|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-241 |
5.05e-97 |
|
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: 284.24 E-value: 5.05e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMM 79
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLkPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQFTTVAFDYTVYETVLMGayRQQAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEI 159
Cdd:COG1120 81 PQEPPAPFGLTVRELVALG--RYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEFLQTIFETD 239
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVE 238
|
..
gi 488286290 240 IV 241
Cdd:COG1120 239 AR 240
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-240 |
2.51e-73 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 223.81 E-value: 2.51e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKelatkVAMM 79
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLpPTSGTVRLFGKPPRRARRR-----IGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQFTTVAFDY--TVYETVLMGAYRQQaqRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDP 157
Cdd:COG1121 81 PQRAEVDWDFpiTVRDVVLMGRYGRR--GLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 158 EIILLDEPNNHLDIRYQQELIQQLNEWsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVaAQGDFQTLASKEFLQTIFE 237
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEEVLTPENLSRAYG 236
|
...
gi 488286290 238 TDI 240
Cdd:COG1121 237 GPV 239
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-221 |
1.74e-70 |
|
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: 214.22 E-value: 1.74e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 3 ELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQ 81
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLkPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 82 fttvafdytvyetvlmgayrqqaqrflpivskqekervlyYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIIL 161
Cdd:cd03214 81 ----------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 162 LDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-218 |
4.24e-65 |
|
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: 201.61 E-value: 4.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 3 ELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKelatkVAMMSQ 81
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkPTSGSIRVFGKPLEKERKR-----IGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 82 FTTVAFDY--TVYETVLMGAYRQQaqRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEI 159
Cdd:cd03235 76 RRSIDRDFpiSVRDVVLMGLYGHK--GLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLNEWsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVA 218
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-240 |
5.33e-64 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 200.31 E-value: 5.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY-SGSVLIDGQEVHGQKRKELATKVAMM 79
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPdSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQFTTVAFDYTVYETVLMGayrqqaqRFlPI----VSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQ 155
Cdd:COG4604 81 RQENHINSRLTVRELVAFG-------RF-PYskgrLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 156 DPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEFLQTI 235
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDI 232
|
....*
gi 488286290 236 FETDI 240
Cdd:COG4604 233 YDTDI 237
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-241 |
7.78e-64 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 199.96 E-value: 7.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHGQKRKELATKVAMM 79
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQFTTVAFDYTVYETVLMGAYRQQAQRflpivsKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQ---- 155
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAPHGSSA------AQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwep 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 156 ---DPEIILLDEPNNHLDIRYQQELIQQLNEWsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEFL 232
Cdd:COG4559 155 vdgGPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELL 233
|
....*....
gi 488286290 233 QTIFETDIV 241
Cdd:COG4559 234 ERVYGADLR 242
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-221 |
1.62e-60 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 191.52 E-value: 1.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHGQKRKELATKVAMM 79
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQFTTVAFDYTVYETVLMGAYRqqaqrfLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQ---- 155
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAP------HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwep 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 156 --DPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK13548 156 dgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-233 |
1.89e-58 |
|
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: 185.23 E-value: 1.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 13 QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMM-----SQFttva 86
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLkPTSGEVLVDGKDITKKNLRELRRKVGLVfqnpdDQL---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 87 FDYTVYETVLMGAYRQQaqrflpiVSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:COG1122 89 FAPTVEEDVAFGPENLG-------LPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286290 166 NNHLDIRYQQELIQQLNEWsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQT-LASKEFLQ 233
Cdd:COG1122 162 TAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREvFSDYELLE 229
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-239 |
9.09e-57 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 181.75 E-value: 9.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMM 79
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLtPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQFTTVAFDYTVYETVLMGayRQQAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEI 159
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYG--RSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 160 ILLDEPNNHLDIRYQQEL---IQQLNewsaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEFLQTIF 236
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELmrlMRELN----TQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVF 235
|
...
gi 488286290 237 ETD 239
Cdd:PRK11231 236 DVE 238
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-239 |
3.59e-54 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 174.86 E-value: 3.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQ-QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELA---TK 75
Cdd:COG3638 2 MLELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVePTSGEILVDGQDVTALRGRALRrlrRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 76 VAMMSQfttvafDY------TVYETVLMG--AYRQQAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRV 147
Cdd:COG3638 82 IGMIFQ------QFnlvprlSVLTNVLAGrlGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 148 FLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLa 227
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL- 234
|
250
....*....|..
gi 488286290 228 SKEFLQTIFETD 239
Cdd:COG3638 235 TDAVLREIYGGE 246
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-221 |
3.67e-54 |
|
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: 173.86 E-value: 3.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHG---QKRKelatkVA 77
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLErPDSGEILIDGRDVTGvppERRN-----IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 78 MMSQfttvafDY------TVYETVLMGAYRQQAQRflpivsKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAK 151
Cdd:cd03259 76 MVFQ------DYalfphlTVAENIAFGLKLRGVPK------AEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 152 LFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-216 |
4.12e-54 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 173.42 E-value: 4.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMM-----SQFttv 85
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLgPTSGEVLVDGKDLTKLSLKELRRKVGLVfqnpdDQF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 86 aFDYTVYETVLMGAyrqqaqRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:cd03225 89 -FGPTVEEEVAFGL------ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488286290 166 NNHLDIRYQQELIQQLNEWsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGK 216
Cdd:cd03225 162 TAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-250 |
4.45e-54 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 174.66 E-value: 4.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHgQKRKELATKVAMM 79
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGlLKPDSGSILIDGEDVR-KEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQFTTVAFDYTVYETVLMGAyrqqaqRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEI 159
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFA------ELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLNEWsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEFLQTIFETD 239
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAF 232
|
250
....*....|.
gi 488286290 240 IVSYFQKQHKV 250
Cdd:COG4555 233 VALIGSEEGEA 243
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-236 |
8.67e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 168.32 E-value: 8.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQkRKELATKVAMMSQFTTVAFDYTVY 92
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLrPTSGEVRVLGEDVARD-PAEVRRRIGYVPQEPALYPDLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVLMGAyrqqaqRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIR 172
Cdd:COG1131 92 ENLRFFA------RLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286290 173 YQQELIQQLNEWsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKeFLQTIF 236
Cdd:COG1131 166 ARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR-LLEDVF 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
14-219 |
4.03e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 167.57 E-value: 4.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKelatkVAMMSQfttvafDY--- 89
Cdd:COG1116 24 VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEkPTSGEVLVDGKPVTGPGPD-----RGVVFQ------EPall 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 ---TVYETVLMGAyrqQAQRflpiVSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:COG1116 93 pwlTVLDNVALGL---ELRG----VPKAErRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488286290 166 NNHLDI--RYQ-QELIQQLneWsAQEGKTLIGVFHDIRLALTLSEKIVFMKQ--GKVAA 219
Cdd:COG1116 166 FGALDAltRERlQDELLRL--W-QETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-218 |
4.38e-51 |
|
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: 166.97 E-value: 4.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTL-QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELAT---KV 76
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVePTSGSVLIDGTDINKLKGKALRQlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 77 AMMSQfttvafDY------TVYETVLMG--AYRQQAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVF 148
Cdd:cd03256 81 GMIFQ------QFnlierlSVLENVLSGrlGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 149 LAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVA 218
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
12-217 |
5.25e-50 |
|
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: 163.43 E-value: 5.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKELA----TKVAMMSQFTTVA 86
Cdd:cd03255 15 EKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVRVDGTDISKLSEKELAafrrRHIGFVFQSFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 87 FDYTVYETVLMgayrqqAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPN 166
Cdd:cd03255 95 PDLTALENVEL------PLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488286290 167 NHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALtLSEKIVFMKQGKV 217
Cdd:cd03255 169 GNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-228 |
6.12e-50 |
|
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: 164.21 E-value: 6.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQ----TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATK 75
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLErPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 76 VAMMSQFTTVAFD--YTVyETVLMGAYRqqAQRFLPIvskqeKERVLYYLERTGLLP-LKDKVVNQLSGGQQQRVFLAKL 152
Cdd:COG1124 81 VQMVFQDPYASLHprHTV-DRILAEPLR--IHGLPDR-----EERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 153 FVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLAS 228
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-222 |
7.95e-50 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 166.81 E-value: 7.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHG---QKRKelatkV 76
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFEtPDSGRILLDGRDVTGlppEKRN-----V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 77 AMMSQfttvafDY------TVYETVlmgAY--RQQAqrflpiVSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRV 147
Cdd:COG3842 80 GMVFQ------DYalfphlTVAENV---AFglRMRG------VPKAEiRARVAELLELVGLEGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 148 FLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-226 |
6.93e-49 |
|
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: 160.92 E-value: 6.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELA---TKV 76
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLrPDSGEILVDGQDITGLSEKELYelrRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 77 AMMSQ----FTtvafDYTVYETVlmgAY--RQQAQrflpiVSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFL 149
Cdd:COG1127 85 GMLFQggalFD----SLTVFENV---AFplREHTD-----LSEAEiRELVLEKLELVGLPGAADKMPSELSGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 150 AKLFVQDPEIILLDEPNNHLDI---RYQQELIQQLNEwsaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTL 226
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPitsAVIDELIRELRD---ELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
2-239 |
7.50e-49 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 161.52 E-value: 7.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMS 80
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALrPDAGTVDLAGVDLHGLSRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 81 QFTTVAFDYTVYETVLMGayRQQAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEII 160
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVALG--RIPHRSLWAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286290 161 LLDEPNNHLDIRYQQELIQQLNEwSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEFLQTIFETD 239
Cdd:TIGR03873 160 LLDEPTNHLDVRAQLETLALVRE-LAATGVTVVAALHDLNLAASYCDHVVVLDGGRVVAAGPPREVLTPALIRAVYGVD 237
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-220 |
1.86e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 157.13 E-value: 1.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELK---KT-AVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKELA-- 73
Cdd:COG1136 4 LLELRnltKSyGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVLIDGQDISSLSERELArl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 74 --TKVAMMSQFttvaF----DYTVYETVLMgayrqqAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRV 147
Cdd:COG1136 84 rrRHIGFVFQF----FnllpELTALENVAL------PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286290 148 FLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLAlTLSEKIVFMKQGKVAAQ 220
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIVSD 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-236 |
4.89e-47 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 157.07 E-value: 4.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQFTTVAFDYTVYET 94
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 VLMGAYRQQaqrflPIVS---KQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDI 171
Cdd:PRK10253 102 VARGRYPHQ-----PLFTrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 172 RYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEFLQTIF 236
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
12-220 |
4.31e-46 |
|
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: 153.40 E-value: 4.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKelatkVAMMSQfttvafDY- 89
Cdd:cd03293 15 GAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLErPTSGEVLVDGEPVTGPGPD-----RGYVFQ------QDa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 -----TVYETVLMGAyrqqaqRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDE 164
Cdd:cd03293 84 llpwlTVLDNVALGL------ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286290 165 PNNHLD--IRYQ-QELIQQLneWSaQEGKTLIGVFHDIRLALTLSEKIVFMKQ--GKVAAQ 220
Cdd:cd03293 158 PFSALDalTREQlQEELLDI--WR-ETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-226 |
4.44e-46 |
|
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: 153.81 E-value: 4.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKEL---ATKVA 77
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLrPDSGEVLIDGEDISGLSEAELyrlRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 78 MMSQFTTVAFDYTVYETVlmgAY--RQQAQRFLPIVSkqekERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQ 155
Cdd:cd03261 81 MLFQSGALFDSLTVFENV---AFplREHTRLSEEEIR----EIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286290 156 DPEIILLDEPNNHLD---IRYQQELIQQLNEwsaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTL 226
Cdd:cd03261 154 DPELLLYDEPTAGLDpiaSGVIDDLIRSLKK---ELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-222 |
6.90e-45 |
|
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: 157.37 E-value: 6.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVH---GQKRKELATKVAMMSQFTTVAFD- 88
Cdd:COG1123 278 VRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLrPTSGSILFDGKDLTklsRRSLRELRRRVQMVFQDPYSSLNp 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 -YTVYETVLMGAyrqqaqRFLPIVSKQE-KERVLYYLERTGLLP-LKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:COG1123 358 rMTVGDIIAEPL------RLHGLLSRAErRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALALEPKLLILDEP 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 166 NNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:COG1123 432 TSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP 488
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-221 |
1.55e-44 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 154.23 E-value: 1.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMM 79
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLtPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQFTTVAFDYTVYETVLMGAYRQQAqRFLPIVSKQEKErVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEI 159
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRS-RFDTWTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 160 ILLDEPNNHLDIRYQ---QELIQQLnewsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK09536 161 LLLDEPTASLDINHQvrtLELVRRL----VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-217 |
2.02e-43 |
|
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: 147.06 E-value: 2.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTL-QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELAT---K 75
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVePSSGSILLEGTDITKLRGKKLRKlrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 76 VAMMSQFTTVAFDYTVYETVLMG--AYRQQAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLF 153
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGrlGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286290 154 VQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-221 |
2.38e-43 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 149.91 E-value: 2.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEV----HGQKRKelatkV 76
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLEtPDSGRIVLNGRDLftnlPPRERR-----V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 77 AMMSQfttvafDY------TVYETVLMGAyrqqaqRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLA 150
Cdd:COG1118 78 GFVFQ------HYalfphmTVAENIAFGL------RVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286290 151 KLFVQDPEIILLDEPNNHLDIRYQQELIQQLNE-WSAQEGKTLIgVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRlHDELGGTTVF-VTHDQEEALELADRVVVMNQGRIEQVG 216
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-251 |
4.36e-43 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 146.52 E-value: 4.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYSGSVLIDGQEVHGQKRKELATKVAMMSQFTTVAFDYTVYEtvl 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQ--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 97 mgaYRQQAQRflPIVSKQEKERVLYYL-ERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQ-DPEI------ILLDEPNNH 168
Cdd:COG4138 89 ---YLALHQP--AGASSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvWPTInpegqlLLLDEPMNS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 169 LDIRYQQELIQQLNEWSAQeGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEFLQTIFETDIVSYFQKQH 248
Cdd:COG4138 164 LDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLEVEGH 242
|
...
gi 488286290 249 KVW 251
Cdd:COG4138 243 RWL 245
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-230 |
4.62e-43 |
|
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: 153.38 E-value: 4.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQFTTVaFDYT 90
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLpPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYL-FAGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETVLMGAyrqqaqrflPIVSKQEKERVLyylERTGLlplkDKVVNQ---------------LSGGQQQRVFLAKLFVQ 155
Cdd:COG4988 427 IRENLRLGR---------PDASDEELEAAL---EAAGL----DEFVAAlpdgldtplgeggrgLSGGQAQRLALARALLR 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 156 DPEIILLDEPNNHLDIRYQQELIQQLNEWSAqeGKTLIGVFHDIRLaLTLSEKIVFMKQGKVAAQGDFQTLASKE 230
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLAL-LAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-235 |
4.70e-43 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 145.91 E-value: 4.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY-SGSVLIDGQEVHGQKRK--ELATKVA 77
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPdSGTITVDGEDLTDSKKDinKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 78 MMSQfttvAF----DYTVYETVLMGayrqqaqrflPI----VSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVF 148
Cdd:COG1126 81 MVFQ----QFnlfpHLTVLENVTLA----------PIkvkkMSKAEaEERAMELLERVGLADKADAYPAQLSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 149 LAKLFVQDPEIILLDEPNNHLDIRYQQE---LIQQLnewsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD--- 222
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPELVGEvldVMRDL----AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPpee 222
|
250
....*....|....*..
gi 488286290 223 -F---QTLASKEFLQTI 235
Cdd:COG1126 223 fFenpQHERTRAFLSKV 239
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-230 |
1.61e-42 |
|
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: 151.84 E-value: 1.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDYT 90
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLdPQSGSITLGGVDLRDLDEDDLRRRIAVVPQ-RPHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETVLMGAyrqqaqrflPIVSKQEKERVLyylERTGLLPLKDKVVN-----------QLSGGQQQRVFLAKLFVQDPEI 159
Cdd:COG4987 425 LRENLRLAR---------PDATDEELWAAL---ERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPI 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLNEWSAqeGKTLIGVFHDiRLALTLSEKIVFMKQGKVAAQGDFQTLASKE 230
Cdd:COG4987 493 LLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHR-LAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-217 |
1.94e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.42 E-value: 1.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY-SGSVLIDGQEVHGQKRKELATKVAMMS 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPtSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 81 QfTTVAFDYTVYEtVLMGAYRQQAQRFLPivskqekERVLYYLERTGLLP-LKDKVVNQLSGGQQQRVFLAKLFVQDPEI 159
Cdd:COG4619 81 Q-EPALWGGTVRD-NLPFPFQLRERKFDR-------ERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-221 |
3.68e-42 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 146.76 E-value: 3.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHG---QKRkelatKV 76
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLeDPTSGEILIGGRDVTDlppKDR-----NI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 77 AMMSQfttvafDY------TVYETVlmgAYRQQAQRflpiVSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFL 149
Cdd:COG3839 78 AMVFQ------SYalyphmTVYENI---AFPLKLRK----VPKAEiDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286290 150 AKLFVQDPEIILLDEPNNHLD--IRYQ-----QELIQQLnewsaqeGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDakLRVEmraeiKRLHRRL-------GTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVG 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
17-222 |
4.02e-42 |
|
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: 143.73 E-value: 4.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHGQKRKELATK-VAMMSQFTTVAFDYTVYET 94
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGfLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 VLMGAYRQQAQRFLPIVSKQEK----ERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPN---N 167
Cdd:cd03219 96 VMVAAQARTGSGLLLARARREErearERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAaglN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 168 HLDIRYQQELIQQLNEwsaqEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:cd03219 176 PEETEELAELIRELRE----RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-216 |
2.46e-41 |
|
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: 139.63 E-value: 2.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEV--HGQKRKELATKVAM 78
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEePDSGSILIDGEDLtdLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 79 MSQFTTVAFDYTVYETVLMGayrqqaqrflpivskqekervlyylertgllplkdkvvnqLSGGQQQRVFLAKLFVQDPE 158
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 159 IILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGK 216
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-236 |
3.77e-41 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 141.85 E-value: 3.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIA-GLVPYSGSVLIDGQEVHGQKRKELATKVAMMSQFTTVAFDYTVYET 94
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGrHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 VLMGAYRQQAQ--RFlpivSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIR 172
Cdd:PRK10575 106 VAIGRYPWHGAlgRF----GAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 173 YQQE---LIQQLnewSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEFLQTIF 236
Cdd:PRK10575 182 HQVDvlaLVHRL---SQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-240 |
3.99e-41 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 141.38 E-value: 3.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP--YSGSVlidgqEVHGQKRK-----ELA 73
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPptYGNDV-----RLFGERRGgedvwELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 74 TKV-----AMMSQFTTvafDYTVYETVL------MGAYRQqaqrflpiVSKQEKERVLYYLERTGLLPLKDKVVNQLSGG 142
Cdd:COG1119 78 KRIglvspALQLRFPR---DETVLDVVLsgffdsIGLYRE--------PTDEQRERARELLELLGLAHLADRPFGTLSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 143 QQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFH---DIRLALTlseKIVFMKQGKVAA 219
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHhveEIPPGIT---HVLLLKDGRVVA 223
|
250 260
....*....|....*....|.
gi 488286290 220 QGDFQTLASKEFLQTIFETDI 240
Cdd:COG1119 224 AGPKEEVLTSENLSEAFGLPV 244
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-230 |
4.05e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 140.66 E-value: 4.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKtaVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHGQ---KRKelatkV 76
Cdd:COG3840 1 MLRLDD--LTYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGfLPPDSGRILWNGQDLTALppaERP-----V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 77 AMMSQFTTVaFDY-TVYETVLMGayRQQAQRFlpivSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQ 155
Cdd:COG3840 74 SMLFQENNL-FPHlTVAQNIGLG--LRPGLKL----TAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 156 DPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKE 230
Cdd:COG3840 147 KRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-222 |
5.69e-41 |
|
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: 146.97 E-value: 5.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTL--QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP----YSGSVLIDGQEVHGQKRKELAT 74
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 75 KVAMMSQFTTVAFD-YTVYETVLMGAYRQQAQRflpivsKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLF 153
Cdd:COG1123 84 RIGMVFQDPMTQLNpVTVGDQIAEALENLGLSR------AEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286290 154 VQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-217 |
9.85e-41 |
|
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: 137.91 E-value: 9.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHgQKRKELATKVAMMS 80
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPDSGEIKVLGKDIK-KEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 81 QFTTVAFDYTVYEtvlmgayrqqaqrflpivskqekervlyYLErtgllplkdkvvnqLSGGQQQRVFLAKLFVQDPEII 160
Cdd:cd03230 80 EEPSLYENLTVRE----------------------------NLK--------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 161 LLDEPNNHLDIRYQQELIQQLNEWsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
17-222 |
2.31e-40 |
|
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: 139.79 E-value: 2.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATK-VAMMSQFTTVAFDYTVYET 94
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYrPTSGRILFDGRDITGLPPHRIARLgIARTFQNPRLFPELTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 VLMGAYRQQAQRF------LPIVSKQEKE---RVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:COG0411 100 VLVAAHARLGRGLlaallrLPRARREEREareRAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 166 N---NHLDIRYQQELIQQLNEwsaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:COG0411 180 AaglNPEETEELAELIRRLRD---ERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-167 |
3.66e-40 |
|
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: 135.85 E-value: 3.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQFTTVAFDYTVYETV 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLsPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 96 LMGAYrqqaqrfLPIVSKQEKERVLY-YLERTGLLPLKDKVV----NQLSGGQQQRVFLAKLFVQDPEIILLDEPNN 167
Cdd:pfam00005 81 RLGLL-------LKGLSKREKDARAEeALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-230 |
5.40e-40 |
|
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: 146.52 E-value: 5.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDYT 90
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLyEPTSGRILIDGIDLRQIDPASLRRQIGVVLQ-DVFLFSGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETVLMGAyrqqaqrflPIVSKqekERVLYYLERTGL------LPLK-DKVV----NQLSGGQQQRVFLAKLFVQDPEI 159
Cdd:COG2274 565 IRENITLGD---------PDATD---EEIIEAARLAGLhdfieaLPMGyDTVVgeggSNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLNEWSAqeGKTLIGVFHdiRLA-LTLSEKIVFMKQGKVAAQGDFQTLASKE 230
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLK--GRTVIIIAH--RLStIRLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
15-221 |
6.46e-40 |
|
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: 137.64 E-value: 6.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHG---QKRKELATKVAMMSQFTTVAFD-- 88
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLkPTSGSIIFDGKDLLKlsrRLRKIRRKEIQMVFQDPMSSLNpr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 YTVYETVLMGAYRQQAQRflpiVSKQEKERVLYYLERTGLLP-LKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNN 167
Cdd:cd03257 99 MTIGEQIAEPLRIHGKLS----KKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488286290 168 HLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:cd03257 175 ALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-216 |
6.51e-40 |
|
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: 135.45 E-value: 6.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 3 ELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMmsq 81
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLkPTSGEILIDGKDIAKLPLEELRRRIGY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 82 fttvafdytvyetvlmgayrqqaqrflpivskqekervlyylertgllplkdkvVNQLSGGQQQRVFLAKLFVQDPEIIL 161
Cdd:cd00267 78 ------------------------------------------------------VPQLSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 162 LDEPNNHLDIRYQQELIQQLNEWsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGK 216
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
16-217 |
7.85e-40 |
|
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: 136.89 E-value: 7.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY-SGSVLIDGQEVHGQKRK--ELATKVAMMSQFTTVAFDYTVY 92
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPdSGTIIIDGLKLTDDKKNinELRQKVGMVFQQFNLFPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVLMGayrqqaqrflPI----VSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNN 167
Cdd:cd03262 95 ENITLA----------PIkvkgMSKAEaEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488286290 168 HLD---IRYQQELIQQLnewsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:cd03262 165 ALDpelVGEVLDVMKDL----AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
13-217 |
9.03e-40 |
|
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: 140.56 E-value: 9.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 13 QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHG---QKRkelatkvammsQFTTVAFD 88
Cdd:TIGR03265 16 AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLeRQTAGTIYQGGRDITRlppQKR-----------DYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 Y------TVYETVLMGAYRQQAQRflpivsKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILL 162
Cdd:TIGR03265 85 YalfpnlTVADNIAYGLKNRGMGR------AEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 163 DEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVI 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-217 |
2.07e-39 |
|
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: 136.60 E-value: 2.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHG---QKRkelatkva 77
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFeTPTSGEILLDGKDITNlppHKR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 78 mmsQFTTVAFDY------TVYETVLMGAYRQQaqrflpiVSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLA 150
Cdd:cd03300 73 ---PVNTVFQNYalfphlTVFENIAFGLRLKK-------LPKAEiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 151 KLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:cd03300 143 RALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
14-233 |
2.73e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 137.56 E-value: 2.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKELATKVAMMSQF-TTVAFDYTV 91
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDpDDQVFSSTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 92 YETVLMGAYRQQAQRflpivsKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDI 171
Cdd:PRK13647 98 WDDVAFGPVNMGLDK------DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286290 172 RYQQELIQQLNEWSaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEFLQ 233
Cdd:PRK13647 172 RGQETLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVE 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-193 |
3.11e-39 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 135.30 E-value: 3.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHgQKRKELATKVAMM 79
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLpPSAGEVLWNGEPIR-DAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQFTTVAFDYTVYETVLMgayrqqAQRFLPIvsKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEI 159
Cdd:COG4133 81 GHADGLKPELTVRENLRF------WAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190
....*....|....*....|....*....|....
