|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-257 |
5.60e-94 |
|
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: 276.92 E-value: 5.60e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNiPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAY 80
Cdd:COG1120 1 MLEAENLSVGYGGR-PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQHSPQTYQYKVLDYVVLGRAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLI 160
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 161 LFDEPTSALDYGNVFKTLSLIKGLSHQQ-FSIIMTTHNPDHPMLLnevipNSKVAILTKSGKLHCGFTEAILTEDNLREL 239
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLARERgRTVVMVLHDLNLAARY-----ADRLVLLKDGRIVAQGPPEEVLTPELLEEV 234
|
250
....*....|....*...
gi 2310524600 240 YQTDLRLIDVPELQRKIC 257
Cdd:COG1120 235 YGVEARVIEDPVTGRPLV 252
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-248 |
2.19e-65 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 203.78 E-value: 2.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNiPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSakqiaRQVAY 80
Cdd:COG1121 6 AIELENLTVSYGGR-PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-----RRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQHSPQTYQY--KVLDYVVLGRAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQ 158
Cdd:COG1121 80 VPQRAEVDWDFpiTVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 159 LILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNpdhpmlLNEVIPN-SKVAILTKsGKLHCGFTEAILTEDNLR 237
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHD------LGAVREYfDRVLLLNR-GLVAHGPPEEVLTPENLS 232
|
250
....*....|.
gi 2310524600 238 ELYQTDLRLID 248
Cdd:COG1121 233 RAYGGPVALLA 243
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-200 |
5.28e-59 |
|
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: 185.33 E-value: 5.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 3 KINQLYFQHQRNiPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVS 82
Cdd:cd03214 1 EVENLSVGYGGR-TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 83 QhspqtyqykvldyvvlgraahlglfgkpreedyhlaerALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILF 162
Cdd:cd03214 80 Q--------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190
....*....|....*....|....*....|....*....
gi 2310524600 163 DEPTSALDYGNVFKTLSLIKGLSHQQ-FSIIMTTHNPDH 200
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERgKTVVMVLHDLNL 160
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-200 |
6.94e-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: 173.04 E-value: 6.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 3 KINQLYFQH-QRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYV 81
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 82 SQHsP--QTYQYKVLDYVVLGraahLGLFGKPREEDYHLAERALAQLSIRHFADK-IYmQMSGGEKQLVNLAKILVQQPQ 158
Cdd:cd03225 81 FQN-PddQFFGPTVEEEVAFG----LENLGLPEEEIEERVEEALELVGLEGLRDRsPF-TLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2310524600 159 LILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPDH 200
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDL 196
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-253 |
3.17e-52 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 170.34 E-value: 3.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQ-HQRniPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVA 79
Cdd:PRK13548 2 MLEARNLSVRlGGR--TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 80 YVSQHSPQTYQYKVLDYVVLGRAAHlglfGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQ---- 155
Cdd:PRK13548 80 VLPQHSSLSFPFTVEEVVAMGRAPH----GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwep 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 156 --QPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQ-FSIIMTTHN-------PDHPMLLnevipnskvailtKSGKLHC- 224
Cdd:PRK13548 156 dgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERgLAVIVVLHDlnlaaryADRIVLL-------------HQGRLVAd 222
|
250 260
....*....|....*....|....*....
gi 2310524600 225 GFTEAILTEDNLRELYQTDLRLIDVPELQ 253
Cdd:PRK13548 223 GTPAEVLTPETLRRVYGADVLVQPHPETG 251
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
16-205 |
3.74e-52 |
|
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: 168.87 E-value: 3.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSakqiaRQVAYVSQHS--PQTYQYKV 93
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVPQRRsiDRDFPISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 94 LDYVVLGRAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGN 173
Cdd:cd03235 88 RDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 2310524600 174 VFKTLSLIKGLSHQQFSIIMTTHNP-------DHPMLLN 205
Cdd:cd03235 168 QEDIYELLRELRREGMTILVVTHDLglvleyfDRVLLLN 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-238 |
2.03e-49 |
|
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: 162.50 E-value: 2.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYV 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 82 SQH------SPqtyqyKVLDYVVLGrAAHLGLfgkPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQ 155
Cdd:COG1122 81 FQNpddqlfAP-----TVEEDVAFG-PENLGL---PREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 156 QPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNpdhpmlLNEVIPNSKVAILTKSGKLHC-GFTEAILTED 234
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHD------LDLVAELADRVIVLDDGRIVAdGTPREVFSDY 225
|
....
gi 2310524600 235 NLRE 238
Cdd:COG1122 226 ELLE 229
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-257 |
1.29e-46 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 155.94 E-value: 1.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQrNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAY 80
Cdd:PRK11231 2 TLRTENLTVGYG-TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQHSPQTYQYKVLDYVVLGRAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLI 160
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 161 LFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNpdhpmlLNEVIPNSKVAILTKSGKL-HCGFTEAILTEDNLREL 239
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHD------LNQASRYCDHLVVLANGHVmAQGTPEEVMTPGLLRTV 234
|
250
....*....|....*...
gi 2310524600 240 YQTDLRLIDVPELQRKIC 257
Cdd:PRK11231 235 FDVEAEIHPEPVSGTPMC 252
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-199 |
1.88e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 149.42 E-value: 1.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQL---YFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIA-- 75
Cdd:COG1136 4 LLELRNLtksYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 76 --RQVAYVSQhspqtyQYKVLDY------VVLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLV 147
Cdd:COG1136 84 rrRHIGFVFQ------FFNLLPEltalenVALP----LLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2310524600 148 NLAKILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQ-FSIIMTTHNPD 199
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVTHDPE 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-199 |
1.95e-43 |
|
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: 146.48 E-value: 1.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRN---IPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIA--- 75
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 76 -RQVAYVSQhspqtyQYKVLDY------VVLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVN 148
Cdd:cd03255 81 rRHIGFVFQ------SFNLLPDltalenVELP----LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2310524600 149 LAKILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQ-FSIIMTTHNPD 199
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVTHDPE 202
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
16-247 |
3.79e-43 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 146.77 E-value: 3.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKP-KCGEIFLQNKEIKQLSAKQIARQVAYVSQHSPQTYQY--K 92
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGERRGGEDVWELRKRIGLVSPALQLRFPRdeT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 93 VLDYVVLGRAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYG 172
Cdd:COG1119 97 VLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLG 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310524600 173 NVFKTLSLIKGLSHQQF-SIIMTTHNPDhpmllnEVIPNSKVAILTKSGK-LHCGFTEAILTEDNLRELYQTDLRLI 247
Cdd:COG1119 177 ARELLLALLDKLAAEGApTLVLVTHHVE------EIPPGITHVLLLKDGRvVAAGPKEEVLTSENLSEAFGLPVEVE 247
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-199 |
1.00e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 144.57 E-value: 1.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQrNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYV 81
Cdd:COG4619 1 LELEGLSFRVG-GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 82 SQHsPQTYQYKVLDYvvLGRAAHLglfgKPREEDYHLAERALAQLSIRH-FADKIYMQMSGGEKQLVNLAKILVQQPQLI 160
Cdd:COG4619 80 PQE-PALWGGTVRDN--LPFPFQL----RERKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2310524600 161 LFDEPTSALDYGNVFKTLSLIKGLSHQ-QFSIIMTTHNPD 199
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPE 192
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-249 |
1.70e-41 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 142.67 E-value: 1.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLkPKCGEIFLQNKEIKQLSAKQIARQVAYVSQHSPQTYQYKVLDYV 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 98 VLGRAAHLglfgkPREEdyhlAERALAQLSIR-HFADKI---YMQMSGGEKQLVNLAKILVQ-------QPQLILFDEPT 166
Cdd:COG4138 91 ALHQPAGA-----SSEA----VEQLLAQLAEAlGLEDKLsrpLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 167 SALDYGNVFKTLSLIKGLSHQQFSIIMTTHNpdhpmlLNEVIPNSKVAILTKSGKLH-CGFTEAILTEDNLRELYQTDLR 245
Cdd:COG4138 162 NSLDVAQQAALDRLLRELCQQGITVVMSSHD------LNHTLRHADRVWLLKQGKLVaSGETAEVMTPENLSEVFGVKFR 235
|
....
gi 2310524600 246 LIDV 249
Cdd:COG4138 236 RLEV 239
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-200 |
1.77e-41 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 140.83 E-value: 1.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIflqnkeikqlsAKQIARQVAYVSQHS--PQTYQYKV 93
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSevPDSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 94 LDYVVLGRAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGN 173
Cdd:NF040873 75 RDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180
....*....|....*....|....*..
