTYDEVYHNPL 254
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-224 |
7.43e-32 |
|
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: 118.42 E-value: 7.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 11 VKKIFSTAKGRVLalDRINLEIKPGELFIILGPSGCGKSTLLNIIAGL--EEPTEGEIFFgdkvvfsDKKHLSLEPFERD 88
Cdd:cd03213 13 VKSSPSKSGKQLL--KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLI-------NGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 89 VAMVFQSYALYPHMTVYQNMAFplknlkykkkkireqvikiAQMLRietllerkpaELSGGQRQRVAIGRALVRTPQVLL 168
Cdd:cd03213 84 IGYVPQDDILHPTLTVRETLMF-------------------AAKLR----------GLSGGERKRVSIALELVSNPSLLF 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 169 MDEPLSNLDAqLRAEMRVELKVLIKDLGITTIYVTHD-QTEAMTLGDRIALLKEGVL 224
Cdd:cd03213 135 LDEPTSGLDS-SSALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
11-205 |
1.41e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 121.22 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 11 VKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVVFSDKKHLSLepFERDV 89
Cdd:PRK11308 17 VKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLKADPEAQKL--LRQKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 90 AMVFQS-YA-LYPHMTVYQNMAFPLKNLKYKKKKIREQviKIAQMLRIETL----LERKPAELSGGQRQRVAIGRALVRT 163
Cdd:PRK11308 95 QIVFQNpYGsLNPRKKVGQILEEPLLINTSLSAAERRE--KALAMMAKVGLrpehYDRYPHMFSGGQRQRIAIARALMLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2500156532 164 PQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHD 205
Cdd:PRK11308 173 PDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-247 |
1.48e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 119.18 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 2 KKTAILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGL-----EEPTEGEIFFGDKVVFSD 76
Cdd:PRK14267 1 MKFAIETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 77 KkhlsLEPFE--RDVAMVFQSYALYPHMTVYQNMAFP------LKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSG 148
Cdd:PRK14267 77 D----VDPIEvrREVGMVFQYPNPFPHLTIYDNVAIGvklnglVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 149 GQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLgiTTIYVTHDQTEAMTLGDRIALLKEGVLQQTG 228
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
250 260
....*....|....*....|...
gi 2500156532 229 SPDELFYCPKN----TFVAGFIG 247
Cdd:PRK14267 231 PTRKVFENPEHelteKYVTGALG 253
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
24-234 |
1.74e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 119.95 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVV-FSDKKHLSLEpfeRDVAMVFQS--YALYP 100
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdYSRKGLMKLR---ESVGMVFQDpdNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 101 hMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQL 180
Cdd:PRK13636 98 -ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 181 RAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK13636 177 VSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-234 |
1.82e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.71 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 2 KKTAILVRNVKkiFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIF-FGDKVVFSDKKHL 80
Cdd:PRK13632 4 KSVMIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKiDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 slepfERDVAMVFQSyalyPH-----MTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVA 155
Cdd:PRK13632 82 -----RKKIGIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 156 IGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAmTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-233 |
2.79e-31 |
|
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: 118.03 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 22 VLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEPFERDVAMVFQSYALYPh 101
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGV----DIRDLNLRWLRSQIGLVSQEPVLFD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 102 MTVYQNMAFplknlkYKKKKIREQVIKIAQMLRI-----------ETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMD 170
Cdd:cd03249 91 GTIAENIRY------GKPDATDEEVEEAAKKANIhdfimslpdgyDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 171 EPLSNLDAQlrAEMRVE--LKVLIKdlGITTIYVTHDQTeamTL--GDRIALLKEGVLQQTGSPDEL 233
Cdd:cd03249 165 EATSALDAE--SEKLVQeaLDRAMK--GRTTIVIAHRLS---TIrnADLIAVLQNGQVVEQGTHDEL 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-246 |
4.35e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.09 E-value: 4.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGL-----EEPTEGEIFFGDKVVFSdkkhL 80
Cdd:PRK14247 4 IEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFK----M 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 SLEPFERDVAMVFQSYALYPHMTVYQNMAFP------LKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRV 154
Cdd:PRK14247 76 DVIELRRRVQMVFQIPNPIPNLSIFENVALGlklnrlVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 155 AIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGIttIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTI--VLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
250
....*....|..
gi 2500156532 235 YCPKNTFVAGFI 246
Cdd:PRK14247 234 TNPRHELTEKYV 245
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-222 |
5.41e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 117.88 E-value: 5.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFStaKGRVL---ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSL 82
Cdd:COG1101 2 LELKNLSKTFN--PGTVNekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK----DVTKLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 83 EPFERDVAMVFQSYAL--YPHMTVYQNMA----------FPLKNLKYKKKKIREQvikIAQM-LRIETLLERKPAELSGG 149
Cdd:COG1101 76 YKRAKYIGRVFQDPMMgtAPSMTIEENLAlayrrgkrrgLRRGLTKKRRELFREL---LATLgLGLENRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 150 QRQRVAIGRALVRTPQVLLMDEPLSNLDAQlRAEMRVEL-KVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-246 |
7.75e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 117.46 E-value: 7.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 3 KTAILVRNVKKIFSTAKGRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSL 82
Cdd:PRK14246 5 KSAEDVFNISRLYLYINDKAI-LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 83 EPFE--RDVAMVFQSYALYPHMTVYQNMAFPLKN-----LKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVA 155
Cdd:PRK14246 84 DAIKlrKEVGMVFQQPNPFPHLSIYDNIAYPLKShgikeKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 156 IGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDlgITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFY 235
Cdd:PRK14246 164 IARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
250
....*....|.
gi 2500156532 236 CPKNTFVAGFI 246
Cdd:PRK14246 242 SPKNELTEKYV 252
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
8-233 |
8.88e-31 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 117.56 E-value: 8.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVkkifSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVVFSDKKHLSlePFE 86
Cdd:PRK11831 10 MRGV----SFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIPAMSRSRLY--TVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 87 RDVAMVFQSYALYPHMTVYQNMAFPlknlKYKKKKIREQVIKIAQMLRIETLLER-----KPAELSGGQRQRVAIGRALV 161
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNVAYP----LREHTQLPAPLLHSTVMMKLEAVGLRgaaklMPSELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 162 RTPQVLLMDEPLSNLDAqlrAEMRVELKV---LIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDP---ITMGVLVKLiseLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-222 |
1.55e-30 |
|
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: 115.05 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 11 VKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvVFSDKKHLslepfeRDVA 90
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK-PIKAKERR------KSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 91 MVFQS--YALYPHmTVYQNMAFPLKNLKYKKKKIREqvikIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLL 168
Cdd:cd03226 75 YVMQDvdYQLFTD-SVREELLLGLKELDAGNEQAET----VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 169 MDEPLSNLDaqlRAEMRvELKVLIKDL---GITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:cd03226 150 FDEPTSGLD---YKNME-RVGELIRELaaqGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
24-234 |
2.44e-30 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 121.90 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDkvvfSDKKHLSLEPFERDVAMVFQSYALYpHMT 103
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDG----VDIRQIDPADLRRNIGYVPQDPRLF-YGT 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 104 VYQNMAFPLKNLKYkkkkirEQVIKIAQMLRIETLLERKP-----------AELSGGQRQRVAIGRALVRTPQVLLMDEP 172
Cdd:TIGR03375 555 LRDNIALGAPYADD------EEILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPILLLDEP 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 173 LSNLDAQLRAEMRVELKVLIKDLgiTTIYVTHdQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:TIGR03375 629 TSAMDNRSEERFKDRLKRWLAGK--TLVLVTH-RTSLLDLVDRIIVMDNGRIVADGPKDQVL 687
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-233 |
3.22e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 116.75 E-value: 3.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEI-FFGDKVVFSDKKHLSLEPFE 86
Cdd:COG4152 4 LKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVlWDGEPLDPEDRRRIGYLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 87 RdvamvfqsyALYPHMTVyqnmafplknlkykkkkiREQVIKIAQ---------MLRIETLLER--------KPAE-LSG 148
Cdd:COG4152 80 R---------GLYPKMKV------------------GEQLVYLARlkglskaeaKRRADEWLERlglgdranKKVEeLSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 149 GQRQRVAIGRALVRTPQVLLMDEPLSNLD---AQLraemrveLKVLIKDL---GITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDpvnVEL-------LKDVIRELaakGTTVIFSSHQMELVEELCDRIVIINKG 205
|
250
....*....|...
gi 2500156532 223 --VLQqtGSPDEL 233
Cdd:COG4152 206 rkVLS--GSVDEI 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-233 |
3.53e-30 |
|
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: 115.08 E-value: 3.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkhLSLEPFER---DVAMVFQSY 96
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI------TGLPPHRIarlGIGYVPEGR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 97 ALYPHMTVYQN--MAFPLKNLKYKKKKIREQVIKI----AQMLRietlleRKPAELSGGQRQRVAIGRALVRTPQVLLMD 170
Cdd:COG0410 88 RIFPSLTVEENllLGAYARRDRAEVRADLERVYELfprlKERRR------QRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 171 EPLSNLDAQLRAEMRVELKvLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:COG0410 162 EPSLGLAPLIVEEIFEIIR-RLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-232 |
4.24e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 115.60 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEPFERDVAMVFQSYALY 99
Cdd:COG4559 13 GRTL-LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR----PLAAWSPWELARRRAVLPQHSSLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 100 PHMTVYQNMAF---PLKNLKYKKKKIREQVIKIAQMLrieTLLERKPAELSGGQRQRVAIGRALV-------RTPQVLLM 169
Cdd:COG4559 88 FPFTVEEVVALgraPHGSSAAQDRQIVREALALVGLA---HLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500156532 170 DEPLSNLDA--QLRAeMRvelkvLIKDL---GITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDE 232
Cdd:COG4559 165 DEPTSALDLahQHAV-LR-----LARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-233 |
5.25e-30 |
|
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: 114.63 E-value: 5.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKkiFSTAKGRvLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEPF 85
Cdd:cd03253 1 IEFENVT--FAYDPGR-PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ----DIREVTLDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYpHMTVYQNMAFPLKNLKYkkkkirEQVIKIAQMLRIETLLERKP-----------AELSGGQRQRV 154
Cdd:cd03253 74 RRAIGVVPQDTVLF-NDTIGYNIRYGRPDATD------EEVIEAAKAAQIHDKIMRFPdgydtivgergLKLSGGEKQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 155 AIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKdlGITTIYVTHDQTEAMTlGDRIALLKEGVLQQTGSPDEL 233
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-234 |
6.30e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 115.99 E-value: 6.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLEPFERDVAMVFQsyalYPHMT 103
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQ----FPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 104 VYQNMAFPLKNLKYKKKKI-REQVIKIA----QMLRI-ETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:PRK13643 97 LFEETVLKDVAFGPQNFGIpKEKAEKIAaeklEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 178 AQLRAEMrVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK13643 177 PKARIEM-MQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-234 |
1.07e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 115.11 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVKKIFSTAKGrvLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVvfsdkkhL 80
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAT--YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-------L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 SLEP---FERDVAMVFQSyalyPH-----MTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQ 152
Cdd:PRK13635 72 SEETvwdVRRQVGMVFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 153 RVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTlGDRIALLKEGVLQQTGSPDE 232
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEE 226
|
..
gi 2500156532 233 LF 234
Cdd:PRK13635 227 IF 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-233 |
1.19e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 115.67 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHL 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 slepfERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRAL 160
Cdd:PRK13537 79 -----RQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 161 VRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDlGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-236 |
1.46e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.46 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 23 LALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDkkhlSLEPFERDVAMVFQ-------- 94
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDD----NFEKLRKHIGIVFQnpdnqfvg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 95 -------SYALYPHMTVYQNMafplknlkykkKKIREQVIKIAQMLrieTLLERKPAELSGGQRQRVAIGRALVRTPQVL 167
Cdd:PRK13648 99 sivkydvAFGLENHAVPYDEM-----------HRRVSEALKQVDML---ERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 168 LMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTlGDRIALLKEGVLQQTGSPDELFYC 236
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
25-234 |
2.14e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 114.06 E-value: 2.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVVFS---DKKHLslepferdVAMVFQSyalyP 100
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEEnvwDIRHK--------IGMVFQN----P 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 101 H-----MTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSN 175
Cdd:PRK13650 91 DnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 176 LDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEaMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK13650 171 LDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-240 |
3.43e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 113.21 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVKKIFSTAKgrvlALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEpTEGEIFFGDKVVFSDK----KHL 80
Cdd:PRK14258 7 AIKVNNLSFYYDTQK----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRVEFFNQniyeRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 SLEPFERDVAMVFQSYALYPhMTVYQNMAFPLKNL----KYKKKKIREQVIKIAQML-RIETLLERKPAELSGGQRQRVA 155
Cdd:PRK14258 82 NLNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVgwrpKLEIDDIVESALKDADLWdEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 156 IGRALVRTPQVLLMDEPLSNLDAQlrAEMRVElkVLIKDLG----ITTIYVTHDQTEAMTLGDRIALLKE-----GVLQQ 226
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPI--ASMKVE--SLIQSLRlrseLTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVE 236
|
250
....*....|....
gi 2500156532 227 TGSPDELFYCPKNT 240
Cdd:PRK14258 237 FGLTKKIFNSPHDS 250
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-233 |
3.74e-29 |
|
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: 112.32 E-value: 3.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 15 FSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFgDKVvfsDKKHLSLEPFERDVAMVFQ 94
Cdd:cd03251 8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILI-DGH---DVRDYTLASLRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 95 SYALYpHMTVYQNMAFPLKNLKykkkkiREQVIKIAQMLRIETLLERKP-----------AELSGGQRQRVAIGRALVRT 163
Cdd:cd03251 84 DVFLF-NDTVAENIAYGRPGAT------REEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 164 PQVLLMDEPLSNLDaqLRAEMRVE--LKVLIKDLgiTTIYVTHDQTEAMTlGDRIALLKEGVLQQTGSPDEL 233
Cdd:cd03251 157 PPILILDEATSALD--TESERLVQaaLERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
5-233 |
4.55e-29 |
|
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: 118.14 E-value: 4.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVkkIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEP 84
Cdd:TIGR03797 451 AIEVDRV--TFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQ----DLAGLDVQA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 FERDVAMVFQSYALYPHmTVYQNMAFPLKNLKykkkkirEQVIKIAQMLRIETLLERKP-------AE----LSGGQRQR 153
Cdd:TIGR03797 525 VRRQLGVVLQNGRLMSG-SIFENIAGGAPLTL-------DEAWEAARMAGLAEDIRAMPmgmhtviSEgggtLSGGQRQR 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 154 VAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELkvliKDLGITTIYVTHDQTEAMTlGDRIALLKEGVLQQTGSPDEL 233
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDNRTQAIVSESL----ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDEL 671
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-234 |
6.33e-29 |
|
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: 111.55 E-value: 6.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKkiFSTAKGRvLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEPF 85
Cdd:cd03254 3 IEFENVN--FSYDEKK-PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI----DIRDISRKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHmTVYQNMAFPLKNLKykkkkiREQVIKIAQMLRIETLLERKP-----------AELSGGQRQRV 154
Cdd:cd03254 76 RSMIGVVLQDTFLFSG-TIMENIRLGRPNAT------DEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 155 AIGRALVRTPQVLLMDEPLSNLDAqlRAEMRVE--LKVLIKdlGITTIYVTHDQTeamTL--GDRIALLKEGVLQQTGSP 230
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDT--ETEKLIQeaLEKLMK--GRTSIIIAHRLS---TIknADKILVLDDGKIIEEGTH 221
|
....