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLI 193
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
16-222 |
7.91e-39 |
|
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: 134.62 E-value: 7.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL------VPYSGSVLIDGQEVHGQK--RKELATKVAMMSQFTTVaF 87
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipgAPDEGEVLLDGKDIYDLDvdVLELRRRVGMVFQKPNP-F 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 88 DYTVYETVlmgAYRQQAQRFLPivSKQEKERVLYYLERTGLLP-LKDK-VVNQLSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:cd03260 94 PGSIYDNV---AYGLRLHGIKL--KEELDERVEEALRKAALWDeVKDRlHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286290 166 NNHLDIRYQQ---ELIQQLN-EWsaqegkTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:cd03260 169 TSALDPISTAkieELIAELKkEY------TIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-221 |
1.06e-38 |
|
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: 133.86 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSkTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVhGQKRKELATKVAMMS 80
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTpPSSGTIRIDGQDV-LKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 81 QFTTVAFDYTVYETVlmgAYRQQAQRflpIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEII 160
Cdd:cd03264 79 QEFGVYPNFTVREFL---DYIAWLKG---IPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 161 LLDEPNNHLD----IRYqQELIQQLNewsaqEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:cd03264 153 IVDEPTAGLDpeerIRF-RNLLSELG-----EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
12-221 |
1.01e-37 |
|
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: 131.56 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDYT 90
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQ-DVTLFYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETVLMGAyrqqaqrflPIVSKqekERVLYYLERTGLLPLKDKVVN-----------QLSGGQQQRVFLAKLFVQDPEI 159
Cdd:cd03245 94 LRDNITLGA---------PLADD---ERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLNEWSAqeGKTLIGVFHDIRLaLTLSEKIVFMKQGKVAAQG 221
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
13-235 |
1.44e-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 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: 132.96 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 13 QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELAT---KVAMMSQFttvA-- 86
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLkPTSGTVTIDGRDITAKKKKKLKDlrkKVGLVFQF---Peh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 87 --FDYTVYETVLMGayrqqaqrflPI---VSKQE-KERVLYYLERTGLLP-LKDKVVNQLSGGQQQRVFLAKLFVQDPEI 159
Cdd:TIGR04521 94 qlFEETVYKDIAFG----------PKnlgLSEEEaEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD-FQTLASKEFLQTI 235
Cdd:TIGR04521 164 LILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTpREVFSDVDELEKI 240
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
15-217 |
2.44e-37 |
|
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: 131.31 E-value: 2.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKElaTKVAMMSQFTTVAFDYTVYE 93
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLeRPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVLMGAYRQQAQRFLPivSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRY 173
Cdd:cd03296 94 NVAFGLRVKPRSERPP--EAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488286290 174 QQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:cd03296 172 RKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-221 |
4.25e-37 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 132.52 E-value: 4.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKtaVTLQ---QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKV 76
Cdd:COG1125 1 MIEFEN--VTKRypdGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIePTSGRILIDGEDIRDLDPVELRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 77 AmmsqfttvafdY-----------TVYE---TV--LMGayrqqaqrflpiVSKQE-KERVLYYLERTGLLP--LKDKVVN 137
Cdd:COG1125 79 G-----------YviqqiglfphmTVAEniaTVprLLG------------WDKERiRARVDELLELVGLDPeeYRDRYPH 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 138 QLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLD-I---RYQQEL--IQQlnewsaQEGKTLIGVFHDIRLALTLSEKIVF 211
Cdd:COG1125 136 ELSGGQQQRVGVARALAADPPILLMDEPFGALDpItreQLQDELlrLQR------ELGKTIVFVTHDIDEALKLGDRIAV 209
|
250
....*....|
gi 488286290 212 MKQGKVAAQG 221
Cdd:COG1125 210 MREGRIVQYD 219
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
12-221 |
8.16e-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: 130.63 E-value: 8.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQE-VHGQKRKELATKVAMM-----SQFtt 84
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLlLPTSGKVTVDGLDtLDEENLWEIRKKVGMVfqnpdNQF-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 85 VAfdYTVYETVLMGAYRQQaqrflpiVSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLD 163
Cdd:TIGR04520 91 VG--ATVEDDVAFGLENLG-------VPREEmRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 164 EPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALtLSEKIVFMKQGKVAAQG 221
Cdd:TIGR04520 162 EATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEG 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-203 |
1.19e-36 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 128.12 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVlidgqevhgqkRKELATKVAMMSQFTTV--AFDYTV 91
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGvLRPTSGTV-----------RRAGGARVAYVPQRSEVpdSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 92 YETVLMGAY-RQQAQRFLpivSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLD 170
Cdd:NF040873 75 RDLVAMGRWaRRGLWRRL---TRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|...
gi 488286290 171 IRYQQELIQQLNEWSAqEGKTLIGVFHDIRLAL 203
Cdd:NF040873 152 AESRERIIALLAEEHA-RGATVVVVTHDLELVR 183
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-217 |
1.33e-36 |
|
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: 128.53 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKElaTKVAMMS 80
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLeEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 81 QFTTVAFDYTVYETVLMGAYrqqaqrfLPIVSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEI 159
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLK-------LRKVPKDEiDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-221 |
2.68e-36 |
|
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: 127.99 E-value: 2.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPIlkDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHGQKRKElaTKVAMMS 80
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLINGVDVTAAPPAD--RPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 81 QFTTVAFDYTVYETVLMGayRQQAQRFLPivskQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEII 160
Cdd:cd03298 77 QENNLFAHLTVEQNVGLG--LSPGLKLTA----EDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286290 161 LLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-217 |
4.35e-36 |
|
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: 128.92 E-value: 4.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 4 LKKTAvtlqQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKEL----ATKVAM 78
Cdd:cd03294 31 LKKTG----QTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIePTSGKVLIDGQDIAAMSRKELrelrRKKISM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 79 MSQFTTVAFDYTVYETVLMGayrqqaqrfLPI--VSKQEK-ERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQ 155
Cdd:cd03294 107 VFQSFALLPHRTVLENVAFG---------LEVqgVPRAEReERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 156 DPEIILLDEPNNHLD--IRYQ-QELIQQLnewSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:cd03294 178 DPDILLMDEAFSALDplIRREmQDELLRL---QAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-216 |
5.57e-36 |
|
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: 125.57 E-value: 5.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQFTTVaFDYTVYE 93
Cdd:cd03228 16 PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFL-FSGTIRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 tvlmgayrqqaqrflpivskqekervlyylertgllplkdkvvNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRY 173
Cdd:cd03228 95 -------------------------------------------NILSGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488286290 174 QQELIQQLNEWSaqEGKTLIGVFHdiRLA-LTLSEKIVFMKQGK 216
Cdd:cd03228 132 EALILEALRALA--KGKTVIVIAH--RLStIRDADRIIVLDDGR 171
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-228 |
1.14e-35 |
|
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: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 13 QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATK-VAMMSQ----FTTVa 86
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLpPRSGSIRFDGRDITGLPPHERARAgIGYVPEgrriFPEL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 87 fdyTVYETVLMGAYRQQAQRFlpivsKQEKERVLYYLERtgLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPN 166
Cdd:cd03224 91 ---TVEENLLLGAYARRRAKR-----KARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 167 NHL------DIryqQELIQQLNEwsaqEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLAS 228
Cdd:cd03224 161 EGLapkiveEI---FEAIRELRD----EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-217 |
4.82e-35 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 124.29 E-value: 4.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 13 QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHgqkRKELATKVAMMSQ-FTTVAFDYT 90
Cdd:cd03226 12 GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLNGKPIK---AKERRKSIGYVMQdVDYQLFTDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETVLMGayrqqaqrfLPIVSKqEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLD 170
Cdd:cd03226 89 VREELLLG---------LKELDA-GNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488286290 171 IRYQQ---ELIQQLnewsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:cd03226 159 YKNMErvgELIREL----AAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
13-230 |
5.41e-35 |
|
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: 125.09 E-value: 5.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 13 QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP-YSGSVLIDGQEVHGQKRKELATK-VAMMSQ----FTTVa 86
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPpRSGSIRFDGEDITGLPPHRIARLgIGYVPEgrriFPSL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 87 fdyTVYETVLMGAYRQQAQRflpiVSKQEKERVLYYLERtgLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPN 166
Cdd:COG0410 94 ---TVEENLLLGAYARRDRA----EVRADLERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 167 NHLDIRYQQEL---IQQLNEwsaqEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKE 230
Cdd:COG0410 165 LGLAPLIVEEIfeiIRRLNR----EGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-221 |
1.10e-34 |
|
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: 124.34 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQFTTVAFDYTVY 92
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIePTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPHMTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVLMgayrqqaqrfLPIVSKQEKE----RVLYYLERTGLLP--LKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPN 166
Cdd:cd03295 94 ENIAL----------VPKLLKWPKEkireRADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 167 NHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:cd03295 164 GALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVG 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-221 |
1.49e-34 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 127.37 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHG---QKRkelatkva 77
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFeTPDSGRIMLDGQDITHvpaENR-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 78 mmsQFTTVAFDY------TVYETVLMGAYRQQaqrflpiVSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLA 150
Cdd:PRK09452 87 ---HVNTVFQSYalfphmTVFENVAFGLRMQK-------TPAAEiTPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286290 151 KLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-220 |
2.22e-34 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 124.20 E-value: 2.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHG--QKRKELATKVAMMSQFTtvafd 88
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLaPSSGEITLDGVPVTGpgADRGVVFQKDALLPWLN----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 ytVYETVLMGayrqqaqrfLPI--VSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:COG4525 93 --VLDNVAFG---------LRLrgVPKAErRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 166 NNHLD--IRYQ-QELIqqLNEWsAQEGKTLIGVFHDIRLALTLSEKIVFMK--QGKVAAQ 220
Cdd:COG4525 162 FGALDalTREQmQELL--LDVW-QRTGKGVFLITHSVEEALFLATRLVVMSpgPGRIVER 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-217 |
3.12e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 122.85 E-value: 3.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKtaVTLQQ---TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHGQKRKELA--- 73
Cdd:COG2884 1 MIRFEN--VSKRYpggREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPTSGQVLVNGQDLSRLKRREIPylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 74 TKVAMMSQfttvafDY------TVYETVLMgayrqqAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRV 147
Cdd:COG2884 79 RRIGVVFQ------DFrllpdrTVYENVAL------PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286290 148 FLAKLFVQDPEIILLDEPNNHLDIRYQQE---LIQQLNewsaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEimeLLEEIN----RRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-233 |
4.37e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 122.89 E-value: 4.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY-SGSVLIDGQEVHGQKRKE-LATKVAM 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEItSGDLIVDGLKVNDPKVDErLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 79 M--SQFTTVAfDYTVYETVLMGAYRQQAQrflpivSKQEKERV-LYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQ 155
Cdd:PRK09493 81 MvfQQFYLFP-HLTALENVMFGPLRVRGA------SKEEAEKQaRELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 156 DPEIILLDEPNNHLDIRYQQELIQQLNEWsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLAS------- 228
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKnppsqrl 232
|
....*
gi 488286290 229 KEFLQ 233
Cdd:PRK09493 233 QEFLQ 237
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
12-221 |
5.03e-34 |
|
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: 129.22 E-value: 5.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQFTTVaFDYT 90
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYqPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRL-FYGT 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETVLMGAyrqqaqrflPIVSKQEkerVLYYLERTGLLPLK-------DKVVNQ----LSGGQQQRVFLAKLFVQDPEI 159
Cdd:TIGR03375 555 LRDNIALGA---------PYADDEE---ILRAAELAGVTEFVrrhpdglDMQIGErgrsLSGGQRQAVALARALLRDPPI 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLNEWSAqeGKTLIGVFHdiRLA-LTLSEKIVFMKQGKVAAQG 221
Cdd:TIGR03375 623 LLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTH--RTSlLDLVDRIIVMDNGRIVADG 681
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
17-229 |
2.74e-33 |
|
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: 120.52 E-value: 2.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHG---QKRkelatkvammsQFTTVAFDY--- 89
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGfIKPDSGKILLNGKDITNlppEKR-----------DISYVPQNYalf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 ---TVYETVLMGAYRQQAQRflpivsKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPN 166
Cdd:cd03299 84 phmTVYKNIAYGLKKRKVDK------KEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286290 167 NHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASK 229
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
14-235 |
3.91e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 121.49 E-value: 3.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHGQKRK--ELATKVAMMSQF-TTVAFDY 89
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGiLKPSSGRILFDGKPIDYSRKGlmKLRESVGMVFQDpDNQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 TVYETVLMGAYRQQaqrfLPivSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHL 169
Cdd:PRK13636 99 SVYQDVSFGAVNLK----LP--EDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 170 DIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDF-QTLASKEFLQTI 235
Cdd:PRK13636 173 DPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPkEVFAEKEMLRKV 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-198 |
4.60e-33 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 125.56 E-value: 4.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQevhgqkrkelaTKVAMMSQFTTVAFDYTVYE 93
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGeLEPDSGEVSIPKG-----------LRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVLMGA--YRQQAQRFLPIVSKQEKE------------------------RVLYYLERTGLLPLK-DKVVNQLSGGQQQR 146
Cdd:COG0488 81 TVLDGDaeLRALEAELEELEAKLAEPdedlerlaelqeefealggweaeaRAEEILSGLGFPEEDlDRPVSELSGGWRRR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488286290 147 VFLAKLFVQDPEIILLDEPNNHLDIryqqELIQQLNEWSAQEGKTLIGVFHD 198
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDL----ESIEWLEEFLKNYPGTVLVVSHD 208
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
3.22e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.94 E-value: 3.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAV--TLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVA 77
Cdd:PRK13632 7 MIKVENVSFsyPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 78 MM-----SQFTTVafdyTVYETVLMGAYRQQAQRflpivsKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKL 152
Cdd:PRK13632 87 IIfqnpdNQFIGA----TVEDDIAFGLENKKVPP------KKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 153 FVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALtLSEKIVFMKQGKVAAQGD-FQTLASKEF 231
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKpKEILNNKEI 235
|
....
gi 488286290 232 LQTI 235
Cdd:PRK13632 236 LEKA 239
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-226 |
3.53e-32 |
|
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: 119.91 E-value: 3.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 32 ILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVhgQKRKELATKVAMMSQFTTVAFDYTVYETVLMGaYRQQAqrflpi 110
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEqPDSGSIMLDGEDV--TNVPPHLRHINMVFQSYALFPHMTVEENVAFG-LKMRK------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 111 VSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEG 189
Cdd:TIGR01187 72 VPRAEiKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 488286290 190 KTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTL 226
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-216 |
4.02e-32 |
|
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: 114.85 E-value: 4.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGsvlidgqevhgqkrkelatkvamms 80
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGeLEPDEG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 81 qfttvafdytvyetvlmgayrqqaqrflpIVSKQEKERVLYYlertgllplkdkvvNQLSGGQQQRVFLAKLFVQDPEII 160
Cdd:cd03221 56 -----------------------------IVTWGSTVKIGYF--------------EQLSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 161 LLDEPNNHLDIRYQQELIQQLNEWSaqegKTLIGVFHDIRLALTLSEKIVFMKQGK 216
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEYP----GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-221 |
7.33e-32 |
|
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: 116.60 E-value: 7.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP----YSGSVLIDGQEVHGQKRKElatKVAMMSQFTTVAFDYTV 91
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggtTSGQILFNGQPRKPDQFQK---CVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 92 YETVLMGAYRQQAQRFLPIVSKQEKERVLyyLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDI 171
Cdd:cd03234 99 RETLTYTAILRLPRKSSDAIRKKRVEDVL--LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488286290 172 RYQQELIQQLNEWsAQEGKTLIGVFHDIRLAL-TLSEKIVFMKQGKVAAQG 221
Cdd:cd03234 177 FTALNLVSTLSQL-ARRNRIVILTIHQPRSDLfRLFDRILLLSSGEIVYSG 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-226 |
1.06e-31 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 119.44 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVhgQKRKELATKVAMMS 80
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLeKPTEGQIFIDGEDV--THRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 81 QFTTVAFDYTVYETVLMGAYRQQaqrflpiVSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEI 159
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLKMLG-------VPKEErKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTL 226
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-240 |
2.01e-31 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 116.19 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 32 ILGPNGCGKTTLLKTIAGLVPYSGSVLIDGQEVHGQKRKELATKVAMMSQFTTVAFDYTVYetvlmgayrQQAQRFLPI- 110
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVF---------QYLTLHQPDk 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 111 VSKQEKERVLYYLerTGLLPLKDKV---VNQLSGGQQQRVFLAKLFVQ-DPEI------ILLDEPNNHLDIRYQQELIQQ 180
Cdd:PRK03695 98 TRTEAVASALNEV--AEALGLDDKLgrsVNQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLDVAQQAALDRL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 181 LNEWSAQeGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEFLQTIFETDI 240
Cdd:PRK03695 176 LSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNF 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-217 |
3.57e-31 |
|
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: 114.43 E-value: 3.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKtaVTLQ---QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELA---T 74
Cdd:cd03292 1 IEFIN--VTKTypnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEElPTSGTIRVNGQDVSDLRGRAIPylrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 75 KVAMMSQFTTVAFDYTVYETVLMgayrqqAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFV 154
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAF------ALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286290 155 QDPEIILLDEPNNHLDIRYQQELIQQLNEwSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
13-217 |
4.24e-31 |
|
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: 113.08 E-value: 4.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 13 QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKELATKVAMMSQFTTVaFDYTV 91
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLlRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDEL-FSGSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 92 YEtvlmgayrqqaqrflpivskqekervlyylertgllplkdkvvNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDI 171
Cdd:cd03246 93 AE-------------------------------------------NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488286290 172 ---RYQQELIQQLNEwsaqEGKTLIGVFHDIRLaLTLSEKIVFMKQGKV 217
Cdd:cd03246 130 egeRALNQAIAALKA----AGATRIVIAHRPET-LASADRILVLEDGRV 173
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
16-222 |
6.07e-31 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 115.28 E-value: 6.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEV------HGQ----KRKELA---TKVAMMSQ 81
Cdd:COG4598 23 VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLeTPDSGEIRVGGEEIrlkpdrDGElvpaDRRQLQrirTRLGMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 82 fttvAFDY----TVYETVLMGayrqqaqrflPI----VSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKL 152
Cdd:COG4598 103 ----SFNLwshmTVLENVIEA----------PVhvlgRPKAEaIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286290 153 FVQDPEIILLDEPNNHLDIRYQQE---LIQQLnewsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:COG4598 169 LAMEPEVMLFDEPTSALDPELVGEvlkVMRDL----AEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGP 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-217 |
8.54e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.40 E-value: 8.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVlidgqeVHGQKrkelaTKVAMM 79
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGeLEPDSGTV------KLGET-----VKIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQFTTvAFDY--TVYETVlmgayrqqaQRFLPIVSKQEkerVLYYLERTGLLPLK-DKVVNQLSGGQQQRVFLAKLFVQD 156
Cdd:COG0488 384 DQHQE-ELDPdkTVLDEL---------RDGAPGGTEQE---VRGYLGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286290 157 PEIILLDEPNNHLDIRYQQELIQQLNEWsaqEGkTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:COG0488 451 PNVLLLDEPTNHLDIETLEALEEALDDF---PG-TVLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-198 |
1.00e-30 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 119.00 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQFTTVaFDYT 90
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLdPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHL-FDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETVLMGAyrqqaqrflPIVSKQEKERVlyyLERTGLLPL-------KDKVVNQ----LSGGQQQRVFLAKLFVQDPEI 159
Cdd:TIGR02868 425 VRENLRLAR---------PDATDEELWAA---LERVGLADWlralpdgLDTVLGEggarLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*....