gi 2310524600 174 VFKTLSLIKGLSHQQFSIIMTTHNPDH 200
Cdd:NF040873 155 RERIIALLAEEHARGATVVVVTHDLEL 181
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
15-237 |
1.20e-40 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 144.21 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 15 IPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQHSPQTYQYKVL 94
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 95 DYVVLGRAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNV 174
Cdd:PRK09536 96 QVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQ 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310524600 175 FKTLSLIKGLSHQQFSIIMTTHNPDHPMLLNEVIpnskvAILTKSGKLHCGFTEAILTEDNLR 237
Cdd:PRK09536 176 VRTLELVRRLVDDGKTAVAAIHDLDLAARYCDEL-----VLLADGRVRAAGPPADVLTADTLR 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-199 |
5.38e-40 |
|
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: 137.65 E-value: 5.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYfQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQiaRQVAYV 81
Cdd:cd03259 1 LELKGLS-KTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 82 SQHsPQTYQYK-VLDYVVLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLI 160
Cdd:cd03259 78 FQD-YALFPHLtVAENIAFG----LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2310524600 161 LFDEPTSALDYGNVFKTLSLIKGLSHQQ-FSIIMTTHNPD 199
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELgITTIYVTHDQE 192
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-199 |
1.79e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 137.53 E-value: 1.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQL---YFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSakqiaRQ 77
Cdd:COG1116 7 ALELRGVskrFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-----PD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 78 VAYVSQhSPQTYQYK-VLDYVVLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKiY-MQMSGGEKQLVNLAKILVQ 155
Cdd:COG1116 82 RGVVFQ-EPALLPWLtVLDNVALG----LELRGVPKAERRERARELLELVGLAGFEDA-YpHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2310524600 156 QPQLILFDEPTSALDYGnvfkT--------LSLIKglsHQQFSIIMTTHNPD 199
Cdd:COG1116 156 DPEVLLMDEPFGALDAL----TrerlqdelLRLWQ---ETGKTVLFVTHDVD 200
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-167 |
2.33e-39 |
|
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: 133.93 E-value: 2.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQHSPQTYQYKVLDYV 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310524600 98 VLGrAAHLGLFGKPREEDyhlAERALAQLSIRHFADKI----YMQMSGGEKQLVNLAKILVQQPQLILFDEPTS 167
Cdd:pfam00005 81 RLG-LLLKGLSKREKDAR---AEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-198 |
4.34e-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: 134.91 E-value: 4.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNiPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAkQIARQVAY 80
Cdd:COG4133 2 MLEAENLSCRRGER-LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSqHSPQTY-QYKVLDYVvlgrAAHLGLFGKPREEDyhLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQL 159
Cdd:COG4133 80 LG-HADGLKpELTVRENL----RFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 2310524600 160 ILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNP 198
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
18-199 |
6.96e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 135.58 E-value: 6.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKqIARQVAYVSQHsPQTYQY-KVLDY 96
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVPQE-PALYPDlTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 97 VVLgraaHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVFK 176
Cdd:COG1131 94 LRF----FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRE 169
|
170 180
....*....|....*....|...
gi 2310524600 177 TLSLIKGLSHQQFSIIMTTHNPD 199
Cdd:COG1131 170 LWELLRELAAEGKTVLLSTHYLE 192
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-257 |
2.18e-38 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 134.44 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQrNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAY 80
Cdd:COG4604 1 MIEIKNVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQHSPQTYQYKVLDYVVLGRAAHLGlfGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLI 160
Cdd:COG4604 80 LRQENHINSRLTVRELVAFGRFPYSK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 161 LFDEPTSALDYGNVFKTLSLIKGLSHQQ-FSIIMTTHN-------PDHpmllnevIpnskVAIltKSGKL-HCGFTEAIL 231
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLADELgKTVVIVLHDinfascyADH-------I----VAM--KDGRVvAQGTPEEII 224
|
250 260
....*....|....*....|....*.
gi 2310524600 232 TEDNLRELYQTDLRLIDVPelQRKIC 257
Cdd:COG4604 225 TPEVLSDIYDTDIEVEEID--GKRIC 248
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-199 |
6.95e-38 |
|
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: 133.00 E-value: 6.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQL---YFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQ 77
Cdd:COG1124 1 MLEVRNLsvsYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 78 VAYVSQHSpqtyqYKVLD-----YVVLGRAAHLglFGKPREEDYhlAERALAQLSI-RHFADKIYMQMSGGEKQLVNLAK 151
Cdd:COG1124 81 VQMVFQDP-----YASLHprhtvDRILAEPLRI--HGLPDREER--IAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2310524600 152 ILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQ-FSIIMTTHNPD 199
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERgLTYLFVSHDLA 200
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-208 |
1.63e-37 |
|
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: 129.29 E-value: 1.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 3 KINQLYFQHQRNiPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVs 82
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 83 qhspqtyqykvldyvvlgraahlglfgkpreedyhlaeralaqlsirhfadkiyMQMSGGEKQLVNLAKILVQQPQLILF 162
Cdd:cd00267 79 ------------------------------------------------------PQLSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2310524600 163 DEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPDHPMLLNEVI 208
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRV 150
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
18-199 |
1.87e-36 |
|
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: 129.22 E-value: 1.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAK---QIARQVAYVSQHSPQTYQYKVL 94
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrQLRRQIGMIFQQFNLIERLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 95 DYVVLGRAAHL----GLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALD 170
Cdd:cd03256 97 ENVLSGRLGRRstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
170 180 190
....*....|....*....|....*....|
gi 2310524600 171 YGNVFKTLSLIKGLSHQ-QFSIIMTTHNPD 199
Cdd:cd03256 177 PASSRQVMDLLKRINREeGITVIVSLHQVD 206
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-247 |
2.95e-36 |
|
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: 128.82 E-value: 2.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQrNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKqIARQVAY 80
Cdd:COG4555 1 MIEVENLSKKYG-KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQHSPQTYQYKVLDYVVLgraaHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLI 160
Cdd:COG4555 79 LPDERGLYDRLTVRENIRY----FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 161 LFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPDhpmLLNEVIpnSKVAILTKSGKLHCGFTEAILTEDNLRELY 240
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQ---EVEALC--DRVVILHKGKVVAQGSLDELREEIGEENLE 229
|
....*..
gi 2310524600 241 QTDLRLI 247
Cdd:COG4555 230 DAFVALI 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-197 |
8.34e-36 |
|
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: 133.10 E-value: 8.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQH----QRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSA---KQ 73
Cdd:COG1123 260 LLEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 74 IARQVAYVSQHsPQTY---QYKVLDYVVLGRAAHLGLfgkPREEDYHLAERALAQ--LSiRHFADKIYMQMSGGEKQLVN 148
Cdd:COG1123 340 LRRRVQMVFQD-PYSSlnpRMTVGDIIAEPLRLHGLL---SRAERRERVAELLERvgLP-PDLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2310524600 149 LAKILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQ-FSIIMTTHN 197
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELgLTYLFISHD 464
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-197 |
1.92e-35 |
|
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: 126.05 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 8 YFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSakqiaRQVAYVSQHsPQ 87
Cdd:cd03293 10 YGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDRGYVFQQ-DA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 88 TYQYK-VLDYVVLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPT 166
Cdd:cd03293 84 LLPWLtVLDNVALG----LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 2310524600 167 SALDYGnvfkT-----LSLIKGLSHQQFSIIMTTHN 197
Cdd:cd03293 160 SALDAL----TreqlqEELLDIWRETGKTVLLVTHD 191
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-199 |
3.18e-35 |
|
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: 131.56 E-value: 3.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQ-HQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKC---GEIFLQNKEIKQLSAKQIAR 76
Cdd:COG1123 4 LLEVRDLSVRyPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 77 QVAYVSQhSPQTYqykvLDYVVLGR--AAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILV 154
Cdd:COG1123 84 RIGMVFQ-DPMTQ----LNPVTVGDqiAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2310524600 155 QQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQ-FSIIMTTHNPD 199
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERgTTVLLITHDLG 204
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
18-196 |
5.57e-35 |
|
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: 124.56 E-value: 5.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAK--QIARQVAYVSQHSPQTYQYKVLD 95
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGMVFQQFNLFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 YVVLgraAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVF 175
Cdd:cd03262 96 NITL---APIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVG 172
|
170 180
....*....|....*....|.
gi 2310524600 176 KTLSLIKGLSHQQFSIIMTTH 196
Cdd:cd03262 173 EVLDVMKDLAEEGMTMVVVTH 193
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-197 |
5.63e-35 |
|
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: 125.24 E-value: 5.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQ-VAYVSQHsPQTYQ-YKVLD 95
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQI-PRLFPeLTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 YVVLGRAAHLGL------FGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSAL 169
Cdd:cd03219 95 NVMVAAQARTGSglllarARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180
....*....|....*....|....*...
gi 2310524600 170 DYGNVFKTLSLIKGLSHQQFSIIMTTHN 197
Cdd:cd03219 175 NPEETEELAELIRELRERGITVLLVEHD 202
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-199 |
5.84e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 128.29 E-value: 5.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQrNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQiaRQVAY 80
Cdd:COG3842 5 ALELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQHspqtyqY------KVLDYVVLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILV 154
Cdd:COG3842 82 VFQD------YalfphlTVAENVAFG----LRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2310524600 155 QQPQLILFDEPTSALDYGNVFKTLSLIKGLsHQQFSI--IMTTHNPD 199
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRL-QRELGItfIYVTHDQE 197
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-199 |
8.89e-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: 123.91 E-value: 8.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 4 INQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKqlsAKQIARQVAYVSQ 83
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 84 HSpqTYQY---KVLDYVVLGRaahlglfgKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLI 160
Cdd:cd03226 79 DV--DYQLftdSVREELLLGL--------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 2310524600 161 LFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPD 199
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYE 187
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-196 |
2.96e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 123.57 E-value: 2.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQL--YFQHQrniPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIkQLSAKQIA--- 75
Cdd:COG1126 1 MIEIENLhkSFGDL---EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINklr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 76 RQVAYVSQHspqtYQ----YKVLDYVVLGRAAHLGLfgkPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAK 151
Cdd:COG1126 77 RKVGMVFQQ----FNlfphLTVLENVTLAPIKVKKM---SKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2310524600 152 ILVQQPQLILFDEPTSALD---YGNVfktLSLIKGLSHQQFSIIMTTH 196
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDpelVGEV---LDVMRDLAKEGMTMVVVTH 194
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-199 |
5.15e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 122.47 E-value: 5.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIA---RQ 77
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 78 VAYVsqhsPQTYQ----YKVLDYVVLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKIL 153
Cdd:COG2884 81 IGVV----FQDFRllpdRTVYENVALP----LRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2310524600 154 VQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPD 199
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-197 |
2.97e-33 |
|
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: 120.69 E-value: 2.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQL--YFQHQRN-IPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQ---I 74
Cdd:cd03257 1 LLEVKNLsvSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkiR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 75 ARQVAYVSQHsPQTY---QYKVLDYVVLGRAAHLGLFGKPREEDYHLAERALAQLSiRHFADKIYMQMSGGEKQLVNLAK 151
Cdd:cd03257 81 RKEIQMVFQD-PMSSlnpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLP-EEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2310524600 152 ILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQ-QFSIIMTTHN 197
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHD 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-198 |
1.64e-32 |
|
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: 117.10 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQ-RNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAY 80
Cdd:cd03228 1 IEFKNVSFSYPgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQHSPqtyqykvldyvvlgraahlgLFGKpreedyhlaeralaqlSIRhfaDKIymqMSGGEKQLVNLAKILVQQPQLI 160
Cdd:cd03228 81 VPQDPF--------------------LFSG----------------TIR---ENI---LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190
....*....|....*....|....*....|....*...