gi 2500156532 231 DELF 234
Cdd:cd03254 222 DELL 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-233 |
1.27e-28 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 111.33 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFSTAKgrvlALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFS-DKKHLSlep 84
Cdd:COG4604 2 IEIKNVSKRYGGKV----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 feRDVAMVFQSYALYPHMTVYQNMAF---------PLknlkykkkkiREQVIKIAQMLR---IETLLERKPAELSGGQRQ 152
Cdd:COG4604 75 --KRLAILRQENHINSRLTVRELVAFgrfpyskgrLT----------AEDREIIDEAIAyldLEDLADRYLDELSGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 153 RVAIGRALVRTPQVLLMDEPLSNLD-AQLRAEMRVeLKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPD 231
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDmKHSVQMMKL-LRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPE 221
|
..
gi 2500156532 232 EL 233
Cdd:COG4604 222 EI 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-228 |
4.28e-28 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 109.73 E-value: 4.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 3 KTAILVRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHlsl 82
Cdd:cd03267 15 KEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKK--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 83 epFERDVAMVF-QSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALV 161
Cdd:cd03267 92 --FLRRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 162 RTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTG 228
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-232 |
4.70e-28 |
|
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: 114.46 E-value: 4.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFsdkkHLSLEPFERDVAMVFQSYALY 99
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS----QWDREELGRHIGYLPQDVELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 100 PHmTVYQNMA-FPLKNlkykkkkiREQVIKIAQMLRI-----------ETLLERKPAELSGGQRQRVAIGRALVRTPQVL 167
Cdd:COG4618 419 DG-TIAENIArFGDAD--------PEKVVAAAKLAGVhemilrlpdgyDTRIGEGGARLSGGQRQRIGLARALYGDPRLV 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 168 LMDEPLSNLDAQ----LRAEMRvelkvLIKDLGITTIYVTHDQTeAMTLGDRIALLKEGVLQQTGSPDE 232
Cdd:COG4618 490 VLDEPNSNLDDEgeaaLAAAIR-----ALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-224 |
4.78e-28 |
|
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: 107.69 E-value: 4.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKkiFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSdkkhLSLEPF 85
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ----WDPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHmTVYQNMafplknlkykkkkireqvikiaqmlrietllerkpaeLSGGQRQRVAIGRALVRTPQ 165
Cdd:cd03246 75 GDHVGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 166 VLLMDEPLSNLDAQlRAEMRVELKVLIKDLGITTIYVTHdQTEAMTLGDRIALLKEGVL 224
Cdd:cd03246 117 ILVLDEPNSHLDVE-GERALNQAIAALKAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
25-234 |
5.23e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 109.72 E-value: 5.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVV--FSDK---KHLSLEPFE---------RDVA 90
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsmLSSRqlaRRLALLPQHhltpegitvRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 91 mvfqSYALYPHMTVYQNMAfplknlkykkKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMD 170
Cdd:PRK11231 98 ----AYGRSPWLSLWGRLS----------AEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 171 EPLSNLDAQlraeMRVELKVLIKDL---GITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK11231 164 EPTTYLDIN----HQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-238 |
6.14e-28 |
|
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: 114.01 E-value: 6.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAIL-VRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKS-TLLNIIAGLEEP---TEGEIFFGDKVVfs 75
Cdd:COG4172 1 MMSMPLLsVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 76 dkkhLSLEPFE------RDVAMVFQ--SYALYPHMTVYQNMAFPLKN-LKYKKKKIREQVIKIAQMLRI---ETLLERKP 143
Cdd:COG4172 79 ----LGLSERElrrirgNRIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 144 AELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDqteamtLG------DRIA 217
Cdd:COG4172 155 HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD------LGvvrrfaDRVA 228
|
250 260
....*....|....*....|.
gi 2500156532 218 LLKEGVLQQTGSPDELFYCPK 238
Cdd:COG4172 229 VMRQGEIVEQGPTAELFAAPQ 249
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-234 |
2.18e-27 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 108.00 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLAldrINLEIKPGELFIILGPSGCGKSTLLNIIAGLeEPTEGEIFFGDKvvfsDKKHLSLEPFERDVAMVFQSYALY 99
Cdd:COG4138 10 GRLGP---ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGR----PLSDWSAAELARHRAYLSQQQSPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 100 PHMTVYQNMAFPLKNLKYKKKKIREqVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVR-------TPQVLLMDEP 172
Cdd:COG4138 82 FAMPVFQYLALHQPAGASSEAVEQL-LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 173 LSNLD-AQLRAemrveLKVLIK---DLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:COG4138 161 MNSLDvAQQAA-----LDRLLRelcQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
24-234 |
2.47e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 108.68 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLEPFERDVAMVFQsyalYPHM- 102
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQ----FPESq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 103 ----TVYQNMAF-PLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:PRK13649 98 lfeeTVLKDVAFgPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 178 AQLRAEMRVELKVLIKDlGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK13649 178 PKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-233 |
3.96e-27 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 107.19 E-value: 3.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 23 LALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVVFSDKKHLslepfERDVAMVFQSYALYpH 101
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdGHDLALADPAWL-----RRQVGVVLQENVLF-N 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 102 MTVYQNMAFPLKNLKykkkkiREQVIKIAQM-----------LRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMD 170
Cdd:cd03252 90 RSIRDNIALADPGMS------MERVIEAAKLagahdfiselpEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 171 EPLSNLDAQLRAEMRVELKVLIKdlGITTIYVTHDQTEAMTlGDRIALLKEGVLQQTGSPDEL 233
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-219 |
7.80e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.01 E-value: 7.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsdkkhlslepfeRDVAMVFQSYAL---YP 100
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------------ARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 101 hMTVYQNMAF----PLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNL 176
Cdd:NF040873 72 -LTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2500156532 177 DAQLRAEMRVELKVLIKDlGITTIYVTHDQTEAMtLGDRIALL 219
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVR-RADPCVLL 191
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
24-234 |
1.08e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.70 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKhlSLEPFERDVAMVFQS---YALYP 100
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKK--SLLEVRKTVGIVFQNpddQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 101 hmTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQL 180
Cdd:PRK13639 95 --TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 181 RAEMRVELKVLIKDlGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK13639 173 ASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
22-234 |
1.30e-26 |
|
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: 110.56 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 22 VLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFgDKVvfsDKKHLSLEPFERDVAMVFQSYALYPH 101
Cdd:TIGR02204 353 QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILL-DGV---DLRQLDPAELRARMALVPQDPVLFAA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 102 mTVYQNMAFPLKNLKykkkkiREQVIKIAQMLRIETLLERKP-----------AELSGGQRQRVAIGRALVRTPQVLLMD 170
Cdd:TIGR02204 429 -SVMENIRYGRPDAT------DEEVEAAARAAHAHEFISALPegydtylgergVTLSGGQRQRIAIARAILKDAPILLLD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 171 EPLSNLDAQLRAEMRVELKVLIKdlGITTIYVTHDQTEAMTlGDRIALLKEGVLQQTGSPDELF 234
Cdd:TIGR02204 502 EATSALDAESEQLVQQALETLMK--GRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELI 562
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
24-233 |
1.50e-26 |
|
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: 110.19 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDkvvfSDKKHLSLEPFERDVAMVFQSYALYPHmT 103
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG----HDLADYTLASLRRQVALVSQDVVLFND-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 104 VYQNMAFPLKNLKYkkkkiREQVIKIAQMLRIETLLERKP-----------AELSGGQRQRVAIGRALVRTPQVLLMDEP 172
Cdd:TIGR02203 422 IANNIAYGRTEQAD-----RAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILILDEA 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 173 LSNLDAQLRAEMRVELKVLIKdlGITTIYVTHDQTeAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:TIGR02203 497 TSALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-205 |
1.79e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.77 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFStakGRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSdkkHLSLEPFER 87
Cdd:COG0488 1 LENLSKSFG---GRPL-LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIG---YLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 88 D-------VAMVFQS-YALYPHM-TVYQNMAFPLKNLKYKKKKIRE-----------QVIKIAQMLRI-ETLLERKPAEL 146
Cdd:COG0488 74 DdltvldtVLDGDAElRALEAELeELEAKLAEPDEDLERLAELQEEfealggweaeaRAEEILSGLGFpEEDLDRPVSEL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 147 SGGQRQRVAIGRALVRTPQVLLMDEPLSNLDaqlrAEMRVELKVLIKDLGITTIYVTHD 205
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSHD 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
8-234 |
5.57e-26 |
|
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: 103.78 E-value: 5.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKH------LS 81
Cdd:cd03218 3 AENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHkrarlgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 82 LEPFErdvAMVFQSyalyphMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALV 161
Cdd:cd03218 79 YLPQE---ASIFRK------LTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 162 RTPQVLLMDEPLSNLDAQLRAEMRVELKVLiKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
24-240 |
6.25e-26 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 103.60 E-value: 6.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEP----TEGEIFFGDKVVfsdkkhLSLEPFERDVAMVFQS--YA 97
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPL------LPLSIRGRHIATIMQNprTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 98 LYPHMTVYQNMAFPLKNLKYKKKKIREQvikIAQMLR------IETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDE 171
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSLGKLSKQARAL---ILEALEavglpdPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 172 PLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNT 240
Cdd:TIGR02770 152 PTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHE 220
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
6-233 |
8.02e-26 |
|
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: 108.20 E-value: 8.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVkkIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDkvvfSDKKHLSLEPF 85
Cdd:TIGR01842 317 LSVENV--TIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG----ADLKQWDRETF 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHmTVYQNMA-FPLKNLKykkkkirEQVIKIAQMLRIETLLERKP-----------AELSGGQRQR 153
Cdd:TIGR01842 391 GKHIGYLPQDVELFPG-TVAENIArFGENADP-------EKIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQR 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 154 VAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLiKDLGITTIYVTHdQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:TIGR01842 463 IALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-237 |
1.31e-25 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 103.72 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 3 KTAILVRNVKKIFSTAKG-----RVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGD-KVVFSD 76
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 77 KKHLSlepfeRDVAMVFQ--SYALYPHMTVYQNMAFPLKNLKYKKKKIREQviKIAQMLRIETLLERK----PAELSGGQ 150
Cdd:PRK15112 82 YSYRS-----QRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREK--QIIETLRQVGLLPDHasyyPHMLAPGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 151 RQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSP 230
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
....*..
gi 2500156532 231 DELFYCP 237
Cdd:PRK15112 235 ADVLASP 241
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-233 |
1.42e-25 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 102.62 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 30 LEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLEPFERDVAMVFQSYALYPHMTVYQNMA 109
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQRHEFAWDFPISVAHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 110 FPLKNLKYKKKKIREQVIKIAQMlrieTLLERKP-AELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQlRAEMRVEL 188
Cdd:TIGR03771 81 GWLRRPCVADFAAVRDALRRVGL----TELADRPvGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMP-TQELLTEL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2500156532 189 KVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLqQTGSPDEL 233
Cdd:TIGR03771 156 FIELAGAGTAILMTTHDLAQAMATCDRVVLLNGRVI-ADGTPQQL 199
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
17-237 |
1.57e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 103.73 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 17 TAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVVFSDKKHLslepfERDVAMVFQS 95
Cdd:PRK13652 12 SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIREV-----RKFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 96 ---YALYPhmTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEP 172
Cdd:PRK13652 87 pddQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 173 LSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCP 237
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
5-234 |
1.68e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 103.76 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVKKIFS-----TAKGrvlaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKH 79
Cdd:PRK13641 2 SIKFENVDYIYSpgtpmEKKG----LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 80 LSLEPFERDVAMVFQsyalYPHM-----TVYQNMAFPLKNLKYKKKKIREQVIK-IAQMLRIETLLERKPAELSGGQRQR 153
Cdd:PRK13641 78 KNLKKLRKKVSLVFQ----FPEAqlfenTVLKDVEFGPKNFGFSEDEAKEKALKwLKKVGLSEDLISKSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 154 VAIGRALVRTPQVLLMDEPLSNLDAQLRAEMrVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
.
gi 2500156532 234 F 234
Cdd:PRK13641 233 F 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-241 |
1.99e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.71 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFSTAKG---RVL----ALDRINLEIKPGELFIILGPSGCGKST----LLNIIAgleepTEGEIFFGDKVV--F 74
Cdd:PRK15134 278 VEQLQVAFPIRKGilkRTVdhnvVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLhnL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 75 SDKKHLslePFERDVAMVFQ--SYALYPHMTVYQNMA--FPLKNLKYKKKKIREQVIKIAQMLRIE-TLLERKPAELSGG 149
Cdd:PRK15134 353 NRRQLL---PVRHRIQVVFQdpNSSLNPRLNVLQIIEegLRVHQPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 150 QRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGS 229
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
250
....*....|..
gi 2500156532 230 PDELFYCPKNTF 241
Cdd:PRK15134 510 CERVFAAPQQEY 521
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-241 |
2.79e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 106.86 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 14 IFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVV--FSDKKhlsLEPFERDVAM 91
Cdd:PRK10261 329 LLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtLSPGK---LQALRRDIQF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 92 VFQS-YA-LYPHMTVYQNMAFPLKNLKYKKKkiREQVIKIAQML-RIETLLE---RKPAELSGGQRQRVAIGRALVRTPQ 165
Cdd:PRK10261 406 IFQDpYAsLDPRQTVGDSIMEPLRVHGLLPG--KAAAARVAWLLeRVGLLPEhawRYPHEFSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTF 241
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPY 559
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
24-205 |
2.87e-25 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 106.29 E-value: 2.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSdkkhLSLEPFERDVAMVFQSyalyPHM- 102
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS----LDQDEVRRRVSVCAQD----AHLf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 103 --TVYQNMAFPLKNLKYkkkkirEQVIKIAQMLRIETLLERKP-----------AELSGGQRQRVAIGRALVRTPQVLLM 169
Cdd:TIGR02868 422 dtTVRENLRLARPDATD------EELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*.
gi 2500156532 170 DEPLSNLDAQLRAEMRVELkvLIKDLGITTIYVTHD 205
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-233 |
3.34e-25 |
|
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: 101.45 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkhLSLEPFER---DVAMVFQSY 96
Cdd:TIGR03410 11 GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDI------TKLPPHERaraGIAYVPQGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 97 ALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRieTLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNL 176
Cdd:TIGR03410 85 EIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVLK--EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 177 DAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:TIGR03410 163 QPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-228 |
3.39e-25 |
|
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: 101.58 E-value: 3.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 22 VLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEptEGEIFFGDkvVFSDKKHLSLEPFERDVAMVFQSYALYPH 101
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQ--ILFNGQPRKPDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 102 MTVYQNMAF--PLKNLKYKKKKIREQVIKIAQMLR--IETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:cd03234 96 LTVRETLTYtaILRLPRKSSDAIRKKRVEDVLLRDlaLTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 178 AQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTG 228
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
20-232 |
4.48e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.77 E-value: 4.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDK--------------VVFSDKKHLSLePF 85
Cdd:PRK13548 14 GRTL-LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspaelarrrAVLPQHSSLSF-PF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 --ERDVAMvfqsyALYPHMTVYQnmafplknlkykkkkiREQVIkIAQMLR---IETLLERKPAELSGGQRQRVAIGRAL 160
Cdd:PRK13548 92 tvEEVVAM-----GRAPHGLSRA----------------EDDAL-VAAALAqvdLAHLAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 161 VR------TPQVLLMDEPLSNLDA--QLRAeMRVeLKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDE 232
Cdd:PRK13548 150 AQlwepdgPPRWLLLDEPTSALDLahQHHV-LRL-ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-233 |
4.85e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 103.76 E-value: 4.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEI-FFGDKVvfSDKKH 79
Cdd:PRK13536 37 MSTVAIDLAGVSKSY----GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPV--PARAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 80 LSlepfERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRA 159
Cdd:PRK13536 111 LA----RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 160 LVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKdLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-231 |
7.57e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 101.16 E-value: 7.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDK-VVFSDKKHLSlEPFE 86
Cdd:PRK11701 9 VRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdGQLRDLYALS-EAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 87 R-----DVAMVFQSYALYPHMTV-----------------YQNmafplknlkykkkkIREQVIKIAQmlRIETLLER--- 141
Cdd:PRK11701 84 RrllrtEWGFVHQHPRDGLRMQVsaggnigerlmavgarhYGD--------------IRATAGDWLE--RVEIDAARidd 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 142 KPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKE 221
Cdd:PRK11701 148 LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
250
....*....|
gi 2500156532 222 GVLQQTGSPD 231
Cdd:PRK11701 228 GRVVESGLTD 237
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
8-241 |
7.74e-25 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 101.06 E-value: 7.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFSTAKGrvlaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDK-VVFSDKKHLSlEPFE 86
Cdd:TIGR02323 6 VSGLSKSYGGGKG----CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRsGAELELYQLS-EAER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 87 R-----DVAMVFQSYALYPHMTVYQNMAF---PLKNLKYKKKKIREQVIKIAQMLRIE-TLLERKPAELSGGQRQRVAIG 157
Cdd:TIGR02323 81 RrlmrtEWGFVHQNPRDGLRMRVSAGANIgerLMAIGARHYGNIRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 158 RALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCP 237
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
....