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLneWSAQEGKTLIGVFHD 198
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-226 |
1.08e-30 |
|
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: 113.37 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 13 QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQkRKELATKVAMMSQFTTVAFDYTV 91
Cdd:cd03263 14 TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELrPTSGTAYINGYSIRTD-RKAARQSLGYCPQFDALFDELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 92 YETVLMGAyrqqaqRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDI 171
Cdd:cd03263 93 REHLRFYA------RLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 172 RYQQELIQQLNEwsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTL 226
Cdd:cd03263 167 ASRRAIWDLILE--VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
17-222 |
1.63e-30 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 113.93 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTI---AGLVP---YSGSVLIDGQEVHGQKR--KELATKVAMMSQFTTvAFD 88
Cdd:TIGR00972 17 LKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrmNDLVPgvrIEGKVLFDGQDIYDKKIdvVELRRRVGMVFQKPN-PFP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 YTVYETVLMGAyrqqaqRFLPIVSKQE-KERVLYYLERTGLL-PLKDKV---VNQLSGGQQQRVFLAKLFVQDPEIILLD 163
Cdd:TIGR00972 96 MSIYDNIAYGP------RLHGIKDKKElDEIVEESLKKAALWdEVKDRLhdsALGLSGGQQQRLCIARALAVEPEVLLLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286290 164 EPNNHLD-IRYQQ--ELIQQLnewsaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:TIGR00972 170 EPTSALDpIATGKieELIQEL-----KKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGP 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-226 |
2.68e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 118.34 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDYTVY 92
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYdPTSGRILIDGVDIRDLTLESLRRQIGVVPQ-DTFLFSGTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVLMGayRQQAQRflpivskqekERVLYYLERTGL------LPLK-DKVVNQ----LSGGQQQRVFLAKLFVQDPEIIL 161
Cdd:COG1132 432 ENIRYG--RPDATD----------EEVEEAAKAAQAhefieaLPDGyDTVVGErgvnLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 162 LDEPNNHLDIRYQQELIQQLNEWSAqeGKTLIGVFHdiRLA-LTLSEKIVFMKQGKVAAQGDFQTL 226
Cdd:COG1132 500 LDEATSALDTETEALIQEALERLMK--GRTTIVIAH--RLStIRNADRILVLDDGRIVEQGTHEEL 561
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-216 |
3.41e-30 |
|
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: 111.96 E-value: 3.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKtaVTLQ---QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHGQKRKELAT-- 74
Cdd:TIGR02673 1 MIEFHN--VSKAypgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGaLTPSRGQVRIAGEDVNRLRGRQLPLlr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 75 -KVAMMSQFTTVAFDYTVYETVLM-----GAYRQQAQRflpivskqekeRVLYYLERTGLLPLKDKVVNQLSGGQQQRVF 148
Cdd:TIGR02673 79 rRIGVVFQDFRLLPDRTVYENVALplevrGKKEREIQR-----------RVGAALRQVGLEHKADAFPEQLSGGEQQRVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 149 LAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQeGKTLIGVFHDIRLALTLSEKIVFMKQGK 216
Cdd:TIGR02673 148 IARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
16-221 |
4.42e-30 |
|
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: 111.60 E-value: 4.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKE---------LATKVAMMSQFttv 85
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIlPDSGEVLFDGKPLDIAARNRigylpeergLYPKMKVIDQL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 86 afdytVYETVLMGAYRQQAQRflpivskqekeRVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:cd03269 92 -----VYLAQLKGLKKEEARR-----------RIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 166 NNHLDIRYQQELIQQLNEWsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:cd03269 156 FSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-222 |
4.44e-30 |
|
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: 112.29 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQT----PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKELAT- 74
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPTSGSVLVDGTDLTLLSGKELRKa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 75 --KVAMMSQFTTVAFDYTVYETVlmgAYRQQAQRflpiVSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAK 151
Cdd:cd03258 81 rrRIGMIFQHFNLLSSRTVFENV---ALPLEIAG----VPKAEiEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286290 152 LFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-217 |
5.81e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 114.80 E-value: 5.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY-SGSVLIDGQEV---HGQKRKelatkVA 77
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQtSGHIRFHGTDVsrlHARDRK-----VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 78 MMSQFTTVAFDYTVYETVLMGayrqqaqrfLPIVSKQE-------KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLA 150
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAFG---------LTVLPRRErpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286290 151 KLFVQDPEIILLDEPNNHLDIRYQQEL---IQQLNEwsaqEGK-TLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELrrwLRQLHE----ELKfTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-212 |
6.33e-30 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 117.00 E-value: 6.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDYTVY 92
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVdPTEGSIAVNGVPLADADADSWRDQIAWVPQ-HPFLFAGTIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVLMGAyrqqaqrflPIVSKQEKERVLyylERTGLLPL-------KDKVV----NQLSGGQQQRVFLAKLFVQDPEIIL 161
Cdd:TIGR02857 414 ENIRLAR---------PDASDAEIREAL---ERAGLDEFvaalpqgLDTPIgeggAGLSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488286290 162 LDEPNNHLDIRYQQELIQQLNEWSaqEGKTLIGVFHDIRLAlTLSEKIVFM 212
Cdd:TIGR02857 482 LDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-221 |
1.10e-29 |
|
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: 111.02 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVH--GQKRKELATKVAMMSQFTtvafdytVYE 93
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEGKQITepGPDRMVVFQNYSLLPWLT-------VRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVLMGAyrqqaQRFLPIVSKQEKERVL-YYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIR 172
Cdd:TIGR01184 74 NIALAV-----DRVLPDLSKSERRAIVeEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488286290 173 YQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-221 |
1.49e-29 |
|
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: 110.46 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 19 DISLVFPtGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQE-VHGQKRKELAT---KVAMMSQFTTVAFDYTVYE 93
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEkPDGGTIVLNGTVlFDSRKKINLPPqqrKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVLMGAYRQQaqrflpivSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRY 173
Cdd:cd03297 95 NLAFGLKRKR--------NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488286290 174 QQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
17-221 |
1.83e-29 |
|
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: 110.15 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRkELATKVAMMSQFTTVAFDYTVYETV 95
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDAGFATVDGFDVVKEPA-EARRRLGFVSDSTGLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 96 -----LMGAYRQQAqrflpivskqeKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLD 170
Cdd:cd03266 100 eyfagLYGLKGDEL-----------TARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488286290 171 I---RYQQELIQQLNEwsaqEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:cd03266 169 VmatRALREFIRQLRA----LGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-221 |
2.42e-29 |
|
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: 110.40 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDYTVYE 93
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYdVSSGSILIDGQDIREVTLDSLRRAIGVVPQ-DTVLFNDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVLMG----------AYRQQAQRFLPIVSKQEK------ERVLYylertgllplkdkvvnqLSGGQQQRVFLAKLFVQDP 157
Cdd:cd03253 94 NIRYGrpdatdeeviEAAKAAQIHDKIMRFPDGydtivgERGLK-----------------LSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286290 158 EIILLDEPNNHLDIRYQQELIQQLNEWSAqeGKTLIGVFHDIRLALTlSEKIVFMKQGKVAAQG 221
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
16-202 |
3.21e-29 |
|
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: 109.24 E-value: 3.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHG----QKRKELATKVAMMSQFTTVAFDYT 90
Cdd:TIGR03608 13 ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLeKFDSGQVYLNGQETPPlnskKASKFRREKLGYLFQNFALIENET 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETVLMGAyrqqaqRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLD 170
Cdd:TIGR03608 93 VEENLDLGL------KYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLD 166
|
170 180 190
....*....|....*....|....*....|..
gi 488286290 171 IRYQQELIQQLNEWsAQEGKTLIGVFHDIRLA 202
Cdd:TIGR03608 167 PKNRDEVLDLLLEL-NDEGKTIIIVTHDPEVA 197
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-236 |
4.59e-29 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 110.74 E-value: 4.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY-SGSVLIDGQEVHGQKRKELatkVAMMSQFTTV--AFDYTVYE 93
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLaSGKISILGQPTRQALQKNL---VAYVPQSEEVdwSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVLMGAYRQQAqrFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRY 173
Cdd:PRK15056 100 VVMMGRYGHMG--WLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286290 174 QQELIQQLNEWSAqEGKTLIGVFHDIRLALTLSEKIVFMKqGKVAAQGDFQTLASKEFLQTIF 236
Cdd:PRK15056 178 EARIISLLRELRD-EGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLELAF 238
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-202 |
4.66e-29 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 108.28 E-value: 4.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKR--KELATKVAMMSQ------FTT 84
Cdd:TIGR01166 5 PEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLrPQSGAVLIDGEPLDYSRKglLERRQRVGLVFQdpddqlFAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 85 vafdyTVYETVLMGAyrqqaqRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDE 164
Cdd:TIGR01166 85 -----DVDQDVAFGP------LNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDE 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 488286290 165 PNNHLDIRYQQELIQQLNEWSAqEGKTLIGVFHDIRLA 202
Cdd:TIGR01166 154 PTAGLDPAGREQMLAILRRLRA-EGMTVVISTHDVDLA 190
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-231 |
1.17e-28 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 108.95 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDG------QEVHGQKRKELAT 74
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLeTPDSGQLNIAGhqfdfsQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 75 KVAMMSQFTTVAFDYTVYETVLmgayrQQAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFV 154
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLI-----EAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 155 QDPEIILLDEPNNHLD--IRYQ-QELIQQLnewsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD---FQTLAS 228
Cdd:COG4161 158 MEPQVLLFDEPTAALDpeITAQvVEIIREL----SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDashFTQPQT 233
|
...
gi 488286290 229 KEF 231
Cdd:COG4161 234 EAF 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-229 |
1.62e-28 |
|
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: 108.08 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 13 QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQFTTVaFDYTV 91
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYdPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFL-FSGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 92 YETVLMGayRQQAQrflpivskqeKERVLYYLERTGLLPLKDKVVN-----------QLSGGQQQRVFLAKLFVQDPEII 160
Cdd:cd03254 94 MENIRLG--RPNAT----------DEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 161 LLDEPNNHLDIRyQQELIQQlNEWSAQEGKTLIGVFHdiRLALTL-SEKIVFMKQGKVAAQGDFQTLASK 229
Cdd:cd03254 162 ILDEATSNIDTE-TEKLIQE-ALEKLMKGRTSIIIAH--RLSTIKnADKILVLDDGKIIEEGTHDELLAK 227
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-221 |
2.18e-28 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 108.76 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYS---------GSVLIDGQEVHGQKRKELATKVAMMSQFTTVA 86
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 87 FDYTVYETVLMGAYrQQAQRfLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQ---------DP 157
Cdd:PRK13547 96 FAFSAREIVLLGRY-PHARR-AGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286290 158 EIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-231 |
2.35e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 108.56 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-----PYS-----GSVLIDGQEVHGQKRK 70
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdksAGShiellGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 71 ELATKVAMMSQFTTVAfDYTVYETVLMGA------YRQQAQRFlpivSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQ 144
Cdd:PRK09984 84 SRANTGYIFQQFNLVN-RLSVLENVLIGAlgstpfWRTCFSWF----TREQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 145 QRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQ 224
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
....*..
gi 488286290 225 TLASKEF 231
Cdd:PRK09984 239 QFDNERF 245
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-202 |
3.23e-28 |
|
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: 107.13 E-value: 3.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQ----QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKELAT- 74
Cdd:COG4181 8 IIELRGLTKTVGtgagELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLdRPTSGTVRLAGQDLFALDEDARARl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 75 ---KVAMMSQ-FTTVAfDYTVYETVLMGayrqqaqrfLPIVSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFL 149
Cdd:COG4181 88 rarHVGFVFQsFQLLP-TLTALENVMLP---------LELAGRRDaRARARALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488286290 150 AKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLA 202
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA 210
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-235 |
3.36e-28 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 108.31 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHGQKRKELAT---KV 76
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGqIAPDHGEILFDGENIPAMSRSRLYTvrkRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 77 AMMSQFTTVAFDYTVYETVlmgAY--RQQAQRFLPIVskqeKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFV 154
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNV---AYplREHTQLPAPLL----HSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 155 QDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLAS------ 228
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAnpdprv 239
|
....*..
gi 488286290 229 KEFLQTI 235
Cdd:PRK11831 240 RQFLDGI 246
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-230 |
7.84e-28 |
|
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: 106.55 E-value: 7.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDYTVY 92
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYdVDSGRILIDGHDVRDYTLASLRRQIGLVSQ-DVFLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVLMG---AYRQQAQRFLPIVSKQEkervlyYLERtglLPLK-DKVVNQ----LSGGQQQRVFLAKLFVQDPEIILLDE 164
Cdd:cd03251 94 ENIAYGrpgATREEVEEAARAANAHE------FIME---LPEGyDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 165 PNNHLDI---RYQQELIQQLnewsaQEGKTLIGVFHdiRLA-LTLSEKIVFMKQGKVAAQGDFQTLASKE 230
Cdd:cd03251 165 ATSALDTeseRLVQAALERL-----MKNRTTFVIAH--RLStIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
32-221 |
8.50e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 107.00 E-value: 8.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 32 ILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKvAMMSQFTTVAF--DYTVYETVLMGAYRQQAQRFL 108
Cdd:PRK11300 36 LIGPNGAGKTTVFNCLTGFYkPTGGTILLRGQHIEGLPGHQIARM-GVVRTFQHVRLfrEMTVIENLLVAQHQQLKTGLF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 109 ------PIVSKQEKE---RVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQ 179
Cdd:PRK11300 115 sgllktPAFRRAESEaldRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDE 194
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488286290 180 QLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK11300 195 LIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-240 |
1.56e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 107.86 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELK---KT-AVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKELAT- 74
Cdd:COG1135 1 MIELEnlsKTfPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLeRPTSGSVLVDGVDLTALSERELRAa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 75 --KVAM-------MSQfttvafdYTVYETV-----LMGayrqqaqrflpiVSKQE-KERVLYYLERTGLLPLKDKVVNQL 139
Cdd:COG1135 81 rrKIGMifqhfnlLSS-------RTVAENValpleIAG------------VPKAEiRKRVAELLELVGLSDKADAYPSQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 140 SGGQQQRVFLAKLFVQDPEIILLDEPNNHLDiryQQ------ELIQQLNEwsaQEGKTLIGVFHDIRLALTLSEKIVFMK 213
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALD---PEttrsilDLLKDINR---ELGLTIVLITHEMDVVRRICDRVAVLE 215
|
250 260 270
....*....|....*....|....*....|....
gi 488286290 214 QGKVAAQGD----F---QTLASKEFLQTIFETDI 240
Cdd:COG1135 216 NGRIVEQGPvldvFanpQSELTRRFLPTVLNDEL 249
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
12-221 |
1.57e-27 |
|
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: 103.93 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHGQKrKELATKVAMMSQFTTVaFDYT 90
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEITLDGVPVSDLE-KALSSLISVLNQRPYL-FDTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETVlmGAyrqqaqrflpivskqekervlyylertgllplkdkvvnQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLD 170
Cdd:cd03247 91 LRNNL--GR--------------------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488286290 171 IRYQQELIQQLneWSAQEGKTLIGVFHDIRlALTLSEKIVFMKQGKVAAQG 221
Cdd:cd03247 131 PITERQLLSLI--FEVLKDKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
16-222 |
2.34e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 105.50 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG---LVP---YSGSVLIDGQEVHGQKRK--ELATKVAMMSQ----FT 83
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPgarVEGEILLDGEDIYDPDVDvvELRRRVGMVFQkpnpFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 84 TvafdyTVYETVLMGAyrqqaqRFLPIVSKQE-KERVLYYLERTGLLP-LKDKvVNQ----LSGGQQQRVFLAKLFVQDP 157
Cdd:COG1117 106 K-----SIYDNVAYGL------RLHGIKSKSElDEIVEESLRKAALWDeVKDR-LKKsalgLSGGQQQRLCIARALAVEP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286290 158 EIILLDEPNNHLD------IryqQELIQQLnewsaqegK---TLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:COG1117 174 EVLLMDEPTSALDpistakI---EELILEL--------KkdyTIVIVTHNMQQAARVSDYTAFFYLGELVEFGP 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-239 |
4.13e-27 |
|
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: 107.12 E-value: 4.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 19 DISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGqEVHGQKRKELAT-----KVAMMSQFTTVAFDYTVY 92
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTrPDEGEIVLNG-RTLFDSRKGIFLppekrRIGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVLMGAYRQQaqrflPIVSKQEKERVLYYLertGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIR 172
Cdd:TIGR02142 94 GNLRYGMKRAR-----PSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 173 YQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEFLQTIFETD 239
Cdd:TIGR02142 166 RKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLARED 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-230 |
4.43e-27 |
|
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: 104.54 E-value: 4.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTllktIAGLV-----PYSGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDY 89
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLerfydPTSGEILLDGVDIRDLNLRWLRSQIGLVSQ-EPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 TVYETVLMGayrqqaqRFLPIVSKQEKERVLYYLERT-GLLPLK-DKVV----NQLSGGQQQRVFLAKLFVQDPEIILLD 163
Cdd:cd03249 92 TIAENIRYG-------KPDATDEEVEEAAKKANIHDFiMSLPDGyDTLVgergSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286290 164 EPNNHLDIRYQQELIQQLNEwsAQEGKTLIGVFHdiRLAlTL--SEKIVFMKQGKVAAQGDFQTLASKE 230
Cdd:cd03249 165 EATSALDAESEKLVQEALDR--AMKGRTTIVIAH--RLS-TIrnADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-222 |
5.61e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 104.67 E-value: 5.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 13 QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVH------GQKR-------KELATKVAM 78
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLeKPSEGSIVVNGQTINlvrdkdGQLKvadknqlRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 79 MSQFTTVAFDYTVYETVLmgayrQQAQRFLPIVSKQEKERVLYYLERTGLLP-LKDKVVNQLSGGQQQRVFLAKLFVQDP 157
Cdd:PRK10619 97 VFQHFNLWSHMTVLENVM-----EAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 158 EIILLDEPNNHLDIRYQQE---LIQQLnewsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEvlrIMQQL----AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-222 |
8.21e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 105.19 E-value: 8.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKtaVTLQ--QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKelatkva 77
Cdd:COG4152 1 MLELKG--LTKRfgDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILaPDSGEVLWDGEPLDPEDRR------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 78 mmsqfttvAFDY-----------TVYETVL-MGAYRQqaqrflpiVSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQ 144
Cdd:COG4152 72 --------RIGYlpeerglypkmKVGEQLVyLARLKG--------LSKAEaKRRADEWLERLGLGDRANKKVEELSKGNQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 145 QRVFLAKLFVQDPEIILLDEPNNHLD------IRyqqELIQQLnewsAQEGKTLIgvF--HDIRLALTLSEKIVFMKQGK 216
Cdd:COG4152 136 QKVQLIAALLHDPELLILDEPFSGLDpvnvelLK---DVIREL----AAKGTTVI--FssHQMELVEELCDRIVIINKGR 206
|
....*.
gi 488286290 217 VAAQGD 222
Cdd:COG4152 207 KVLSGS 212
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
4-222 |
8.82e-27 |
|
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: 103.02 E-value: 8.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 4 LKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHGQKRKElaTKVAMMSQF 82
Cdd:TIGR01277 1 LALDKVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGfIEPASGSIKVNDQSHTGLAPYQ--RPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 83 TTVAFDYTVYETVLMGAYRQQAqrflpiVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILL 162
Cdd:TIGR01277 79 NNLFAHLTVRQNIGLGLHPGLK------LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 163 DEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:TIGR01277 153 DEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-217 |
1.36e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.04 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTL---QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKELATKV 76
Cdd:PRK13650 4 IIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLlEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 77 AMMSQFTTVAF-DYTVYETVLMGAYRQQaqrflpIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQ 155
Cdd:PRK13650 84 GMVFQNPDNQFvGATVEDDVAFGLENKG------IPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286290 156 DPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRlALTLSEKIVFMKQGKV 217
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLD-EVALSDRVLVMKNGQV 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-230 |
1.42e-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: 103.01 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEV---HGQKRKELAtkVAMMSQFTTVAFDY 89
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPDSGKILLDGQDItklPMHKRARLG--IGYLPQEASIFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 TVYETVLMgayrqqAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHL 169
Cdd:cd03218 91 TVEENILA------VLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 170 D---IRYQQELIQQLNEWSaqegktlIGVF---HDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKE 230
Cdd:cd03218 165 DpiaVQDIQKIIKILKDRG-------IGVLitdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
2.74e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 103.56 E-value: 2.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQ-QTPI----LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKR----KE 71
Cdd:PRK13634 3 ITFQKVEHRYQyKTPFerraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqPTSGTVTIGERVITAGKKnkklKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 72 LATKVAMMSQFTTVA-FDYTVYETVLMGayrqqaqrflPI---VSKQE-KERVLYYLERTGLLP-LKDKVVNQLSGGQQQ 145
Cdd:PRK13634 83 LRKKVGIVFQFPEHQlFEETVEKDICFG----------PMnfgVSEEDaKQKAREMIELVGLPEeLLARSPFELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 146 RVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-230 |
2.87e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 106.83 E-value: 2.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIA-GLVPYSGSVLIDGQEVHGQKRKELATKVAMMSQFTTVaFDYT 90
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHL-FSAT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETVLMGAyrqqaqrflpivSKQEKERVLYYLERTGLLPL--KDKVVN--------QLSGGQQQRVFLAKLFVQDPEII 160
Cdd:PRK11160 430 LRDNLLLAA------------PNASDEALIEVLQQVGLEKLleDDKGLNawlgeggrQLSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286290 161 LLDEPNNHLDIRYQQELIQQLNEWSAqeGKTLIGVFHdiRL-ALTLSEKIVFMKQGKVAAQGDFQTLASKE 230
Cdd:PRK11160 498 LLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH--RLtGLEQFDRICVMDNGQIIEQGTHQELLAQQ 564
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-222 |
3.55e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.26 E-value: 3.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVH-GQKRKELATKVAMMSQ-FTTV-AFdyTVY 92
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYqPDSGEILIDGKPVRiRSPRDAIALGIGMVHQhFMLVpNL--TVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVLMGAyrqqAQRFLPIVS-KQEKERVLYYLERTGL-LPLkDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLD 170
Cdd:COG3845 99 ENIVLGL----EPTKGGRLDrKAARARIRELSERYGLdVDP-DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 171 iryQQE------LIQQLnewsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:COG3845 174 ---PQEadelfeILRRL----AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVD 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-226 |
4.57e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.14 E-value: 4.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSV-----LIDGQEVHGQKR---KE 71
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLeQPEAGTIrvgdiTIDTARSLSQQKgliRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 72 LATKVAMMSQFTTVAFDYTVYETVLMGayrqqaqrflPIVSKQEK-----ERVLYYLERTGLLPLKDKVVNQLSGGQQQR 146
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEG----------PVIVKGEPkeeatARARELLAKVGLAGKETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 147 VFLAKLFVQDPEIILLDEPNNHLDIRYQQEL---IQQLnewsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDF 223
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVlntIRQL----AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
|
...