gi 2310524600 161 LFDEPTSALDYGNVFKTLSLIKGLSHQQfSIIMTTHNP 198
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGK-TVIVIAHRL 155
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-196 |
1.67e-32 |
|
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: 118.84 E-value: 1.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 3 KINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQ---IARQVA 79
Cdd:cd03258 6 NVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkARRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 80 YVSQHspqtyqYKVLD-YVVLGRAAH-LGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQP 157
Cdd:cd03258 86 MIFQH------FNLLSsRTVFENVALpLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2310524600 158 QLILFDEPTSALDYGNVFKTLSLIKGLsHQQF--SIIMTTH 196
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDI-NRELglTIVLITH 199
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-199 |
2.31e-32 |
|
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: 116.73 E-value: 2.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRNiPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQlSAKQIARQVAYV 81
Cdd:cd03230 1 IEVRNLSKRYGKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 82 SQHSPQTYQYKVLDYVVLgraahlglfgkpreedyhlaeralaqlsirhfadkiymqmSGGEKQLVNLAKILVQQPQLIL 161
Cdd:cd03230 79 PEEPSLYENLTVRENLKL----------------------------------------SGGMKQRLALAQALLHDPELLI 118
|
170 180 190
....*....|....*....|....*....|....*...
gi 2310524600 162 FDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPD 199
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILE 156
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-249 |
3.07e-32 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 118.50 E-value: 3.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 24 ELKAGELLTILGANGTGKSTLLNCIAGLLkPKCGEIFLQNKEIKQLSAKQIARQVAYVSQHSPQTYQYKVLDYVVLGRAA 103
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 104 hlglfGKPREEDYHLAERALAQLSIrhfADKIYM---QMSGGEKQLVNLAKILVQ-------QPQLILFDEPTSALDYGN 173
Cdd:PRK03695 97 -----KTRTEAVASALNEVAEALGL---DDKLGRsvnQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310524600 174 VFKTLSLIKGLSHQQFSIIMTTHNpdhpmlLNEVIPNSKVAILTKSGKLH-CGFTEAILTEDNLRELYQTDLRLIDV 249
Cdd:PRK03695 169 QAALDRLLSELCQQGIAVVMSSHD------LNHTLRHADRVWLLKQGKLLaSGRRDEVLTPENLAQVFGVNFRRLDV 239
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
16-199 |
4.99e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 120.25 E-value: 4.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIK-QLSAKQiaRQVAYVSQHspqtyqY--- 91
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRE--RRVGFVFQH------Yalf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 92 ---KVLDYVvlgrAAHLGLFGKPREEdyhLAERALAQLS---IRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEP 165
Cdd:COG1118 88 phmTVAENI----AFGLRVRPPSKAE---IRARVEELLElvqLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 2310524600 166 TSALDYgNVFKTL--SLIKGLSHQQFSIIMTTHNPD 199
Cdd:COG1118 161 FGALDA-KVRKELrrWLRRLHDELGGTTVFVTHDQE 195
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-170 |
7.51e-32 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 117.66 E-value: 7.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQL---YFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKqiaRQ 77
Cdd:COG4525 3 MLTVRHVsvrYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD---RG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 78 VayVSQHSPQTYQYKVLDYVVLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQP 157
Cdd:COG4525 80 V--VFQKDALLPWLNVLDNVAFG----LRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170
....*....|...
gi 2310524600 158 QLILFDEPTSALD 170
Cdd:COG4525 154 RFLLMDEPFGALD 166
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-196 |
3.31e-31 |
|
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: 115.46 E-value: 3.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNiPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQ---IARQ 77
Cdd:COG1127 5 MIEVRNLTKSFGDR-VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyeLRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 78 VAYVSQH----SPQTyqykVLDYVVLGRAAHLGLfgkPREEDYHLAERALAQLSIRHFADKiyM--QMSGGEKQLVNLAK 151
Cdd:COG1127 84 IGMLFQGgalfDSLT----VFENVAFPLREHTDL---SEAEIRELVLEKLELVGLPGAADK--MpsELSGGMRKRVALAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2310524600 152 ILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQ-QFSIIMTTH 196
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTH 200
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
18-235 |
3.54e-31 |
|
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: 115.29 E-value: 3.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQ---IARQVAYVSQHSPQTYQYKVL 94
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrLRRRMGMLFQSGALFDSLTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 95 DYVVLGRAAHLGLfgkPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNV 174
Cdd:cd03261 96 ENVAFPLREHTRL---SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIAS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310524600 175 FKTLSLIKGLS-HQQFSIIMTTHNpdhpmlLNEVIPNS-KVAILTKSGKLHCGFTEAILTEDN 235
Cdd:cd03261 173 GVIDDLIRSLKkELGLTSIMVTHD------LDTAFAIAdRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-233 |
1.10e-30 |
|
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: 115.05 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQI----ARQVAYVSQHSPQTYQYKV 93
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 94 LDYVVLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDygn 173
Cdd:cd03294 120 LENVAFG----LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD--- 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 174 vfktlSLIKG---------LSHQQFSIIMTTHNPDHPMLLNEVIpnskvAILtKSGKL-HCGFTEAILTE 233
Cdd:cd03294 193 -----PLIRRemqdellrlQAELQKTIVFITHDLDEALRLGDRI-----AIM-KDGRLvQVGTPEEILTN 251
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
18-197 |
1.40e-30 |
|
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: 114.37 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQ-VAYvsqhspqTYQ----YK 92
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIAR-------TFQnprlFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 93 ---VLDYVVLGRAAHLGL--------FGKPREEDYHLAERA---LAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQ 158
Cdd:COG0411 93 eltVLENVLVAAHARLGRgllaallrLPRARREEREARERAeelLERVGLADRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2310524600 159 LILFDEPTSALDYGNVFKTLSLIKGLSHQQF-SIIMTTHN 197
Cdd:COG0411 173 LLLLDEPAAGLNPEETEELAELIRRLRDERGiTILLIEHD 212
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-166 |
1.79e-30 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 113.54 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLyfqHQR--NIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQ- 77
Cdd:COG0410 3 MLEVENL---HAGygGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 78 VAYVSQH----SPQTyqykVLDYVVLGRAAH-------------LGLFgkPReedyhLAERaLAQLSirhfadkiyMQMS 140
Cdd:COG0410 80 IGYVPEGrrifPSLT----VEENLLLGAYARrdraevradlervYELF--PR-----LKER-RRQRA---------GTLS 138
|
170 180
....*....|....*....|....*.
gi 2310524600 141 GGEKQLVNLAKILVQQPQLILFDEPT 166
Cdd:COG0410 139 GGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-197 |
2.62e-30 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 114.11 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQHSPQTYQYKVLDY 96
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 97 VVLGRAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVFK 176
Cdd:PRK10575 106 VAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180
....*....|....*....|..
gi 2310524600 177 TLSLIKGLSHQQ-FSIIMTTHN 197
Cdd:PRK10575 186 VLALVHRLSQERgLTVIAVLHD 207
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-196 |
4.62e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 115.17 E-value: 4.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQiaRQVAYVSQhspqtyQY------ 91
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMVFQ------SYalyphm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 92 KVLDYVVLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDY 171
Cdd:COG3839 91 TVYENIAFP----LKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA 166
|
170 180 190
....*....|....*....|....*....|.
gi 2310524600 172 gnvfK----TLSLIKGLsHQQFSI--IMTTH 196
Cdd:COG3839 167 ----KlrveMRAEIKRL-HRRLGTttIYVTH 192
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
18-224 |
4.76e-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: 111.83 E-value: 4.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQlSAKQIARQVAYVSQHSPQTYQYKVLDYV 97
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDELTVREHL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 98 VLgraaHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYG---NV 174
Cdd:cd03263 97 RF----YARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAsrrAI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2310524600 175 FKTLSLIKGLShqqfSIIMTTHNpdhpMLLNEVIPNsKVAILTKsGKLHC 224
Cdd:cd03263 173 WDLILEVRKGR----SIILTTHS----MDEAEALCD-RIAIMSD-GKLRC 212
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-170 |
9.63e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 112.10 E-value: 9.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNiPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKqiaRQVay 80
Cdd:PRK11248 1 MLQISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE---RGV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQHSPQTYQYKVLDYVVLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLI 160
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFG----LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170
....*....|
gi 2310524600 161 LFDEPTSALD 170
Cdd:PRK11248 151 LLDEPFGALD 160
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-199 |
1.26e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 111.00 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRnipLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQiaRQVAY 80
Cdd:COG3840 1 MLRLDDLTYRYGD---FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQ------HspqtyqYKVLDYVVLGRAAHLglfgKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILV 154
Cdd:COG3840 76 LFQennlfpH------LTVAQNIGLGLRPGL----KLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2310524600 155 QQPQLILFDEPTSALDYGNVFKTLSLIKGLSH-QQFSIIMTTHNPD 199
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPE 191
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-208 |
1.57e-29 |
|
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: 116.86 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQH-QRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAY 80
Cdd:COG2274 474 IELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQHsPQTYQYKVLDYVVLGRAAHlglfgkPREEDYHLAERALAQLSIRHFADKIYMQM-------SGGEKQLVNLAKIL 153
Cdd:COG2274 554 VLQD-VFLFSGTIRENITLGDPDA------TDEEIIEAARLAGLHDFIEALPMGYDTVVgeggsnlSGGQRQRLAIARAL 626
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2310524600 154 VQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQfSIIMTTHNPDHPMLLNEVI 208
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLKGR-TVIIIAHRLSTIRLADRII 680
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
17-196 |
2.12e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 111.00 E-value: 2.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEI---KQLSA-----KQIARQVAYVSQHSPQT 88
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQqkgliRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 89 YQYKVLDYVVLGRAAhlgLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSA 168
Cdd:PRK11264 98 PHRTVLENIIEGPVI---VKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180
....*....|....*....|....*...