gi 2500156532 238 KNTF 241
Cdd:TIGR02323 241 QHPY 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-222 |
1.00e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 104.61 E-value: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 22 VLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVVFSDKKhlslEPFERDVAMVFQSYALYP 100
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEMRFASTT----AALAAGVAIIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 101 HMTVYQNM---AFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:PRK11288 93 EMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 178 A-----------QLRAEMRVelkvlikdlgitTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:PRK11288 173 AreieqlfrvirELRAEGRV------------ILYVSHRMEEIFALCDAITVFKDG 216
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
25-233 |
1.02e-24 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 105.41 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEPFERDVAMVFQSYALYpHMTV 104
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGI----PREEIPREVLANSVAMVDQDIFLF-EGTV 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 105 YQNMAF-----PLknlkykkkkirEQVIKIAQMLRIETLLERKP-----------AELSGGQRQRVAIGRALVRTPQVLL 168
Cdd:TIGR03796 570 RDNLTLwdptiPD-----------ADLVRACKDAAIHDVITSRPggydaelaeggANLSGGQRQRLEIARALVRNPSILI 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 169 MDEPLSNLDAQlraemrVELKVL--IKDLGITTIYVTHdQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:TIGR03796 639 LDEATSALDPE------TEKIIDdnLRRRGCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEEL 698
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
8-234 |
2.20e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.47 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIF-STAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEG-----EIFFGDKVVFSD----- 76
Cdd:PRK13631 24 VKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgDIYIGDKKNNHElitnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 77 --KKHLSLEPFERDVAMVFQ--SYALYPHmTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRI-ETLLERKPAELSGGQR 151
Cdd:PRK13631 104 ysKKIKNFKELRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 152 QRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMrVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPD 231
Cdd:PRK13631 183 RRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPY 261
|
...
gi 2500156532 232 ELF 234
Cdd:PRK13631 262 EIF 264
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
8-233 |
2.26e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 99.72 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFstaKGRVlALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSD------KKHLS 81
Cdd:COG1137 6 AENLVKSY---GKRT-VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhkraRLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 82 LEPFErdvAMVFQsyalypHMTVYQN-MAfplknlkykkkkIREQVI--KIAQMLRIETLLE--------RKPA-ELSGG 149
Cdd:COG1137 82 YLPQE---ASIFR------KLTVEDNiLA------------VLELRKlsKKEREERLEELLEefgithlrKSKAySLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 150 QRQRVAIGRALVRTPQVLLMDEPLSNLD----AQLRAEMRvELK-----VLIKD------LGITtiyvthdqteamtlgD 214
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEPFAGVDpiavADIQKIIR-HLKergigVLITDhnvretLGIC---------------D 204
|
250
....*....|....*....
gi 2500156532 215 RIALLKEGVLQQTGSPDEL 233
Cdd:COG1137 205 RAYIISEGKVLAEGTPEEI 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
24-234 |
2.54e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 100.62 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLEPFERDVAMVFQsyalYPHM- 102
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQ----FPESq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 103 ----TVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIE-TLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:PRK13646 98 lfedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 178 AQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-245 |
3.06e-24 |
|
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: 104.33 E-value: 3.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVKKIFSTAkGRVlALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkHLSLEP 84
Cdd:TIGR01257 928 GVCVKNLVKIFEPS-GRP-AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-----ETNLDA 1000
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 FERDVAMVFQSYALYPHMTVYQNMAFplkNLKYKKKKIREQVIKIAQMLRIETLLERKPAE---LSGGQRQRVAIGRALV 161
Cdd:TIGR01257 1001 VRQSLGMCPQHNILFHHLTVAEHILF---YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEaqdLSGGMQRKLSVAIAFV 1077
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 162 RTPQVLLMDEPLSNLDAQLRaemRVELKVLIK-DLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPdeLFYcpKNT 240
Cdd:TIGR01257 1078 GDAKVVVLDEPTSGVDPYSR---RSIWDLLLKyRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP--LFL--KNC 1150
|
....*
gi 2500156532 241 FVAGF 245
Cdd:TIGR01257 1151 FGTGF 1155
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-234 |
4.83e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.78 E-value: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 23 LALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFgDKVVFSDKKHLSlePFERDVAMVFQSyalyPH- 101
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV-DGLDTSDEENLW--DIRNKAGMVFQN----PDn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 102 ----MTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:PRK13633 97 qivaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 178 AQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTlGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-225 |
4.83e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.84 E-value: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 3 KTAILVRNVKKIFstaKGRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFS--DKKHL 80
Cdd:COG0488 313 KKVLELEGLSKSY---GDKTL-LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGyfDQHQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 SLEpferdvamvfqsyalyPHMTVYQNMAfplknlkykkkkireQVIKIAQMLRIETLLER---------KPAE-LSGGQ 150
Cdd:COG0488 389 ELD----------------PDKTVLDELR---------------DGAPGGTEQEVRGYLGRflfsgddafKPVGvLSGGE 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 151 RQRVAIGRALVRTPQVLLMDEPLSNLDaqlrAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQ 225
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLD----IETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-239 |
5.77e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 98.69 E-value: 5.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVKKIFSTAKgrvlALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGL-----EEPTEGEIFFGDKVVFS 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 76 DKKHlSLEpFERDVAMVFQSYALYPhMTVYQNMAFPLKNLKYKKKKIREQVI----KIAQML-RIETLLERKPAELSGGQ 150
Cdd:PRK14239 77 PRTD-TVD-LRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVekslKGASIWdEVKDRLHDSALGLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 151 RQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLgiTTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSP 230
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDT 231
|
....*....
gi 2500156532 231 DELFYCPKN 239
Cdd:PRK14239 232 KQMFMNPKH 240
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-204 |
1.58e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.42 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVKkiFSTAKGRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF--GDKVVF-SDKKHL- 80
Cdd:COG4178 362 ALALEDLT--LRTPDGRPL-LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFlPQRPYLp 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 --SLepfeRDVAmvfqsyaLYPHmtvyQNMAFPlknlkykkkkiREQVIKIAQMLRIETLLERKPAE------LSGGQRQ 152
Cdd:COG4178 439 lgTL----REAL-------LYPA----TAEAFS-----------DAELREALEAVGLGHLAERLDEEadwdqvLSLGEQQ 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 153 RVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMrveLKVLIKDL-GITTIYVTH 204
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
25-233 |
2.17e-23 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 101.36 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVVFSDKKHLslepfERDVAMVFQSYALYPHmT 103
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVdGVDLAIADPAWL-----RRQMGVVLQENVLFSR-S 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 104 VYQNMAFPLKNLKYkkkkirEQVIKIAQMLRIETLLERKP-----------AELSGGQRQRVAIGRALVRTPQVLLMDEP 172
Cdd:TIGR01846 547 IRDNIALCNPGAPF------EHVIHAAKLAGAHDFISELPqgyntevgekgANLSGGQRQRIAIARALVGNPRILIFDEA 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 173 LSNLDAQLRAEMRVELKVLIKdlGITTIYVTHdQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:TIGR01846 621 TSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-222 |
3.00e-23 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 95.61 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSdkkhlSLEPFerdvamvFQSyalyphMT 103
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYV-----SQEPW-------IQN------GT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 104 VYQNMAFplknlkykKKKIREQ----VIKIAQMLR--------IETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDE 171
Cdd:cd03250 82 IRENILF--------GKPFDEEryekVIKACALEPdleilpdgDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 172 PLSNLDAQLrAEMRVElKVLIKDL--GITTIYVTHdQTEAMTLGDRIALLKEG 222
Cdd:cd03250 154 PLSAVDAHV-GRHIFE-NCILGLLlnNKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-224 |
3.25e-23 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 96.00 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 22 VLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfSDKKHLSLEpfeRDVAMVFQSYALYPH 101
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI-SQYEHKYLH---SKVSLVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 102 mTVYQNMAFplKNLKYKKKKIREQVIK------IAQM-LRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLS 174
Cdd:cd03248 103 -SLQDNIAY--GLQSCSFECVKEAAQKahahsfISELaSGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2500156532 175 NLDAQlrAEMRVElKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVL 224
Cdd:cd03248 180 ALDAE--SEQQVQ-QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-232 |
3.47e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 96.30 E-value: 3.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 4 TAILVRNVKKIF------------------STAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGE 65
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 66 IFFGDKVVFsdkkhlslePFErdVAMVFQsyalyPHMTVYQNMAFplknlkykkkkireqvikIAQML---RIETlLERK 142
Cdd:COG1134 83 VEVNGRVSA---------LLE--LGAGFH-----PELTGRENIYL------------------NGRLLglsRKEI-DEKF 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 143 P-----AEL-----------SGGQRQRVAIGRALVRTPQVLLMDEPLSNLDA--QLRAEMRveLKVLIKDlGITTIYVTH 204
Cdd:COG1134 128 DeivefAELgdfidqpvktySSGMRARLAFAVATAVDPDILLVDEVLAVGDAafQKKCLAR--IRELRES-GRTVIFVSH 204
|
250 260
....*....|....*....|....*...
gi 2500156532 205 DQTEAMTLGDRIALLKEGVLQQTGSPDE 232
Cdd:COG1134 205 SMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-233 |
5.96e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.21 E-value: 5.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLepfERDVAMVFQSYALY 99
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA---RMGVVRTFQHVRLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 100 PHMTVYQNM--------------------AFPLKNlkykkkkiREQVIKIAQMLRIETLLE---RKPAELSGGQRQRVAI 156
Cdd:PRK11300 93 REMTVIENLlvaqhqqlktglfsgllktpAFRRAE--------SEALDRAATWLERVGLLEhanRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 157 GRALVRTPQVLLMDEPLSNLDAQlraEMRvELKVLIKDL----GITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDE 232
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPK---ETK-ELDELIAELrnehNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
.
gi 2500156532 233 L 233
Cdd:PRK11300 241 I 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-241 |
6.75e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.93 E-value: 6.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFfGDKVVFSDKKHLSLEPFER 87
Cdd:PRK10261 15 VENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ-CDKMLLRRRSRQVIELSEQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 88 -----------DVAMVFQS--YALYPHMTVYQNMAfplKNLKYKKKKIREQVIKIAQ-ML---RI---ETLLERKPAELS 147
Cdd:PRK10261 94 saaqmrhvrgaDMAMIFQEpmTSLNPVFTVGEQIA---ESIRLHQGASREEAMVEAKrMLdqvRIpeaQTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 148 GGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQT 227
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
|
250
....*....|....
gi 2500156532 228 GSPDELFYCPKNTF 241
Cdd:PRK10261 251 GSVEQIFHAPQHPY 264
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-217 |
7.65e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 96.00 E-value: 7.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLALDRINLEIKPGELFIILGPSGCGKSTLL-------NIIAGLEepTEGEIFFGDKVVFSDKkhlsLEPFE--RDVA 90
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFR--VEGKVTFHGKNLYAPD----VDPVEvrRRIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 91 MVFQSYALYPHmTVYQNMAFPLKNL--KYKKKKIREQVIKIAQML-RIETLLERKPAELSGGQRQRVAIGRALVRTPQVL 167
Cdd:PRK14243 95 MVFQKPNPFPK-SIYDNIAYGARINgyKGDMDELVERSLRQAALWdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 168 LMDEPLSNLD--AQLRAEMrvelkvLIKDLG--ITTIYVTHDQTEAMTLGDRIA 217
Cdd:PRK14243 174 LMDEPCSALDpiSTLRIEE------LMHELKeqYTIIIVTHNMQQAARVSDMTA 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-232 |
7.85e-23 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 95.77 E-value: 7.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 28 INLEIKPGELFIILGPSGCGKSTLLNIIAGLeEPTEGEIFFGDKVVfsdkKHLSLEPFERDVAMVFQSYALYPHMTVYQN 107
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPL----EAWSAAELARHRAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 108 MAFpLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRV-------AIGRALVRTPQVLLMDEPLSNLD-AQ 179
Cdd:PRK03695 90 LTL-HQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEPMNSLDvAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 180 LRAemrveLKVLIKDL---GITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDE 232
Cdd:PRK03695 169 QAA-----LDRLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-233 |
1.61e-22 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 98.34 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLE--EPTEGEIFFG----DKVVFSDKKH 79
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHvalcEKCGYVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 80 L----------SLEPFERD---------------VAMVFQ-SYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQML 133
Cdd:TIGR03269 77 KvgepcpvcggTLEPEEVDfwnlsdklrrrirkrIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 134 RIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHdQTEAMT-L 212
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH-WPEVIEdL 235
|
250 260
....*....|....*....|.
gi 2500156532 213 GDRIALLKEGVLQQTGSPDEL 233
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEV 256
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
2-239 |
1.69e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 98.58 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 2 KKTAILVRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPteGEIFFGDKVVfsDKKHLS 81
Cdd:TIGR00955 18 GSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLL--NGMPID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 82 LEPFERDVAMVFQSYALYPHMTVYQNMAFplknlkYKKKKIREQVIKIAQMLRIETLLE----RKPAE-----------L 146
Cdd:TIGR00955 94 AKEMRAISAYVQQDDLFIPTLTVREHLMF------QAHLRMPRRVTKKEKRERVDEVLQalglRKCANtrigvpgrvkgL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 147 SGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMrveLKVLiKDL---GITTIYVTHDQT-EAMTLGDRIALLKEG 222
Cdd:TIGR00955 168 SGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV---VQVL-KGLaqkGKTIICTIHQPSsELFELFDKIILMAEG 243
|
250 260
....*....|....*....|....*
gi 2500156532 223 VLQQTGSPDEL--------FYCPKN 239
Cdd:TIGR00955 244 RVAYLGSPDQAvpffsdlgHPCPEN 268
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-233 |
1.75e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 98.64 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 22 VLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFgDKVVFSDKKHLSLEpfeRDVAMVFQSYALYPH 101
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL-DGVPLVQYDHHYLH---RQVALVGQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 102 mTVYQNMAFPLKNLKYkkkkirEQVIKIAQMLR-----------IETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMD 170
Cdd:TIGR00958 570 -SVRENIAYGLTDTPD------EEIMAAAKAANahdfimefpngYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 171 EPLSNLDAQLRAemrvELKVLIKDLGITTIYVTHdQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:TIGR00958 643 EATSALDAECEQ----LLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQL 700
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-233 |
2.84e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.80 E-value: 2.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 11 VKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEI-FFGDKVVFSDKKHLslepfERDV 89
Cdd:PRK13647 7 VEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGREVNAENEKWV-----RSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 90 AMVFQSyalyPH-----MTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTP 164
Cdd:PRK13647 82 GLVFQD----PDdqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 165 QVLLMDEPLSNLDAQLRAEMRVELKVLIKDlGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-230 |
3.22e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.15 E-value: 3.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFSTAKGRVL-ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEI--FFGDKVvfSDKKHLSL 82
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEK--NKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 83 EPF--------------------ERDVAMVFQ--SYALYpHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRI-ETLL 139
Cdd:PRK13651 81 EKVleklviqktrfkkikkikeiRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 140 ERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDlGITTIYVTHDQTEAMTLGDRIALL 219
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|.