gi 488286290 224 QTL 226
Cdd:PRK11264 229 KAL 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-221 |
5.12e-26 |
|
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: 101.64 E-value: 5.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGqEVHGQKRKELATKVA-MMSQFTTVAFDY 89
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPTSGEVRVAG-LVPWKRRKKFLRRIGvVFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 TVYETVLMGA--YRQQAQRFlpivskqeKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNN 167
Cdd:cd03267 111 PVIDSFYLLAaiYDLPPARF--------KKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488286290 168 HLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-221 |
6.47e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 102.40 E-value: 6.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMM-----SQF--T 83
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLlPEAGTITVGGMVLSEETVWDVRRQVGMVfqnpdNQFvgA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 84 TVAFDytvyetVLMGAYRQQAQRflpivsKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLD 163
Cdd:PRK13635 98 TVQDD------VAFGLENIGVPR------EEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 164 EPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTlSEKIVFMKQGKVAAQG 221
Cdd:PRK13635 166 EATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-222 |
2.02e-25 |
|
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: 100.65 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVH---GQKRKELATKVAMMSQFTTVAF 87
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEkPAQGTVSFRGQDLYqldRKQRRAFRRDVQLVFQDSPSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 88 D--YTVYETVlmgayRQQAQRFLPIVSKQEKERVLYYLERTGLLP-LKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDE 164
Cdd:TIGR02769 102 NprMTVRQII-----GEPLRHLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 165 PNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECD 234
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-222 |
2.24e-25 |
|
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: 104.06 E-value: 2.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQftTVA-FDY 89
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWpPTAGSVRLDGADLSQWDREELGRHIGYLPQ--DVElFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 TVyetvlmgayrqqAQ---RFLPIvskqEKERVLYYLERTGL------LPLK-DKVV----NQLSGGQQQRVFLAKLFVQ 155
Cdd:COG4618 421 TI------------AEniaRFGDA----DPEKVVAAAKLAGVhemilrLPDGyDTRIgeggARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 156 DPEIILLDEPNNHLDIRYQQELIQQLNEWSAQeGKTLIGVFHDIRLaLTLSEKIVFMKQGKVAAQGD 222
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSL-LAAVDKLLVLRDGRVQAFGP 549
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-220 |
2.59e-25 |
|
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: 97.88 E-value: 2.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKE-LATKVAMmsqfttvafdytV 91
Cdd:cd03216 13 VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYkPDSGEILVDGKEVSFASPRDaRRAGIAM------------V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 92 YetvlmgayrqqaqrflpivskqekervlyylertgllplkdkvvnQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDI 171
Cdd:cd03216 81 Y---------------------------------------------QLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488286290 172 RYQQELIQQLNEWSAQeGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQ 220
Cdd:cd03216 116 AEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
17-232 |
3.47e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.26 E-value: 3.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHGQKRKELATKVAMMSQFTT-VAFDYTVYET 94
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGiLKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDdQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 VLMGAYRqqaqrfLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQ 174
Cdd:PRK13652 100 IAFGPIN------LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 175 QELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEFL 232
Cdd:PRK13652 174 KELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-221 |
3.63e-25 |
|
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: 98.83 E-value: 3.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 3 ELKKTavtLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVhgQKRKELATKVAMMSQ 81
Cdd:cd03268 5 DLTKT---YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIkPDSGEITFDGKSY--QKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 82 FTTVaFDY-TVYETVLMGAyrqqaqrFLPIVSKQEKERVlyyLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEII 160
Cdd:cd03268 80 APGF-YPNlTARENLRLLA-------RLLGIRKKRIDEV---LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286290 161 LLDEPNNHLD---IRYQQELIQQLNEwsaqEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:cd03268 149 ILDEPTNGLDpdgIKELRELILSLRD----QGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-228 |
3.67e-25 |
|
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: 101.72 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKktaVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQE-VHGQKRKELAT---K 75
Cdd:COG4148 2 MLEVD---FRLRRGGFTLDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLErPDSGRIRLGGEVlQDSARGIFLPPhrrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 76 VAMMSQfttvafD------YTVYETVLMGAYRQQAQRflpivSKQEKERVLyylERTGLLPLKDKVVNQLSGGQQQRVFL 149
Cdd:COG4148 79 IGYVFQ------EarlfphLSVRGNLLYGRKRAPRAE-----RRISFDEVV---ELLGIGHLLDRRPATLSGGERQRVAI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286290 150 AKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLAS 228
Cdd:COG4148 145 GRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-215 |
4.23e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 99.77 E-value: 4.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYS-GSVLIDGQEVHGQkrkelATKVAMM 79
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQhGSITLDGKPVEGP-----GAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQFTTVAFDYTVYETVLMGAYrqqaqrfLPIVSKQEKE-RVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPE 158
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQ-------LAGVEKMQRLeIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 159 IILLDEPNNHLD--IRYQ-QELIQQLneWsAQEGKTLIGVFHDIRLALTLSEKIVFMKQG 215
Cdd:PRK11248 149 LLLLDEPFGALDafTREQmQTLLLKL--W-QETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-226 |
4.78e-25 |
|
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: 100.90 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 19 DISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY----SGSVLIDGQEVHGQKRKEL----ATKVAMMSQ--FTtvAFD 88
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgitSGEILFDGEDLLKLSEKELrkirGREIQMIFQdpMT--SLN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 --YTVYETVLMGAYRQQaqrflpIVSKQE-KERVLYYLERTGLlPLKDKVVN----QLSGGQQQRVFLAKLFVQDPEIIL 161
Cdd:COG0444 101 pvMTVGDQIAEPLRIHG------GLSKAEaRERAIELLERVGL-PDPERRLDryphELSGGMRQRVMIARALALEPKLLI 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 162 LDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTL 226
Cdd:COG0444 174 ADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
17-221 |
5.71e-25 |
|
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: 98.60 E-value: 5.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRkELATKVAMMSQFTTVAFDYTVYETV 95
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLkPTSGRATVAGHDVVREPR-EVRRRIGIVFQDLSVDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 96 LMGAyrqqaqRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQ 175
Cdd:cd03265 95 YIHA------RLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488286290 176 ---ELIQQLNEwsaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:cd03265 169 hvwEYIEKLKE---EFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
16-232 |
9.00e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.55 E-value: 9.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDG------QEVHGQKRKELATKVAMMSQFTTVAFD 88
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLeMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 YTVYETVLmgayrQQAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNH 168
Cdd:PRK11124 97 LTVQQNLI-----EAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286290 169 LD--IRYQ-QELIQQLnewsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD---F---QTLASKEFL 232
Cdd:PRK11124 172 LDpeITAQiVSIIREL----AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDascFtqpQTEAFKNYL 240
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
13-216 |
9.05e-25 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 97.87 E-value: 9.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 13 QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIaGLVPY--SGSVLIDGQEV----HGQK---RKELatkVAMMSQFT 83
Cdd:NF038007 17 KTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNII-GMFDSldSGSLTLAGKEVtnlsYSQKiilRREL---IGYIFQSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 84 TVAFDYTVYETV-LMGAYRQQAQrflpivsKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILL 162
Cdd:NF038007 93 NLIPHLSIFDNVaLPLKYRGVAK-------KERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488286290 163 DEPNNHLDIRYQQELIQQLNEWSaQEGKTLIGVFHDiRLALTLSEKIVFMKQGK 216
Cdd:NF038007 166 DEPTGNLDSKNARAVLQQLKYIN-QKGTTIIMVTHS-DEASTYGNRIINMKDGK 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
13-220 |
1.03e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 98.35 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 13 QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVH---GQKRKELAT-KVAMMSQFTTVAF 87
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPMSklsSAAKAELRNqKLGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 88 DYTVYETVLM-----GAYRQQAQrflpivskqekERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILL 162
Cdd:PRK11629 101 DFTALENVAMplligKKKPAEIN-----------SRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 163 DEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKiVFMKQGKVAAQ 220
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ-LEMRDGRLTAE 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
9-228 |
3.19e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 101.07 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 9 VTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYSGSVLIDGQEVH----GQKRKELATkVAMMSQFtt 84
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELReldpESWRKHLSW-VGQNPQL-- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 85 vaFDYTVYETVLMG---AYRQQAQRFLpivskqEKERVLYYLER--TGL-LPLKDKVVNqLSGGQQQRVFLAKLFVQDPE 158
Cdd:PRK11174 435 --PHGTLRDNVLLGnpdASDEQLQQAL------ENAWVSEFLPLlpQGLdTPIGDQAAG-LSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286290 159 IILLDEPNNHLDIRYQQELIQQLNEwsAQEGKTLIGVFHdiRL-ALTLSEKIVFMKQGKVAAQGDFQTLAS 228
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNA--ASRRQTTLMVTH--QLeDLAQWDQIWVMQDGQIVQQGDYAELSQ 572
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
13-222 |
1.05e-23 |
|
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: 95.28 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 13 QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP-YSGSVLIDGQEVHGQKRKELATK-VAMMSQ----FTTVa 86
Cdd:TIGR03410 12 QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPvKSGSIRLDGEDITKLPPHERARAgIAYVPQgreiFPRL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 87 fdyTVYETVLMGAYRqqaqrfLPIVSKQEKERVLyylertGLLPLKDKVVNQ----LSGGQQQRVFLAKLFVQDPEIILL 162
Cdd:TIGR03410 91 ---TVEENLLTGLAA------LPRRSRKIPDEIY------ELFPVLKEMLGRrggdLSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286290 163 DEPNNHLdiryQQELIQQ----LNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:TIGR03410 156 DEPTEGI----QPSIIKDigrvIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
1.08e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.92 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELK---KT--AVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHGQKRKELAT 74
Cdd:COG1101 1 MLELKnlsKTfnPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGsLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 75 KVA------MMsqftTVAFDYTVYETVLMGAYRQQAQRFLPIVSKQEKERVLYYLERTGL-LP--LKDKvVNQLSGGQQQ 145
Cdd:COG1101 81 YIGrvfqdpMM----GTAPSMTIEENLALAYRRGKRRGLRRGLTKKRRELFRELLATLGLgLEnrLDTK-VGLLSGGQRQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286290 146 RVFL--AKLfvQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:COG1101 156 ALSLlmATL--TKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
14-221 |
1.50e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 97.41 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY-SGSVLIDGQ---EVHGQKRKelatkVAMMSQFTTVAFDY 89
Cdd:PRK11000 16 VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDItSGDLFIGEKrmnDVPPAERG-----VGMVFQSYALYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 TVYETVLMGAYrqqaqrfLPIVSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNH 168
Cdd:PRK11000 91 SVAENMSFGLK-------LAGAKKEEiNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 169 LD--IRYQQEL-IQQLNEwsaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK11000 164 LDaaLRVQMRIeISRLHK---RLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-230 |
1.53e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.03 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDYTVYE 93
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLyQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQ-EPVLFSGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVLMGAYRQQAQRFLPIVSKQEKERVLYYLErTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRY 173
Cdd:TIGR00958 574 NIAYGLTDTPDEEIMAAAKAANAHDFIMEFP-NGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC 652
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 174 QqeliQQLNEWSAQEGKTLIGVFHdiRLALTL-SEKIVFMKQGKVAAQGDFQTLASKE 230
Cdd:TIGR00958 653 E----QLLQESRSRASRTVLLIAH--RLSTVErADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
14-221 |
1.55e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 95.91 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHGQKRK--ELATKVAMMSQFT-TVAFDY 89
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPTSGEVLIKGEPIKYDKKSllEVRKTVGIVFQNPdDQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 TVYETVLMGayrqqaqrflPI---VSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:PRK13639 95 TVEEDVAFG----------PLnlgLSKEEvEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 166 NNHLDIRYQQELIQQLNEWSaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEG 219
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-224 |
1.75e-23 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 98.81 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVlidgqevhgqKRKELAtKVAMMS 80
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGeLEPDSGTV----------KWSENA-NIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 81 QFTTVAF--DYTVYEtvLMGAYRQQaqrflpivsKQEKERVLYYLERtgLLPLKD---KVVNQLSGGQQQRVFLAKLFVQ 155
Cdd:PRK15064 389 QDHAYDFenDLTLFD--WMSQWRQE---------GDDEQAVRGTLGR--LLFSQDdikKSVKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286290 156 DPEIILLDEPNNHLDIryqqELIQQLNewSAQE---GkTLIGVFHDIRLALTLSEKIVFMKQGKVAaqgDFQ 224
Cdd:PRK15064 456 KPNVLVMDEPTNHMDM----ESIESLN--MALEkyeG-TLIFVSHDREFVSSLATRIIEITPDGVV---DFS 517
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-221 |
2.14e-23 |
|
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: 98.57 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY-SGSVLIDGQEVHGQKRKELATKVAMMSQFTTVaFDYT 90
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPtSGSVRLDGADLKQWDRETFGKHIGYLPQDVEL-FPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETVlmgayrqqaQRFLPIVSKQ---EKERVLYYLERTGLLPLK-DKVVNQ----LSGGQQQRVFLAKLFVQDPEIILL 162
Cdd:TIGR01842 408 VAENI---------ARFGENADPEkiiEAAKLAGVHELILRLPDGyDTVIGPggatLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488286290 163 DEPNNHLDIRYQQELIQQLNEWSAQeGKTLIGVFHDIRLaLTLSEKIVFMKQGKVAAQG 221
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSL-LGCVDKILVLQDGRIARFG 535
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-230 |
2.59e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 94.26 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLvfPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEvHGQ----KRKelatk 75
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFDLTV--ERGERVAILGPSGAGKSTLLNLIAGfLTPASGSLTLNGQD-HTTtppsRRP----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 76 VAMMSQFTTVAFDYTVYETVLMG---AYRqqaqrflpiVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKL 152
Cdd:PRK10771 73 VSMLFQENNLFSHLTVAQNIGLGlnpGLK---------LNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 153 FVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKE 230
Cdd:PRK10771 144 LVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
7-221 |
3.06e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.50 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 7 TAVTLQQTPI----LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRK--ELATKVAMM 79
Cdd:PRK13637 9 THIYMEGTPFekkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPTSGKIIIDGVDITDKKVKlsDIRKKVGLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQFTTVA-FDYTVYETVLMGAyrqqaqRFLPIVSKQEKERVLYYLERTGL--LPLKDKVVNQLSGGQQQRVFLAKLFVQD 156
Cdd:PRK13637 89 FQYPEYQlFEETIEKDIAFGP------INLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 157 PEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-202 |
3.27e-23 |
|
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: 93.19 E-value: 3.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQkRKELATKVAMMSQFTTVAFDYTVY 92
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLrPDSGEVRWNGTPLAEQ-RDEPHENILYLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVlmgayrqqaqRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIR 172
Cdd:TIGR01189 92 ENL----------HFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180 190
....*....|....*....|....*....|
gi 488286290 173 YQQELIQQLNEWSAQEGKTLIGVFHDIRLA 202
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-221 |
4.82e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 92.61 E-value: 4.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 13 QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY---SGSVLIDGQEVHgqkRKELATKVAMMSQFTTVAFDY 89
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgvSGEVLINGRPLD---KRSFRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 TVYETVLMGAYrqqaqrflpivskqekervlyylertgllpLKdkvvnQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHL 169
Cdd:cd03213 98 TVRETLMFAAK------------------------------LR-----GLSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 170 D-IRYQQ--ELIQQLnewsAQEGKTLIGVFHDIR-LALTLSEKIVFMKQGKVAAQG 221
Cdd:cd03213 143 DsSSALQvmSLLRRL----ADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-184 |
5.37e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 92.93 E-value: 5.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP----YSGSVLIDGQEVHG---QKRKela 73
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafsASGEVLLNGRRLTAlpaEQRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 74 tkVAMMSQfTTVAFDY-TVYETVLMGayrqqaqrfLP--IVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLA 150
Cdd:COG4136 78 --IGILFQ-DDLLFPHlSVGENLAFA---------LPptIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALL 145
|
170 180 190
....*....|....*....|....*....|....
gi 488286290 151 KLFVQDPEIILLDEPNNHLDiryqQELIQQLNEW 184
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLD----AALRAQFREF 175
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-198 |
5.69e-23 |
|
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: 97.31 E-value: 5.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 13 QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGlvpysgsvlIDgQEVHGQKRKELATKVAMMSQFTTVAFDYTVY 92
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---------VD-KDFNGEARPQPGIKVGYLPQEPQLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVLMGAYRQQA--QRFLPIVSK------------QEKERVLYYLERTGL---------------LPLKDKVVNQLSGGQ 143
Cdd:TIGR03719 87 ENVEEGVAEIKDalDRFNEISAKyaepdadfdklaAEQAELQEIIDAADAwdldsqleiamdalrCPPWDADVTKLSGGE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 144 QQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAqegkTLIGVFHD 198
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTHD 217
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-221 |
6.11e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.82 E-value: 6.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY------SGSVLIDGQEVHGQKRKELATK 75
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearvSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 76 VAMMSQFTTVAFDYTVYETVLMGAyrqQAQRFlpIVSKQE-KERVLYYLERTGLL-PLKDKV---VNQLSGGQQQRVFLA 150
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGL---KLNRL--VKSKKElQERVRWALEKAQLWdEVKDRLdapAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286290 151 KLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEwsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLE--LKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-228 |
1.14e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.60 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKELAT---KVAMMSQFTTVAFD--Y 89
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLeSPSQGNVSWRGEPLAKLNRAQRKAfrrDIQMVFQDSISAVNprK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 TVYETVlmgayrQQAQRFLPIVSKQEKE-RVLYYLERTGLLP-LKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNN 167
Cdd:PRK10419 107 TVREII------REPLRHLLSLDKAERLaRASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286290 168 HLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV---AAQGDFQTLAS 228
Cdd:PRK10419 181 NLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIvetQPVGDKLTFSS 244
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-221 |
1.95e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.88 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP----YSGSVLIDGQEVHGQKRKELAtkvAMMSQFTTVAFDYTV 91
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvkGSGSVLLNGMPIDAKEMRAIS---AYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 92 YETvLMGAYRQQAQRFLPivSKQEKERVLYYLERTGLLPLKDKVVNQ------LSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:TIGR00955 117 REH-LMFQAHLRMPRRVT--KKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 166 NNHLDIRYQQELIQQLNEWsAQEGKTLIGVFHDIRLAL-TLSEKIVFMKQGKVAAQG 221
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGL-AQKGKTIICTIHQPSSELfELFDKIILMAEGRVAYLG 249
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-235 |
2.63e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.51 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKELATKVAMM-----SQF--TTVAFD 88
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIeKVKSGEIFYNNQAITDDNFEKLRKHIGIVfqnpdNQFvgSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 ytvyetVLMGAYRQQaqrflpIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNH 168
Cdd:PRK13648 105 ------VAFGLENHA------VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 169 LDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTlSEKIVFMKQGKVAAQGDFQTLASK-EFLQTI 235
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHaEELTRI 239
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
12-216 |
3.96e-22 |
|
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: 90.61 E-value: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVlidgqEVHGqkrkelatKVAMMSQFTTVAFDyT 90
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEKLSGSV-----SVPG--------SIAYVSQEPWIQNG-T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETVLMGayrqqaQRFlpivskqEKERVLYYLERTGL------LPLKD------KVVNqLSGGQQQRVFLAKLFVQDPE 158
Cdd:cd03250 82 IRENILFG------KPF-------DEERYEKVIKACALepdleiLPDGDlteigeKGIN-LSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 159 IILLDEPNNHLDIRYQQELIQQ--LNEWsaQEGKTLIGVFHDIRLaLTLSEKIVFMKQGK 216
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIFENciLGLL--LNNKTRILVTHQLQL-LPHADQIVVLDNGR 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-230 |
4.72e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.56 E-value: 4.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELAtKVAMMS 80
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLThPDAGSISLCGEPVPSRARHARQ-RVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 81 QFTTVAFDYTVYETVLMGAyrqqaqRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEII 160
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFG------RYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 161 LLDEPNNHLDIRYQQELIQQLNEWSAQeGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKE 230
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
16-217 |
6.09e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.28 E-value: 6.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYSGSVLIDGQEVHGQKRKElatkVAMMSQFTTVAFDYTVYETV 95
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED----TRLMFQDARLLPWKKVIDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 96 ---LMGAYRQQAQRFLPIVSKQEkervlyyleRTGLLPLKdkvvnqLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLD-- 170
Cdd:PRK11247 103 glgLKGQWRDAALQALAAVGLAD---------RANEWPAA------LSGGQKQRVALARALIHRPGLLLLDEPLGALDal 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488286290 171 IRYQ-QELIQQLneWSaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:PRK11247 168 TRIEmQDLIESL--WQ-QHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-222 |
7.05e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 92.98 E-value: 7.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQE---VHGQKRKelatkV 76
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMLDGVDlshVPPYQRP-----I 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 77 AMMSQFTTVAFDYTVYETVLMGAyrqqAQRFLPivsKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQ 155
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGL----KQDKLP---KAEiASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286290 156 DPEIILLDEPNNHLDI----RYQQELIQQLNewsaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:PRK11607 167 RPKLLLLDEPMGALDKklrdRMQLEVVDILE----RVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-217 |
1.52e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 91.83 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY-SGSVLIDGQEVHGQKRKElaTKVAMMSQfttvafDY--- 89
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERItSGEIWIGGRVVNELEPAD--RDIAMVFQ------NYaly 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 ---TVYETVlmgAYRqqaqrfLPI--VSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLD 163
Cdd:PRK11650 89 phmSVRENM---AYG------LKIrgMPKAEiEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 164 EPNNHLD--IRYQQEL-IQQLNewsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:PRK11650 160 EPLSNLDakLRVQMRLeIQRLH---RRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-232 |
1.53e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 91.30 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 5 KKTAVTLQqtpILKDISLVFPTGSKTCILGPNGCGKTTLLKTI-AGLVPYSGSVLIDGQEVHGQKR-------------- 69
Cdd:PRK13651 14 KKLPTELK---ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLnALLLPDTGTIEWIFKDEKNKKKtkekekvleklviq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 70 ----------KELATKVAMMSQFTTVA-FDYTVYETVLMGayrqqaqrflPI---VSKQE-KERVLYYLERTGL-LPLKD 133
Cdd:PRK13651 91 ktrfkkikkiKEIRRRVGVVFQFAEYQlFEQTIEKDIIFG----------PVsmgVSKEEaKKRAAKYIELVGLdESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 134 KVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSaQEGKTLIGVFHDIRLALTLSEKIVFMK 213
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
250 260
....*....|....*....|
gi 488286290 214 QGKVAAQGD-FQTLASKEFL 232
Cdd:PRK13651 240 DGKIIKDGDtYDILSDNKFL 259
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-223 |
2.10e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 89.79 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHgqKRKElaTKVAMMS-----QFTTVAFDYT 90
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTrPDSGSVLFGGTDLT--GLDE--HEIARLGigrkfQKPTVFEELT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETVL--MGAYRQQAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPN-- 166
Cdd:COG4674 102 VFENLElaLKGDRGVFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVag 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 167 -NHLDIRYQQELIQQLNewsaqEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDF 223
Cdd:COG4674 182 mTDAETERTAELLKSLA-----GKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSL 234
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-222 |
2.37e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.07 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATK--VAMMSQFTTVAFD 88
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKPLDYSKRGLLALRqqVATVFQDPEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 YTVYETVLMGAYRQqaqrfLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNH 168
Cdd:PRK13638 92 YTDIDSDIAFSLRN-----LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488286290 169 LDIRYQQELIQQLNEWSAQeGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-222 |
4.29e-21 |
|
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: 91.67 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYSGSVLIDGQEVHGQKRKELATKVAMMsQfttVAF-D------- 88
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRRALRPLRRRM-Q---VVFqDpfgslsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 -YTVYETVLMGAYRQQaqrflPIVSKQEKE-RVLYYLERTGLLP-LKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:COG4172 378 rMTVGQIIAEGLRVHG-----PGLSAAERRaRVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 166 NNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:COG4172 453 TSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGP 509
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-221 |
4.78e-21 |
|
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: 91.70 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDYTVYE 93
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYePDSGQILLDGHDLADYTLASLRRQVALVSQ-DVVLFNDTIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVLMGAYRQqaqrflpiVSKQEKERVL---YYLERTGLLPLK-DKVVNQ----LSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:TIGR02203 425 NIAYGRTEQ--------ADRAEIERALaaaYAQDFVDKLPLGlDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEA 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 166 NNHLDI---RYQQELIQQLnewsaQEGKTLIGVFHdiRLA-LTLSEKIVFMKQGKVAAQG 221
Cdd:TIGR02203 497 TSALDNeseRLVQAALERL-----MQGRTTLVIAH--RLStIEKADRIVVMDDGRIVERG 549
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-198 |
5.27e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 88.23 E-value: 5.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMM 79
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQfTTVAFDYTVYETVLMG-AYRQQAqrflpivskQEKERVLYYLERTGL-LPLKDKVVNQLSGGQQQRVFLAKLFVQDP 157
Cdd:PRK10247 87 AQ-TPTLFGDTVYDNLIFPwQIRNQQ---------PDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488286290 158 EIILLDEPNNHLD---IRYQQELIQQLNEwsaQEGKTLIGVFHD 198
Cdd:PRK10247 157 KVLLLDEITSALDesnKHNVNEIIHRYVR---EQNIAVLWVTHD 197
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
12-221 |
6.20e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.99 E-value: 6.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTI-AGLVPYSGSVLIDGQEVHGQKRK-ELATKVAMMSQF---TTVA 86
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMnALLIPSEGKVYVDGLDTSDEENLwDIRNKAGMVFQNpdnQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 87 fdYTVYETVLMGAYRqqaqrfLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPN 166
Cdd:PRK13633 101 --TIVEEDVAFGPEN------LGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 167 NHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTlSEKIVFMKQGKVAAQG 221
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-226 |
7.55e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.89 E-value: 7.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELAtKVAMMS 80
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTsPDAGKITVLGVPVPARARLARA-RIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 81 QFTTVAFDYTVYETVLMGAyrqqaqRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEII 160
Cdd:PRK13536 121 QFDNLDLEFTVRENLLVFG------RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 161 LLDEPNNHLDIRYQQELIQQLNEWSAQeGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTL 226
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
32-170 |
1.04e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 86.78 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 32 ILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQkRKELATKVAMMSQFTTVAFDYTVYETVLMgayrqqaqrFLPI 110
Cdd:PRK13538 32 IEGPNGAGKTSLLRILAGLArPDAGEVLWQGEPIRRQ-RDEYHQDLLYLGHQPGIKTELTALENLRF---------YQRL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 111 VSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLD 170
Cdd:PRK13538 102 HGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
10-234 |
1.61e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 88.75 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 10 TLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLI------------DGQEVHGQKR----KEL 72
Cdd:PRK13631 35 QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkSKYGTIQVgdiyigdkknnhELITNPYSKKiknfKEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 73 ATKVAMMSQFTtvafDYTVYETVLmgayrQQAQRFLPI---VSKQE-KERVLYYLERTGL-LPLKDKVVNQLSGGQQQRV 147
Cdd:PRK13631 115 RRRVSMVFQFP----EYQLFKDTI-----EKDIMFGPValgVKKSEaKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 148 FLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEwSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD-FQTL 226
Cdd:PRK13631 186 AIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTpYEIF 264
|
....*...
gi 488286290 227 ASKEFLQT 234
Cdd:PRK13631 265 TDQHIINS 272
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-230 |
1.94e-20 |
|
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: 86.77 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDYTVYET 94
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWLRRQVGVVLQ-ENVLFNRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 VLMGayRQQAQRflpivskqekERVLYYLERTGL------LPLK-DKVVNQ----LSGGQQQRVFLAKLFVQDPEIILLD 163
Cdd:cd03252 96 IALA--DPGMSM----------ERVIEAAKLAGAhdfiseLPEGyDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 164 EPNNHLDirYQQELIQQLNEWSAQEGKTLIGVFHdiRL-ALTLSEKIVFMKQGKVAAQGDFQTLASKE 230
Cdd:cd03252 164 EATSALD--YESEHAIMRNMHDICAGRTVIIIAH--RLsTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-235 |
1.99e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.55 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQT--PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGS---VLIDGQEVHGQKRKELATK 75
Cdd:PRK13640 6 VEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDNPnskITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 76 VAMMSQFTTVAF-DYTVYETVLMGAYRQQaqrflpiVSKQEKERVLY-YLERTGLLPLKDKVVNQLSGGQQQRVFLAKLF 153
Cdd:PRK13640 86 VGIVFQNPDNQFvGATVGDDVAFGLENRA-------VPRPEMIKIVRdVLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 154 VQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLAlTLSEKIVFMKQGKVAAQGDFQTLASK-EFL 232
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKvEML 237
|
...
gi 488286290 233 QTI 235
Cdd:PRK13640 238 KEI 240
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-230 |
2.29e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 86.62 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVhgqkrkelaTKVAM- 78
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVkPDSGRIFLDGEDI---------THLPMh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 79 ---------MSQFTTVAFDYTVYETVLMgayrqqAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFL 149
Cdd:COG1137 74 krarlgigyLPQEASIFRKLTVEDNILA------VLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 150 AKLFVQDPEIILLDEP---------NnhlDIryqQELIQQLnewsAQEGktlIGVF---HDIRLALTLSEKIVFMKQGKV 217
Cdd:COG1137 148 ARALATNPKFILLDEPfagvdpiavA---DI---QKIIRHL----KERG---IGVLitdHNVRETLGICDRAYIISEGKV 214
|
250
....*....|...