gi 2310524600 169 LDYGNVFKTLSLIKGLSHQQFSIIMTTH 196
Cdd:PRK11264 175 LDPELVGEVLNTIRQLAQEKRTMVIVTH 202
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-250 |
2.90e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 111.23 E-value: 2.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 21 IDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQHSPQTYQYKVLDYVVLG 100
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 101 RAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVFKTLSL 180
Cdd:PRK10253 106 RYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310524600 181 IKGLSHQQ-FSIIMTTHNpdhpmlLNEVIPNSKVAILTKSGKLHC-GFTEAILTEDNLRELYQTDLRLIDVP 250
Cdd:PRK10253 186 LSELNREKgYTLAAVLHD------LNQACRYASHLIALREGKIVAqGAPKEIVTAELIERIYGLRCMIIDDP 251
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
28-256 |
3.26e-29 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 111.13 E-value: 3.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 28 GELLTILGANGTGKSTLLNCIAGLLKPKCGEIflqnkEIKQLSAKQIARQ--VAYVSQHSPQTYQYKVL--DYVVLGRAA 103
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQALQKnlVAYVPQSEEVDWSFPVLveDVVMMGRYG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 104 HLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVFKTLSLIKG 183
Cdd:PRK15056 108 HMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRE 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310524600 184 LSHQQFSIIMTTHNpdhpmlLNEVIPNSKVAILTKSGKLHCGFTEAILTEDNLRELYQTDLRLIDVPELQRKI 256
Cdd:PRK15056 188 LRDEGKTMLVSTHN------LGSVTEFCDYTVMVKGTVLASGPTETTFTAENLELAFSGVLRHVALNGSEESI 254
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-199 |
6.80e-29 |
|
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: 109.03 E-value: 6.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 6 QLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIA---RQVAYVS 82
Cdd:cd03292 5 NVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 83 QHSPQTYQYKVLDYVVLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILF 162
Cdd:cd03292 85 QDFRLLPDRNVYENVAFA----LEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 2310524600 163 DEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPD 199
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKE 197
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
18-196 |
6.96e-29 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 109.89 E-value: 6.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIK-------QLSA---KQIAR---QVAYVSQH 84
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgELVPadrRQLQRirtRLGMVFQS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 85 ----SPQTyqykVLDYVVlgrAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLI 160
Cdd:COG4598 104 fnlwSHMT----VLENVI---EAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVM 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 2310524600 161 LFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTH 196
Cdd:COG4598 177 LFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-198 |
7.05e-29 |
|
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: 114.48 E-value: 7.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQH-QRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAY 80
Cdd:COG4987 334 LELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQHspqtyqykvldyvvlgraAHL--G------LFGKPR--EEDyhlAERALAQLSIRHFADKIY-----------MQM 139
Cdd:COG4987 414 VPQR------------------PHLfdTtlrenlRLARPDatDEE---LWAALERVGLGDWLAALPdgldtwlgeggRRL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2310524600 140 SGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQfSIIMTTHNP 198
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR-TVLLITHRL 530
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
15-169 |
9.22e-29 |
|
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: 108.68 E-value: 9.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 15 IPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQ-VAYVsqhsPQtyqykv 93
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV----PE------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 94 ldyvvlGRaahlGLFgkPR---EEDYHLAERALAQLSIRHFADKIYM--------------QMSGGEKQLVNLAKILVQQ 156
Cdd:cd03224 83 ------GR----RIF--PEltvEENLLLGAYARRRAKRKARLERVYElfprlkerrkqlagTLSGGEQQMLAIARALMSR 150
|
170
....*....|...
gi 2310524600 157 PQLILFDEPTSAL 169
Cdd:cd03224 151 PKLLLLDEPSEGL 163
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-200 |
1.49e-28 |
|
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: 106.36 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 14 NIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEikqlsakqiarqvayVSQHSPQtyqykv 93
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE---------------VSFASPR------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 94 ldyvvlgRAAHLGlfgkpreedyhlaeralaqlsirhfadkIYM--QMSGGEKQLVNLAKILVQQPQLILFDEPTSALDY 171
Cdd:cd03216 71 -------DARRAG----------------------------IAMvyQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180
....*....|....*....|....*....
gi 2310524600 172 GNVFKTLSLIKGLSHQQFSIIMTTHNPDH 200
Cdd:cd03216 116 AEVERLFKVIRRLRAQGVAVIFISHRLDE 144
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
13-198 |
1.50e-28 |
|
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: 107.70 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 13 RNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIAR----QVAYVSQHspqt 88
Cdd:TIGR03608 9 GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKfrreKLGYLFQN---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 89 yqYKVLDYVVLGRAAHLGLFGK--PREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPT 166
Cdd:TIGR03608 85 --FALIENETVEENLDLGLKYKklSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPT 162
|
170 180 190
....*....|....*....|....*....|..
gi 2310524600 167 SALDYGNVFKTLSLIKGLSHQQFSIIMTTHNP 198
Cdd:TIGR03608 163 GSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP 194
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-199 |
2.21e-28 |
|
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: 112.93 E-value: 2.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYV 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 82 SQHSpqtyqykvldYVVLGR-AAHLgLFGKPREEDYHLaERALAQLSIRHFADKIY-----------MQMSGGEKQLVNL 149
Cdd:COG4988 417 PQNP----------YLFAGTiRENL-RLGRPDASDEEL-EAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLAL 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2310524600 150 AKILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQfSIIMTTHNPD 199
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR-TVILITHRLA 533
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-199 |
3.45e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 108.63 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIK--QLSAKQIARQV 78
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 79 AYVSQHSP-QTYQYKVLDYVVLGrAAHLGLfgkPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQP 157
Cdd:PRK13639 81 GIVFQNPDdQLFAPTVEEDVAFG-PLNLGL---SKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2310524600 158 QLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPD 199
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVD 198
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-251 |
6.49e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 107.77 E-value: 6.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAY 80
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQHSPQTyQYkvldyvvLGRAAHLGL-FGK-----PREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILV 154
Cdd:PRK13644 81 IVFQNPET-QF-------VGRTVEEDLaFGPenlclPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 155 QQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNpdhpmlLNEVIPNSKVAILTKSGKLHCGFTEAILTED 234
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHN------LEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
250
....*....|....*..
gi 2310524600 235 NLRELYQTDLRLIDVPE 251
Cdd:PRK13644 227 SLQTLGLTPPSLIELAE 243
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-198 |
7.08e-28 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 104.99 E-value: 7.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVsqhsPQTYQykvld 95
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL----PQDDE----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 yvvlgraahlgLFGKpreedyhlaeralaqlSIrhfADKIymqMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVF 175
Cdd:cd03246 87 -----------LFSG----------------SI---AENI---LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180
....*....|....*....|...
gi 2310524600 176 KTLSLIKGLSHQQFSIIMTTHNP 198
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHRP 156
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
18-196 |
1.18e-27 |
|
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: 106.17 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQiaRQVAYVSQHSPQTYQYKVLDYV 97
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVFQNYALFPHLTVFENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 98 VLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYgNVFKT 177
Cdd:cd03300 94 AFG----LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL-KLRKD 168
|
170 180
....*....|....*....|..
gi 2310524600 178 LSL-IKGLsHQQFSI--IMTTH 196
Cdd:cd03300 169 MQLeLKRL-QKELGItfVFVTH 189
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-198 |
2.87e-27 |
|
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: 103.78 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPK--CGEIFLQNKeikQLSAKQIARQVAYVSQHspqtyqykv 93
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGR---PLDKRSFRKIIGYVPQD--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 94 ldyvvlgraahlglfgkpreeDYHLAeralaQLSIR---HFADKIyMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALD 170
Cdd:cd03213 91 ---------------------DILHP-----TLTVRetlMFAAKL-RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180
....*....|....*....|....*...