gi 2500156532 220 KEGVLQQTGSP 230
Cdd:PRK13651 239 KDGKIIKDGDT 249
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
24-234 |
6.04e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.92 E-value: 6.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGD-KVVFSDKKHLSLEPFERDVAMVFQ--SYALYP 100
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyAIPANLKKIKEVKRLRKEIGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 101 HmTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRI-ETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQ 179
Cdd:PRK13645 106 E-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 180 LRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-222 |
1.18e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 95.77 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 9 RNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLeEPT---EGEIFF-GDKVVFSDKKhlslEP 84
Cdd:PRK13549 9 KNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFeGEELQASNIR----DT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 FERDVAMVFQSYALYPHMTVYQNMaFplknlkYKKKKIREQVIKIAQM-LRIETLLER---------KPAELSGGQRQRV 154
Cdd:PRK13549 80 ERAGIAIIHQELALVKELSVLENI-F------LGNEITPGGIMDYDAMyLRAQKLLAQlkldinpatPVGNLGLGQQQLV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 155 AIGRALVRTPQVLLMDEPLSNLDAQlraEMRVeLKVLIKDL---GITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASLTES---ETAV-LLDIIRDLkahGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-207 |
1.30e-21 |
|
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: 89.91 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVkkIFSTAKGRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFgdkvvfsdkkhlslePF 85
Cdd:cd03223 1 IELENL--SLATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------------PE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSyalyPHMTVyqnmafplknlkykkKKIREQVIKIAQMlrietllerkpaELSGGQRQRVAIGRALVRTPQ 165
Cdd:cd03223 63 GEDLLFLPQR----PYLPL---------------GTLREQLIYPWDD------------VLSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2500156532 166 VLLMDEPLSNLDAQlraemrVELKV--LIKDLGITTIYVTHDQT 207
Cdd:cd03223 112 FVFLDEATSALDEE------SEDRLyqLLKELGITVISVGHRPS 149
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-247 |
1.32e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.85 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEG-----EIFFGDKVVFSDKKHLSlepFERDVAMVFQSYALY 99
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLE---FRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 100 PhMTVYQNM-----AFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLS 174
Cdd:PRK14271 114 P-MSIMDNVlagvrAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 175 NLDAQLRAEMRVELKVLIKDLgiTTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNT----FVAGFIG 247
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAetarYVAGLSG 267
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
16-229 |
2.01e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.48 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 16 STAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdKKHLSLEPFERDVAMVFQS 95
Cdd:PRK11614 12 SAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI---TDWQTAKIMREAVAIVPEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 96 YALYPHMTVYQNMAFplKNLKYKKKKIREQVIKIAQMLriETLLERK---PAELSGGQRQRVAIGRALVRTPQVLLMDEP 172
Cdd:PRK11614 89 RRVFSRMTVEENLAM--GGFFAERDQFQERIKWVYELF--PRLHERRiqrAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 173 LSNLD-----------AQLRAEmrvelkvlikdlGITTIYVTHDQTEAMTLGDRIALLKEG--VLQQTGS 229
Cdd:PRK11614 165 SLGLApiiiqqifdtiEQLREQ------------GMTIFLVEQNANQALKLADRGYVLENGhvVLEDTGD 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-228 |
2.71e-21 |
|
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: 89.68 E-value: 2.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKkiFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSlepf 85
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALS---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 eRDVAMVFQSYALYpHMTVYQNMAfplknlkykkkkireqvikiaqmlrietllerkpAELSGGQRQRVAIGRALVRTPQ 165
Cdd:cd03247 75 -SLISVLNQRPYLF-DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMrveLKVLIKDL-GITTIYVTHDQTeAMTLGDRIALLKEGVLQQTG 228
Cdd:cd03247 119 IVLLDEPTVGLDPITERQL---LSLIFEVLkDKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
16-233 |
4.28e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.37 E-value: 4.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 16 STAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSdkkhLSLEPFERDVAMVFQS 95
Cdd:PRK09536 10 SVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEA----LSARAASRRVASVPQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 96 YALYPHMTVYQNMAF---PLKNLKYKKKKIREQVIKIAqMLRIET--LLERKPAELSGGQRQRVAIGRALVRTPQVLLMD 170
Cdd:PRK09536 86 TSLSFEFDVRQVVEMgrtPHRSRFDTWTETDRAAVERA-MERTGVaqFADRPVTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 171 EPLSNLDAQlRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:PRK09536 165 EPTASLDIN-HQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-222 |
4.33e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 91.23 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 3 KTAILVRNVKKIFSTAKgrvlALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGL---EEPTEGEI-FFGDKVVFSDKK 78
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIeLLGRTVQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 79 HLSLEPFERDVAMVFQSYALYPHMTVYQNM--------AFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQ 150
Cdd:PRK09984 78 ARDIRKSRANTGYIFQQFNLVNRLSVLENVligalgstPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 151 RQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-233 |
1.18e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.99 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 14 IFStAKGRVLAlDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEePTEGEIffgdKVVFSDKKHLSLEPFERDVAMVF 93
Cdd:PRK11174 357 ILS-PDGKTLA-GPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSL----KINGIELRELDPESWRKHLSWVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 94 QSYALyPHMTVYQN--MAFPLKNLKYKkkkirEQVIKIAQmlrIETLLERKP-----------AELSGGQRQRVAIGRAL 160
Cdd:PRK11174 430 QNPQL-PHGTLRDNvlLGNPDASDEQL-----QQALENAW---VSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARAL 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 161 VRTPQVLLMDEPLSNLDAQlrAEMRVeLKVLIKD-LGITTIYVTH--DQTEAMtlgDRIALLKEGVLQQTGSPDEL 233
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAH--SEQLV-MQALNAAsRRQTTLMVTHqlEDLAQW---DQIWVMQDGQIVQQGDYAEL 570
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-222 |
1.26e-20 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 92.48 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 9 RNVKKIFSTAKgrvlALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVVFSDKKhlslEPFER 87
Cdd:PRK10982 2 SNISKSFPGVK----ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFqGKEIDFKSSK----EALEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 88 DVAMVFQSYALYPHMTVYQNM---AFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTP 164
Cdd:PRK10982 74 GISMVHQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 165 QVLLMDEPLSNLdaqlrAEMRVE--LKVL--IKDLGITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:PRK10982 154 KIVIMDEPTSSL-----TEKEVNhlFTIIrkLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-222 |
1.75e-20 |
|
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: 87.49 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVVFSD-----KKHLSLEPFERdvamvfQSYA 97
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdGKPVTRRSprdaiRAGIAYVPEDR------KREG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 98 LYPHMTVYQNMAFPLKnlkykkkkireqvikiaqmlrietllerkpaeLSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:cd03215 89 LVLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2500156532 178 ----AQLRAEMRvELkvliKDLGITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:cd03215 137 vgakAEIYRLIR-EL----ADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-234 |
1.84e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 89.66 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFG--DKVVFSdkkhlSLEPFERDVAMVFQS-YALYP 100
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgiDTGDFS-----KLQGIRKLVGIVFQNpETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 101 HMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQL 180
Cdd:PRK13644 92 GRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 181 RAEMRVELKVLiKDLGITTIYVTHDqTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK13644 172 GIAVLERIKKL-HEKGKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
8-247 |
1.98e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 90.55 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKS----TLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLE 83
Cdd:PRK09473 15 VKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIGGSATFNGREILNLPEKELNKL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 84 PFERdVAMVFQS--YALYPHMTV-YQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERK---PAELSGGQRQRVAIG 157
Cdd:PRK09473 95 RAEQ-ISMIFQDpmTSLNPYMRVgEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 158 RALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCP 237
Cdd:PRK09473 174 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
250
....*....|
gi 2500156532 238 KNTFVAGFIG 247
Cdd:PRK09473 254 SHPYSIGLLN 263
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
25-234 |
3.56e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.00 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGeiffgdkVVFSDKKHLSLEP---FERDVAMVFQSY-ALYP 100
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG-------KVKIDGELLTAENvwnLRRKIGMVFQNPdNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 101 HMTVYQNMAFPLKNLKYKkkkiREQVIK-IAQMLRIETLLE---RKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNL 176
Cdd:PRK13642 96 GATVEDDVAFGMENQGIP----REEMIKrVDEALLAVNMLDfktREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2500156532 177 DAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTlGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-233 |
4.73e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.04 E-value: 4.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVKkiFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEP 84
Cdd:PRK11160 338 SLTLNNVS--FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQ----PIADYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 FERDVAMVFQSYALYPHmTVYQN--MAFPLKNLkykkkkirEQVIKIAQMLRIETLLERKPA----------ELSGGQRQ 152
Cdd:PRK11160 412 LRQAISVVSQRVHLFSA-TLRDNllLAAPNASD--------EALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 153 RVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMrveLKVLIKD-LGITTIYVTHDQTeAMTLGDRIALLKEGVLQQTGSPD 231
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQI---LELLAEHaQNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQ 558
|
..
gi 2500156532 232 EL 233
Cdd:PRK11160 559 EL 560
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-216 |
1.02e-19 |
|
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: 86.33 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 4 TAILVRNVKKIFS--TAKGRVL-ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHL 80
Cdd:COG4778 3 TLLEVENLSKTFTlhLQGGKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 SlepfERDVAMVFQSYALY--------PHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRI-ETLLERKPAELSGGQR 151
Cdd:COG4778 83 S----PREILALRRRTIGYvsqflrviPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 152 QRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMrVELKVLIKDLGITTIYVTHDqTEAM-TLGDRI 216
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVV-VELIEEAKARGTAIIGIFHD-EEVReAVADRV 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-222 |
1.48e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.46 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIffgdkvVFSDKKHL 80
Cdd:PRK09700 1 MATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI------TINNINYN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 SLEP---FERDVAMVFQSYALYPHMTVYQNMaFPLKNLKYKKKKI-----REQVIKIAQMLRIETL---LERKPAELSGG 149
Cdd:PRK09700 71 KLDHklaAQLGIGIIYQELSVIDELTVLENL-YIGRHLTKKVCGVniidwREMRVRAAMMLLRVGLkvdLDEKVANLSIS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 150 QRQRVAIGRALVRTPQVLLMDEPLSNLDA----QLRAEMRvelkvLIKDLGITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:PRK09700 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLTNkevdYLFLIMN-----QLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-245 |
1.69e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.98 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVVFSDKKHLSLEpfeRDVAMVFQSyalyPHMT 103
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWqGKPLDYSKRGLLALR---QQVATVFQD----PEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 104 VY-----QNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDA 178
Cdd:PRK13638 90 IFytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 179 QLRAEMRVELKVLIKDlGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPKNTFVAGF 245
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGL 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-206 |
2.06e-19 |
|
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: 83.27 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFStakGRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFsdkkhlslepf 85
Cdd:cd03221 1 IELENLSKTYG---GKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKI----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 erdvamvfqSYalyphmtvyqnmafplknlkykkkkireqvikIAQmlrietllerkpaeLSGGQRQRVAIGRALVRTPQ 165
Cdd:cd03221 66 ---------GY--------------------------------FEQ--------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2500156532 166 VLLMDEPLSNLDaqlrAEMRVELKVLIKDLGITTIYVTHDQ 206
Cdd:cd03221 91 LLLLDEPTNHLD----LESIEALEEALKEYPGTVILVSHDR 127
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-216 |
2.96e-19 |
|
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: 85.54 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 31 EIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEI-FFGDKVVFsdkKHLSLEPferdvamvfqsyaLYPhMTVYQNMA 109
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIeIELDTVSY---KPQYIKA-------------DYE-GTVRDLLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 110 FPLKNLKYKKKKIREqvikIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELK 189
Cdd:cd03237 84 SITKDFYTHPYFKTE----IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
170 180
....*....|....*....|....*..
gi 2500156532 190 VLIKDLGITTIYVTHDQTEAMTLGDRI 216
Cdd:cd03237 160 RFAENNEKTAFVVEHDIIMIDYLADRL 186
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-228 |
4.36e-19 |
|
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: 84.51 E-value: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 12 KKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIffgdkvvfsdKKHlslepfERDVAM 91
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV----------TVR------GRVSSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 92 VFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDE 171
Cdd:cd03220 89 LGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 172 PLSNLDAQLRAEMRVELKVLIKDlGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTG 228
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-234 |
5.18e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 85.62 E-value: 5.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVKkiFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEiffgDKVVFSDKKHL 80
Cdd:PRK13640 1 MKDNIVEFKHVS--FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNP----NSKITVDGITL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 SLEPF----ERdVAMVFQSY-ALYPHMTVYQNMAFPLKNLKYKkkkiREQVIKI-AQMLRIETLLE---RKPAELSGGQR 151
Cdd:PRK13640 75 TAKTVwdirEK-VGIVFQNPdNQFVGATVGDDVAFGLENRAVP----RPEMIKIvRDVLADVGMLDyidSEPANLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 152 QRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAmTLGDRIALLKEGVLQQTGSPD 231
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPV 228
|
...
gi 2500156532 232 ELF 234
Cdd:PRK13640 229 EIF 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-233 |
8.64e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.87 E-value: 8.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIF-FGDKVvfsDKKHLSLepfERDVAMVFQSYALYPHM 102
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlFGQPV---DAGDIAT---RRRVGYMSQAFSLYGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 103 TVYQNMA-----FplknlkykkkKIREQVIK--IAQMLR---IETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEP 172
Cdd:NF033858 355 TVRQNLElharlF----------HLPAAEIAarVAEMLErfdLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 173 LSNLDAQLRA---EMRVEL----KVlikdlgitTIYV-THDQTEAMTLgDRIALLKEG-VLqQTGSPDEL 233
Cdd:NF033858 425 TSGVDPVARDmfwRLLIELsredGV--------TIFIsTHFMNEAERC-DRISLMHAGrVL-ASDTPAAL 484
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-222 |
9.62e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 87.19 E-value: 9.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEE--PTEGEIFF-GDKVVFSDKKhlslEP 84
Cdd:TIGR02633 4 MKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWsGSPLKASNIR----DT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 FERDVAMVFQSYALYPHMTVYQN------MAFPLKNLKYKKKKIREQviKIAQMLRIETLLERKP-AELSGGQRQRVAIG 157
Cdd:TIGR02633 76 ERAGIVIIHQELTLVPELSVAENiflgneITLPGGRMAYNAMYLRAK--NLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500156532 158 RALVRTPQVLLMDEPLSNLDaqlRAEMRVELKvLIKDL---GITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLT---EKETEILLD-IIRDLkahGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
8-233 |
1.12e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.03 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFSTakgrVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFsdkkHLS-LEPFE 86
Cdd:PRK15439 14 ARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA----RLTpAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 87 RDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKkkirEQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQV 166
Cdd:PRK15439 86 LGIYLVPQEPLLFPNLSVKENILFGLPKRQASM----QKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 167 LLMDEPLS--------NLDAQLRAemrvelkvlIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:PRK15439 162 LILDEPTAsltpaeteRLFSRIRE---------LLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-233 |
1.63e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 86.61 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 3 KTAILVRNVkkIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFgDKVvfsDKKHLSL 82
Cdd:PRK11176 339 KGDIEFRNV--TFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-DGH---DLRDYTL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 83 EPFERDVAMVFQSYALYpHMTVYQNMAFPLKNLKYkkkkiREQVIKIAQMLR-----------IETLLERKPAELSGGQR 151
Cdd:PRK11176 413 ASLRNQVALVSQNVHLF-NDTIANNIAYARTEQYS-----REQIEEAARMAYamdfinkmdngLDTVIGENGVLLSGGQR 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 152 QRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLgiTTIYVTHdQTEAMTLGDRIALLKEGVLQQTGSPD 231
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAH-RLSTIEKADEILVVEDGEIVERGTHA 563
|
..