gi 488286290 218 AAQGDFQTLASKE 230
Cdd:COG1137 215 LAEGTPEEILNNP 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
10-217 |
2.37e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.58 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 10 TLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKR----KELATKVAMMSQFTT 84
Cdd:PRK13641 16 TPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLkPSSGTITIAGYHITPETGnknlKKLRKKVSLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 85 VA-FDYTVYETVLMGAyrqqaqRFLPIVSKQEKERVLYYLERTGLlplKDKVVN----QLSGGQQQRVFLAKLFVQDPEI 159
Cdd:PRK13641 96 AQlFENTVLKDVEFGP------KNFGFSEDEAKEKALKWLKKVGL---SEDLISkspfELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLNEWSAqEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQK-AGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
9-204 |
2.51e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.48 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 9 VTLQ---QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY-SGSVLIDGQEvhgqkrkelatKVAMMSQftt 84
Cdd:COG4178 368 LTLRtpdGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYgSGRIARPAGA-----------RVLFLPQ--- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 85 vafdyTVYetVLMG------AYRQQAQRFlpivskqEKERVLYYLERTGLLPLKDKV------VNQLSGGQQQRVFLAKL 152
Cdd:COG4178 434 -----RPY--LPLGtlrealLYPATAEAF-------SDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARL 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 153 FVQDPEIILLDEPNNHLDIRYQQELIQQLNEwsAQEGKTLIGV--------FHDIRLALT 204
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVghrstlaaFHDRVLELT 557
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-229 |
3.26e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 87.84 E-value: 3.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHgQKRKELATKVAM-MSQFTTVAFDYTVYET 94
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVPTSGEVRVLGYVPF-KRRKEFARRIGVvFGQRSQLWWDLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 -VLMGA-YRqqaqrflpiVSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDI 171
Cdd:COG4586 117 fRLLKAiYR---------IPDAEyKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 172 RYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASK 229
Cdd:COG4586 188 VSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-247 |
3.89e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.55 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 4 LKKTAVTLQqtpiLKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELA----TKVAM 78
Cdd:PRK10070 35 LEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTRGQVLIDGVDIAKISDAELRevrrKKIAM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 79 MSQFTTVAFDYTVYETVLMGayrqqaQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPE 158
Cdd:PRK10070 111 VFQSFALMPHMTVLDNTAFG------MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 159 IILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG---DFQTLASKEFLQTI 235
Cdd:PRK10070 185 ILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGtpdEILNNPANDYVRTF 264
|
250
....*....|...
gi 488286290 236 FE-TDIVSYFQKQ 247
Cdd:PRK10070 265 FRgVDISQVFSAK 277
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
15-226 |
5.63e-20 |
|
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: 88.64 E-value: 5.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDYTVYE 93
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFqARSGEILLNGFSLKDIDRHTLRQFINYLPQ-EPYIFSGSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVLMGAYRQqaqrflpiVSKQEKERVLYYLErtgllpLKDKVVN--------------QLSGGQQQRVFLAKLFVQDPEI 159
Cdd:TIGR01193 567 NLLLGAKEN--------VSQDEIWAACEIAE------IKDDIENmplgyqtelseegsSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLnewSAQEGKTLIGVFHDIRLAlTLSEKIVFMKQGKVAAQGDFQTL 226
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNL---LNLQDKTIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
15-230 |
7.44e-20 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 85.40 E-value: 7.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEV-----HGQKRkelaTKVAMMSQFTTVAFD 88
Cdd:TIGR04406 15 KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVrPDAGKILIDGQDIthlpmHERAR----LGIGYLPQEASIFRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 YTVYETvLMGAYrqQAQRFLPivSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNH 168
Cdd:TIGR04406 91 LTVEEN-IMAVL--EIRKDLD--RAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 169 LD-IRYQQelIQQLNEWSAQEGktlIGVF---HDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKE 230
Cdd:TIGR04406 166 VDpIAVGD--IKKIIKHLKERG---IGVLitdHNVRETLDICDRAYIISDGKVLAEGTPAEIVANE 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-221 |
1.16e-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: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVlidgqEVHGQKRKELATKVAMMSqfttvafDYTVYET 94
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYpPDSGTV-----TVRGRVSSLLGLGGGFNP-------ELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 VLMGAyrqqaqRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQ 174
Cdd:cd03220 105 IYLNG------RLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488286290 175 QELIQQLNEWSAQeGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:cd03220 179 EKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-202 |
1.32e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 83.70 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHgQKRKELATKVAMMSQFTTVAFDYTVYET 94
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSpPLAGRVLLNGGPLD-FQRDSIARGLLYLGHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 VlmgayrqqaqRFL-PIVSKqekERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRY 173
Cdd:cd03231 94 L----------RFWhADHSD---EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|....*....
gi 488286290 174 QQELIQQLNEWSAQEGKTLIGVFHDIRLA 202
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-221 |
1.35e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 84.89 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYS------GSVLIDGQEVHGQKRK--ELA 73
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearveGEVRLFGRNIYSPDVDpiEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 74 TKVAMMSQFTTVAFDYTVYETVLMGAYRQQAQRflpivSKQE-KERVLYYLERTGLLP-----LKDKVVNqLSGGQQQRV 147
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVK-----SKKElDERVEWALKKAALWDevkdrLNDYPSN-LSGGQRQRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 148 FLAKLFVQDPEIILLDEPNNHLD---IRYQQELIQQLnewsaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDpvgTAKIEELLFEL-----KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
32-217 |
1.39e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.16 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 32 ILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKE---LATKVAMMSQFTTVAFDYTVYETVLM-----GAYRQ 102
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIErPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMDRTVYDNVAIpliiaGASGD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 103 QAQRflpivskqekeRVLYYLERTGLLplkDKVVN---QLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQ 179
Cdd:PRK10908 113 DIRR-----------RVSAALDKVGLL---DKAKNfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILR 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 488286290 180 QLNEWSaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:PRK10908 179 LFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-170 |
2.36e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 86.71 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGlvpysgsvlIDgQEVHGQKRKELATKVAMMSQFTTVAFDYTVYET 94
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---------VD-KEFEGEARPAPGIKVGYLPQEPQLDPEKTVREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 VLMGAYRQQA--QRFLPIVSK------------QEKERVLYYLERTGL---------------LPLKDKVVNQLSGGQQQ 145
Cdd:PRK11819 91 VEEGVAEVKAalDRFNEIYAAyaepdadfdalaAEQGELQEIIDAADAwdldsqleiamdalrCPPWDAKVTKLSGGERR 170
|
170 180
....*....|....*....|....*
gi 488286290 146 RVFLAKLFVQDPEIILLDEPNNHLD 170
Cdd:PRK11819 171 RVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
18-221 |
2.41e-19 |
|
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: 84.11 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 18 KDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSV---LIDGQEV------HGQKRKELATKVAMMSQF----- 82
Cdd:TIGR02323 20 RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGrLAPDHGTAtyiMRSGAELelyqlsEAERRRLMRTEWGFVHQNprdgl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 83 -TTVAFDYTVYETVL------MGAYRQQAQRFLpivskqekERVLYYLERTGLLPlkdkvvNQLSGGQQQRVFLAKLFVQ 155
Cdd:TIGR02323 100 rMRVSAGANIGERLMaigarhYGNIRATAQDWL--------EEVEIDPTRIDDLP------RAFSGGMQQRLQIARNLVT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 156 DPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:TIGR02323 166 RPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
32-215 |
2.57e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.53 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 32 ILGPNGCGKTTLLKTIAGLVPYS-GSVLIDGQEVHGQKRKELATK---VAMMSQFTTVAFD--YTVYETVlmgayRQQAQ 105
Cdd:PRK15079 52 VVGESGCGKSTFARAIIGLVKATdGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLASLNprMTIGEII-----AEPLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 106 RFLPIVSKQE-KERVLYYLERTGLLPlkdKVVN----QLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQ 180
Cdd:PRK15079 127 TYHPKLSRQEvKDRVKAMMLKVGLLP---NLINryphEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNL 203
|
170 180 190
....*....|....*....|....*....|....*
gi 488286290 181 LNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQG 215
Cdd:PRK15079 204 LQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
16-236 |
3.05e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.79 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY-SGSVLIDGQEV-----HGQKRKelatKVAMMSQFTTVAFDY 89
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRdAGNIIIDDEDIsllplHARARR----GIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 TVYETvLMGAYRQQAQrflpIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPN--- 166
Cdd:PRK10895 94 SVYDN-LMAVLQIRDD----LSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFagv 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 167 ---NHLDIRyqqELIQQLNEWSaqegktlIGVF---HDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEFLQTIF 236
Cdd:PRK10895 169 dpiSVIDIK---RIIEHLRDSG-------LGVLitdHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-226 |
3.28e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 86.23 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKE-LATKVAMMSQFTTVAFDYTVYET 94
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYqPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 VLMGayrQQAQRFLPIVSKQEKERVLYYLERTGL-LPLkDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDiry 173
Cdd:COG1129 100 IFLG---REPRRGGLIDWRAMRRRARELLARLGLdIDP-DTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLT--- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286290 174 QQE------LIQQLnewsAQEGKTLIGVFHdiRLA--LTLSEKIVFMKQGKVAAQGDFQTL 226
Cdd:COG1129 173 EREverlfrIIRRL----KAQGVAIIYISH--RLDevFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-223 |
3.62e-19 |
|
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: 82.57 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY---SGSVLIDGQEVhgqkrKELatkvammsqfttvafdyTVY 92
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevtEGEILFKGEDI-----TDL-----------------PPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVLMGAYrqqaqrflpiVSKQEKERVlyylerTGlLPLKDKV--VNQ-LSGGQQQRVFLAKLFVQDPEIILLDEPNNHL 169
Cdd:cd03217 73 ERARLGIF----------LAFQYPPEI------PG-VKNADFLryVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 170 DIRYQQELIQQLNEWsAQEGKTLIGVFHDIRLALTL-SEKIVFMKQGKVAAQGDF 223
Cdd:cd03217 136 DIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
17-222 |
4.32e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.67 E-value: 4.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL------VPYSGSVLIDGQEVHGQKRK--ELATKVAMMSQFTTvAFD 88
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTITGSIVYNGHNIYSPRTDtvDLRKEIGMVFQQPN-PFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 YTVYETVLMGayrqqaqrfLPIVSKQEKERVLYYLERTgllpLK-----DKVVNQL-------SGGQQQRVFLAKLFVQD 156
Cdd:PRK14239 100 MSIYENVVYG---------LRLKGIKDKQVLDEAVEKS----LKgasiwDEVKDRLhdsalglSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 157 PEIILLDEPNNHLDIRYQQELIQQLneWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETL--LGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYND 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-214 |
4.82e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.24 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVlidgqevhgqkRKELATKVAMM 79
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVaPDEGVI-----------KRNGKLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQftTVAFDYTVYETVlmgayrqqaQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEI 159
Cdd:PRK09544 73 PQ--KLYLDTTLPLTV---------NRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQ 214
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-170 |
5.03e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 84.85 E-value: 5.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQ----TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKELAT- 74
Cdd:PRK11153 1 MIELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLeRPTSGRVLVDGQDLTALSEKELRKa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 75 --KVAMMSQFTTVAFDYTVYETVlmgayrqqaqrFLPI----VSKQE-KERVLYYLERTGLLPLKDKVVNQLSGGQQQRV 147
Cdd:PRK11153 81 rrQIGMIFQHFNLLSSRTVFDNV-----------ALPLelagTPKAEiKARVTELLELVGLSDKADRYPAQLSGGQKQRV 149
|
170 180
....*....|....*....|...
gi 488286290 148 FLAKLFVQDPEIILLDEPNNHLD 170
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALD 172
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-228 |
5.38e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.73 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVH-GQKRKELATKVAMMSQFTTVAFDYTVYET 94
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNyQPDAGSILIDGQEMRfASTTAALAAGVAIIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 VLMGayrQQAQRFLPIVSKQEKERVLYYLERTGL-----LPLKDkvvnqLSGGQQQRVFLAKLFVQDPEIILLDEPNNHL 169
Cdd:PRK11288 100 LYLG---QLPHKGGIVNRRLLNYEAREQLEHLGVdidpdTPLKY-----LSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488286290 170 DIRYQQELIQQLNEWSAqEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAqgDFQTLAS 228
Cdd:PRK11288 172 SAREIEQLFRVIRELRA-EGRVILYVSHRMEEIFALCDAITVFKDGRYVA--TFDDMAQ 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-222 |
6.12e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.82 E-value: 6.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 4 LKKTAVTLQQTP-----ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGqevhgqkrkelatKVA 77
Cdd:COG1134 24 LKELLLRRRRTRreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILePTSGRVEVNG-------------RVS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 78 MMSQFTTvAF--DYTVYETV-----LMGAYRQQAQRFLP-IVSKQEKERVLYylertglLPLKdkvvnQLSGGQQQRVFL 149
Cdd:COG1134 91 ALLELGA-GFhpELTGRENIylngrLLGLSRKEIDEKFDeIVEFAELGDFID-------QPVK-----TYSSGMRARLAF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286290 150 AKLFVQDPEIILLDEpnnHL---DIRYQQ---ELIQQLnewsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:COG1134 158 AVATAVDPDILLVDE---VLavgDAAFQKkclARIREL----RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-228 |
7.37e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.22 E-value: 7.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL------VPYSGSVLIDGQEVHGQKRK-ELATKVAMMSQFTTvAFD 88
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgYRYSGDVLLGGRSIFNYRDVlEFRRRVGMLFQRPN-PFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 YTVYETVLMGAyrqQAQRFLPivSKQEKERVLYYLERTGLL-PLKDKVVN---QLSGGQQQRVFLAKLFVQDPEIILLDE 164
Cdd:PRK14271 115 MSIMDNVLAGV---RAHKLVP--RKEFRGVAQARLTEVGLWdAVKDRLSDspfRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286290 165 PNNHLDIRYQQELIQQLNewSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLAS 228
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIR--SLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-235 |
9.96e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 82.87 E-value: 9.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQ-TPI----LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKR----KE 71
Cdd:PRK13649 3 INLQNVSYTYQAgTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLhVPTQGSVRVDDTLITSTSKnkdiKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 72 LATKVAMMSQFT-TVAFDYTVYETVLMGAyrqqaQRFLpiVSKQEKERVLyyLERTGLLPLKDKVVNQ----LSGGQQQR 146
Cdd:PRK13649 83 IRKKVGLVFQFPeSQLFEETVLKDVAFGP-----QNFG--VSQEEAEALA--REKLALVGISESLFEKnpfeLSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 147 VFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD---- 222
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKpkdi 232
|
250
....*....|...
gi 488286290 223 FQTLaskEFLQTI 235
Cdd:PRK13649 233 FQDV---DFLEEK 242
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-217 |
1.44e-18 |
|
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: 81.36 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDYTVY 92
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYqPQGGQVLLDGKPISQYEHKYLHSKVSLVGQ-EPVLFARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVlmgAYRQQAQRFLPIVSKQEKERVLYYLERTGLLPLKD--KVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLD 170
Cdd:cd03248 106 DNI---AYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEvgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488286290 171 IRYQQELIQQLNEWSaqEGKTLIGVFHDIRLaLTLSEKIVFMKQGKV 217
Cdd:cd03248 183 AESEQQVQQALYDWP--ERRTVLVIAHRLST-VERADQILVLDGGRI 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-211 |
1.86e-18 |
|
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: 84.07 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 32 ILGPNGCGKTTLLKTIAG-LVPYSGSVlidgqevhgqkrkELATKVAMMSQFTTVAFDYTVyETVLMGAYRQqaqrflPI 110
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGvLKPDEGEV-------------DEDLKISYKPQYISPDYDGTV-EEFLRSANTD------DF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 111 VSKQEKERVLyylERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDI--RYQ-QELIQQLNEwsaQ 187
Cdd:COG1245 431 GSSYYKTEII---KPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqRLAvAKAIRRFAE---N 504
|
170 180
....*....|....*....|....*
gi 488286290 188 EGKTLIGVFHDIRLALTLSEKI-VF 211
Cdd:COG1245 505 RGKTAMVVDHDIYLIDYISDRLmVF 529
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
15-215 |
2.40e-18 |
|
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: 80.94 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQE-----VHGQKRKELA---TKVAMMSQFTTV 85
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPDSGSILVRHDGgwvdlAQASPREILAlrrRTIGYVSQFLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 86 -----AFDyTVYETVL-MGAYRQQAQRflpivskqEKERVLYYL---ERT-GLLPlkdkvvNQLSGGQQQRVFLAKLFVQ 155
Cdd:COG4778 105 iprvsALD-VVAEPLLeRGVDREEARA--------RARELLARLnlpERLwDLPP------ATFSGGEQQRVNIARGFIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286290 156 DPEIILLDEPNNHLDIRYQQ---ELIQQLnewsAQEGKTLIGVFHDIRLALTLSEKIVFMKQG 215
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAvvvELIEEA----KARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-224 |
3.37e-18 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 83.76 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PIL-KDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLidgqevhgqkrKELATKVAMMSQFTTVAFDYTVY 92
Cdd:PLN03073 522 PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGeLQPSSGTVF-----------RSAKVRMAVFSQHHVDGLDLSSN 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVLMgayrqqaQRFLPIVSKQEKERVLYYLERTGLLPLKDkvVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIR 172
Cdd:PLN03073 591 PLLYM-------MRCFPGVPEQKLRAHLGSFGVTGNLALQP--MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD 661
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488286290 173 YQQELIQQLNEWsaqEGKTLIgVFHDIRLALTLSEKIVFMKQGKVAA-QGDFQ 224
Cdd:PLN03073 662 AVEALIQGLVLF---QGGVLM-VSHDEHLISGSVDELWVVSEGKVTPfHGTFH 710
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
12-252 |
3.95e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.59 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPI----LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHG-----QKRKELATKVAMMSQ 81
Cdd:PRK13645 18 KKTPFefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiISETGQTIVGDYAIPAnlkkiKEVKRLRKEIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 82 FTtvafDYTVYETVLmgayrQQAQRFLPIVSKQEKERVLYYL-ERTGLLPLKDKVVN----QLSGGQQQRVFLAKLFVQD 156
Cdd:PRK13645 98 FP----EYQLFQETI-----EKDIAFGPVNLGENKQEAYKKVpELLKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 157 PEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD-FQTLASKEFLQTI 235
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSpFEIFSNQELLTKI 248
|
250
....*....|....*..
gi 488286290 236 fETDIVSYFQKQHKVWE 252
Cdd:PRK13645 249 -EIDPPKLYQLMYKLKN 264
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-235 |
4.39e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.19 E-value: 4.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQ-TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHG-QKRKELATKVA 77
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQKGKVLVSGIDTGDfSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 78 MMSQFTTVAF-DYTVYETVLMGAyrqqAQRFLPIVskQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQD 156
Cdd:PRK13644 81 IVFQNPETQFvGRTVEEDLAFGP----ENLCLPPI--EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286290 157 PEIILLDEPNNHLDIRYQQELIQQLNEWSaQEGKTLIGVFHDIRlALTLSEKIVFMKQGKVAAQGDFQTLASKEFLQTI 235
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-181 |
5.12e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 5.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKE----LATKVAMMSQFttvafdy 89
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLpPAAGTIKLDGGDIDDPDVAEachyLGHRNAMKPAL------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 TVYETVLMGAyrqqaqRFLpivsKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHL 169
Cdd:PRK13539 89 TVAENLEFWA------AFL----GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170
....*....|..
gi 488286290 170 DiRYQQELIQQL 181
Cdd:PRK13539 159 D-AAAVALFAEL 169
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
37-219 |
5.26e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.76 E-value: 5.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 37 GCGKTTLLKTIAGLVP-YSGSVLIDGQEVHGQK-RKELATKVAMMS---QFTTVAFDYTVYETVLMGAYRQQAqRFLPIV 111
Cdd:COG1129 288 GAGRTELARALFGADPaDSGEIRLDGKPVRIRSpRDAIRAGIAYVPedrKGEGLVLDLSIRENITLASLDRLS-RGGLLD 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 112 SKQEKERVLYYLERTGL-LPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDI--RYQ-QELIQQLnewsAQ 187
Cdd:COG1129 367 RRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVgaKAEiYRLIREL----AA 442
|
170 180 190
....*....|....*....|....*....|..
gi 488286290 188 EGKTLIGVFHDIRLALTLSEKIVFMKQGKVAA 219
Cdd:COG1129 443 EGKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-221 |
6.20e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 80.98 E-value: 6.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQ-TPI----LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQ-KRKELAT 74
Cdd:PRK13646 3 IRFDNVSYTYQKgTPYehqaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLkPTTGTVTVDDITITHKtKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 75 ---KVAMMSQF-TTVAFDYTVYETVLMGAyrqqaQRF-LPIvsKQEKERVLYYLERTGL-LPLKDKVVNQLSGGQQQRVF 148
Cdd:PRK13646 83 vrkRIGMVFQFpESQLFEDTVEREIIFGP-----KNFkMNL--DEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286290 149 LAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
12-202 |
7.29e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 79.82 E-value: 7.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYS-GSVLIDGQEVHG---QKRKEL-ATKVAMMSQFTTVA 86
Cdd:PRK10584 21 HELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSsGEVSLVGQPLHQmdeEARAKLrAKHVGFVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 87 FDYTVYETVLMGAY-RQQAQRflpivskQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:PRK10584 101 PTLNALENVELPALlRGESSR-------QSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 488286290 166 NNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLA 202
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-217 |
9.14e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.52 E-value: 9.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP-YSGSVLIDGQEVHGQKRKELATKVAMMSQFTTVAF-DYTVYET 94
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEeFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFvGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 VLMGAYRQQAQRflpivsKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQ 174
Cdd:PRK13642 103 VAFGMENQGIPR------EEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488286290 175 QELIQQLNEWSAQEGKTLIGVFHDIRLALTlSEKIVFMKQGKV 217
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-245 |
1.44e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEvHGQKRKELATK--VA 77
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIhEPTKGTITINNIN-YNKLDHKLAAQlgIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 78 MMSQFTTVAFDYTVYETVLMGayRQQAQRFL--PIVS-KQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFV 154
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIG--RHLTKKVCgvNIIDwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 155 QDPEIILLDEPNNHL---DIRYQQELIQQLNewsaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEF 231
Cdd:PRK09700 162 LDAKVIIMDEPTSSLtnkEVDYLFLIMNQLR----KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDI 237
|
250
....*....|....
gi 488286290 232 LQTIFETDIVSYFQ 245
Cdd:PRK09700 238 VRLMVGRELQNRFN 251
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-238 |
1.81e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 81.60 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP-YSGSVLIDGQEVHgQKRKELATKVAMMSQFTTVAFDYTVYE 93
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPpTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVLMgaYRQQAQRflpivSKQEKE-RVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIR 172
Cdd:TIGR01257 1023 HILF--YAQLKGR-----SWEEAQlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 173 YQQELIQQLNEWsaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGdfqtlaSKEFLQTIFET 238
Cdd:TIGR01257 1096 SRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG------TPLFLKNCFGT 1153
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-230 |
2.29e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 81.15 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPysgsvLIDGQEVHGQKrkelaTKVAMMSQFTTVAFDYTVYE 93
Cdd:PRK11147 16 APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVL-----LDDGRIIYEQD-----LIVARLQQDPPRNVEGTVYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVLMG-----AYRQQAQRFLPIVSKQEKERVLYYLERT--------------------GLLPLK-DKVVNQLSGGQQQRV 147
Cdd:PRK11147 86 FVAEGieeqaEYLKRYHDISHLVETDPSEKNLNELAKLqeqldhhnlwqlenrinevlAQLGLDpDAALSSLSGGWLRKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 148 FLAKLFVQDPEIILLDEPNNHLDIryqqELIQQLNEWSAQEGKTLIGVFHD---IRlalTLSEKIVFMKQGKVAA-QGDF 223
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDrsfIR---NMATRIVDLDRGKLVSyPGNY 238
|
....*...