gi 2310524600 171 YGNVFKTLSLIKGLSHQQFSIIMTTHNP 198
Cdd:cd03213 144 SSSALQVMSLLRRLADTGRTIICSIHQP 171
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
14-170 |
2.95e-27 |
|
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: 105.11 E-value: 2.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 14 NIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQiaRQVAYVSQHSPQTYQYKV 93
Cdd:cd03296 14 DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 94 LDYVVlgraahLGLFGKPREEDYHLAERA--------LAQLSirHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEP 165
Cdd:cd03296 92 FDNVA------FGLRVKPRSERPPEAEIRakvhellkLVQLD--WLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
....*
gi 2310524600 166 TSALD 170
Cdd:cd03296 164 FGALD 168
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-225 |
4.07e-27 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 104.66 E-value: 4.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLL---KPKCGEIFLQNKEikqLSAKQIARQVAYVSQHS---PQTYQ 90
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQP---RKPDQFQKCVAYVRQDDillPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 91 YKVLDYVVLGRAAHLGLFGKPREEDYHLAERALAQLSIRHfadKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALD 170
Cdd:cd03234 99 RETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGG---NLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2310524600 171 YGNVFKTLSLIKGLSHQQFSIIMTTHNPDHPM--LLnevipnSKVAILTKSGKLHCG 225
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIHQPRSDLfrLF------DRILLLSSGEIVYSG 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-199 |
4.26e-27 |
|
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: 103.04 E-value: 4.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFqHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSA--KQIARQVA 79
Cdd:cd03229 1 LELKNVSK-RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 80 YVSQHSpqtyqykvldyvvlgraahlGLFgkPReedyhlaeralaqLSIRhfaDKIYMQMSGGEKQLVNLAKILVQQPQL 159
Cdd:cd03229 80 MVFQDF--------------------ALF--PH-------------LTVL---ENIALGLSGGQQQRVALARALAMDPDV 121
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2310524600 160 ILFDEPTSALDYGNVFKTLSLIKGLsHQQF--SIIMTTHNPD 199
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSL-QAQLgiTVVLVTHDLD 162
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-197 |
5.26e-27 |
|
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: 104.16 E-value: 5.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 13 RNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQ-VAYVSQHSPQTYQY 91
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLPQEASIFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 92 KVLDYVvlgrAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDY 171
Cdd:cd03218 91 TVEENI----LAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180
....*....|....*....|....*.
gi 2310524600 172 GNVFKTLSLIKGLSHQQFSIIMTTHN 197
Cdd:cd03218 167 IAVQDIQKIIKILKDRGIGVLITDHN 192
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
15-203 |
5.53e-27 |
|
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: 103.82 E-value: 5.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 15 IPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQHsPQTYQYKVL 94
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQD-VTLFYGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 95 DYVVLG----------RAAHLG-----LFGKPREEDYHLAERAlaqlsirhfadkiyMQMSGGEKQLVNLAKILVQQPQL 159
Cdd:cd03245 96 DNITLGapladderilRAAELAgvtdfVNKHPNGLDLQIGERG--------------RGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2310524600 160 ILFDEPTSALDYGNVFKTLSLIKGLSHQQfSIIMTTHNPdhPML 203
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDK-TLIIITHRP--SLL 202
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-222 |
9.35e-27 |
|
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: 103.95 E-value: 9.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQiaRQVAYVSQHS---PQTYQYKVL 94
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYalfPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 95 DYvvlgraaHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNV 174
Cdd:cd03299 93 AY-------GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2310524600 175 FKTLSLIKGLSHQ-QFSIIMTTHNPDHPMLLNEvipnsKVAILtKSGKL 222
Cdd:cd03299 166 EKLREELKKIRKEfGVTVLHVTHDFEEAWALAD-----KVAIM-LNGKL 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
18-198 |
1.09e-26 |
|
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: 103.41 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGL--LKPKC---GEIFLQNKEIKQLSAKQIA--RQVAYVSQHsPQTYQ 90
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndLIPGApdeGEVLLDGKDIYDLDVDVLElrRRVGMVFQK-PNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 91 YKVLDYVVLGRAAHlGLfgKPREEDYHLAERAL--AQLSiRHFADKIYM-QMSGGEKQLVNLAKILVQQPQLILFDEPTS 167
Cdd:cd03260 95 GSIYDNVAYGLRLH-GI--KLKEELDERVEEALrkAALW-DEVKDRLHAlGLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180 190
....*....|....*....|....*....|.
gi 2310524600 168 ALDYGNVFKTLSLIKGLsHQQFSIIMTTHNP 198
Cdd:cd03260 171 ALDPISTAKIEELIAEL-KKEYTIVIVTHNM 200
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-199 |
2.17e-26 |
|
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: 102.19 E-value: 2.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 22 DLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQnkEIKQLSAKQIARQVAYVSQHSPQTYQYKVLDYVVLGR 101
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN--GVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 102 AAHLGLfgkpREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVFKTLSLI 181
Cdd:cd03298 96 SPGLKL----TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170
....*....|....*....
gi 2310524600 182 KGLSHQ-QFSIIMTTHNPD 199
Cdd:cd03298 172 LDLHAEtKMTVLMVTHQPE 190
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-197 |
5.91e-26 |
|
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: 103.59 E-value: 5.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQL---YFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKC---GEIFLQNKEIKQLSAKQI 74
Cdd:COG0444 1 LLEVRNLkvyFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 75 ----ARQVAYVSQhSPQTY---QYKVLDYVVLGRAAHLGLfgkPREEDYHLAERALAQLSIRHFADKIYM---QMSGGEK 144
Cdd:COG0444 81 rkirGREIQMIFQ-DPMTSlnpVMTVGDQIAEPLRIHGGL---SKAEARERAIELLERVGLPDPERRLDRyphELSGGMR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2310524600 145 QLVNLAKILVQQPQLILFDEPTSALDygnVfkT-----LSLIKGLSHQ-QFSIIMTTHN 197
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALD---V--TiqaqiLNLLKDLQRElGLAILFITHD 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
7-199 |
6.52e-26 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 101.36 E-value: 6.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 7 LYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKE----IKQLSAKQI----ARQV 78
Cdd:COG4778 16 LHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQASPREIlalrRRTI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 79 AYVSQHspqtyqYKV------LDyVVLGRAAHLGLfgkPREEDYHLAERALAQLSIRH---------FadkiymqmSGGE 143
Cdd:COG4778 96 GYVSQF------LRViprvsaLD-VVAEPLLERGV---DREEARARARELLARLNLPErlwdlppatF--------SGGE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2310524600 144 KQLVNLAKILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPD 199
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEE 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
16-171 |
6.90e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 104.26 E-value: 6.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQiaRQVAYVSQHSPQTYQYKVLD 95
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RHVNTVFQSYALFPHMTVFE 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310524600 96 YVVLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDY 171
Cdd:PRK09452 106 NVAFG----LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY 177
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-198 |
7.32e-26 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 100.51 E-value: 7.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLsAKQIARQVAYVSqHSPQTYQykvld 95
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-RDEPHENILYLG-HLPGLKP----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 yvVLGRAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVF 175
Cdd:TIGR01189 87 --ELSALENLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|...
gi 2310524600 176 KTLSLIKGLSHQQFSIIMTTHNP 198
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLTTHQD 187
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-199 |
7.79e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.62 E-value: 7.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIkQLSAKQIA--RQV 78
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMklRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 79 AYVSQHSP--QTYQYKVLDYVVLGrAAHLGLfgkPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQ 156
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFG-AVNLKL---PEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2310524600 157 PQLILFDEPTSALDYGNVFKTLSLIKGLSHQ-QFSIIMTTHNPD 199
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDID 203
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-207 |
1.15e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.11 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQ-IARQVAYVSQH----SPQTyqyk 92
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGMVHQHfmlvPNLT---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 93 VLDYVVLGRAAHLGLFGKPREedyhlAERALAQLSIR-HFA---DKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSA 168
Cdd:COG3845 97 VAENIVLGLEPTKGGRLDRKA-----ARARIRELSERyGLDvdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2310524600 169 L-----DygNVFKTLsliKGLSHQQFSIIMTTHNpdhpmlLNEV 207
Cdd:COG3845 172 LtpqeaD--ELFEIL---RRLAAEGKSIIFITHK------LREV 204
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-197 |
1.91e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.93 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLY---FQHQRN-IPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIAR 76
Cdd:COG1101 1 MLELKNLSktfNPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 77 QVAYVSQhSPQtyqykvldyvvLGRAAHL----------------GL-FGKPREEDYHLAERaLAQLSIrHFADKIYMQM 139
Cdd:COG1101 81 YIGRVFQ-DPM-----------MGTAPSMtieenlalayrrgkrrGLrRGLTKKRRELFREL-LATLGL-GLENRLDTKV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310524600 140 ---SGGEKQLVNLAKILVQQPQLILFDEPTSALDYgnvfKTLSLIKGLSHQ-----QFSIIMTTHN 197
Cdd:COG1101 147 gllSGGQRQALSLLMATLTKPKLLLLDEHTAALDP----KTAALVLELTEKiveenNLTTLMVTHN 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-202 |
2.04e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 102.47 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 3 KINQlYFQHQRnipLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQiaRQVAYVS 82
Cdd:PRK10851 7 NIKK-SFGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 83 QHSPQTYQYKVLDYVVLGraahlgLFGKPREEDYHLAE------RALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQ 156
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFG------LTVLPRRERPNAAAikakvtQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2310524600 157 PQLILFDEPTSALDyGNVFKTL-SLIKGLsHQQ--FSIIMTTHNPDHPM 202
Cdd:PRK10851 155 PQILLLDEPFGALD-AQVRKELrRWLRQL-HEElkFTSVFVTHDQEEAM 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-198 |
3.00e-25 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 99.10 E-value: 3.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAkQIARQVAYVSQHSPQTYQYKVLDY 96
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLGHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 97 VVLGRAAHlglfgkpreeDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVFK 176
Cdd:cd03231 94 LRFWHADH----------SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|..