gi 2500156532 232 EL 233
Cdd:PRK11176 564 EL 565
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-233 |
1.64e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 86.69 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkKHLSLEPFERDVAMVFQSYALYPHmT 103
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL----TKLQLDSWRSRLAVVSQTPFLFSD-T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 104 VYQNMAF--PLKNLKYKkkkirEQVIKIAQ----MLRI----ETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPL 173
Cdd:PRK10789 405 VANNIALgrPDATQQEI-----EHVARLASvhddILRLpqgyDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 174 SNLDAqlraemRVELKVLiKDL-----GITTIYVTHdQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:PRK10789 480 SAVDG------RTEHQIL-HNLrqwgeGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQL 536
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-234 |
1.67e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.40 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 19 KGRVLALDrINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFgdkvvfsDKKHLSLEPFE----RDVAMVFQ 94
Cdd:PRK10895 14 KGRRVVED-VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIII-------DDEDISLLPLHararRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 95 SYALYPHMTVYQN-MAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPL 173
Cdd:PRK10895 86 EASIFRRLSVYDNlMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 174 SNLDAQLRAEMRVELKVLiKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-222 |
2.14e-18 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 82.31 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 9 RNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPT---EGEIFFGDKVVFSDKkhlslEPF 85
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFA-----EKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQSYALYPHMTVYQNMAFPLKnlkykkkkireqvIKIAQMLRietllerkpaELSGGQRQRVAIGRALVRTPQ 165
Cdd:cd03233 82 PGEIIYVSEEDVHFPTLTVRETLDFALR-------------CKGNEFVR----------GISGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 166 VLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIyVTHDQT--EAMTLGDRIALLKEG 222
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTF-VSLYQAsdEIYDLFDKVLVLYEG 196
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-233 |
2.29e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.50 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF-GDKVvfsdkKHLSLEPFERDVAMVFQSYAL 98
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHI-----QHYASKEVARRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 99 YPHMTVYQNMA---FPLKNLKYKKKKIREQVIKIA-QMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLS 174
Cdd:PRK10253 93 PGDITVQELVArgrYPHQPLFTRWRKEDEEAVTKAmQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 175 NLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:PRK10253 173 WLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
10-241 |
2.32e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 84.41 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 10 NVKKI---FSTAKGRVLALDRINLEIKPGELFIILGPSGCGKS-TLLNIIAGLEEPteGEIFfGDKVVFSDKKHLSLEPF 85
Cdd:PRK11022 5 NVDKLsvhFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVM-AEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ER------DVAMVFQS--YALYPHMTV-YQNMAFPLKNLKYKKKKIREQVIKIAQMLRI---ETLLERKPAELSGGQRQR 153
Cdd:PRK11022 82 ERrnlvgaEVAMIFQDpmTSLNPCYTVgFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 154 VAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
....*...
gi 2500156532 234 FYCPKNTF 241
Cdd:PRK11022 242 FRAPRHPY 249
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-233 |
2.58e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.30 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 4 TAILVRNVKkiFSTAkGRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSdkkhLSLE 83
Cdd:PRK10575 10 TTFALRNVS--FRVP-GRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLES----WSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 84 PFERDVAMVFQSYALYPHMTVYQNMA---FP-LKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRA 159
Cdd:PRK10575 82 AFARKVAYLPQQLPAAEGMTVRELVAigrYPwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAML 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 160 LVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-178 |
3.82e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIffgdkvVFSDKKHLSLEPFERdVAMVFQSYALY 99
Cdd:PRK13539 14 GRVL-FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI------KLDGGDIDDPDVAEA-CHYLGHRNAMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 100 PHMTVYQNMAFPLKNLKYKKKKIREQvikiAQMLRIETLLERKPAELSGGQRQRVAIGRALV-RTPqVLLMDEPLSNLDA 178
Cdd:PRK13539 86 PALTVAENLEFWAAFLGGEELDIAAA----LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVsNRP-IWILDEPTAALDA 160
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-233 |
4.74e-18 |
|
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: 85.26 E-value: 4.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEPFERDVAMVFQSYALYpHMTV 104
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ----DIRDVTQASLRAAIGIVPQDTVLF-NDTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 105 YQNMAF--PLKNlkykkkkiREQVIKIAQMLRIETLLERKPA-----------ELSGGQRQRVAIGRALVRTPQVLLMDE 171
Cdd:COG5265 449 AYNIAYgrPDAS--------EEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500156532 172 PLSNLDAQLRAEMRVELKVLIKdlGITTIYVTH------DqteamtlGDRIALLKEGVLQQTGSPDEL 233
Cdd:COG5265 521 ATSALDSRTERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAEL 579
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-233 |
4.83e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 85.01 E-value: 4.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIffgdKVVFSDKKHLSLEPFERDVAMVFQSYALY 99
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI----LIDGTDIRTVTRASLRRNIAVVFQDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 100 pHMTVYQNmafplknlkykkkkIR--------EQVIKIAQMLRIETLLERKPA-----------ELSGGQRQRVAIGRAL 160
Cdd:PRK13657 422 -NRSIEDN--------------IRvgrpdatdEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 161 VRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKdlGITTIYVTHDQT---EAmtlgDRIALLKEGVLQQTGSPDEL 233
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLStvrNA----DRILVFDNGRVVESGSFDEL 556
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-233 |
1.06e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 82.44 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVKKIFSTAKGR-----------------VLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIF 67
Cdd:COG4586 1 IIEVENLSKTYRVYEKEpglkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 68 FGDKVVFSDKKHlslepFERDVAMVF-------------QSYALYPHMtvYQnmafplknlkYKKKKIREQVIKIAQMLR 134
Cdd:COG4586 81 VLGYVPFKRRKE-----FARRIGVVFgqrsqlwwdlpaiDSFRLLKAI--YR----------IPDAEYKKRLDELVELLD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 135 IETLLeRKPA-ELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLG 213
Cdd:COG4586 144 LGELL-DTPVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALC 222
|
250 260
....*....|....*....|
gi 2500156532 214 DRIALLKEGVLQQTGSPDEL 233
Cdd:COG4586 223 DRVIVIDHGRIIYDGSLEEL 242
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-205 |
1.67e-17 |
|
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: 83.68 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 31 EIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVvfsdkkhlSLEP--FERDVamvfqsyalypHMTVYQNM 108
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKI--------SYKPqyISPDY-----------DGTVEEFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 109 AFPLKNLKYKKKKIREqvikIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVEL 188
Cdd:COG1245 423 RSANTDDFGSSYYKTE----IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 498
|
170
....*....|....*..
gi 2500156532 189 KVLIKDLGITTIYVTHD 205
Cdd:COG1245 499 RRFAENRGKTAMVVDHD 515
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-179 |
3.19e-17 |
|
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: 78.94 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSlepfeRDVAMVFQSYALY 99
Cdd:TIGR01189 12 ERML-FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPH-----ENILYLGHLPGLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 100 PHMTVYQNMAFPLKNLKYKKKKIrEQVIKIAQMLRIETLLerkPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQ 179
Cdd:TIGR01189 86 PELSALENLHFWAAIHGGAQRTI-EDALAAVGLTGFEDLP---AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
26-241 |
5.06e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.06 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 26 DRINLEIKPGELFIILGPSGCGKS-TLLNIIAGLEEP----TEGEIFF-GDKVVFSDKKHLslepfeRDV-----AMVFQ 94
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFhGESLLHASEQTL------RGVrgnkiAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 95 S--YALYPHMTVYQNMAfplknlkykkkkireQVIKIAQMLRIE-------TLLERK------------PAELSGGQRQR 153
Cdd:PRK15134 100 EpmVSLNPLHTLEKQLY---------------EVLSLHRGMRREaargeilNCLDRVgirqaakrltdyPHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 154 VAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
....*...
gi 2500156532 234 FYCPKNTF 241
Cdd:PRK15134 245 FSAPTHPY 252
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-205 |
6.67e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.78 E-value: 6.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 31 EIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVF-----SDKKHLSLEPFERDVAMVFQSyalyphmTVY 105
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYkpqyiKPDYDGTVEDLLRSITDDLGS-------SYY 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 106 QNmafplknlkykkkkireqviKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMR 185
Cdd:PRK13409 434 KS--------------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 493
|
170 180
....*....|....*....|
gi 2500156532 186 VELKVLIKDLGITTIYVTHD 205
Cdd:PRK13409 494 KAIRRIAEEREATALVVDHD 513
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-178 |
8.10e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.46 E-value: 8.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 32 IKPGELFIILGPSGCGKSTLLNIIAGleePTEGEIFFGdKVVFSDKKhlSLEPFERDVAMVFQSYALYPHMTVYQNMAF- 110
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAG---RIQGNNFTG-TILANNRK--PTKQILKRTGFVTQDDILYPHLTVRETLVFc 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 111 -----PLKNLKYKKKKIREQVIKIAQMLRIETLLERKP--AELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDA 178
Cdd:PLN03211 165 sllrlPKSLTKQEKILVAESVISELGLTKCENTIIGNSfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
25-231 |
1.23e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 77.18 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLE--EPTEGEIFFGDKVVfsdkkhLSLEPFER---DVAMVFQsyalY 99
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDI------TDLPPEERarlGIFLAFQ----Y 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 100 PhmtvyqnMAFPLknlkykkkkireqvIKIAQMLRI--ETllerkpaeLSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:cd03217 86 P-------PEIPG--------------VKNADFLRYvnEG--------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 178 AQlraEMRVELKVL--IKDLGITTIYVTH-----DQTEAmtlgDRIALLKEGVLQQTGSPD 231
Cdd:cd03217 137 ID---ALRLVAEVInkLREEGKSVLIITHyqrllDYIKP----DRVHVLYDGRIVKSGDKE 190
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-222 |
1.35e-16 |
|
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: 77.76 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLEPFERDVAMVFQSYALYpHMTV 104
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 105 YQNMAFPLKNLKYkkkkiREQVIKIAQMLRI---------ETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSN 175
Cdd:cd03290 96 EENITFGSPFNKQ-----RYKAVTDACSLQPdidllpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2500156532 176 LDAQLRAEMRVE--LKVLiKDLGITTIYVTHdQTEAMTLGDRIALLKEG 222
Cdd:cd03290 171 LDIHLSDHLMQEgiLKFL-QDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-222 |
2.93e-16 |
|
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: 76.13 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 17 TAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEP--TEGEIFFGDKVVFSDkkhlslepFERDVAMVFQ 94
Cdd:cd03232 15 VKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDKN--------FQRSTGYVEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 95 SYALYPHMTVyqnmafplknlkykkkkiREqVIKIAQMLRietllerkpaELSGGQRQRVAIGRALVRTPQVLLMDEPLS 174
Cdd:cd03232 87 QDVHSPNLTV------------------RE-ALRFSALLR----------GLSVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2500156532 175 NLDAQlRAEMRVELKVLIKDLGITTIYVTHdQTEAMTLG--DRIALLKEG 222
Cdd:cd03232 138 GLDSQ-AAYNIVRFLKKLADSGQAILCTIH-QPSASIFEkfDRLLLLKRG 185
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-233 |
3.06e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 79.63 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKkhlsLEPFERDVAMVFQSYALYPHMT 103
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ----PEDYRKLFSAVFTDFHLFDQLL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 104 VYQNMAfplknlkyKKKKIREQVIKIAQM---LRIE--TLLERKpaeLSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDA 178
Cdd:PRK10522 414 GPEGKP--------ANPALVEKWLERLKMahkLELEdgRISNLK---LSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 179 QLRAEMRVELKVLIKDLGITTIYVTHDQtEAMTLGDRIALLKEGVLQQ-TGSPDEL 233
Cdd:PRK10522 483 HFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQLSElTGEERDA 537
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
28-233 |
4.13e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.29 E-value: 4.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 28 INLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVV-FSD-----KKHLSLEPFERdvamvfQSYALYPH 101
Cdd:COG1129 271 VSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrIRSprdaiRAGIAYVPEDR------KGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 102 MTVYQNMAFPLKNLKYKKKKI-----REQVIKIAQMLRIETL-LERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSN 175
Cdd:COG1129 345 LSIRENITLASLDRLSRGGLLdrrreRALAEEYIKRLRIKTPsPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRG 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 176 LD--AqlraemRVELKVLIKDL---GITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:COG1129 425 IDvgA------KAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-179 |
5.64e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.61 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKkhlslEPFERDVAMVFQSYALY 99
Cdd:PRK13538 13 ERIL-FSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-----DEYHQDLLYLGHQPGIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 100 PHMTVYQNMAFPLknlkykkkkireqviKIAQMLRIETLL-----------ERKPAE-LSGGQRQRVAIGRALVRTPQVL 167
Cdd:PRK13538 87 TELTALENLRFYQ---------------RLHGPGDDEALWealaqvglagfEDVPVRqLSAGQQRRVALARLWLTRAPLW 151
|
170
....*....|..
gi 2500156532 168 LMDEPLSNLDAQ 179
Cdd:PRK13538 152 ILDEPFTAIDKQ 163
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
23-230 |
6.16e-16 |
|
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: 75.61 E-value: 6.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 23 LALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEPFERDVAMVFQSYALYPHm 102
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGV----DISKIGLHDLRSRISIIPQDPVLFSG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 103 TVYQNMAFPLKNLKYKKKKIREQV----IKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDA 178
Cdd:cd03244 93 TIRSNLDPFGEYSDEELWQALERVglkeFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 179 QLRAEMRVELKVLIKDlgITTIYVTHdQTEAMTLGDRIALLKEGVLQQTGSP 230
Cdd:cd03244 173 ETDALIQKTIREAFKD--CTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
24-233 |
7.52e-16 |
|
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: 78.63 E-value: 7.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGdkvvfsdkkHLSLEPFERDVAMVFQSY-ALYPHM 102
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN---------GFSLKDIDRHTLRQFINYlPQEPYI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 103 ---TVYQNM---AFPLKNLKYKKKKIREQVIK--IAQM-LRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPL 173
Cdd:TIGR01193 560 fsgSILENLllgAKENVSQDEIWAACEIAEIKddIENMpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 174 SNLDaqlraeMRVELKVLIKDLGI---TTIYVTHDQTEAmTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:TIGR01193 640 SNLD------TITEKKIVNNLLNLqdkTIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-234 |
1.22e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.84 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVKkiFSTAKGRvLALDRINLEIkPGELFIIL-GPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSdkkhLSLE 83
Cdd:PRK10790 340 RIDIDNVS--FAYRDDN-LVLQNINLSV-PSRGFVALvGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSS----LSHS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 84 PFERDVAMVFQSYALYPHmTVYQNMAFPLKNLKYKKKKIREQViKIAQMLR-----IETLLERKPAELSGGQRQRVAIGR 158
Cdd:PRK10790 412 VLRQGVAMVQQDPVVLAD-TFLANVTLGRDISEEQVWQALETV-QLAELARslpdgLYTPLGEQGNNLSVGQKQLLALAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 159 ALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDlgiTTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-206 |
1.99e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.22 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEE--PTEGEIFFGDkvvfsdkkhlslEPFERDVAMVfqsYALYPHM 102
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPD------------NQFGREASLI---DAIGRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 103 TVYQNMAFplknlkykkkkireqvikIAQM-LRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLr 181
Cdd:COG2401 111 DFKDAVEL------------------LNAVgLSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT- 171
|
170 180
....*....|....*....|....*..