gi 488286290 224 QT-LASKE 230
Cdd:PRK11147 239 DQyLLEKE 246
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-235 |
4.52e-17 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 77.83 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 32 ILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQevhgqkrkelatKVAMMSQFTTVAFDYTVYEtVLMGayrqQAQRFLpi 110
Cdd:cd03237 30 ILGPNGIGKTTFIKMLAGVLkPDEGDIEIELD------------TVSYKPQYIKADYEGTVRD-LLSS----ITKDFY-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 111 VSKQEKERVLYYLertGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIryQQELI--QQLNEWSAQE 188
Cdd:cd03237 91 THPYFKTEIAKPL---QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV--EQRLMasKVIRRFAENN 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488286290 189 GKTLIGVFHDIRLALTLSEK-IVFmkQGKVAAQGDF---QTLAS--KEFLQTI 235
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRlIVF--EGEPSVNGVAnppQSLRSgmNRFLKNL 216
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-211 |
5.84e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.85 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 32 ILGPNGCGKTTLLKTIAG-LVPYSGSVLIDgqevhgqkrkelaTKVAMMSQFTTVAFDYTVYEtVLmgayRQQAQRFLpi 110
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGvLKPDEGEVDPE-------------LKISYKPQYIKPDYDGTVED-LL----RSITDDLG-- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 111 vSKQEKERVLyylERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDI--RYQ-QELIQQLNEwsaQ 187
Cdd:PRK13409 430 -SSYYKSEII---KPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqRLAvAKAIRRIAE---E 502
|
170 180
....*....|....*....|....*
gi 488286290 188 EGKTLIGVFHDIRLALTLSEK-IVF 211
Cdd:PRK13409 503 REATALVVDHDIYMIDYISDRlMVF 527
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-221 |
7.19e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 78.24 E-value: 7.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQ-QTPI----LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLI-DGQEVHGQKRKELA 73
Cdd:PRK13643 1 MIKFEKVNYTYQpNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTVgDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 74 ---TKVAMMSQF-TTVAFDYTVYETVLMGAyrqqaQRFLpiVSKQEKERVLY-YLERTGLLP-LKDKVVNQLSGGQQQRV 147
Cdd:PRK13643 81 pvrKKVGVVFQFpESQLFEETVLKDVAFGP-----QNFG--IPKEKAEKIAAeKLEMVGLADeFWEKSPFELSGGQMRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286290 148 FLAKLFVQDPEIILLDEPNNHLDIRYQQELIqQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMM-QLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
17-211 |
1.27e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.13 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKT---IAGLVP---YSGSVLIDGQEVHGQKRK--ELATKVAMMSQFTTvAFD 88
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPgfrVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPN-PFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 YTVYETVLMGAYRQQAQRFL-PIVSKQEKERVLYYlertgllPLKDKVVNQ---LSGGQQQRVFLAKLFVQDPEIILLDE 164
Cdd:PRK14243 105 KSIYDNIAYGARINGYKGDMdELVERSLRQAALWD-------EVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488286290 165 PNNHLD---IRYQQELIQQLnewsaQEGKTLIGVFHDIRLALTLSEKIVF 211
Cdd:PRK14243 178 PCSALDpisTLRIEELMHEL-----KEQYTIIIVTHNMQQAARVSDMTAF 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-203 |
1.28e-16 |
|
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: 74.88 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKK-TAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY-SGSVLIDGQEvhgqkrkelatKVAMM 79
Cdd:cd03223 1 IELENlSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWgSGRIGMPEGE-----------DLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQfttvafdytvyetvlmgayrqqaQRFLPIVSKqeKERVLYylertgllPLKDKvvnqLSGGQQQRVFLAKLFVQDPEI 159
Cdd:cd03223 70 PQ-----------------------RPYLPLGTL--REQLIY--------PWDDV----LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLNEwsaqEGKTLIGV--------FHDIRLAL 203
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKE----LGITVISVghrpslwkFHDRVLDL 160
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
12-227 |
1.53e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 78.60 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYS-GSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDYT 90
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSeGDIRFHDIPLTKLQLDSWRSRLAVVSQ-TPFLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETVLMGAyrqqaqrflPIVSKQEKERVlyylerTGLLPLKDKVVN--------------QLSGGQQQRVFLAKLFVQD 156
Cdd:PRK10789 405 VANNIALGR---------PDATQQEIEHV------ARLASVHDDILRlpqgydtevgergvMLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286290 157 PEIILLDEPNNHLDIRYQQELIQQLNEWSaqEGKTLIGVFHdiRL-ALTLSEKIVFMKQGKVAAQGDFQTLA 227
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWG--EGRTVIISAH--RLsALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-219 |
2.14e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 78.23 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRKELAtkvammsQFTTVAFDYT 90
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLdKPTSGTYRVAGQDVATLDADALA-------QLRREHFGFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETVLMgAYRQQAQRF-LPIV-----SKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDE 164
Cdd:PRK10535 92 FQRYHLL-SHLTAAQNVeVPAVyagleRKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 165 PNNHLDIRYQQE---LIQQLNewsaQEGKTLIGVFHDIRLAlTLSEKIVFMKQGKVAA 219
Cdd:PRK10535 171 PTGALDSHSGEEvmaILHQLR----DRGHTVIIVTHDPQVA-AQAERVIEIRDGEIVR 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-199 |
2.82e-16 |
|
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: 77.90 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 27 GSKTCILGPNGCGKTTLLKTIAG-LVP-----------------YSGSVLIDgqevHGQKRKELATKVAMMSQFTTV--- 85
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGeLKPnlgdydeepswdevlkrFRGTELQD----YFKKLANGEIKVAHKPQYVDLipk 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 86 AFDYTVYEtVLMGAyrqqaqrflpivskQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:COG1245 175 VFKGTVRE-LLEKV--------------DERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....*...
gi 488286290 166 NNHLDIrYQQ----ELIQQLnewsAQEGKTLIGVFHDI 199
Cdd:COG1245 240 SSYLDI-YQRlnvaRLIREL----AEEGKYVLVVEHDL 272
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-198 |
4.08e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 77.24 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 9 VTLQ--QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHGQKRKElatkvammsQFttv 85
Cdd:PRK15064 7 ITMQfgAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGdLEPSAGNVSLDPNERLGKLRQD---------QF--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 86 AF-DYTVYETVLMG-----AYRQQAQRF--LPIVSKQEKERVL-----------YYLE-RTGLLPLKDKV--------VN 137
Cdd:PRK15064 75 AFeEFTVLDTVIMGhtelwEVKQERDRIyaLPEMSEEDGMKVAdlevkfaemdgYTAEaRAGELLLGVGIpeeqhyglMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286290 138 QLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAqegkTLIGVFHD 198
Cdd:PRK15064 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNS----TMIIISHD 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-226 |
4.41e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.05 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 10 TLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYSGSVLIDGQEVHGQKRKELatkVAMMSQFTTVAFD- 88
Cdd:PRK15134 295 TVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQL---LPVRHRIQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 -------YTVYETVLMGAYRQQaqrflPIVSKQEKE-RVLYYLERTGLLP-LKDKVVNQLSGGQQQRVFLAKLFVQDPEI 159
Cdd:PRK15134 372 nsslnprLNVLQIIEEGLRVHQ-----PTLSAAQREqQVIAVMEEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTL 226
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-217 |
5.34e-16 |
|
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: 73.62 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQK-RKELATKVAmmsqfttvafdytvyet 94
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLrPPASGEITLDGKPVTRRSpRDAIRAGIA----------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 vlmgayrqqaqrFLPivskqeKERVlyyleRTGL---LPLKDKVV--NQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHL 169
Cdd:cd03215 79 ------------YVP------EDRK-----REGLvldLSVAENIAlsSLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488286290 170 DIRYQQELIQQLNEwSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:cd03215 136 DVGAKAEIYRLIRE-LADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
12-221 |
9.81e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.44 E-value: 9.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQFTTVAFDYt 90
Cdd:PRK15112 24 QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIePTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPSTSLNP- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 vyetvlmgayRQQAQRFLPI-------VSKQEKE-RVLYYLERTGLLPlkDKVV---NQLSGGQQQRVFLAKLFVQDPEI 159
Cdd:PRK15112 103 ----------RQRISQILDFplrlntdLEPEQREkQIIETLRQVGLLP--DHASyypHMLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286290 160 ILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK15112 171 IIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERG 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-215 |
1.21e-15 |
|
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: 73.52 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLL-------KTIAGLVPYSGSVLIDGQEVHGQKRKELAtkVAMMSQFTTVaF 87
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLlailgemQTLEGKVHWSNKNESEPSFEATRSRNRYS--VAYAAQKPWL-L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 88 DYTVYETVLMGA--YRQQAQRFLPIVSKQEKERVLYYLERTgllPLKDKVVNqLSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:cd03290 92 NATVEENITFGSpfNKQRYKAVTDACSLQPDIDLLPFGDQT---EIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488286290 166 NNHLDIRYQQELIQQ-LNEWSAQEGKTLIGVFHDIRLaLTLSEKIVFMKQG 215
Cdd:cd03290 168 FSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQY-LPHADWIIAMKDG 217
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
15-221 |
1.21e-15 |
|
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: 73.30 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDYTVye 93
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVeLSSGSILIDGVDISKIGLHDLRSRISIIPQ-DPVLFSGTI-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 tvlmgayrqqaqRF-LPIVSKQEKERVLYYLERTGL------LPLK-DKVV----NQLSGGQQQRVFLAKLFVQDPEIIL 161
Cdd:cd03244 95 ------------RSnLDPFGEYSDEELWQALERVGLkefvesLPGGlDTVVeeggENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286290 162 LDEPNNHLDIRyQQELIQQ-LNEWSAqeGKTLIGVFHDIRlALTLSEKIVFMKQGKVAAQG 221
Cdd:cd03244 163 LDEATASVDPE-TDALIQKtIREAFK--DCTVLTIAHRLD-TIIDSDRILVLDKGRVVEFD 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-226 |
1.27e-15 |
|
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: 76.01 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDYTVYE 93
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYdVTSGRILIDGQDIRDVTQASLRAAIGIVPQ-DTVLFNDTIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVlmgAY-RQQAqrflpivSKQEKERV------LYYLERtglLP-----------LKdkvvnqLSGGQQQRVFLAKLFVQ 155
Cdd:COG5265 451 NI---AYgRPDA-------SEEEVEAAaraaqiHDFIES---LPdgydtrvgergLK------LSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286290 156 DPEIILLDEPNNHLDIRYQQELIQQLNEwsAQEGKTLIGVFHdiRLAlTL--SEKIVFMKQGKVAAQGDFQTL 226
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALRE--VARGRTTLVIAH--RLS-TIvdADEILVLEAGRIVERGTHAEL 579
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
32-182 |
1.48e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 74.77 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 32 ILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELAT---KVAMMSQfttvafD--------YTVYETVlmga 99
Cdd:COG4608 49 LVGESGCGKSTLGRLLLRLEePTSGEILFDGQDITGLSGRELRPlrrRMQMVFQ------DpyaslnprMTVGDII---- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 100 yrQQAQRFLPIVSKQE-KERVLYYLERTGLLP-LKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLD--IRYQ- 174
Cdd:COG4608 119 --AEPLRIHGLASKAErRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDvsIQAQv 196
|
170
....*....|..
gi 488286290 175 ----QELIQQLN 182
Cdd:COG4608 197 lnllEDLQDELG 208
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-237 |
1.59e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.78 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY--SGSVLIDGQevhgqkrkelatkVAMMSQFTTVaFDYTVY 92
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaeTSSVVIRGS-------------VAYVPQVSWI-FNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVLMGAyRQQAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNqLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIR 172
Cdd:PLN03232 697 ENILFGS-DFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 173 YQQELIQQLNEWSAQeGKTLIGVFHDIRLaLTLSEKIVFMKQGKVAAQGDFQTLA-SKEFLQTIFE 237
Cdd:PLN03232 775 VAHQVFDSCMKDELK-GKTRVLVTNQLHF-LPLMDRIILVSEGMIKEEGTFAELSkSGSLFKKLME 838
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-221 |
1.77e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.54 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-------PYSGSVLIDGQEVHGQKRKELATKVAMMSQFTTVAFD 88
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 YTVYETVlmgAYRQQAQrflPIVSKQEKERVLYY-LERTGLLP-LKDKV---VNQLSGGQQQRVFLAKLFVQDPEIILLD 163
Cdd:PRK14246 105 LSIYDNI---AYPLKSH---GIKEKREIKKIVEEcLRKVGLWKeVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 164 EPNNHLDIRYQQELIQQLNEWSAQegKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWG 234
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-171 |
1.81e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 75.36 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIdGQEVH----GQKRKELATkvammsqfttvafDYT 90
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEqPDSGTIEI-GETVKlayvDQSRDALDP-------------NKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETV-------LMGAY----RQQAQRFLPIVSKQEKErvlyylertgllplkdkvVNQLSGGQQQRVFLAKLFVQDPEI 159
Cdd:TIGR03719 403 VWEEIsggldiiKLGKReipsRAYVGRFNFKGSDQQKK------------------VGQLSGGERNRVHLAKTLKSGGNV 464
|
170
....*....|..
gi 488286290 160 ILLDEPNNHLDI 171
Cdd:TIGR03719 465 LLLDEPTNDLDV 476
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-219 |
2.55e-15 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 74.83 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 20 ISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQEVHGQKRkelatkVAMMSQFTTVAFDYTVYEtvlmg 98
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLyRPESGEILLDGQPVTADNR------EAYRQLFSAVFSDFHLFD----- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 99 ayrqqaqRFLPIVSKQEKERVLYYLERtglLPLKDKV-VN-------QLSGGQQQRVFLAKLFVQDPEIILLDE------ 164
Cdd:COG4615 420 -------RLLGLDGEADPARARELLER---LELDHKVsVEdgrfsttDLSQGQRKRLALLVALLEDRPILVFDEwaadqd 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 165 PNNHlDIRYqQELIQQLnewsAQEGKTLIGVFHDIR---LAltlsEKIVFMKQGKVAA 219
Cdd:COG4615 490 PEFR-RVFY-TELLPEL----KARGKTVIAISHDDRyfdLA----DRVLKMDYGKLVE 537
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
14-171 |
2.56e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 72.57 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGqevHGQKRKELATKVAMMSQFTTVAFDYTVY 92
Cdd:PRK13543 24 EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLhVESGQIQIDG---KTATRGDRSRFMAYLGHLPGLKADLSTL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETV--LMGAYRQQAQRF----LPIVskqekervlyylertGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPN 166
Cdd:PRK13543 101 ENLhfLCGLHGRRAKQMpgsaLAIV---------------GLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
....*
gi 488286290 167 NHLDI 171
Cdd:PRK13543 166 ANLDL 170
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
15-199 |
2.77e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.84 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDislvfptGSKTCILGPNGCGKTTLLKTIAG-LVP-----------------YSGSVLIDgqevHGQKRKELATKV 76
Cdd:PRK13409 94 PIPKE-------GKVTGILGPNGIGKTTAVKILSGeLIPnlgdyeeepswdevlkrFRGTELQN----YFKKLYNGEIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 77 AMMSQFTTV---AFDYTVYEtVLMGAyrqqaqrflpivskQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLF 153
Cdd:PRK13409 163 VHKPQYVDLipkVFKGKVRE-LLKKV--------------DERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488286290 154 VQDPEIILLDEPNNHLDIRyQQ----ELIQQLnewsaQEGKTLIGVFHDI 199
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDIR-QRlnvaRLIREL-----AEGKYVLVVEHDL 271
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-236 |
2.86e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.60 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEV-HGQKRKELATKVAM 78
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPrATSGRIVFDGKDItDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 79 MSQFTTVAFDYTVYETVLMGAYRQQAQRFlpivsKQEKERVLYYLERtgLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPE 158
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQF-----QERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 159 IILLDEPNNHL-DIRYQQ--ELIQQLNEwsaqEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEFLQTI 235
Cdd:PRK11614 158 LLLLDEPSLGLaPIIIQQifDTIEQLRE----QGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSA 233
|
.
gi 488286290 236 F 236
Cdd:PRK11614 234 Y 234
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
32-221 |
2.86e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.01 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 32 ILGPNGCGKTTLLKTIAGLVPYSGSVLIDGQEVHG---------QKRKELATKVAMMSQ--FTTVAFDYTV-YEtvLMGA 99
Cdd:PRK11022 38 IVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGqdlqrisekERRNLVGAEVAMIFQdpMTSLNPCYTVgFQ--IMEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 100 YR--QQAQRflpivsKQEKERVLYYLERTGLL-PLK--DKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQ 174
Cdd:PRK11022 116 IKvhQGGNK------KTRRQRAIDLLNQVGIPdPASrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488286290 175 QELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK11022 190 AQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
19-221 |
3.14e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.04 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 19 DISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQ-----EVHG----QKRKELATKVAMMSQF------ 82
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSArLAPDAGEVHYRMRdgqlrDLYAlseaERRRLLRTEWGFVHQHprdglr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 83 TTVAFDYTVYETvLM-------GAYRQQAQRFLpivskqekERVLYYLERTGLLPlkdkvvNQLSGGQQQRVFLAKLFVQ 155
Cdd:PRK11701 104 MQVSAGGNIGER-LMavgarhyGDIRATAGDWL--------ERVEIDAARIDDLP------TTFSGGMQQRLQIARNLVT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 156 DPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK11701 169 HPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-198 |
1.45e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.68 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVlidgqevhgqkrkELATK--VAMMSQFTtVAFD--YT 90
Cdd:PRK11147 334 LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGqLQADSGRI-------------HCGTKleVAYFDQHR-AELDpeKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETVLMGayrqqaqrflpivsKQE-----KER-VLYYLERTGLLPLKDKV-VNQLSGGQQQRVFLAKLFVQDPEIILLD 163
Cdd:PRK11147 400 VMDNLAEG--------------KQEvmvngRPRhVLGYLQDFLFHPKRAMTpVKALSGGERNRLLLARLFLKPSNLLILD 465
|
170 180 190
....*....|....*....|....*....|....*
gi 488286290 164 EPNNHLDIryqqELIQQLNEWSAQEGKTLIGVFHD 198
Cdd:PRK11147 466 EPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-232 |
2.36e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.96 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 32 ILGPNG---CGKTTLLKTIAGLVPY-SGSVLIDGQEVHGQKRKE-LATKVAMMSQFTT---VAFDYTVYETVLMGAYRQQ 103
Cdd:PRK10762 280 ILGVSGlmgAGRTELMKVLYGALPRtSGYVTLDGHEVVTRSPQDgLANGIVYISEDRKrdgLVLGMSVKENMSLTALRYF 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 104 AQRFLPIVSKQEKERVLYYLE----RTgllPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQ 179
Cdd:PRK10762 360 SRAGGSLKHADEQQAVSDFIRlfniKT---PSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488286290 180 QLNEWSaQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAaqGDFQ-TLASKEFL 232
Cdd:PRK10762 437 LINQFK-AEGLSIILVSSEMPEVLGMSDRILVMHEGRIS--GEFTrEQATQEKL 487
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-209 |
2.75e-14 |
|
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: 70.47 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 27 GSKTCILGPNGCGKTTLLKTIAG-LVPYSGSV--------LID---GQEVHG--QKRKELATKVAMMSQFTTV---AFDY 89
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGkLKPNLGKFddppdwdeILDefrGSELQNyfTKLLEGDVKVIVKPQYVDLipkAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 TVYETvlmgayrqqaqrflpIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHL 169
Cdd:cd03236 106 KVGEL---------------LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488286290 170 DIRYQ---QELIQQLNEwsaqEGKTLIGVFHDIRLALTLSEKI 209
Cdd:cd03236 171 DIKQRlnaARLIRELAE----DDNYVLVVEHDLAVLDYLSDYI 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-226 |
5.91e-14 |
|
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: 70.87 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKT-TLLkTIAGLVPY-----SGSVLIDGQEVHGQKRKELAT----KVAM--- 78
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvTAL-SILRLLPDpaahpSGSILFDGQDLLGLSERELRRirgnRIAMifq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 79 --MSQFTTVafdYTV----YETVL--MGAYRQQAQrflpivskqekERVLYYLERTGLlPLKDKVVN----QLSGGQQQR 146
Cdd:COG4172 100 epMTSLNPL---HTIgkqiAEVLRlhRGLSGAAAR-----------ARALELLERVGI-PDPERRLDayphQLSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 147 VFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTL 226
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-229 |
6.44e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 70.76 E-value: 6.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLktiaGLV-----PYSGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDY 89
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLLqrvfdPQSGRILIDGTDIRTVTRASLRRNIAVVFQ-DAGLFNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 TVYETVLMG------------AYRQQAQRFlpiVSKQEKervlyylertGLlplkDKVV----NQLSGGQQQRVFLAKLF 153
Cdd:PRK13657 424 SIEDNIRVGrpdatdeemraaAERAQAHDF---IERKPD----------GY----DTVVgergRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 154 VQDPEIILLDEPNNHLDIRYQQELIQQLNEWSaqEGKTLIGVFHdiRLAlTLSE--KIVFMKQGKVAAQGDFQTLASK 229
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAH--RLS-TVRNadRILVFDNGRVVESGSFDELVAR 559
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
7-197 |
1.08e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.29 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 7 TAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP---YSGSVLIDGqevhGQKRKELATKVAMMSQFT 83
Cdd:PLN03211 74 ETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnnFTGTILANN----RKPTKQILKRTGFVTQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 84 TVAFDYTVYETVLMGAYrqqaQRFLPIVSKQEKERVL-YYLERTGLLPLKDKVVNQ-----LSGGQQQRVFLAKLFVQDP 157
Cdd:PLN03211 150 ILYPHLTVRETLVFCSL----LRLPKSLTKQEKILVAeSVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINP 225
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488286290 158 EIILLDEPNNHLDIRYQQELIQQLNEWsAQEGKTLIGVFH 197
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMH 264
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
18-171 |
1.43e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.76 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 18 KDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIdGQEVH----GQKRKELATkvammsqfttvafDYTVY 92
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQeQPDSGTIKI-GETVKlayvDQSRDALDP-------------NKTVW 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVLMGayrqqaQRFLPIVSKQEKERVlyYLER---TGllPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHL 169
Cdd:PRK11819 407 EEISGG------LDIIKVGNREIPSRA--YVGRfnfKG--GDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDL 476
|
..