gi 2310524600 177 TLSLIKGLSHQQFSIIMTTHNP 198
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTHQD 185
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-207 |
3.06e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.56 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQ-IARQVAYVSQH---SPQ-Tyqyk 92
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQElnlVPNlS---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 93 VLDYVVLGR-AAHLGLFGKPREedYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDY 171
Cdd:COG1129 96 VAENIFLGRePRRGGLIDWRAM--RRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTE 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 2310524600 172 GNVFKTLSLIKGLSHQQFSIIMTTHNpdhpmlLNEV 207
Cdd:COG1129 174 REVERLFRIIRRLKAQGVAIIYISHR------LDEV 203
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
18-204 |
5.04e-25 |
|
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: 98.48 E-value: 5.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQiaRQVAYVSQHSPQTYQYKVLDYV 97
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNYALYPHMTVYDNI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 98 VLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVFKT 177
Cdd:cd03301 94 AFG----LKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQM 169
|
170 180
....*....|....*....|....*...
gi 2310524600 178 LSLIKGLSHQ-QFSIIMTTHNPDHPMLL 204
Cdd:cd03301 170 RAELKRLQQRlGTTTIYVTHDQVEAMTM 197
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-223 |
6.68e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 99.70 E-value: 6.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQH-QRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAY 80
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQhSP--QTYQYKVLDYVVLGRAAHlglfGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQ 158
Cdd:PRK13635 86 VFQ-NPdnQFVGATVQDDVAFGLENI----GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310524600 159 LILFDEPTSALDYGNVFKTLSLIKGLSHQQ-FSIIMTTHNpdhpmlLNEVIPNSKVAILTKsGKLH 223
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKgITVLSITHD------LDEAAQADRVIVMNK-GEIL 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
18-170 |
1.05e-24 |
|
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: 98.27 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIAR----QVAYVSQhSPQ-----T 88
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARlrarHVGFVFQ-SFQllptlT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 89 yqykVLDYVVLGraahLGLFGKPREEDyhLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSA 168
Cdd:COG4181 107 ----ALENVMLP----LELAGRRDARA--RARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGN 176
|
..
gi 2310524600 169 LD 170
Cdd:COG4181 177 LD 178
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
18-200 |
1.15e-24 |
|
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: 97.74 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIkqlsAKQIARQVAYVSQHSPQTYQYKVLDYV 97
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLPEERGLYPKMKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 98 V-LGRaahlgLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVFK 176
Cdd:cd03269 92 VyLAQ-----LKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVEL 166
|
170 180
....*....|....*....|....
gi 2310524600 177 TLSLIKGLSHQQFSIIMTTHNPDH 200
Cdd:cd03269 167 LKDVIRELARAGKTVILSTHQMEL 190
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-196 |
1.47e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.16 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 4 INQLYFQHQrnipLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEI---KQLSAKQIA---RQ 77
Cdd:COG4161 8 INCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRllrQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 78 VAYVSQhspqtyQY------KVLDYVVlgrAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAK 151
Cdd:COG4161 84 VGMVFQ------QYnlwphlTVMENLI---EAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2310524600 152 ILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTH 196
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTH 199
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
18-197 |
1.60e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.18 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQiaRQVAYVSQhspqtyQYKVLDYV 97
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQ------SYALFPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 98 VLGRAAHLGL--FGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDyGNVF 175
Cdd:PRK11432 94 SLGENVGYGLkmLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD-ANLR 172
|
170 180
....*....|....*....|....*
gi 2310524600 176 KTL-SLIKGLsHQQFSI--IMTTHN 197
Cdd:PRK11432 173 RSMrEKIREL-QQQFNItsLYVTHD 196
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
8-196 |
2.09e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 98.12 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 8 YFQHQrnipLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAK------------QIA 75
Cdd:PRK10619 15 YGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 76 R-QVAYVSQHSPQTYQYKVLDYVVLGRAAHLGLfgkPREEDYHLAERALAQLSIRHFADKIY-MQMSGGEKQLVNLAKIL 153
Cdd:PRK10619 91 RtRLTMVFQHFNLWSHMTVLENVMEAPIQVLGL---SKQEARERAVKYLAKVGIDERAQGKYpVHLSGGQQQRVSIARAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2310524600 154 VQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTH 196
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTH 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-199 |
3.37e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 97.77 E-value: 3.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQrNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIA--RQV 78
Cdd:PRK13638 1 MLATSDLWFRYQ-DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 79 AYVSQHSPQTYQYKVLDYVVlgrAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQ 158
Cdd:PRK13638 80 ATVFQDPEQQIFYTDIDSDI---AFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2310524600 159 LILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPD 199
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDID 197
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-170 |
5.77e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 98.33 E-value: 5.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 4 INQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIA---RQVAY 80
Cdd:PRK11153 7 ISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRkarRQIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQH----SPQTyqykVLDYVVLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQ 156
Cdd:PRK11153 87 IFQHfnllSSRT----VFDNVALP----LELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170
....*....|....
gi 2310524600 157 PQLILFDEPTSALD 170
Cdd:PRK11153 159 PKVLLCDEATSALD 172
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-170 |
6.20e-24 |
|
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: 100.05 E-value: 6.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQHsPQTYQYKVLD 95
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQH-PFLFAGTIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 YVVLGRaahlglfgkpREEDYHLAERALAQLSIRHFADKIYMQ-----------MSGGEKQLVNLAKILVQQPQLILFDE 164
Cdd:TIGR02857 415 NIRLAR----------PDASDAEIREALERAGLDEFVAALPQGldtpigeggagLSGGQAQRLALARAFLRDAPLLLLDE 484
|
....*.
gi 2310524600 165 PTSALD 170
Cdd:TIGR02857 485 PTAHLD 490
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-250 |
8.55e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 96.60 E-value: 8.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNI-PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVA 79
Cdd:PRK13632 7 MIKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 80 YVSQHSpqtyqykvlDYVVLGRAAH----LGLFGK--PREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKIL 153
Cdd:PRK13632 87 IIFQNP---------DNQFIGATVEddiaFGLENKkvPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 154 VQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQF-SIIMTTHNpdhpmlLNEVIPNSKVAILTKSGKLHCGFTEAILT 232
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHD------MDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
250
....*....|....*...
gi 2310524600 233 EDNLRELYQtdlrlIDVP 250
Cdd:PRK13632 232 NKEILEKAK-----IDSP 244
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-208 |
1.05e-23 |
|
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: 95.61 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKqiaRQVAYvsqhspQTYQY----KV 93
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD---RMVVF------QNYSLlpwlTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 94 LDYVVLgrAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALD--- 170
Cdd:TIGR01184 72 RENIAL--AVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDalt 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 2310524600 171 YGNVFKTLSLIKGLSHqqFSIIMTTHNPDHPMLLNEVI 208
Cdd:TIGR01184 150 RGNLQEELMQIWEEHR--VTVLMVTHDVDEALLLSDRV 185
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-170 |
1.34e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.86 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFqHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKP--KC-GEIFLQNKEIKQLSAKQiaRQ 77
Cdd:COG4136 1 MLSLENLTI-TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafSAsGEVLLNGRRLTALPAEQ--RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 78 VAYVSQHSPQTYQYKVLDYVVLGRAAHLGlfgkpREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQP 157
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFALPPTIG-----RAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170
....*....|...
gi 2310524600 158 QLILFDEPTSALD 170
Cdd:COG4136 153 RALLLDEPFSKLD 165
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
16-196 |
1.44e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 95.54 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAK--QIARQVAYVSQhspQTY---Q 90
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDerLIRQEAGMVFQ---QFYlfpH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 91 YKVLDYVVLGRaahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALD 170
Cdd:PRK09493 92 LTALENVMFGP---LRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180
....*....|....*....|....*.
gi 2310524600 171 YGNVFKTLSLIKGLSHQQFSIIMTTH 196
Cdd:PRK09493 169 PELRHEVLKVMQDLAEEGMTMVIVTH 194
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
9-170 |
1.94e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 98.70 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 9 FQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQhspqt 88
Cdd:COG1132 347 FSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQ----- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 89 yqykvlDYVVLGR--AAHLgLFGKP---REEDYHLAERALAQLSIRHFADKIY-------MQMSGGEKQLVNLAKILVQQ 156
Cdd:COG1132 422 ------DTFLFSGtiRENI-RYGRPdatDEEVEEAAKAAQAHEFIEALPDGYDtvvgergVNLSGGQRQRIAIARALLKD 494
|
170
....*....|....
gi 2310524600 157 PQLILFDEPTSALD 170
Cdd:COG1132 495 PPILILDEATSALD 508
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-199 |
2.02e-23 |
|
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: 94.28 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 21 IDLELKaGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLqNKEIKQLSAKQI-----ARQVAYVSQHS---PQTYQYK 92
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL-NGTVLFDSRKKInlppqQRKIGLVFQQYalfPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 93 VLDYvvlgraahlGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYG 172
Cdd:cd03297 95 NLAF---------GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180
....*....|....*....|....*....