gi 2500156532 182 aEMRVELKV--LIKDLGITTIYVTHDQ 206
Cdd:COG2401 172 -AKRVARNLqkLARRAGITLVVATHHY 197
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
25-177 |
2.25e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 74.72 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLE--EPTEGEIFFGDKVVfsdkkhLSLEPFER---DVAMVFQsyalY 99
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDI------LELSPDERaraGIFLAFQ----Y 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 100 PH-----------MTVYQNMAFPLKNLKYKKKKIREqvikIAQMLRI-ETLLERKPAE-LSGGQRQRVAIGRALVRTPQV 166
Cdd:COG0396 86 PVeipgvsvsnflRTALNARRGEELSAREFLKLLKE----KMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKL 161
|
170
....*....|.
gi 2500156532 167 LLMDEPLSNLD 177
Cdd:COG0396 162 AILDETDSGLD 172
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
8-246 |
3.71e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 75.22 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEptEGEIFFGDKVVFSDKKHLSLEPFER 87
Cdd:PRK15093 6 IRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK--DNWRVTADRMRFDDIDLLRLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 88 ------DVAMVFQ--SYALYPHMTVYQNM--AFPLKNLKYKKKkireQVIKIAQMLRIEtLLERK------------PAE 145
Cdd:PRK15093 84 rklvghNVSMIFQepQSCLDPSERVGRQLmqNIPGWTYKGRWW----QRFGWRKRRAIE-LLHRVgikdhkdamrsfPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 146 LSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQ 225
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250 260
....*....|....*....|.
gi 2500156532 226 QTGSPDELFYCPKNTFVAGFI 246
Cdd:PRK15093 239 ETAPSKELVTTPHHPYTQALI 259
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-262 |
4.16e-15 |
|
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: 74.51 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLEPFERDVAMVFQSYALYPHMTV 104
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 105 YQnmafplknlkykKKKIREQVIKIAQmlRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDaqLRAEM 184
Cdd:cd03291 133 VK------------ACQLEEDITKFPE--KDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD--VFTEK 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500156532 185 RVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELfYCPKNTFVAGFIGTPSMNFLSAEIIKSI 262
Cdd:cd03291 197 EIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL-QSLRPDFSSKLMGYDTFDQFSAERRNSI 273
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-262 |
4.38e-15 |
|
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: 76.87 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLEPFERDVAMVFQSYALYPHMTV 104
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSV 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 105 YQnmafplknlkykKKKIREQVIKIAQmlRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEM 184
Cdd:TIGR01271 522 IK------------ACQLEEDIALFPE--KDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 185 --RVELKVLIKDlgiTTIYVThDQTEAMTLGDRIALLKEGVLQQTGSPDELfYCPKNTFVAGFIGTPSMNFLSAEIIKSI 262
Cdd:TIGR01271 588 feSCLCKLMSNK---TRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSEL-QAKRPDFSSLLLGLEAFDNFSAERRNSI 662
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-179 |
1.11e-14 |
|
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: 71.76 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkkHLSLEPFERDVAMVFQSYALY 99
Cdd:cd03231 12 GRAL-FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-----DFQRDSIARGLLYLGHAPGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 100 PHMTVYQNMAFplknlkYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQ 179
Cdd:cd03231 86 TTLSVLENLRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-177 |
3.26e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.36 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 23 LALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDkkhlsLEPFERDVAMVFQSYALYPHM 102
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKD-----LCTYQKQLCFVGHRSGINPYL 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 103 TVYQNMAFPLKNLKYKKkkireQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:PRK13540 90 TLRENCLYDIHFSPGAV-----GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
8-237 |
4.31e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 72.25 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 8 VRNVKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTegEIFFGDKVVFSDKKHLSLEPFER 87
Cdd:COG4170 6 IRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN--WHVTADRFRWNGIDLLKLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 88 ------DVAMVFQ--SYALYPHMTVYQNM--AFPLKNLKYKKKKIREQVIKIAQML--RI-----ETLLERKPAELSGGQ 150
Cdd:COG4170 84 rkiigrEIAMIFQepSSCLDPSAKIGDQLieAIPSWTFKGKWWQRFKWRKKRAIELlhRVgikdhKDIMNSYPHELTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 151 RQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMrveLKVLIK--DLGITTI-YVTHDQTEAMTLGDRIALLKEGVLQQT 227
Cdd:COG4170 164 CQKVMIAMAIANQPRLLIADEPTNAMESTTQAQI---FRLLARlnQLQGTSIlLISHDLESISQWADTITVLYCGQTVES 240
|
250
....*....|
gi 2500156532 228 GSPDELFYCP 237
Cdd:COG4170 241 GPTEQILKSP 250
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
16-219 |
7.91e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.53 E-value: 7.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 16 STAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIffgdkvvfsdKKHLSLEpferdVAMVFQS 95
Cdd:PRK09544 11 SVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----------KRNGKLR-----IGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 96 YALYPHM--TVYQNMAFPLKNLkykkkkiREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPL 173
Cdd:PRK09544 76 LYLDTTLplTVNRFLRLRPGTK-------KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2500156532 174 SNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALL 219
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
25-205 |
1.03e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.89 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF--GDKVvfsdkKHLSLEPF---ERDV-AMVFQSYAL 98
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqpGIKV-----GYLPQEPQldpTKTVrENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 99 YPHM-----TVYQNMAFPLKNLKYKkkkIREQ-----VIKIAQMLRIETLLE------RKP------AELSGGQRQRVAI 156
Cdd:TIGR03719 96 IKDAldrfnEISAKYAEPDADFDKL---AAEQaelqeIIDAADAWDLDSQLEiamdalRCPpwdadvTKLSGGERRRVAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2500156532 157 GRALVRTPQVLLMDEPLSNLDaqlrAEMRVELKVLIKDLGITTIYVTHD 205
Cdd:TIGR03719 173 CRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
11-233 |
1.21e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.60 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 11 VKKIFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdkKHLSlePFERDVA 90
Cdd:COG3845 260 VENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI----TGLS--PRERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 91 MVF------QSYALYPHMTVYQNMAFPLKNLKYK-------KKKIREQVIKIAQMLRIETLLERKPAE-LSGGQRQRVAI 156
Cdd:COG3845 334 GVAyipedrLGRGLVPDMSVAENLILGRYRRPPFsrggfldRKAIRAFAEELIEEFDVRTPGPDTPARsLSGGNQQKVIL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 157 GRALVRTPQVLLMDEPLSNLD----AQLRAEMrVELkvliKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDE 232
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDvgaiEFIHQRL-LEL----RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAE 488
|
.
gi 2500156532 233 L 233
Cdd:COG3845 489 A 489
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-177 |
1.33e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.98 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFSTAKGRVLALDrINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfSDKKHLSLEPF 85
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEIYKD-LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS---HNLKDINLKWW 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAMVFQ-------------SYALYP-----HMTVYQNM-AFPLKNLKYKKKKIR----------------------- 123
Cdd:PTZ00265 459 RSKIGVVSQdpllfsnsiknniKYSLYSlkdleALSNYYNEdGNDSQENKNKRNSCRakcagdlndmsnttdsneliemr 538
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 124 --------EQVIKIAQMLRI-----------ETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:PTZ00265 539 knyqtikdSEVVDVSKKVLIhdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-217 |
1.45e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.50 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFStakGRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVvfsdkkhlslepf 85
Cdd:TIGR03719 323 IEAENLTKAFG---DKLL-IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 erDVAMVFQSY-ALYPHMTVYQNMAFPLKNLKYKKKKI--REQVIKI-----AQmlrietllERKPAELSGGQRQRVAIG 157
Cdd:TIGR03719 386 --KLAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIpsRAYVGRFnfkgsDQ--------QKKVGQLSGGERNRVHLA 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 158 RALVRTPQVLLMDEPLSNLDAQ-LRAemrveLKVLIKDLGITTIYVTHDQteaMTLgDRIA 217
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDVEtLRA-----LEEALLNFAGCAVVISHDR---WFL-DRIA 507
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-222 |
2.30e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.29 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 21 RVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAglEEPTEGEIFFGDKVVFSDKKHLSlepFERDVAMVFQSYALYP 100
Cdd:TIGR00956 776 RVI-LNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGRPLDSS---FQRSIGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 101 HMTVYQNMAF------PLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAE-LSGGQRQRVAIGRALVRTPQVLL-MDEP 172
Cdd:TIGR00956 850 TSTVRESLRFsaylrqPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 173 LSNLDAQLRAEMRVELKVLIkDLGiTTIYVTHDQTEAMTLG--DRIALLKEG 222
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLA-DHG-QAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-248 |
3.84e-13 |
|
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: 70.81 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 3 KTAILVRN-VKKIFSTAKGRvlALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSdkkhls 81
Cdd:TIGR01257 1934 KTDILRLNeLTKVYSGTSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------ 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 82 lepferDVAMVFQSYALYPHMTVYQNMaFPLKNLKYKKKKIR----EQVIKIA----QMLRIETLLERKPAELSGGQRQR 153
Cdd:TIGR01257 2006 ------NISDVHQNMGYCPQFDAIDDL-LTGREHLYLYARLRgvpaEEIEKVAnwsiQSLGLSLYADRLAGTYSGGNKRK 2078
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 154 VAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDlGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
250
....*....|....*
gi 2500156532 234 fycpKNTFVAGFIGT 248
Cdd:TIGR01257 2158 ----KSKFGDGYIVT 2168
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-230 |
7.96e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.93 E-value: 7.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGleEPTEGEIFFGDKVvfSDKKHLSLEPFER-DVAMVFQSYALYPHMT 103
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGGGAPRGARV--TGDVTLNGEPLAAiDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 104 vyqNMAFPLKNLKYKK------------KKIREQVIKIAQMLRI--ETLLERKPAELSGGQRQRVAIGRAL--------- 160
Cdd:PRK13547 93 ---QPAFAFSAREIVLlgrypharragaLTHRDGEIAWQALALAgaTALVGRDVTTLSGGELARVQFARVLaqlwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 161 VRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSP 230
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-205 |
1.42e-12 |
|
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: 68.67 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 28 INLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDkkhlSLEPFERDVAMVFQSYALYPHMTVYQN 107
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD----NREAYRQLFSAVFSDFHLFDRLLGLDG 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 108 MAFPLknlkykkkkireqviKIAQMLriETL-LERKPA---------ELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:COG4615 427 EADPA---------------RARELL--ERLeLDHKVSvedgrfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQD 489
|
170 180 190
....*....|....*....|....*....|.
gi 2500156532 178 AQLRaemRV---ELKVLIKDLGITTIYVTHD 205
Cdd:COG4615 490 PEFR---RVfytELLPELKARGKTVIAISHD 517
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-229 |
1.48e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.04 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFfgdkvvfsdkkhlslepFERDVAMVFQSyALYPHMTV 104
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------------AERSIAYVPQQ-AWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 105 YQNMAFPLKNLKYKKkkirEQVIKIAQM---LR-----IETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNL 176
Cdd:PTZ00243 738 RGNILFFDEEDAARL----ADAVRVSQLeadLAqlgggLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 177 DAQLrAEMRVELKVLIKDLGITTIYVTHdQTEAMTLGDRIALLKEGVLQQTGS 229
Cdd:PTZ00243 814 DAHV-GERVVEECFLGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGS 864
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-234 |
1.49e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.82 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNVKkiFSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGeiffgdkvvfsdkkHLSLEP 84
Cdd:TIGR00957 636 SITVHNAT--FTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG--------------HVHMKG 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 ferDVAMVFQSyALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRI----ETLLERKPAELSGGQRQRVAIGRAL 160
Cdd:TIGR00957 700 ---SVAYVPQQ-AWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILpsgdRTEIGEKGVNLSGGQKQRVSLARAV 775
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 161 VRTPQVLLMDEPLSNLDAQLRA---EMRVELKVLIKdlGITTIYVTHDQTeAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:TIGR00957 776 YSNADIYLFDDPLSAVDAHVGKhifEHVIGPEGVLK--NKTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-233 |
1.97e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.61 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 5 AILVRNvkKIFS-TAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGlEEPT--EGEIFFGDKVVFSDKkhls 81
Cdd:PLN03130 614 AISIKN--GYFSwDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPPrsDASVVIRGTVAYVPQ---- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 82 lepferdVAMVFQSyalyphmTVYQNMAFPLKNLKYKKkkirEQVIKIAQMLRIETLL---------ERKpAELSGGQRQ 152
Cdd:PLN03130 687 -------VSWIFNA-------TVRDNILFGSPFDPERY----ERAIDVTALQHDLDLLpggdlteigERG-VNISGGQKQ 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 153 RVAIGRALVRTPQVLLMDEPLSNLDAQLRAE-----MRVELKvlikdlGITTIYVThDQTEAMTLGDRIALLKEGVLQQT 227
Cdd:PLN03130 748 RVSMARAVYSNSDVYIFDDPLSALDAHVGRQvfdkcIKDELR------GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEE 820
|
....*.
gi 2500156532 228 GSPDEL 233
Cdd:PLN03130 821 GTYEEL 826
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-224 |
2.36e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.05 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSdkkHLSLEPfERDVA-MVF---------Q 94
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVA---RLQQDP-PRNVEgTVYdfvaegieeQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 95 SYAL--YpHMTVYQNMAFPLKNLKYKKKKIREQV---------IKIAQMLrieTLLERKP----AELSGGQRQRVAIGRA 159
Cdd:PRK11147 95 AEYLkrY-HDISHLVETDPSEKNLNELAKLQEQLdhhnlwqleNRINEVL---AQLGLDPdaalSSLSGGWLRKAALGRA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 160 LVRTPQVLLMDEPLSNLDaqlraemrVE----LKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVL 224
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLD--------IEtiewLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
11-226 |
2.72e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 11 VKKIFSTAKGRVlalDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdKKHLSLEPFERDVA 90
Cdd:PRK09700 268 VRNVTSRDRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI---SPRSPLDAVKKGMA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 91 MVFQSY---ALYPHMTVYQNMAFPLKNLKY-------KKKKIREQVIKIAQ--MLRIE-TLLERKPAELSGGQRQRVAIG 157
Cdd:PRK09700 342 YITESRrdnGFFPNFSIAQNMAISRSLKDGgykgamgLFHEVDEQRTAENQreLLALKcHSVNQNITELSGGNQQKVLIS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 158 RALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLiKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQ 226
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
90-234 |
3.17e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.75 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 90 AMVFQSYALYpHMTVYQNMAFplknlkYKKKKIREQVIKIAQMLRIETLLERKPAE-----------LSGGQRQRVAIGR 158
Cdd:PTZ00265 1299 SIVSQEPMLF-NMSIYENIKF------GKEDATREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIAR 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 159 ALVRTPQVLLMDEPLSNLDAQlrAEMRVELKVL-IKDLGITTIYVTHDQTEAMTLGDRIALLKE-----GVLQQTGSPDE 232
Cdd:PTZ00265 1372 ALLREPKILLLDEATSSLDSN--SEKLIEKTIVdIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEE 1449
|
..