gi 488286290 170 DI 171
Cdd:PRK11819 477 DV 478
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-165 |
1.90e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.77 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 33 LGPNGCGKTTLLKTIAGLVPYS-GSVLIDGQEVHGqkrKELAT--KVAMMSQfttvAFdyTVYE--TVlmgayRQ----Q 103
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASeGEAWLFGQPVDA---GDIATrrRVGYMSQ----AF--SLYGelTV-----RQnlelH 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286290 104 AQRF-LPivSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:NF033858 364 ARLFhLP--AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-237 |
2.16e-13 |
|
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: 69.06 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL---VPYSGSVL-----------IDGQEVHGQ 67
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyEPTSGRIIyhvalcekcgyVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 68 K----------------------RKELATKVAMMSQFTTVAF-DYTVYETVLmgayrqqaqRFLPIVSKQEKE---RVLY 121
Cdd:TIGR03269 81 PcpvcggtlepeevdfwnlsdklRRRIRKRIAIMLQRTFALYgDDTVLDNVL---------EALEEIGYEGKEavgRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 122 YLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRL 201
Cdd:TIGR03269 152 LIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEV 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 488286290 202 ALTLSEKIVFMKQGKVAAQGDFQTLASKeFLQTIFE 237
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEEGTPDEVVAV-FMEGVSE 266
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
32-230 |
2.43e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.23 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 32 ILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRkelatkVAMMSQFTTVAFDYTVYETvLMGAYRQQAqrflpi 110
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYqPQSGEILLDGKPVTAEQP------EDYRKLFSAVFTDFHLFDQ-LLGPEGKPA------ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 111 vskqEKERVLYYLERTGL---LPLKD-KVVN-QLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWS 185
Cdd:PRK10522 421 ----NPALVEKWLERLKMahkLELEDgRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLL 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488286290 186 AQEGKTLIGVFHDiRLALTLSEKIVFMKQGKVAA-QGDFQTLASKE 230
Cdd:PRK10522 497 QEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSElTGEERDAASRD 541
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
7-228 |
2.58e-13 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 67.96 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 7 TAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGqevhgqkrkelatKVAMMSQFTTV 85
Cdd:cd03291 43 SNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEPSEGKIKHSG-------------RISFSSQFSWI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 86 aFDYTVYETVLMGAYRQQaQRFLPIVSKQEKErvlyylERTGLLPLKDKVVN-----QLSGGQQQRVFLAKLFVQDPEII 160
Cdd:cd03291 110 -MPGTIKENIIFGVSYDE-YRYKSVVKACQLE------EDITKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286290 161 LLDEPNNHLDIRYQQELIQQ-LNEWSAQegKTLIGVFHDIRlALTLSEKIVFMKQGKVAAQGDFQTLAS 228
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIFEScVCKLMAN--KTRILVTSKME-HLKKADKILILHEGSSYFYGTFSELQS 247
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
15-230 |
2.84e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.98 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYS-GSVLIDGQEVHGQKRKELATKVAMMSQFTTVAFDyTVYE 93
Cdd:PRK10790 355 LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTeGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLAD-TFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVLMGAYRQQAQRFlpivskQEKERV-LYYLERT---GLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHL 169
Cdd:PRK10790 434 NVTLGRDISEEQVW------QALETVqLAELARSlpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANI 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286290 170 DIRYQQELIQQLNEwsAQEGKTLIGVFHdiRLA-LTLSEKIVFMKQGKVAAQGDFQTLASKE 230
Cdd:PRK10790 508 DSGTEQAIQQALAA--VREHTTLVVIAH--RLStIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-227 |
2.85e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.36 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY---SGSVLIDGQEVhgqkRKELATKVA 77
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYkilEGDILFKGESI----LDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 78 MMSQFttVAFDYTVY------ETVLMGAY--RQQAQ--------RFLPIVSKQekervlyyLERTGLLP--LKDKVVNQL 139
Cdd:CHL00131 83 HLGIF--LAFQYPIEipgvsnADFLRLAYnsKRKFQglpeldplEFLEIINEK--------LKLVGMDPsfLSRNVNEGF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 140 SGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEgKTLIGVFHDIRLALTLS-EKIVFMKQGKVA 218
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSE-NSIILITHYQRLLDYIKpDYVHVMQNGKII 231
|
....*....
gi 488286290 219 AQGDfQTLA 227
Cdd:CHL00131 232 KTGD-AELA 239
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-234 |
3.47e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.82 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQevhgqkrkelatkVAMMSQFTTVAFDyTVYE 93
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAeMDKVEGHVHMKGS-------------VAYVPQQAWIQND-SLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVLMGA------YRQ--QAQRFLPIVskqekeRVLYYLERTgllPLKDKVVNqLSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:TIGR00957 718 NILFGKalnekyYQQvlEACALLPDL------EILPSGDRT---EIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 166 NNHLDIRYQQELIQQ-LNEWSAQEGKTLIGVFHDIRLaLTLSEKIVFMKQGKVAAQGDFQTLASK-----EFLQT 234
Cdd:TIGR00957 788 LSAVDAHVGKHIFEHvIGPEGVLKNKTRILVTHGISY-LPQVDVIIVMSGGKISEMGSYQELLQRdgafaEFLRT 861
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-230 |
3.61e-13 |
|
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: 68.78 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 7 TAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGqevhgqkrkelatKVAMMSQFTTV 85
Cdd:TIGR01271 432 SNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEGKIKHSG-------------RISFSPQTSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 86 aFDYTVYETVLMGAYRQQAqRFLPIVSKQEKErvlyylERTGLLPLKDKVV-----NQLSGGQQQRVFLAKLFVQDPEII 160
Cdd:TIGR01271 499 -MPGTIKDNIIFGLSYDEY-RYTSVIKACQLE------EDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLY 570
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 161 LLDEPNNHLDIRYQQELIQQLnEWSAQEGKTLIGVFHDIRlALTLSEKIVFMKQGKVAAQGDFQTLASKE 230
Cdd:TIGR01271 571 LLDSPFTHLDVVTEKEIFESC-LCKLMSNKTRILVTSKLE-HLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
15-218 |
4.22e-13 |
|
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: 66.28 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELATKVAMMSQfttvafDytvyE 93
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKIEIDGIDISTIPLEDLRSSLTIIPQ------D----P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVLMGAYRQQAQRFlpivSKQEKERVLyylertGLLPLKDKVVNqLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDirY 173
Cdd:cd03369 92 TLFSGTIRSNLDPF----DEYSDEEIY------GALRVSEGGLN-LSQGQRQLLCLARALLKRPRVLVLDEATASID--Y 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488286290 174 QQE-LIQQL--NEWSaqeGKTLIGVFHDIRLALTLsEKIVFMKQGKVA 218
Cdd:cd03369 159 ATDaLIQKTirEEFT---NSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-228 |
5.51e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.19 E-value: 5.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY------SGSVLIDGQEVHGQKRKEL----ATKVAMMSQ 81
Cdd:PRK15134 20 TVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvypSGDIRFHGESLLHASEQTLrgvrGNKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 82 FTTVAFD--YTV----YETV-LMGAYRQQAQRflpivskqekERVLYYLERTGLLPLKDKVVN---QLSGGQQQRVFLAK 151
Cdd:PRK15134 100 EPMVSLNplHTLekqlYEVLsLHRGMRREAAR----------GEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 152 LFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLAS 228
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFS 246
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-213 |
1.39e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.83 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYSGSVLIDGQ-EVHGQKRKE-------LA 73
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRvEFFNQNIYErrvnlnrLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 74 TKVAMM----SQFTTVAFDYTVYETVLMGaYRQQAQrFLPIVSKQEKERVLYYLERTGLlplkDKVVNQLSGGQQQRVFL 149
Cdd:PRK14258 88 RQVSMVhpkpNLFPMSVYDNVAYGVKIVG-WRPKLE-IDDIVESALKDADLWDEIKHKI----HKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286290 150 AKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMK 213
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFK 225
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
12-201 |
1.44e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.59 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVhgqkRKELAT---KVAMMSQFTTVAF 87
Cdd:PRK13540 12 HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLnPEKGEILFERQSI----KKDLCTyqkQLCFVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 88 DYTVYETVLMGAYRQQAQRFLPIVSKqekervLYYLERtgllpLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNN 167
Cdd:PRK13540 88 YLTLRENCLYDIHFSPGAVGITELCR------LFSLEH-----LIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190
....*....|....*....|....*....|....
gi 488286290 168 HLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRL 201
Cdd:PRK13540 157 ALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPL 190
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-226 |
1.83e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.11 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQtPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP-----YSGSVLIDGQEVHGQKRKelATKV 76
Cdd:PRK10418 5 IELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrqTAGRVLLDGKPVAPCALR--GRKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 77 AMMSQFTTVAFD------YTVYETVL-MG--AYRQQAQRFLPIVSKQEKERVLyylertGLLPLkdkvvnQLSGGQQQRV 147
Cdd:PRK10418 82 ATIMQNPRSAFNplhtmhTHARETCLaLGkpADDATLTAALEAVGLENAARVL------KLYPF------EMSGGMLQRM 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286290 148 FLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTL 226
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-222 |
2.01e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.05 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 19 DISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQE-VHGQKRKELAT---KVAMMSQFTTVAFDYTVYE 93
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTrPQKGRIVLNGRVlFDAEKGICLPPekrRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVLMGAYRQQAQRFLPIVSkqekerVLyylertGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRY 173
Cdd:PRK11144 96 NLRYGMAKSMVAQFDKIVA------LL------GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488286290 174 QQELIQQLnEWSAQEGKT-LIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:PRK11144 164 KRELLPYL-ERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-223 |
2.28e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.00 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 19 DISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP--YSGSVLIDGQEVHGQK-RKELATKVAMMSQFTT---VAFDYTVY 92
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgkFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRKrhgIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVLMGAYRQQAQRfLPIVSKQEKERVLYYLERtglLPLK----DKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNH 168
Cdd:TIGR02633 358 KNITLSVLKSFCFK-MRIDAAAELQIIGSAIQR---LKVKtaspFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488286290 169 LDIRYQQELIQQLNEWsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVaaQGDF 223
Cdd:TIGR02633 434 VDVGAKYEIYKLINQL-AQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL--KGDF 485
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-217 |
6.90e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.81 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVlidgqevhgqkrkELAtKVAMMSQFTTVAFDY-TVYE 93
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAPVSGEI-------------GLA-KGIKLGYFAQHQLEFlRADE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVLmgayrQQAQRFLPivskQEKERVLY-YLERTGLLplKDKVVN---QLSGGQQQRVFLAKLFVQDPEIILLDEPNNHL 169
Cdd:PRK10636 393 SPL-----QHLARLAP----QELEQKLRdYLGGFGFQ--GDKVTEetrRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488286290 170 DIRYQQELIQQLNEWsaqEGkTLIGVFHDIRLALTLSEKIVFMKQGKV 217
Cdd:PRK10636 462 DLDMRQALTEALIDF---EG-ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-234 |
8.55e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 8.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIA-----------GLVPYSGsvlIDGQEVHGQKRKElatkVAMMSQfTT 84
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdgfhigveGVITYDG---ITPEEIKKHYRGD----VVYNAE-TD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 85 VAFDY-TVYETVLMGAYRQQAQRFLPIVSKQE--KERVLYYLERTGLLPLKD-KVVNQL----SGGQQQRVFLAKLFVQD 156
Cdd:TIGR00956 148 VHFPHlTVGETLDFAARCKTPQNRPDGVSREEyaKHIADVYMATYGLSHTRNtKVGNDFvrgvSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 157 PEIILLDEPNNHLDIRYQQELIQQLNEwSAQEGKT--LIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTlaSKEFLQT 234
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALKT-SANILDTtpLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADK--AKQYFEK 304
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-222 |
1.17e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 63.45 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLlktiAGLV-----PYSGSVLIDGQEVHG---QKRKELATKVAMMSQ--FTTVA 86
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTL----ARLLtmietPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQnpYGSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 87 FDYTVyetvlmgayRQQAQRFLPI---VSKQE-KERVLYYLERTGLLP-LKDKVVNQLSGGQQQRVFLAKLFVQDPEIIL 161
Cdd:PRK11308 107 PRKKV---------GQILEEPLLIntsLSAAErREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286290 162 LDEPNNHLDIRYQQeliQQLNEW-SAQEGKTLIGVF--HDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:PRK11308 178 ADEPVSALDVSVQA---QVLNLMmDLQQELGLSYVFisHDLSVVEHIADEVMVMYLGRCVEKGT 238
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-229 |
1.26e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.89 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY---SGSVLIDGQEVHGQKRKELATKVA 77
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevtGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 78 MMsqfttvAFDYTV----------YETVL--MGAYRQQA--QRFLPIVSKQEKERVLYYLERtgllpLKDKVVNQ-LSGG 142
Cdd:PRK09580 81 FM------AFQYPVeipgvsnqffLQTALnaVRSYRGQEplDRFDFQDLMEEKIALLKMPED-----LLTRSVNVgFSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 143 QQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNewSAQEGK-TLIGVFHDIRLALTLSEKIV-FMKQGKVAAQ 220
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVN--SLRDGKrSFIIVTHYQRILDYIKPDYVhVLYQGRIVKS 227
|
....*....
gi 488286290 221 GDFqTLASK 229
Cdd:PRK09580 228 GDF-TLVKQ 235
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-228 |
1.33e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.37 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 13 QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP--YSGSVLIDGqevhgqkrkelatKVAMMSQFTTVaFDYT 90
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPprSDASVVIRG-------------TVAYVPQVSWI-FNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETVLMGAyRQQAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNqLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLD 170
Cdd:PLN03130 695 VRDNILFGS-PFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 171 IRYQQELIQQLNEWSAQeGKTLIGVFHDIRLaLTLSEKIVFMKQGKVAAQGDFQTLAS 228
Cdd:PLN03130 773 AHVGRQVFDKCIKDELR-GKTRVLVTNQLHF-LSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
3-215 |
1.74e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 63.71 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 3 ELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP---YSGSVLIDGqevHGQKRKELATKVAMM 79
Cdd:PLN03140 882 EMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggyIEGDIRISG---FPKKQETFARISGYC 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQFTTVAFDYTVYETVLMGAYRQqaqrfLPI-VSKQEKER-VLYYLERTGLLPLKDKVV-----NQLSGGQQQRVFLAKL 152
Cdd:PLN03140 959 EQNDIHSPQVTVRESLIYSAFLR-----LPKeVSKEEKMMfVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVE 1033
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 153 FVQDPEIILLDEPNNHLDIRYQQELIQQLNEwSAQEGKTLIGVFH----DIRLALtlsEKIVFMKQG 215
Cdd:PLN03140 1034 LVANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHqpsiDIFEAF---DELLLMKRG 1096
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-230 |
1.91e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.50 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQ--QTPILKDISLVFPTGSKTCILGPNGCGKTtllkTIAGLVP-----YSGSVLIDGQEVHGQKRKELAT 74
Cdd:PRK11176 342 IEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKS----TIANLLTrfydiDEGEILLDGHDLRDYTLASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 75 KVAMMSQFTTVaFDYTVYETVlmgAYRQQAQrflpiVSKQEKE---RVLYYLE-----RTGLlplkDKVVNQ----LSGG 142
Cdd:PRK11176 418 QVALVSQNVHL-FNDTIANNI---AYARTEQ-----YSREQIEeaaRMAYAMDfinkmDNGL----DTVIGEngvlLSGG 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 143 QQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEwsAQEGKTLIGVFHdiRLAlTL--SEKIVFMKQGKVAAQ 220
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDE--LQKNRTSLVIAH--RLS-TIekADEILVVEDGEIVER 559
|
250
....*....|
gi 488286290 221 GDFQTLASKE 230
Cdd:PRK11176 560 GTHAELLAQN 569
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
32-222 |
5.58e-11 |
|
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: 62.13 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 32 ILGPNGCGKTTLLKTIAGLV-PYSGSV-------LIDGQEVHGQKRKELATKVAMMSQfttvafDYTVY--ETVLmGAYR 101
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAGVLePTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQ------EYDLYphRTVL-DNLT 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 102 QQAQRFLPivSKQEKERVLYYLERTGLLPLK-----DKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQE 176
Cdd:TIGR03269 388 EAIGLELP--DELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVD 465
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488286290 177 LIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:TIGR03269 466 VTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-223 |
5.89e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 5.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP--YSGSVLIDGQEVHGQK-RKELATKVAMMS----QFTTVAfD 88
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgrWEGEIFIDGKPVKIRNpQQAIAQGIAMVPedrkRDGIVP-V 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 YTVYETVLMGAYRQQAQRFLpIVSKQEKERVLYYLERtgllpLKDKV------VNQLSGGQQQRVFLAKLFVQDPEIILL 162
Cdd:PRK13549 356 MGVGKNITLAALDRFTGGSR-IDDAAELKTILESIQR-----LKVKTaspelaIARLSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286290 163 DEPNNHLDIRYQQE---LIQQLnewsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVaaQGDF 223
Cdd:PRK13549 430 DEPTRGIDVGAKYEiykLINQL----VQQGVAIIVISSELPEVLGLSDRVLVMHEGKL--KGDL 487
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-220 |
8.53e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.47 E-value: 8.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 37 GCGKTTLLKTIAGLV-PYSGSVLIDGQEV----------HG-----QKRKELATkVAMMSqfttvafdytVYETVLMGAY 100
Cdd:PRK11288 289 GAGRSELMKLLYGATrRTAGQVYLDGKPIdirsprdairAGimlcpEDRKAEGI-IPVHS----------VADNINISAR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 101 RQQAQRFLPIVSKQEKERVLYYLERTGL-LPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQ 179
Cdd:PRK11288 358 RHHLRAGCLINNRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYN 437
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488286290 180 QLNEWsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQ 220
Cdd:PRK11288 438 VIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-254 |
1.12e-10 |
|
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: 60.99 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP---YSGSVLIDGQEVHGQKRKELATK-V 76
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtWDGEIYWSGSPLKASNIRDTERAgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 77 AMMSQFTTVAFDYTVYETVLMGayrqqAQRFLPIVSKQEKERVLYYLERTGLLPLKD----KVVNQLSGGQQQRVFLAKL 152
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLG-----NEITLPGGRMAYNAMYLRAKNLLRELQLDAdnvtRPVGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 153 FVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQeGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEFL 232
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDII 234
|
250 260
....*....|....*....|...
gi 488286290 233 QTIFETDIVS-YFQKQHKVWETI 254
Cdd:TIGR02633 235 TMMVGREITSlYPHEPHEIGDVI 257
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
54-228 |
1.55e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.20 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 54 SGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDYTVYETVLMG---AYRQQAQRFLPIVSKQEKERVLYYLERTGLLP 130
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDLRNLFSIVSQ-EPMLFNMSIYENIKFGkedATREDVKRACKFAAIDEFIESLPNKYDTNVGP 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 131 LKdkvvNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRlALTLSEKIV 210
Cdd:PTZ00265 1355 YG----KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIKRSDKIV 1429
|
170 180
....*....|....*....|...
gi 488286290 211 FM----KQGK-VAAQGDFQTLAS 228
Cdd:PTZ00265 1430 VFnnpdRTGSfVQAHGTHEELLS 1452
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-233 |
2.89e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 9 VTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY-SGSVLIDGQEVHGQKRKElatkvAMMSQFTTVAf 87
Cdd:PRK10982 256 LTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKsAGTITLHGKKINNHNANE-----AINHGFALVT- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 88 dytvYETVLMGAYRQQAQRFLPIVSKQEKervlyYLERTGLL--------------------PLKDKVVNQLSGGQQQRV 147
Cdd:PRK10982 330 ----EERRSTGIYAYLDIGFNSLISNIRN-----YKNKVGLLdnsrmksdtqwvidsmrvktPGHRTQIGSLSGGNQQKV 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 148 FLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWsAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLA 227
Cdd:PRK10982 401 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTT 479
|
....*.
gi 488286290 228 SKEFLQ 233
Cdd:PRK10982 480 QNEILR 485
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-165 |
5.31e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.37 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 7 TAVTLQ--QTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDG----QEVHgqkRKELATKVAMM 79
Cdd:NF033858 5 EGVSHRygKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGArKIQQGRVEVLGgdmaDARH---RRAVCPRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQ------FTTVafdyTVYETV-----LMG---AYRQQaqrflpivskqekeRVLYYLERTGLLPLKDKVVNQLSGGQQQ 145
Cdd:NF033858 82 PQglgknlYPTL----SVFENLdffgrLFGqdaAERRR--------------RIDELLRATGLAPFADRPAGKLSGGMKQ 143
|
170 180
....*....|....*....|
gi 488286290 146 RVFLAKLFVQDPEIILLDEP 165
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEP 163
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-221 |
5.37e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.10 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVH---GQKRKELATKVAMMSQFTTVAFD---- 88
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVeSQGGEIIFNGQRIDtlsPGKLQALRRDIQFIFQDPYASLDprqt 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 --YTVYETVLMgayrqqaQRFLPivSKQEKERVLYYLERTGLLPLKD-KVVNQLSGGQQQRVFLAKLFVQDPEIILLDEP 165
Cdd:PRK10261 420 vgDSIMEPLRV-------HGLLP--GKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 166 NNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQG 221
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
12-203 |
5.69e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.66 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPysgsvlidgqevhgqKRKELATKVAMMSQFTTvafDYTV 91
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK---------------GTPVAGCVDVPDNQFGR---EASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 92 YETVLmgayrqqaqrflpivSKQEKERVLYYLERTGL--LPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHL 169
Cdd:COG2401 103 IDAIG---------------RKGDFKDAVELLNAVGLsdAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 488286290 170 DIRYQQELIQQLNEWSAQEGKTLIGVFH--DIRLAL 203
Cdd:COG2401 168 DRQTAKRVARNLQKLARRAGITLVVATHhyDVIDDL 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-200 |
7.53e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.79 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP---YSGSVLIDGQEVHGQKRKELATK-VAMMSQFTTVAFDYTVY 92
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtYEGEIIFEGEELQASNIRDTERAgIAIIHQELALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVLMGAYRQQAQR--FLPIVSKQEKervlyYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLd 170
Cdd:PRK13549 101 ENIFLGNEITPGGImdYDAMYLRAQK-----LLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL- 174
|
170 180 190
....*....|....*....|....*....|
gi 488286290 171 iryqqeliqqlnewSAQEGKTLIGVFHDIR 200
Cdd:PRK13549 175 --------------TESETAVLLDIIRDLK 190
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
128-219 |
8.36e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.64 E-value: 8.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 128 LLPLKDKVVNQ----LSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQElIQQLNEWSAQEGKTLIGVFHDIRLAL 203
Cdd:PRK09700 395 LLALKCHSVNQniteLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAE-IYKVMRQLADDGKVILMVSSELPEII 473
|
90
....*....|....*.
gi 488286290 204 TLSEKIVFMKQGKVAA 219
Cdd:PRK09700 474 TVCDRIAVFCEGRLTQ 489
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-242 |
8.36e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.02 E-value: 8.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYS-GSVLIdgqevhgqkrkelATKVAMMSQFTTVaFDYTVYET 94
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISeGRVWA-------------ERSIAYVPQQAWI-MNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 VLMGAyRQQAQRFLPIVSKQEKERVLYYLErTGL-LPLKDKVVNqLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRY 173
Cdd:PTZ00243 741 ILFFD-EEDAARLADAVRVSQLEADLAQLG-GGLeTEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488286290 174 QQELIQQLNeWSAQEGKTLIGVFHDIRLaLTLSEKIVFMKQGKVAAQGDfqtlaSKEFLQTIFETDIVS 242
Cdd:PTZ00243 818 GERVVEECF-LGALAGKTRVLATHQVHV-VPRADYVVALGDGRVEFSGS-----SADFMRTSLYATLAA 879
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-224 |
1.09e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.33 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 12 QQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYSGS---------------VLIDGQEVHGQKRKELATKV 76
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlvqcdkmllrrrsrqVIELSEQSAAQMRHVRGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 77 AMMSQ--FTTVAFDYTVYETVL------MGAYRQ----QAQRFLPIVSKQEKERVLyylertgllplkDKVVNQLSGGQQ 144
Cdd:PRK10261 107 AMIFQepMTSLNPVFTVGEQIAesirlhQGASREeamvEAKRMLDQVRIPEAQTIL------------SRYPHQLSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 145 QRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQ 224
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVE 254
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-197 |
1.52e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP--YSGSVLIDG-QEVHGQKRKELATKVAM 78
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPqgYSNDLTLFGrRRGSGETIWDIKKHIGY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 79 MSqfTTVAFDYTVYETVL----------MGAYRQqaqrflpiVSKQEKERVLYYLERTGL-LPLKDKVVNQLSGGQQQRV 147
Cdd:PRK10938 341 VS--SSLHLDYRVSTSVRnvilsgffdsIGIYQA--------VSDRQQKLAQQWLDILGIdKRTADAPFHSLSWGQQRLA 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488286290 148 FLAKLFVQDPEIILLDEPNNHLDIRYQQeLIQQLNEWSAQEGKT-LIGVFH 197
Cdd:PRK10938 411 LIVRALVKHPTLLILDEPLQGLDPLNRQ-LVRRFVDVLISEGETqLLFVSH 460
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-216 |
1.56e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.82 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKE-LATKVAMMSQFTTVAFDYTVYET 94
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYqKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 VLMGAYRQQAqrFLPIVSKQEKERVLYYLERTGLLPLKDKVVNqLSGGQQQRVFLAKLFVQDPEIILLDEPNNHL---DI 171
Cdd:PRK10982 94 MWLGRYPTKG--MFVDQDKMYRDTKAIFDELDIDIDPRAKVAT-LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtekEV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488286290 172 RYQQELIQQLNEwsaqEGKTLIGVFHDIRLALTLSEKIVFMKQGK 216
Cdd:PRK10982 171 NHLFTIIRKLKE----RGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-197 |
1.75e-09 |
|
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: 57.84 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYSGSVLidgqevhgqkrkelaTKVAMMSQFTTVAFDYtvyetV 95
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL---------------TKPAKGKLFYVPQRPY-----M 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 96 LMGAYRQQA-------QRFLPIVSKQEKERVL------YYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILL 162
Cdd:TIGR00954 527 TLGTLRDQIiypdsseDMKRRGLSDKDLEQILdnvqltHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*
gi 488286290 163 DEPNNHLDIRYQQELIQQLNEWsaqeGKTLIGVFH 197
Cdd:TIGR00954 607 DECTSAVSVDVEGYMYRLCREF----GITLFSVSH 637
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-235 |
2.03e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYSGSVLidgqEVHGQKRKELATKVA------MMSQFTTVAFD 88
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL----EIGGNPCARLTPAKAhqlgiyLVPQEPLLFPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 YTVYETVLMGAYRQQAqrflpivskqEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNH 168
Cdd:PRK15439 101 LSVKENILFGLPKRQA----------SMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 169 LDIRYQQELIQQLNEWSAQeGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASKEFLQTI 235
Cdd:PRK15439 171 LTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAI 236
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
32-222 |
4.74e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.89 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 32 ILGPNGCGKTTLLKTIAGLVP----YSGSVLIDGQEVHGQKRKEL----ATKVAMMSQ--FTTVAFDYTVYET---VLM- 97
Cdd:PRK09473 47 IVGESGSGKSQTAFALMGLLAangrIGGSATFNGREILNLPEKELnklrAEQISMIFQdpMTSLNPYMRVGEQlmeVLMl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 98 --GAYRQQA----QRFLPIVSKQEKERvlyyleRTGLLPlkdkvvNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDI 171
Cdd:PRK09473 127 hkGMSKAEAfeesVRMLDAVKMPEARK------RMKMYP------HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488286290 172 RYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGD 222
Cdd:PRK09473 195 TVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-170 |
5.15e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.58 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 10 TLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY----SGSVLIDGQEVHGQKRKELATkVAMMSQ---- 81
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsvEGDIHYNGIPYKEFAEKYPGE-IIYVSEedvh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 82 FTTVafdyTVYETVlmgayrqqaqrflpivskqekervlyyleRTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIIL 161
Cdd:cd03233 95 FPTL----TVRETL-----------------------------DFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLC 141
|
....*....