gi 2310524600 173 NVFKTLSLIKGLsHQQFSI--IMTTHNPD 199
Cdd:cd03297 166 LRLQLLPELKQI-KKNLNIpvIFVTHDLS 193
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-214 |
2.32e-23 |
|
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: 97.10 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 21 IDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLqNKEIKQLSAKQI-----ARQVAYVSQHSPQTYQYKVLD 95
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVL-NGRTLFDSRKGIflppeKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 YVVLGRAAHLGLFGKPREEdyhlaeRALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVF 175
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFE------RVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2310524600 176 KTLSLIKGLS-HQQFSIIMTTHNPDHPMLLNE---VIPNSKVA 214
Cdd:TIGR02142 169 EILPYLERLHaEFGIPILYVSHSLQEVLRLADrvvVLEDGRVA 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-208 |
3.70e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.01 E-value: 3.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNiPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAY 80
Cdd:PRK10247 7 LLQLQNVGYLAGDA-KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQhSPQTYQYKVLDYVVLGRAahlgLFGKPREEDYHLAEraLAQLSI-RHFADKIYMQMSGGEKQLVNLAKILVQQPQL 159
Cdd:PRK10247 86 CAQ-TPTLFGDTVYDNLIFPWQ----IRNQQPDPAIFLDD--LERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2310524600 160 ILFDEPTSALDYGNVFKTLSLIKGL-SHQQFSIIMTTHNPDHPMLLNEVI 208
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINHADKVI 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-170 |
3.75e-23 |
|
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: 94.21 E-value: 3.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 3 KINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVS 82
Cdd:cd03254 4 EFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 83 QhSPQTYQYKVLDYVVLGRAahlglfGKPREEDYHLAERALAQLSIRHFADKIYMQM-------SGGEKQLVNLAKILVQ 155
Cdd:cd03254 84 Q-DTFLFSGTIMENIRLGRP------NATDEEVIEAAKEAGAHDFIMKLPNGYDTVLgenggnlSQGERQLLAIARAMLR 156
|
170
....*....|....*
gi 2310524600 156 QPQLILFDEPTSALD 170
Cdd:cd03254 157 DPKILILDEATSNID 171
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-198 |
4.75e-23 |
|
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: 97.82 E-value: 4.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYV 81
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 82 SQhSPQTYQYKVLDYVVLGRAahlglfGKPREEDYHLAERA-LAQLsIRHFADKIYMQM-------SGGEKQLVNLAKIL 153
Cdd:TIGR02868 415 AQ-DAHLFDTTVRENLRLARP------DATDEELWAALERVgLADW-LRALPDGLDTVLgeggarlSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2310524600 154 VQQPQLILFDEPTSALDYGNVFKTLS-LIKGLSHQqfSIIMTTHNP 198
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEdLLAALSGR--TVVLITHHL 530
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-255 |
4.90e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.54 E-value: 4.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEI--FLQNKEIKQLS----------------------AKQ 73
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTkekekvleklviqktrfkkikkIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 74 IARQVAYVSQHSP-QTYQYKVLDYVVLGRAAhlglFGKPREEDYhlaERALAQLSI----RHFADKIYMQMSGGEKQLVN 148
Cdd:PRK13651 103 IRRRVGVVFQFAEyQLFEQTIEKDIIFGPVS----MGVSKEEAK---KRAAKYIELvgldESYLQRSPFELSGGQKRRVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 149 LAKILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPDHpmllneVIPNSKVAILTKSGKL-HCGFT 227
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDN------VLEWTKRTIFFKDGKIiKDGDT 249
|
250 260 270
....*....|....*....|....*....|
gi 2310524600 228 EAILTEDN-LRELYQTDLRLID-VPELQRK 255
Cdd:PRK13651 250 YDILSDNKfLIENNMEPPKLLNfVNKLEKK 279
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-256 |
7.22e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.48 E-value: 7.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAY 80
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQHSP-QTYQYKVLDYVVLGrAAHLGLfgkPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQL 159
Cdd:PRK13652 83 VFQNPDdQIFSPTVEQDIAFG-PINLGL---DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 160 ILFDEPTSALDYGNVFKTLSLIKGLSHQQ-FSIIMTTHNPDhpmLLNEVIpnSKVAILTKSGKLHCGFTEAILTEDNLre 238
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYgMTVIFSTHQLD---LVPEMA--DYIYVMDKGRIVAYGTVEEIFLQPDL-- 231
|
250
....*....|....*...
gi 2310524600 239 LYQTDLRLIDVPELQRKI 256
Cdd:PRK13652 232 LARVHLDLPSLPKLIRSL 249
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-233 |
7.97e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.42 E-value: 7.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNIPL----LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKP-----KCGEIFLQNKEiKQLSA 71
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPtegkvTVGDIVVSSTS-KQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 72 KQIARQVAYVSQH-SPQTYQYKVLDYVVLGRAAhlglFGKPREEDYHLAERALAQLSI-RHFADKIYMQMSGGEKQLVNL 149
Cdd:PRK13643 80 KPVRKKVGVVFQFpESQLFEETVLKDVAFGPQN----FGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 150 AKILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHnpdhpmLLNEVIPNSK-VAILTKSGKLHCGFTE 228
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH------LMDDVADYADyVYLLEKGHIISCGTPS 229
|
....*
gi 2310524600 229 AILTE 233
Cdd:PRK13643 230 DVFQE 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-170 |
8.56e-23 |
|
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: 93.37 E-value: 8.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 14 NIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQhSPQTYQYKV 93
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQ-EPVLFDGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 94 LDYVVLGRaahlglFGKPREEDYHLAERALAQLSIRHFADKIY-------MQMSGGEKQLVNLAKILVQQPQLILFDEPT 166
Cdd:cd03249 94 AENIRYGK------PDATDEEVEEAAKKANIHDFIMSLPDGYDtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
....
gi 2310524600 167 SALD 170
Cdd:cd03249 168 SALD 171
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-197 |
9.21e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 93.59 E-value: 9.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 11 HQRNIplLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAK-----QIARQVAYvsqhs 85
Cdd:PRK11247 23 GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDtrlmfQDARLLPW----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 86 pqtyqYKVLDYVvlgraaHLGLFGKPREEdyhlAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEP 165
Cdd:PRK11247 96 -----KKVIDNV------GLGLKGQWRDA----ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190
....*....|....*....|....*....|...
gi 2310524600 166 TSALDYGNVFKTLSLIKGLSHQQ-FSIIMTTHN 197
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHgFTVLLVTHD 193
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-208 |
9.94e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.03 E-value: 9.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNI--PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQV 78
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 79 AYVSQH-SPQTYQYKVLDYVVLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQP 157
Cdd:PRK13650 84 GMVFQNpDNQFVGATVEDDVAFG----LENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2310524600 158 QLILFDEPTSALDYGNVFKTLSLIKGLSHQ-QFSIIMTTHNPDHPMLLNEVI 208
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVL 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-170 |
1.35e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.29 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEikqlsakqiarQVAYVSQHSPQTYQYKVLD 95
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 YVVLG------------RAAHLGLFGKPREEDYHL----------------AERALAQLSI-RHFADKIYMQMSGGEKQL 146
Cdd:COG0488 81 TVLDGdaelraleaeleELEAKLAEPDEDLERLAElqeefealggweaearAEEILSGLGFpEEDLDRPVSELSGGWRRR 160
|
170 180
....*....|....*....|....
gi 2310524600 147 VNLAKILVQQPQLILFDEPTSALD 170
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLD 184
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-197 |
1.36e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 92.78 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQ-VAYVSQHSPQTYQYKVLDY 96
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIGYLPQEASIFRKLTVEDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 97 VvlgRAAhLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVFK 176
Cdd:COG1137 99 I---LAV-LELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVAD 174
|
170 180
....*....|....*....|.
gi 2310524600 177 TLSLIKGLSHQQFSIIMTTHN 197
Cdd:COG1137 175 IQKIIRHLKERGIGVLITDHN 195
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-199 |
1.51e-22 |
|
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: 94.78 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINqlyFQHQRNIPLLNgIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLqNKEIKQLSAKQI-----A 75
Cdd:COG4148 2 MLEVD---FRLRRGGFTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRL-GGEVLQDSARGIflpphR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 76 RQVAYVSQHS---PqtyQYKV---LDYvvlgraahlGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNL 149
Cdd:COG4148 77 RRIGYVFQEArlfP---HLSVrgnLLY---------GRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAI 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2310524600 150 AKILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLsHQQFSI--IMTTHNPD 199
Cdd:COG4148 145 GRALLSSPRLLLMDEPLAALDLARKAEILPYLERL-RDELDIpiLYVSHSLD 195
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
18-196 |
2.21e-22 |
|
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: 91.49 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGeLLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQlSAKQIARQVAYVSQH---SPQTYQYKVL 94
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEfgvYPNFTVREFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 95 DYVVLgraahlgLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNV 174
Cdd:cd03264 94 DYIAW-------LKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEER 166
|
170 180
....*....|....*....|..
gi 2310524600 175 FKTLSLIKGLShQQFSIIMTTH 196
Cdd:cd03264 167 IRFRNLLSELG-EDRIVILSTH 187
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-251 |
2.26e-22 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 92.97 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNIpLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKC--------GEIFLQNKEIKQLSAK 72
Cdd:PRK13547 1 MLTADHLHVARRHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 73 QIARQVAYVSQHSPQTYQYKVLDYVVLGRAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKI 152
Cdd:PRK13547 80 RLARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 153 LVQ---------QPQLILFDEPTSALDYGNVFKTLSLIKGLSHQ-QFSIIMTTHNPD----HPmllnevipnSKVAILTK 218
Cdd:PRK13547 160 LAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNlaarHA---------DRIAMLAD 230
|
250 260 270
....*....|....*....|....*....|...