gi 2500156532 233 LF 234
Cdd:PTZ00265 1450 LL 1451
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-238 |
4.41e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.49 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 21 RVLaLDRINLEIKPGELFIILGPSGCGKS----TLLNII-AGLEEpTEGEIffgdkvvfsdkkHLSLEPFE------RDV 89
Cdd:PRK10418 16 QPL-VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQ-TAGRV------------LLDGKPVApcalrgRKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 90 AMVFQS--YALYPhmtvYQNMAfplkNLKYKKKKIREQVIKIAQMLRI---------ETLLERKPAELSGGQRQRVAIGR 158
Cdd:PRK10418 82 ATIMQNprSAFNP----LHTMH----THARETCLALGKPADDATLTAAleavglenaARVLKLYPFEMSGGMLQRMMIAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 159 ALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFYCPK 238
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-177 |
7.67e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.10 E-value: 7.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 28 INLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFgdkvvfsDKKHLSLEPFERDVAMVFQSYALYPHMTVYQN 107
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-------DGKTATRGDRSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 108 MAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERkpaELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:PRK13543 103 LHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVR---QLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-233 |
9.49e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.30 E-value: 9.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 20 GRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEI--FFGDkvvFSDKKHlslepfeRD-----VAMV 92
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevLGGD---MADARH-------RRavcprIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 93 FQSYA--LYPHMTVYQNMAF-------PLKNlkykkkkiREQvikiaqmlRIETLLER--------KPA-ELSGGQRQRV 154
Cdd:NF033858 82 PQGLGknLYPTLSVFENLDFfgrlfgqDAAE--------RRR--------RIDELLRAtglapfadRPAgKLSGGMKQKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 155 AIGRALVRTPQVLLMDE------PLS-----NLDAQLRAEmRVELKVLikdlgITTIYVthDQTEAMtlgDRIALLKEGV 223
Cdd:NF033858 146 GLCCALIHDPDLLILDEpttgvdPLSrrqfwELIDRIRAE-RPGMSVL-----VATAYM--EEAERF---DWLVAMDAGR 214
|
250
....*....|
gi 2500156532 224 LQQTGSPDEL 233
Cdd:NF033858 215 VLATGTPAEL 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-222 |
1.25e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 22 VLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEI-FFGDKVVFSDKKHLSlepfERDVAMVFQSYALYP 100
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlYLGKEVTFNGPKSSQ----EAGIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 101 HMTVYQNM----AFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNL 176
Cdd:PRK10762 93 QLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2500156532 177 -DAQLRAEMRV--ELKVliKDLGIttIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:PRK10762 173 tDTETESLFRVirELKS--QGRGI--VYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-268 |
1.60e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVKkifSTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEI-FFGDKVVFSDKKH 79
Cdd:PRK15056 2 MQQAGIVVNDVT---VTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsILGQPTRQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 80 LslepferdVAMVFQSYAL---YP-------HMTVYQNMAFplknlkYKKKKIREQVIKIAQMLRIETL--LERKPAELS 147
Cdd:PRK15056 79 L--------VAYVPQSEEVdwsFPvlvedvvMMGRYGHMGW------LRRAKKRDRQIVTAALARVDMVefRHRQIGELS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 148 GGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLiKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLqqT 227
Cdd:PRK15056 145 GGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVL--A 221
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2500156532 228 GSPDELFYCPKNTFVA--GFIGTPSMNFLSAEIIKSIKKPNIT 268
Cdd:PRK15056 222 SGPTETTFTAENLELAfsGVLRHVALNGSEESIITDDERPFIS 264
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-204 |
1.84e-11 |
|
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: 65.16 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 17 TAKGRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGL--------EEPTEGEIFFgdkvvfsdkkhlslepferd 88
Cdd:TIGR00954 461 TPNGDVL-IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFY-------------------- 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 89 vamVFQSyalyPHMTV---YQNMAFPLKNLKYKKKKIREQV-IKIAQMLRIETLLERKPA---------ELSGGQRQRVA 155
Cdd:TIGR00954 520 ---VPQR----PYMTLgtlRDQIIYPDSSEDMKRRGLSDKDlEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIA 592
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2500156532 156 IGRALVRTPQVLLMDEPLSnldaQLRAEMRVELKVLIKDLGITTIYVTH 204
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTS----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
24-230 |
2.04e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 62.43 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKvvfsDKKHLSLEPFERDVAMVFQSYALYPHmT 103
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI----DISTIPLEDLRSSLTIIPQDPTLFSG-T 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 104 VYQNMafplknlkykKKKIREQVIKIAQMLRIetllERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAE 183
Cdd:cd03369 98 IRSNL----------DPFDEYSDEEIYGALRV----SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 184 MRVELKVLIKDLGITTIyvthdqteAMTLG-----DRIALLKEGVLQQTGSP 230
Cdd:cd03369 164 IQKTIREEFTNSTILTI--------AHRLRtiidyDKILVMDAGEVKEYDHP 207
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
25-205 |
2.52e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFF--GDKVVFsdkkhLSLEP-----------FERDVAM 91
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPapGIKVGY-----LPQEPqldpektvrenVEEGVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 92 VFQSYALYPHmtVYQNMAFPlknLKYKKKKIREQ-----VIKIAQMLRIETLLER------------KPAELSGGQRQRV 154
Cdd:PRK11819 98 VKAALDRFNE--IYAAYAEP---DADFDALAAEQgelqeIIDAADAWDLDSQLEIamdalrcppwdaKVTKLSGGERRRV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 155 AIGRALVRTPQVLLMDEPLSNLDAQlraemRVE-LKVLIKDLGITTIYVTHD 205
Cdd:PRK11819 173 ALCRLLLEKPDMLLLDEPTNHLDAE-----SVAwLEQFLHDYPGTVVAVTHD 219
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-259 |
3.14e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 62.77 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 33 KPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEifFGDkvvfsdkkhlslEPFERDVAMVFQSYALYPHMTVYQNMAFPL 112
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDD------------PPDWDEILDEFRGSELQNYFTKLLEGDVKV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 113 KNLKYKKKKI-----------------REQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSN 175
Cdd:cd03236 90 IVKPQYVDLIpkavkgkvgellkkkdeRGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 176 LDAQLRAEMRVELKVLIKDlGITTIYVTHDQTEAMTLGDRIALLkegvlqqTGSPDE--LFYCPK------NTFVAGFIG 247
Cdd:cd03236 170 LDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL-------YGEPGAygVVTLPKsvregiNEFLDGYLP 241
|
250
....*....|..
gi 2500156532 248 TPSMNFLSAEII 259
Cdd:cd03236 242 TENMRFREESIE 253
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-222 |
3.64e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.04 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 9 RNVKKIFstakGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLeEPT---EGEIFF-GDKVVFSDKKhlslEP 84
Cdd:NF040905 5 RGITKTF----PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFdGEVCRFKDIR----DS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 85 FERDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERkPAELSG----GQRQRVAIGRAL 160
Cdd:NF040905 76 EALGIVIIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDES-PDTLVTdigvGKQQLVEIAKAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 161 VRTPQVLLMDEP---LSNLDAQLRAEMRVELkvliKDLGITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:NF040905 155 SKDVKLLILDEPtaaLNEEDSAALLDLLLEL----KAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-209 |
4.24e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGlEEP---TEGEIFFGDK-----VVFSDKKH-------LSLE----PF 85
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPqgySNDLTLFGRRrgsgeTIWDIKKHigyvsssLHLDyrvsTS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 ERDVAM--VFQSYALYPHMTVYQNmafplknlkykkkkireqviKIAQ----MLRIETLLERKP-AELSGGQRQRVAIGR 158
Cdd:PRK10938 355 VRNVILsgFFDSIGIYQAVSDRQQ--------------------KLAQqwldILGIDKRTADAPfHSLSWGQQRLALIVR 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 159 ALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIYVTHDQTEA 209
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-234 |
5.09e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGleeptegeiffgdkvvfsdkkhlSLEPFERDVAMVFQSYALYPHM-- 102
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------------ELSHAETSSVVIRGSVAYVPQVsw 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 103 ----TVYQNMAFPLKNLKYKKKKIREqVIKIAQML-----RIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPL 173
Cdd:PLN03232 690 ifnaTVRENILFGSDFESERYWRAID-VTALQHDLdllpgRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 174 SNLDAQLRAE-----MRVELKvlikdlGITTIYVThDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PLN03232 769 SALDAHVAHQvfdscMKDELK------GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-321 |
5.88e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.97 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 32 IKPGELFIILGPSGCGKSTLLNIIAGleePTEGEIFFGDKVVFSDKkhLSLEPFER----DVAMVFQSYALYPHMTVYQN 107
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAS---NTDGFHIGVEGVITYDG--ITPEEIKKhyrgDVVYNAETDVHFPHLTVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 108 MAFPLK---NLKYKKKKIREQVIK-IAQM-LRIETLLERKPAE--------LSGGQRQRVAIGRALVRTPQVLLMDEPLS 174
Cdd:TIGR00956 159 LDFAARcktPQNRPDGVSREEYAKhIADVyMATYGLSHTRNTKvgndfvrgVSGGERKRVSIAEASLGGAKIQCWDNATR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 175 NLDAQLRAEMRVELKVlIKDLGITTIYVTHDQT--EAMTLGDRIALLKEGVLQQTGSPDEL--------FYCPKNTFVAG 244
Cdd:TIGR00956 239 GLDSATALEFIRALKT-SANILDTTPLVAIYQCsqDAYELFDKVIVLYEGYQIYFGPADKAkqyfekmgFKCPDRQTTAD 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500156532 245 FIgTPSMNFLSAEIIKSIKKPnitIGIRPQDIEIRPPNKgiiNAFVKLVEKIgDKYLVHVDYRKQKIIIETSNFSKE 321
Cdd:TIGR00956 318 FL-TSLTSPAERQIKPGYEKK---VPRTPQEFETYWRNS---PEYAQLMKEI-DEYLDRCSESDTKEAYRESHVAKQ 386
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
28-182 |
1.06e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 60.27 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 28 INLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKhlslePFerdVAMVFQSYALYPHMTVYQN 107
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK-----PY---CTYIGHNLGLKLEMTVFEN 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500156532 108 MAFPLKNLKYKkkkirEQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRA 182
Cdd:PRK13541 91 LKFWSEIYNSA-----ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
31-216 |
1.45e-10 |
|
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: 59.51 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 31 EIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFgdkvvfsDKKHLSLEPferdvamvfqsyalyphmtvyqnmaf 110
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-------DGITPVYKP-------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 111 plknlkykkkkireQVIKiaqmlrietllerkpaeLSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKV 190
Cdd:cd03222 68 --------------QYID-----------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180
....*....|....*....|....*.
gi 2500156532 191 LIKDLGITTIYVTHDQTEAMTLGDRI 216
Cdd:cd03222 117 LSEEGKKTALVVEHDLAVLDYLSDRI 142
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
25-177 |
6.64e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.65 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLE--EPTEGEiffgdkVVFSDKKHLSLEPFER---DVAMVFQsyalY 99
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGT------VEFKGKDLLELSPEDRageGIFMAFQ----Y 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 100 PHMTVYQNMAFPLKNLKYKKKKIREQVI------------KIAQMLRIETLLERKPAE-LSGGQRQRVAIGRALVRTPQV 166
Cdd:PRK09580 87 PVEIPGVSNQFFLQTALNAVRSYRGQEPldrfdfqdlmeeKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPEL 166
|
170
....*....|.
gi 2500156532 167 LLMDEPLSNLD 177
Cdd:PRK09580 167 CILDESDSGLD 177
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-177 |
1.01e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.50 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAIL-VRNVKkifsTAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGleEP----TEGEIFFGDKVVfs 75
Cdd:CHL00131 2 NKNKPILeIKNLH----ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESI-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 76 dkkhLSLEPFERDVAMVFQSYAlYP-HMTVYQNMAF--------------PLKNLKYKKKKIREQvIKIAQMlrIETLLE 140
Cdd:CHL00131 74 ----LDLEPEERAHLGIFLAFQ-YPiEIPGVSNADFlrlaynskrkfqglPELDPLEFLEIINEK-LKLVGM--DPSFLS 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 2500156532 141 RKPAE-LSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:CHL00131 146 RNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLD 183
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-182 |
1.15e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 6 ILVRNVKKIFStakGRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVvfsdkkhlslepf 85
Cdd:PRK11819 325 IEAENLSKSFG---DRLL-IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV------------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 86 erDVAMVFQSY-ALYPHMTVYQNmafplknlkykkkkIRE--QVIKIA-------------------QmlrietllERKP 143
Cdd:PRK11819 388 --KLAYVDQSRdALDPNKTVWEE--------------ISGglDIIKVGnreipsrayvgrfnfkggdQ--------QKKV 443
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2500156532 144 AELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQ-LRA 182
Cdd:PRK11819 444 GVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVEtLRA 483
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-225 |
1.36e-09 |
|
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: 59.07 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPT-EGEIFFGDKVVfsDKKHlSLEPFERDVAMVFQS---YALYP 100
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPV--DIRN-PAQAIRAGIAMVPEDrkrHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 101 HMTVYQNMAFPLKNLKYKKKKI----REQVIKIA-QMLRIETLLERKP-AELSGGQRQRVAIGRALVRTPQVLLMDEPLS 174
Cdd:TIGR02633 353 ILGVGKNITLSVLKSFCFKMRIdaaaELQIIGSAiQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 175 NLDAQLRAEMRVELKVLIKDlGITTIYVTHDQTEAMTLGDRIALLKEGVLQ 225
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-224 |
1.59e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 28 INLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSLE------PFERdvamvfQSYALYPH 101
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLArglvylPEDR------QSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 102 MTVYQNM-AFPLKNLKYKKKKIREQVI--KIAQMLRIETLLERKPAE-LSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:PRK15439 356 APLAWNVcALTHNRRGFWIKPARENAVleRYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2500156532 178 AQLRAemrvELKVLIKDL---GITTIYVTHDQTEAMTLGDRIALLKEGVL 224
Cdd:PRK15439 436 VSARN----DIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-222 |
2.15e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.09 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 33 KPGELFIILGPSGCGKSTLLNIIAGLEEP--TEGEIffgdKVVFSDKKHlslEPFERDVAMVFQSYALYPHMTVYQNMAF 110
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDI----RISGFPKKQ---ETFARISGYCEQNDIHSPQVTVRESLIY 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 111 PLKNLKYKKKKIREQVIKIAQMLRIETLLERKPA--------ELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRA 182
Cdd:PLN03140 977 SAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAivglpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1056
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2500156532 183 -EMRVELKVLikDLGITTIYVTH----DQTEAMtlgDRIALLKEG 222
Cdd:PLN03140 1057 iVMRTVRNTV--DTGRTVVCTIHqpsiDIFEAF---DELLLMKRG 1096
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-233 |
2.70e-09 |
|
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: 58.80 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 23 LALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFG---------------------DKVVFSDKKHLS 81
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDglniakiglhdlrfkitiipqDPVLFSGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 82 LEPF----ERDVAMVFQSYALYPHMTvyqnmAFPLKnlkykkkkireqvikiaqmlrietlLERKPAE----LSGGQRQR 153
Cdd:TIGR00957 1380 LDPFsqysDEEVWWALELAHLKTFVS-----ALPDK-------------------------LDHECAEggenLSVGQRQL 1429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 154 VAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDLGITTIyvTHDQTEAMTLgDRIALLKEGVLQQTGSPDEL 233
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTI--AHRLNTIMDY-TRVIVLDKGEVAEFGAPSNL 1506
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
141-233 |
3.29e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.82 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 141 RKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDlGITTIYVTHDQTEAMTLGDRIALLK 220
Cdd:NF000106 140 RAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVID 218
|
90
....*....|...