gi 488286290 162 LDEPNNHLD 170
Cdd:cd03233 142 WDNSTRGLD 150
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-211 |
8.00e-09 |
|
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: 8.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 26 TGSKTCILGPNGCGKTTLLKTIAGLV--PYSGSVLIDGQEVHGQKRKELatkvammsqfttvafdytvyetvlmgayrqq 103
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELgpPGGGVIYIDGEDILEEVLDQL------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 104 aqrflpivskqekervlyylertgLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELI----- 178
Cdd:smart00382 50 ------------------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleel 105
|
170 180 190
....*....|....*....|....*....|....*....
gi 488286290 179 QQLNEWSAQEGKTLIGV------FHDIRLALTLSEKIVF 211
Cdd:smart00382 106 RLLLLLKSEKNLTVILTtndekdLGPALLRRRFDRRIVL 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-225 |
1.16e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 2 IELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIA-----GLvPYSGSVLIDGQEVHG---------- 66
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGI-PKNCQILHVEQEVVGddttalqcvl 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 67 ----QKRKELATKVAMMSQFTTVAF-----------DYTVYETVLMGAYRQQAQRFLPIVSKQEKERVLYYLERTGLLP- 130
Cdd:PLN03073 257 ntdiERTQLLEEEAQLVAQQRELEFetetgkgkganKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPe 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 131 LKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSaqegKTLIGVFHDIRLALTLSEKIV 210
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP----KTFIVVSHAREFLNTVVTDIL 412
|
250
....*....|....*.
gi 488286290 211 FMKQGK-VAAQGDFQT 225
Cdd:PLN03073 413 HLHGQKlVTYKGDYDT 428
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-229 |
2.66e-08 |
|
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: 54.25 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 32 ILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGqevhgqkrKELATKVAMMSQFTTVAFDYTVYETVLMGAYRQQAQRFLPI 110
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGdTTVTSGDATVAG--------KSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 111 VSKQEKERVLYY-LERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELiqqlneWSA--- 186
Cdd:TIGR01257 2042 VPAEEIEKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML------WNTivs 2115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488286290 187 --QEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASK 229
Cdd:TIGR01257 2116 iiREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSK 2160
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-197 |
3.14e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 52.25 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 15 PILKDISLVFPTGSKTCILGPNGCGKTTLLKTIA-----GLVpySGSVLIDGQevhgQKRKELATKVAMMSQFTTVAFDY 89
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktaGVI--TGEILINGR----PLDKNFQRSTGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 TVYETVLMGAYrqqaqrflpivskqekervlyylertgllpLKDkvvnqLSGGQQQRVFLAKLFVQDPEIILLDEPNNHL 169
Cdd:cd03232 95 TVREALRFSAL------------------------------LRG-----LSVEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
170 180
....*....|....*....|....*...
gi 488286290 170 DIRYQQELIQQLNEWsAQEGKTLIGVFH 197
Cdd:cd03232 140 DSQAAYNIVRFLKKL-ADSGQAILCTIH 166
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-218 |
4.51e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 18 KDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP-YSGSVLIDGQEVHGQKRKE-LATKVAMMS---QFTTVAFDYTVY 92
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPaRGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 93 ETVLMGAYRQQAqrfLPIVSKQEKERVLYYLERTGL-LPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDI 171
Cdd:PRK15439 360 WNVCALTHNRRG---FWIKPARENAVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488286290 172 RYQQElIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVA 218
Cdd:PRK15439 437 SARND-IYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
10-205 |
5.11e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 10 TLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLI-DGQEVHGQKRKELATKVAMMSQ----FT 83
Cdd:PTZ00265 394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPTEGDIIInDSHNLKDINLKWWRSKIGVVSQdpllFS 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 84 TVA---FDYTVYETVLMGAYRQQAQRFLPIVSKQEKER-------------VLYYLERTGLLPLK--------DKVVN-- 137
Cdd:PTZ00265 474 NSIknnIKYSLYSLKDLEALSNYYNEDGNDSQENKNKRnscrakcagdlndMSNTTDSNELIEMRknyqtikdSEVVDvs 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 138 -------------------------QLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTL 192
Cdd:PTZ00265 554 kkvlihdfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
250
....*....|....*.
gi 488286290 193 IGVFH---DIRLALTL 205
Cdd:PTZ00265 634 IIIAHrlsTIRYANTI 649
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
106-229 |
1.10e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.04 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 106 RFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWs 185
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM- 190
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 488286290 186 AQEGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASK 229
Cdd:NF000106 191 VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-170 |
1.28e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.64 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILkDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLV-PYSGSVLIDGQEVHGQKRKELatkvAMM 79
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMqPSSGNIYYKNCNINNIAKPYC----TYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 80 SQFTTVAFDYTVYETVLMGAYRQQAQRFLPIvskqekerVLYYLERTGLLplkDKVVNQLSGGQQQRVFLAKLFVQDPEI 159
Cdd:PRK13541 76 GHNLGLKLEMTVFENLKFWSEIYNSAETLYA--------AIHYFKLHDLL---DEKCYSLSSGMQKIVAIARLIACQSDL 144
|
170
....*....|.
gi 488286290 160 ILLDEPNNHLD 170
Cdd:PRK13541 145 WLLDEVETNLS 155
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-216 |
1.76e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.63 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIaglvpysgsvlidgqevhgqkrkeLATKVAMMSQFTTVAFDYTvyetvl 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG------------------------LYASGKARLISFLPKFSRN------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 97 mgayrqqaqrfLPIVSKQekervLYYLERTGL--LPLkDKVVNQLSGGQQQRVFLAKLFVQDPE--IILLDEPNNHLDIR 172
Cdd:cd03238 61 -----------KLIFIDQ-----LQFLIDVGLgyLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488286290 173 YQQELIQQLNEWsAQEGKTLIGVFHDIRLaLTLSEKIVFM--KQGK 216
Cdd:cd03238 124 DINQLLEVIKGL-IDLGNTVILIEHNLDV-LSSADWIIDFgpGSGK 167
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
17-184 |
2.05e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 50.77 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSK-TCILGPNGCGKTTLLKTIA--------GLVPYSG-SVLIDGQEVH---------GQKRKELATKVA 77
Cdd:COG3950 14 FEDLEIDFDNPPRlTVLVGENGSGKTTLLEAIAlalsgllsRLDDVKFrKLLIRNGEFGdsaklilyyGTSRLLLDGPLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 78 MMSQFTTVAFD-YTVYETVLMGAYRQQ--AQRFLPIVSKQEKE-----------------------RVLYYLERTGLLPL 131
Cdd:COG3950 94 KLERLKEEYFSrLDGYDSLLDEDSNLRefLEWLREYLEDLENKlsdeldekleavrealnkllpdfKDIRIDRDPGRLVI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286290 132 KDKV-----VNQLSGGQQQ----------RVFLAKLFVQDPE----IILLDEPNNHLDIRYQQELIQQLNEW 184
Cdd:COG3950 174 LDKNgeelpLNQLSDGERSllalvgdlarRLAELNPALENPLegegIVLIDEIDLHLHPKWQRRILPDLRKI 245
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-246 |
2.25e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVpySGSVLIDGQE-VHGQKRKE-LATKVAMMSQFTTVAFDYTVYE 93
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGDRlVNGRPLDSsFQRSIGYVQQQDLHLPTSTVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 94 TVLMGAYRQQAQRflpiVSKQEKER-VLYYLERTGLLPLKDKVVNQ----LSGGQQQRVFLAKLFVQDPEIIL-LDEPNN 167
Cdd:TIGR00956 856 SLRFSAYLRQPKS----VSKSEKMEyVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTS 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 168 HLDIRYQQELIQQLNEwSAQEGKTLIGVFHDIRlALTLSE--KIVFMKQG-KVAAQGDFqtlasKEFLQTIFEtdivsYF 244
Cdd:TIGR00956 932 GLDSQTAWSICKLMRK-LADHGQAILCTIHQPS-AILFEEfdRLLLLQKGgQTVYFGDL-----GENSHTIIN-----YF 999
|
..
gi 488286290 245 QK 246
Cdd:TIGR00956 1000 EK 1001
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-249 |
3.04e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 50.24 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 14 TPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYSGSVLIDG---QEVHGQK-RKELATKVAMMSQFTtvafdy 89
Cdd:cd03289 17 NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGvswNSVPLQKwRKAFGVIPQKVFIFS------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 90 tvyetvlmGAYRQQaqrfLPIVSKQEKERVLYYLERTGLLPLKDKVVNQL-----------SGGQQQRVFLAKLFVQDPE 158
Cdd:cd03289 91 --------GTFRKN----LDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 159 IILLDEPNNHLDIRYQQELIQQLNEwsAQEGKTLIGVFHDIRlALTLSEKIVFMKQGKVAAQGDFQTLASKE--FLQTIF 236
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQ--AFADCTVILSEHRIE-AMLECQRFLVIEENKVRQYDSIQKLLNEKshFKQAIS 235
|
250
....*....|...
gi 488286290 237 ETDIVSYFQKQHK 249
Cdd:cd03289 236 PSDRLKLFPRRNS 248
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-234 |
3.47e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.81 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVlidgqEVHGQKrKELATKVAMMSQFTTVafDYTVYETV 95
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGsLSPTVGKV-----DRNGEV-SVIAISAGLSGQLTGI--ENIEFKML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 96 LMGAYRQQAQRFLP-IVSKQEKERVLYylertgllplkdKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQ 174
Cdd:PRK13546 112 CMGFKRKEIKAMTPkIIEFSELGEFIY------------QPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286290 175 QELIQQLNEWSAQeGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLASK--EFLQT 234
Cdd:PRK13546 180 QKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKyeAFLND 240
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-199 |
6.34e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 1 MIELKKTAVTLQQTPILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVHG------QKRKELA 73
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGeLPLLSGERQSQFSHITRlsfeqlQKLVSDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 74 TK---VAMMSQFTTvAFDYTVYETVLMGAyrqqaqrflpivskQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLA 150
Cdd:PRK10938 83 WQrnnTDMLSPGED-DTGRTTAEIIQDEV--------------KDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLC 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488286290 151 KLFVQDPEIILLDEPNNHLDIRYQQELIQQLNEWSaQEGKTLIGV---FHDI 199
Cdd:PRK10938 148 QALMSEPDLLILDEPFDGLDVASRQQLAELLASLH-QSGITLVLVlnrFDEI 198
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
23-210 |
8.77e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.95 E-value: 8.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 23 VFPTGSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQEVhgqkrkelatkvammsqfttvafdytvyetvlmgAYR 101
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGqLIPNGDNDEWDGITP----------------------------------VYK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 102 QQaqrflpivskqekervlyYLErtgllplkdkvvnqLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQELIQQL 181
Cdd:cd03222 67 PQ------------------YID--------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
170 180
....*....|....*....|....*....
gi 488286290 182 NEWSAQEGKTLIGVFHDIRLALTLSEKIV 210
Cdd:cd03222 115 RRLSEEGKKTALVVEHDLAVLDYLSDRIH 143
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-187 |
1.15e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 23 VFPtGSKTCILGPNGCGKTTLLKTIAGLvpYS---GSVLIDGQEVH--GQKRKELAtKVAMMSQFTTVAFDYTVYETVLM 97
Cdd:PRK10762 27 VYP-GRVMALVGENGAGKSTMMKVLTGI--YTrdaGSILYLGKEVTfnGPKSSQEA-GIGIIHQELNLIPQLTIAENIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 98 GayRQQAQRFLPIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQEL 177
Cdd:PRK10762 103 G--REFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESL 180
|
170
....*....|
gi 488286290 178 IQQLNEWSAQ 187
Cdd:PRK10762 181 FRVIRELKSQ 190
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
133-193 |
2.06e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 2.06e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286290 133 DKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDIRYQQE---LIQQLnewsAQEGKTLI 193
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEiytIINEL----AAEGKGVI 458
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
5-238 |
2.38e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.30 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 5 KKTAVTlqqtpILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAG---------------------LVPYSGSVLIDGQE 63
Cdd:PLN03140 174 KKTKLT-----ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGkldpslkvsgeityngyrlneFVPRKTSAYISQND 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 64 VHgqkrkelatkVAMMSQFTTVAFDY------TVYETVLMGAYRQ---------QAQRFLPIVSKQEKERVL---YYLER 125
Cdd:PLN03140 249 VH----------VGVMTVKETLDFSArcqgvgTRYDLLSELARREkdagifpeaEVDLFMKATAMEGVKSSLitdYTLKI 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 126 TGLLPLKDKVVNQ-----LSGGQQQRVFLAKLFVQDPEIILLDEPNNHLD--IRYQ-QELIQQLNEWSaqEGKTLIGVFH 197
Cdd:PLN03140 319 LGLDICKDTIVGDemirgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDssTTYQiVKCLQQIVHLT--EATVLMSLLQ 396
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 488286290 198 DIRLALTLSEKIVFMKQGKVAAQGdfqtlaSKEFLQTIFET 238
Cdd:PLN03140 397 PAPETFDLFDDIILLSEGQIVYQG------PRDHILEFFES 431
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-236 |
3.17e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPY-SGSVLIDGQEVHGQKRKELATKVAMMSQfTTVAFDYTVyet 94
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVcGGEIRVNGREIGAYGLRELRRQFSMIPQ-DPVLFDGTV--- 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 vlmgayRQQAQRFLPIVSkqekERVLYYLERTGllpLKDKVVNQLSG--------------GQQQRVFLAK-LFVQDPEI 159
Cdd:PTZ00243 1401 ------RQNVDPFLEASS----AEVWAALELVG---LRERVASESEGidsrvleggsnysvGQRQLMCMARaLLKKGSGF 1467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 160 ILLDEPNNHLDIRYQQELiqQLNEWSAQEGKTLIGVFHdiRL-ALTLSEKIVFMKQGKVAAQGDFQTLASKEflQTIF 236
Cdd:PTZ00243 1468 ILMDEATANIDPALDRQI--QATVMSAFSAYTVITIAH--RLhTVAQYDKIIVMDHGAVAEMGSPRELVMNR--QSIF 1539
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-233 |
4.91e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGL-VPYSGSVLIDGQevhgqkrkelATKVAMMS----QFTTVafDYTV 91
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtMPNKGTVDIKGS----------AALIAISSglngQLTGI--ENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 92 YETVLMGAYRQQAQRFLPIVskqekervlyyLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLDEPNNHLDI 171
Cdd:PRK13545 108 LKGLMMGLTKEKIKEIIPEI-----------IEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488286290 172 RYQQELIQQLNEWSAQeGKTLIGVFHDIRLALTLSEKIVFMKQGKVAAQGDFQTLAS--KEFLQ 233
Cdd:PRK13545 177 TFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDhyDEFLK 239
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-165 |
1.13e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVP---YSGSVLIDGQEVH------GQKR------KELATkVAMMSq 81
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgsYEGEILFDGEVCRfkdirdSEALgiviihQELAL-IPYLS- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 82 fttvafdytVYETVLMGayRQQAQRFLpIVSKQEKERVLYYLERTGLLPLKDKVVNQLSGGQQQRVFLAKLFVQDPEIIL 161
Cdd:NF040905 95 ---------IAENIFLG--NERAKRGV-IDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
....
gi 488286290 162 LDEP 165
Cdd:NF040905 163 LDEP 166
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-174 |
1.39e-05 |
|
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: 46.06 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYSGSVLIDG---QEVHGQK-RKELAT---KVAMMSQFTTVAFD 88
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGvswNSVTLQTwRKAFGVipqKVFIFSGTFRKNLD 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 89 -YTVYETVLMgaYRQQAQRFLPIVSKQEKERVLYYLERTGLLplkdkvvnqLSGGQQQRVFLAKLFVQDPEIILLDEPNN 167
Cdd:TIGR01271 1314 pYEQWSDEEI--WKVAEEVGLKSVIEQFPDKLDFVLVDGGYV---------LSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
....*...
gi 488286290 168 HLD-IRYQ 174
Cdd:TIGR01271 1383 HLDpVTLQ 1390
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
24-213 |
1.83e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 24 FPTGSKTCILGPNGCGKTTLLKTIAglvpysgsvLIDGQEVHGQKRKELAtkvammsqfttvafdytvyetvlmgayrqQ 103
Cdd:cd03227 18 FGEGSLTIITGPNGSGKSTILDAIG---------LALGGAQSATRRRSGV-----------------------------K 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 104 AQRFLPIVSkqekervlyyLERTGLLPlkdkvvnQLSGGQQQRVFLAKLF----VQDPEIILLDEPNNHLDIRYQQELIQ 179
Cdd:cd03227 60 AGCIVAAVS----------AELIFTRL-------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAE 122
|
170 180 190
....*....|....*....|....*....|....
gi 488286290 180 QLNEwSAQEGKTLIGVFHDIRLALtLSEKIVFMK 213
Cdd:cd03227 123 AILE-HLVKGAQVIVITHLPELAE-LADKLIHIK 154
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-193 |
3.92e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.22 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGsKTCILGPNGCGKTTLLKTIAGLVPYSGSVLIDGQEVHGQKRKELATKV------AMMSQFTTVAFDYT 90
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEieltfgSLLSRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 VYETV------LMGAYRQQAQRFLPIVSKQ-----------------EKERVLYYLErtglLPLKDKV---VNQLSGGQQ 144
Cdd:COG3593 93 DKEELeealeeLNEELKEALKALNELLSEYlkelldgldlelelsldELEDLLKSLS----LRIEDGKelpLDRLGSGFQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488286290 145 QRVFLAkLFVQ--------DPEIILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLI 193
Cdd:COG3593 169 RLILLA-LLSAlaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVII 224
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-214 |
9.97e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 27 GSKTCILGPNGCGKTTLLKTIAG-LVPYSGSVLIDGQevhgqkrkelaTKVAMMSQFTTvAFDYTVYETVLMG--AYRQQ 103
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNeISADGGSYTFPGN-----------WQLAWVNQETP-ALPQPALEYVIDGdrEYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 104 AQRFLPIVSKQE-------------------KERVLYYLERTGLL-PLKDKVVNQLSGGQQQRVFLAKLFVQDPEIILLD 163
Cdd:PRK10636 95 EAQLHDANERNDghaiatihgkldaidawtiRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488286290 164 EPNNHLDIryqqELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQ 214
Cdd:PRK10636 175 EPTNHLDL----DAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-179 |
1.17e-04 |
|
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: 43.01 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 16 ILKDISLVFPTGSKTCILGPNGCGKTTL-LKTIAGLVPYSGSVLIDGQEVHGQKRKELATKVAMMSQfttvafdytvyET 94
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQ-----------DP 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 95 VLM-GAYRQQAQRFlpivSKQEKERVLYYLE----RTGLLPLKDKVVNQ-------LSGGQQQRVFLAKLFVQDPEIILL 162
Cdd:TIGR00957 1370 VLFsGSLRMNLDPF----SQYSDEEVWWALElahlKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVL 1445
|
170
....*....|....*..
gi 488286290 163 DEPNNHLDIRyQQELIQ 179
Cdd:TIGR00957 1446 DEATAAVDLE-TDNLIQ 1461
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-216 |
2.21e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.71 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 20 ISLVFPTGSKTCILGPNGCGKTTLLKTIAGLVPYSGSVLIDG---------QEVHGQKRKELATKVAMMSQFTTVAFDYT 90
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRmrfddidllRLSPRERRKLVGHNVSMIFQEPQSCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 91 vyETV---LMGA-----YRQQ-AQRFlpivsKQEKERVLYYLERTGLLPLKDKVVN---QLSGGQQQRVFLAKLFVQDPE 158
Cdd:PRK15093 106 --ERVgrqLMQNipgwtYKGRwWQRF-----GWRKRRAIELLHRVGIKDHKDAMRSfpyELTEGECQKVMIAIALANQPR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488286290 159 IILLDEPNNHLDIRYQQELIQQLNEWSAQEGKTLIGVFHDIRLALTLSEKIVFMKQGK 216
Cdd:PRK15093 179 LLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
29-202 |
3.58e-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: 41.54 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 29 KTCilgpNGCGKTtllktiaGLVPYSGSVLIDGQEVHgqkrkelatKVAMMSQFTTVAFDYTVYetvLMGAYRQQAQRFL 108
Cdd:TIGR00630 406 RPC----PSCGGT-------RLKPEALAVTVGGKSIA---------DVSELSIREAHEFFNQLT---LTPEEKKIAEEVL 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 109 pivsKQEKERvLYYLERTGL--LPLkDKVVNQLSGGQQQRVFLAK---------LFVqdpeiilLDEPNNHLDIRYQQEL 177
Cdd:TIGR00630 463 ----KEIRER-LGFLIDVGLdyLSL-SRAAGTLSGGEAQRIRLATqigsgltgvLYV-------LDEPSIGLHQRDNRRL 529
|
170 180
....*....|....*....|....*...
gi 488286290 178 IQQLNEWSAQeGKTLIGVFHD---IRLA 202
Cdd:TIGR00630 530 INTLKRLRDL-GNTLIVVEHDedtIRAA 556
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
17-66 |
9.94e-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: 40.38 E-value: 9.94e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488286290 17 LKDISLVFPTGSKTCILGPNGCGKTTLLKTIagLVPYSGSVLIDGQEVHG 66
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDT--LYPALANRLNGAKTVPG 671
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
133-202 |
1.41e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.78 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286290 133 DKVVNQLSGGQQQRVFLAK---------LFVqdpeiilLDEPNNHLDIRYQQELIQQLNEWSAQeGKTLIGVFHD---IR 200
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATqigsgltgvLYV-------LDEPSIGLHPRDNDRLIETLKRLRDL-GNTVLVVEHDedtIR 203
|
..
gi 488286290 201 LA 202
Cdd:cd03270 204 AA 205
|
|
| Srp102 |
COG2229 |
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, ... |
34-89 |
1.85e-03 |
|
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 441830 [Multi-domain] Cd Length: 189 Bit Score: 38.27 E-value: 1.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488286290 34 GPNGCGKTTLLKTIAGLVPysgsvlidgqevhgqkrkeLATKVAMMS------QFTTVAFDY 89
Cdd:COG2229 19 GPFGAGKTTFVRSISEIEP-------------------LSTEGRLTDasletkTTTTVAFDF 61
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
111-183 |
6.75e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.37 E-value: 6.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286290 111 VSKQEKERVLYYLERTGLLPLkdkVVNQLSGGQQQRVFLAKLFVQDPE---IILLDEPNNHLDIRYQQELIQQLNE 183
Cdd:pfam13304 212 VDDRLRERGLILLENGGGGEL---PAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKE 284
|
|
| |