gi 2500156532 221 EGVLQQTGSPDEL 233
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
14-233 |
6.65e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 6.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 14 IFSTAKGRVLALDriNLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIffgdKVVFSDKKHLSLEPFERDVAMVF 93
Cdd:PRK10938 10 TFRLSDTKTLQLP--SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER----QSQFSHITRLSFEQLQKLVSDEW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 94 Q---SYALYPH-----MTVYQnmafplknlkykkkKIREQV------IKIAQMLRIETLLERKPAELSGGQRQRVAIGRA 159
Cdd:PRK10938 84 QrnnTDMLSPGeddtgRTTAE--------------IIQDEVkdparcEQLAQQFGITALLDRRFKYLSTGETRKTLLCQA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500156532 160 LVRTPQVLLMDEPLSNLDAQLRAEMRVELKVLIKDlGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:PRK10938 150 LMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-232 |
6.83e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 1 MKKTAILVRNVKKIFStakGRVLaLDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHL 80
Cdd:PRK15064 315 LHRNALEVENLTKGFD---NGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 81 SLEPFERDvamvfqsyalyphMTVYQNMAfplknlKYKKKKIREQVIK--IAQMLRIETLLERKPAELSGGQRQRVAIGR 158
Cdd:PRK15064 391 HAYDFEND-------------LTLFDWMS------QWRQEGDDEQAVRgtLGRLLFSQDDIKKSVKVLSGGEKGRMLFGK 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500156532 159 ALVRTPQVLLMDEPLSNLDAQlraemRVE-LKVLIKDLGITTIYVTHDQTEAMTLGDRIALLK-EGVLQQTGSPDE 232
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDME-----SIEsLNMALEKYEGTLIFVSHDREFVSSLATRIIEITpDGVVDFSGTYEE 522
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
40-177 |
9.86e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.79 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 40 ILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKV---VFS----DKKHLSLEPFerdvamvfqsyalyphmtVYQNMAFPl 112
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVFRSAKVrmaVFSqhhvDGLDLSSNPL------------------LYMMRCFP- 600
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500156532 113 knlkykkkKIREQVIKiAQM--LRIETLLERKPA-ELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:PLN03073 601 --------GVPEQKLR-AHLgsFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-222 |
1.03e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.55 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVFSDKKHLSL--------EPFERDvamvfqsy 96
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLangivyisEDRKRD-------- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 97 ALYPHMTVYQNMA------FPLKNLKYKKKKIREQVIKIAQMLRIET-LLERKPAELSGGQRQRVAIGRALVRTPQVLLM 169
Cdd:PRK10762 340 GLVLGMSVKENMSltalryFSRAGGSLKHADEQQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 170 DEPLSNLDAQLRAEMrVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:PRK10762 420 DEPTRGVDVGAKKEI-YQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-224 |
1.06e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 28 INLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIF-FGDKVVFSDKKH-----LSLEPFERdvamvfQSYALYPH 101
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYlDGKPIDIRSPRDairagIMLCPEDR------KAEGIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 102 MTVYQNMAFPLKNLKYKKKKI------REQVIKIAQMLRIETL-LERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLS 174
Cdd:PRK11288 346 HSVADNINISARRHHLRAGCLinnrweAENADRFIRSLNIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 175 NLDAQLRAemrvELKVLIKDL---GITTIYVTHDQTEAMTLGDRIALLKEGVL 224
Cdd:PRK11288 426 GIDVGAKH----EIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-218 |
1.47e-08 |
|
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: 53.15 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 34 PGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFgdkvvfsdkkhLSLEPFERDVAmvfqsyalyphmtvyqnmafplk 113
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------IDGEDILEEVL----------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 114 nlkykkkkireqvikiaqMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRVE-----L 188
Cdd:smart00382 47 ------------------DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlL 108
|
170 180 190
....*....|....*....|....*....|
gi 2500156532 189 KVLIKDLGITTIYVTHDQTEAMTLGDRIAL 218
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-205 |
2.39e-08 |
|
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: 55.56 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 33 KPGELFIILGPSGCGKSTLLNIIAGLEEPTegeifFGDkvvfsdkkhLSLEPFERDVAMVFQSYALYPHMT-VYQNM--- 108
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPN-----LGD---------YDEEPSWDEVLKRFRGTELQDYFKkLANGEikv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 109 --------AFPLKNLKYKKKKI-----REQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSN 175
Cdd:COG1245 163 ahkpqyvdLIPKVFKGTVRELLekvdeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190
....*....|....*....|....*....|....*
gi 2500156532 176 LDAQLRaemrveLKV--LIKDL---GITTIYVTHD 205
Cdd:COG1245 243 LDIYQR------LNVarLIRELaeeGKYVLVVEHD 271
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
3-233 |
7.51e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.90 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 3 KTAILVRNVKKIFstakgrvLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIffgdkvvfsdKKHlsl 82
Cdd:PRK13546 25 KDALIPKHKNKTF-------FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV----------DRN--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 83 epfeRDVAMVFQSYALYPHMTVYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVR 162
Cdd:PRK13546 85 ----GEVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 163 TPQVLLMDEPLSNLDaQLRAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:PRK13546 161 NPDILVIDEALSVGD-QTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-225 |
9.44e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 9.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 26 DRINLEIKPGELFIILGPSGCGKSTLLNIIAGL-EEPTEGEIFFGDKVVfsdKKHLSLEPFERDVAMVFQS---YALYPH 101
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPV---KIRNPQQAIAQGIAMVPEDrkrDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 102 MTVYQNMAFPLKNLKYKKKKIRE-----QVIKIAQMLRIETL-LERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSN 175
Cdd:PRK13549 356 MGVGKNITLAALDRFTGGSRIDDaaelkTILESIQRLKVKTAsPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2500156532 176 LDAQLRAemrvELKVLIKDL---GITTIYVTHDQTEAMTLGDRIALLKEGVLQ 225
Cdd:PRK13549 436 IDVGAKY----EIYKLINQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-205 |
1.22e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 7 LVRNvkkiFSTAkgrVLALDRINLeikpgelfiiLGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVvfsdkkhlslepfe 86
Cdd:PRK11147 334 LVKD----FSAQ---VQRGDKIAL----------IGPNGCGKTTLLKLMLGQLQADSGRIHCGTKL-------------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 87 rDVAMvFQSY--ALYPHMTVYQNMAfplknlkykkkkirE--QVIKIAQMLR-IETLLE---------RKPAE-LSGGQR 151
Cdd:PRK11147 383 -EVAY-FDQHraELDPEKTVMDNLA--------------EgkQEVMVNGRPRhVLGYLQdflfhpkraMTPVKaLSGGER 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2500156532 152 QRVAIGRALVRTPQVLLMDEPLSNLDaqlraemrVE----LKVLIKDLGITTIYVTHD 205
Cdd:PRK11147 447 NRLLLARLFLKPSNLLILDEPTNDLD--------VEtlelLEELLDSYQGTVLLVSHD 496
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
129-205 |
1.47e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 1.47e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2500156532 129 IAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDaqLRAEMRVELkvLIKDL--GITTIYVTHD 205
Cdd:PRK13409 196 VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--IRQRLNVAR--LIRELaeGKYVLVVEHD 270
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-234 |
1.68e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 32 IKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDkvvfSDKKHLSLEPFERDVAMVFQSYALYPHMTVYQNMAFP 111
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD----CDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFS 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 112 LKNLKYKKKKIREQVIKIAqMLRIETLLERKPAE----LSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMRve 187
Cdd:PLN03232 1335 EHNDADLWEALERAHIKDV-IDRNPFGLDAEVSEggenFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ-- 1411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2500156532 188 lKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELF 234
Cdd:PLN03232 1412 -RTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-241 |
7.69e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 19 KGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIffgdKVVFSDKKHLSLEPFERDVAMVFQSYAL 98
Cdd:PTZ00243 1320 EGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEI----RVNGREIGAYGLRELRRQFSMIPQDPVL 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 99 YPHmTVYQNM-----AFPLKN-LKYKKKKIREQVIkiAQMLRIETLLERKPAELSGGQRQRVAIGRALV-RTPQVLLMDE 171
Cdd:PTZ00243 1396 FDG-TVRQNVdpfleASSAEVwAALELVGLRERVA--SESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDE 1472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 172 PLSNLDAQLraEMRVELKVLIKDLGITTIYVTHD-QTEAMTlgDRIALLKEGVLQQTGSPDELFYCPKNTF 241
Cdd:PTZ00243 1473 ATANIDPAL--DRQIQATVMSAFSAYTVITIAHRlHTVAQY--DKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
25-233 |
1.98e-06 |
|
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: 48.70 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEpTEGEIFFgDKVVFSDkkhLSLEPFERDVAMVFQSYALYPHmTV 104
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQI-DGVSWNS---VPLQKWRKAFGVIPQKVFIFSG-TF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 105 YQNMAfPLKNLKYkkkkirEQVIKIAQMLRIETLLERKPAE-----------LSGGQRQRVAIGRALVRTPQVLLMDEPL 173
Cdd:cd03289 94 RKNLD-PYGKWSD------EEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 174 SNLDAqlrAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDEL 233
Cdd:cd03289 167 AHLDP---ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKL 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
28-222 |
2.06e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 28 INLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDKVVfsdKKHLSLEPFERDVAMVFQ---SYALYPHMTV 104
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI---NNHNANEAINHGFALVTEerrSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 105 -----YQNM-AFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKP-AELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:PRK10982 344 gfnslISNIrNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2500156532 178 AQLRAEM-RVELKVLIKDLGIttIYVTHDQTEAMTLGDRIALLKEG 222
Cdd:PRK10982 424 VGAKFEIyQLIAELAKKDKGI--IIISSEMPELLGITDRILVMSNG 467
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
24-216 |
9.04e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.39 E-value: 9.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNiiAGLEEPTEGEI------FFGDKVVFSDKkhLSLepferdvamvfqsya 97
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARLisflpkFSRNKLIFIDQ--LQF--------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 98 lyphmtvyqnmafplknlkykkkkireqVIKIAqmlrIETL-LERKPAELSGGQRQRVAIGRALVRTPQ--VLLMDEPLS 174
Cdd:cd03238 71 ----------------------------LIDVG----LGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPST 118
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2500156532 175 NLDAQLRAEMRVELKVLIkDLGITTIYVTHDQTeAMTLGDRI 216
Cdd:cd03238 119 GLHQQDINQLLEVIKGLI-DLGNTVILIEHNLD-VLSSADWI 158
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
24-174 |
1.40e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.81 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIffgdkvvfsDKKHlslepferDVAMVFQSYALYPHMT 103
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV---------DIKG--------SAALIAISSGLNGQLT 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500156532 104 VYQNMAFPLKNLKYKKKKIREQVIKIAQMLRIETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLS 174
Cdd:PRK13545 102 GIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-206 |
2.90e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 16 STAKGRVLALDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGdkvvfsdkKHLSLEPFERDvamvfQS 95
Cdd:PRK10636 319 SAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA--------KGIKLGYFAQH-----QL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 96 YALYPHMTVYQNMAfplknlkykkkKIREQVIKiaQMLR------------IETLLERkpaeLSGGQRQRVAIGRALVRT 163
Cdd:PRK10636 386 EFLRADESPLQHLA-----------RLAPQELE--QKLRdylggfgfqgdkVTEETRR----FSGGEKARLVLALIVWQR 448
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2500156532 164 PQVLLMDEPLSNLDaqlrAEMRVELKVLIKDLGITTIYVTHDQ 206
Cdd:PRK10636 449 PNLLLLDEPTNHLD----LDMRQALTEALIDFEGALVVVSHDR 487
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
25-248 |
1.00e-04 |
|
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: 43.36 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFgDKVvfsDKKHLSLEPFERDVAMVFQSYALYPhmtv 104
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI-DGI---DISKLPLHTLRSRLSIILQDPILFS---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 105 yQNMAFPLKNLKYKKKKIREQVIKIAQ---MLR-----IETLLERKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNL 176
Cdd:cd03288 109 -GSIRFNLDPECKCTDDRLWEALEIAQlknMVKslpggLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 177 DAqlrAEMRVELKVLIKDLGITTIYVTHDQTEAMTLGDRIALLKEGVLQQTGSPDELFyCPKNTFVAGFIGT 248
Cdd:cd03288 188 DM---ATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL-AQEDGVFASLVRT 255
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-233 |
1.23e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.96 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 25 LDRINLEIKPGELFIILGPSGCGKSTLLNIIAGLEEPTEGEIFFGDkvvfSDKKHLSLEPFERDVAMVFQSYALYPHmTV 104
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG----CDISKFGLMDLRKVLGIIPQAPVLFSG-TV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 105 YQNM-AFPLKNLKYKKKKIREQVIKiaQMLRIETL-LERKPAE----LSGGQRQRVAIGRALVRTPQVLLMDEPLSNL-- 176
Cdd:PLN03130 1330 RFNLdPFNEHNDADLWESLERAHLK--DVIRRNSLgLDAEVSEagenFSVGQRQLLSLARALLRRSKILVLDEATAAVdv 1407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500156532 177 --DAQLRAEMRVELK---VLIKDLGITTIYVThdqteamtlgDRIALLKEGVLQQTGSPDEL 233
Cdd:PLN03130 1408 rtDALIQKTIREEFKsctMLIIAHRLNTIIDC----------DRILVLDAGRVVEFDTPENL 1459
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
139-238 |
1.48e-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: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 139 LERKPAELSGGQRQRVA----IGRALVRTPQVLlmDEPLSNLDAQLRAEMRVELKVLiKDLGITTIYVTHDQtEAMTLGD 214
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRlatqIGSGLTGVLYVL--DEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDE-DTIRAAD 557
|
90 100 110
....*....|....*....|....*....|
gi 2500156532 215 RI------ALLKEGVLQQTGSPDELFYCPK 238
Cdd:TIGR00630 558 YVidigpgAGEHGGEVVASGTPEEILANPD 587
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
139-216 |
2.48e-04 |
|
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: 41.86 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 139 LERKPAELSGGQRQRVA----IGRALVRTPQVLlmDEPLSNLDAQLRAEMRVELKVLiKDLGITTIYVTHDQtEAMTLGD 214
Cdd:cd03270 131 LSRSAPTLSGGEAQRIRlatqIGSGLTGVLYVL--DEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE-DTIRAAD 206
|
..
gi 2500156532 215 RI 216
Cdd:cd03270 207 HV 208
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
141-177 |
2.85e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 2.85e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2500156532 141 RKPAELSGGQRQRVAIGRALVRTPQVLLMDEPLSNLD 177
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-205 |
5.90e-04 |
|
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: 40.67 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 37 LFIILGPSGCGKSTLLNIIA----GLEEPTEGEIFFGDKVVFSDKKHLSLEpferdvaMVFQSYALYPhMTVYQNMAfpl 112
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKyaltGELPPNSKGGAHDPKLIREGEVRAQVK-------LAFENANGKK-YTITRSLA--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 113 knlkykkkkIREQVIKIAQMlRIETLLERKPAELSGGQRQ------RVAIGRAL-VRTPqVLLMDEPLSNLDAQLRAEMR 185
Cdd:cd03240 93 ---------ILENVIFCHQG-ESNWPLLDMRGRCSGGEKVlasliiRLALAETFgSNCG-ILALDEPTTNLDEENIEESL 161
|
170 180
....*....|....*....|.
gi 2500156532 186 VELKVLIKDLGI-TTIYVTHD 205
Cdd:cd03240 162 AEIIEERKSQKNfQLIVITHD 182
|
|
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
24-56 |
1.37e-03 |
|
checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).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: 129690 [Multi-domain] Cd Length: 637 Bit Score: 40.71 E-value: 1.37e-03
10 20 30
....*....|....*....|....*....|...
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIA 56
Cdd:TIGR00602 99 WLKAQVLENAPKRILLITGPSGCGKSTTIKILS 131
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
24-56 |
6.84e-03 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 37.25 E-value: 6.84e-03
10 20 30
....*....|....*....|....*....|...
gi 2500156532 24 ALDRINLEIKPGELFIILGPSGCGKSTLLNIIA 56
Cdd:pfam03215 34 WLDAMFLENAKHRILLISGPSGCGKSTVIKELS 66
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
146-246 |
8.65e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 38.29 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500156532 146 LSGGQRQRVAIGRALVRTPQVLLMDEPLSNLDAQLRAEMrVELKVLIKDLGITTIYVTHDQ--TEAMTLGDRIALLKEGV 223
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQI-VKCLQQIVHLTEATVLMSLLQpaPETFDLFDDIILLSEGQ 415
|
90 100 110
....*....|....*....|....*....|.
gi 2500156532 224 LQQTGSPDEL--------FYCPKNTFVAGFI 246
Cdd:PLN03140 416 IVYQGPRDHIleffescgFKCPERKGTADFL 446
|
|
| |