gi 2310524600 219 SGKLHCGFTEAILTEDNLRELYQTDLRLIDVPE 251
Cdd:PRK13547 231 GAIVAHGAPADVLTPAHIARCYGFAVRLVDAGD 263
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-196 |
2.66e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 92.00 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 4 INQLYFQHQrnipLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEI---KQLSAKQIA---RQ 77
Cdd:PRK11124 8 INCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRelrRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 78 VAYVSQhspqtyQYK------VLDYVVLGRAAHLGLfgkPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAK 151
Cdd:PRK11124 84 VGMVFQ------QYNlwphltVQQNLIEAPCRVLGL---SKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2310524600 152 ILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTH 196
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTH 199
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
16-170 |
4.30e-22 |
|
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: 91.59 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQHSPQTYQYKVLD 95
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPHMTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 YVVLgraaHLGLFGKPREEdyhLAERA-----LAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALD 170
Cdd:cd03295 95 NIAL----VPKLLKWPKEK---IRERAdellaLVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-199 |
5.38e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.18 E-value: 5.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQrNIPLLngIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQiaRQVAY 80
Cdd:PRK10771 1 MLKLTDITWLYH-HLPMR--FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQHSPQTYQYKVLDYVVLGRAAHLGLFGKPREEDYHLAEralaQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLI 160
Cdd:PRK10771 76 LFQENNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIAR----QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2310524600 161 LFDEPTSALDYGNVFKTLSLIKGLSHQ-QFSIIMTTHNPD 199
Cdd:PRK10771 152 LLDEPFSALDPALRQEMLTLVSQVCQErQLTLLMVSHSLE 191
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-197 |
7.43e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 91.65 E-value: 7.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRNIPL----LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEI--KQLSAKQIA 75
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 76 RQVAYVSQHSP-QTYQYKVLDYVVLGrAAHLGLfgkPREEDYHLAERA--LAQLSIRHFADKIYMQMSGGEKQLVNLAKI 152
Cdd:PRK13637 83 KKVGLVFQYPEyQLFEETIEKDIAFG-PINLGL---SEEEIENRVKRAmnIVGLDYEDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2310524600 153 LVQQPQLILFDEPTSALDYGNVFKTLSLIKGLsHQQF--SIIMTTHN 197
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKEL-HKEYnmTIILVSHS 204
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-196 |
7.50e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 92.45 E-value: 7.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQL---YFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQI--A 75
Cdd:COG1135 1 MIELENLsktFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 76 RQ-VAYVSQH----SPQTyqykVLDYVvlgrAAHLGLFGKPREEdyhLAERALAQLSIRHFADKIYM---QMSGGEKQLV 147
Cdd:COG1135 81 RRkIGMIFQHfnllSSRT----VAENV----ALPLEIAGVPKAE---IRKRVAELLELVGLSDKADAypsQLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2310524600 148 NLAKILVQQPQLILFDEPTSALDYgnvfKT----LSLIKGLsHQQF--SIIMTTH 196
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDP----ETtrsiLDLLKDI-NRELglTIVLITH 199
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
17-216 |
7.56e-22 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 89.89 E-value: 7.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKC--GEIFLQNKEIKQLSAKQIARQVAYVSQHSPQTYQ-YKV 93
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVteGEILFKGEDITDLPPEERARLGIFLAFQYPPEIPgVKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 94 LDYVvlgRAAHLGLfgkpreedyhlaeralaqlsirhfadkiymqmSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGN 173
Cdd:cd03217 95 ADFL---RYVNEGF--------------------------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2310524600 174 VFKTLSLIKGLSHQQFSIIMTTHnpdHPMLLNEVIPNsKVAIL 216
Cdd:cd03217 140 LRLVAEVINKLREEGKSVLIITH---YQRLLDYIKPD-RVHVL 178
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
16-197 |
7.60e-22 |
|
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: 90.80 E-value: 7.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQ-VAYVSQHSPQTYQYKVL 94
Cdd:TIGR04406 15 KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLgIGYLPQEASIFRKLTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 95 DYV--VLGRAAHLglfgkPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYG 172
Cdd:TIGR04406 95 ENImaVLEIRKDL-----DRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPI 169
|
170 180
....*....|....*....|....*
gi 2310524600 173 NVFKTLSLIKGLSHQQFSIIMTTHN 197
Cdd:TIGR04406 170 AVGDIKKIIKHLKERGIGVLITDHN 194
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-208 |
2.79e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.81 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNIPL-LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVA 79
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 80 YVSQHSPQTYQYKVLDYVVlgrAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQL 159
Cdd:PRK13648 87 IVFQNPDNQFVGSIVKYDV---AFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2310524600 160 ILFDEPTSALDYGNVFKTLSLIKGL-SHQQFSIIMTTHNPDHPMLLNEVI 208
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAMEADHVI 213
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-170 |
4.32e-21 |
|
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: 88.68 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQHsPQTYQYKVLD 95
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQE-PVLFARSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 YVVlgraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYM-------QMSGGEKQLVNLAKILVQQPQLILFDEPTSA 168
Cdd:cd03248 107 NIA------YGLQSCSFECVKEAAQKAHAHSFISELASGYDTevgekgsQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
..
gi 2310524600 169 LD 170
Cdd:cd03248 181 LD 182
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
18-196 |
4.32e-21 |
|
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: 88.20 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQlSAKQIARQVAYVSqhspqtyQYKVLDYV 97
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVF-------QDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 98 VLGR---AAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNV 174
Cdd:cd03265 88 LTGWenlYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180
....*....|....*....|...
gi 2310524600 175 FKTLSLIKGLSHQQ-FSIIMTTH 196
Cdd:cd03265 168 AHVWEYIEKLKEEFgMTILLTTH 190
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-199 |
9.46e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 91.32 E-value: 9.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 4 INQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARqvaYVSQ 83
Cdd:PRK10535 10 IRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ---LRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 84 HSPQTYQ-YKVLDYVVLGR-----AAHLGLFGKPREEdyhlaeRALAQLSIRHFADKIYM---QMSGGEKQLVNLAKILV 154
Cdd:PRK10535 87 HFGFIFQrYHLLSHLTAAQnvevpAVYAGLERKQRLL------RAQELLQRLGLEDRVEYqpsQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2310524600 155 QQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPD 199
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQ 205
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-256 |
1.98e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 87.91 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRNIPL----LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEI----KQLSAKQ 73
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 74 IARQVAYVSQH-SPQTYQYKVLDYVVLGRAAhlglFGKPREEDYHLAERALAQLSI-RHFADKIYMQMSGGEKQLVNLAK 151
Cdd:PRK13646 83 VRKRIGMVFQFpESQLFEDTVEREIIFGPKN----FKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 152 ILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQF-SIIMTTHNpdhpmlLNEVIPNSKVAILTKSGKlhcgfteaI 230
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENkTIILVSHD------MNEVARYADEVIVMKEGS--------I 224
|
250 260 270
....*....|....*....|....*....|...
gi 2310524600 231 LTEDNLRELYQTDLRL----IDVPE---LQRKI 256
Cdd:PRK13646 225 VSQTSPKELFKDKKKLadwhIGLPEivqLQYDF 257
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-254 |
2.95e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.10 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYV 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 82 SQH-SPQTYQYKVLDYVVLGrAAHLGLFGKPREEDyhlAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLI 160
Cdd:PRK13647 85 FQDpDDQVFSSTVWDDVAFG-PVNMGLDKDEVERR---VEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 161 LFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPDHPMLLNEVIpnskvaILTKSGKLHCGFTEAILTEDNLREly 240
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQV------IVLKEGRVLAEGDKSLLTDEDIVE-- 232
|
250 260
....*....|....*....|.
gi 2310524600 241 QTDLRL-------IDVPELQR 254
Cdd:PRK13647 233 QAGLRLplvaqifEDLPELGQ 253
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-197 |
3.31e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.41 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIA----RQVAYVsqhspqtYQYK 92
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFI-------YQFH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 93 VL--DYVVLGRAAHLGLFG-KPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSAL 169
Cdd:PRK11629 97 HLlpDFTALENVAMPLLIGkKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180
....*....|....*....|....*....
gi 2310524600 170 DYGNVFKTLSLIKGLSHQQ-FSIIMTTHN 197
Cdd:PRK11629 177 DARNADSIFQLLGELNRLQgTAFLVVTHD 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
18-197 |
4.18e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 85.70 E-value: 4.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIA---RQVAYVSQHSPQTYQYKVL 94
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrRQIGMIFQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 95 DYVvlgrAAHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNV 174
Cdd:PRK10908 98 DNV----AIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180
....*....|....*....|...
gi 2310524600 175 FKTLSLIKGLSHQQFSIIMTTHN 197
Cdd:PRK10908 174 EGILRLFEEFNRVGVTVLMATHD 196
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-196 |
4.18e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.11 E-value: 4.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSA----KQIARQVAYVSQH-SPQTYQ 90
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGLVFQFpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 91 YKVLDYVVLGRAAhlglFGKPREEDYHLAERALAQLSI-RHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSAL 169
Cdd:PRK13649 101 ETVLKDVAFGPQN----FGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180
....*....|....*....|....*..
gi 2310524600 170 DYGNVFKTLSLIKGLSHQQFSIIMTTH 196
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
4.42e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.60 E-value: 4.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLY--FQHQRNIPL--LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQN------------- 63
Cdd:PRK13631 21 ILRVKNLYcvFDEKQENELvaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 64 -----KEIKQlsAKQIARQVAYVSQHSP-QTYQYKVLDYVVLGRAAhlglFGKPREEDYHLAERALAQLSIRH-FADKIY 136
Cdd:PRK13631 101 tnpysKKIKN--FKELRRRVSMVFQFPEyQLFKDTIEKDIMFGPVA----LGVKKSEAKKLAKFYLNKMGLDDsYLERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 137 MQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPDHPM-LLNEVIPNSKVAI 215
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLeVADEVIVMDKGKI 254
|
250
....*....|....*..
gi 2310524600 216 LTKSGKLHCGFTEAILT 232
Cdd:PRK13631 255 LKTGTPYEIFTDQHIIN 271
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-198 |
6.16e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 6.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 14 NIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAkqiARQVAYVSQHSPQTYQYKV 93
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEACHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 94 LDYVVLGRAahlgLFGKPREEdyhlAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGN 173
Cdd:PRK13539 91 AENLEFWAA----FLGGEELD----IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180
....*....|....*....|....*
gi 2310524600 174 VFKTLSLIKGLSHQQFSIIMTTHNP 198
Cdd:PRK13539 163 VALFAELIRAHLAQGGIVIAATHIP 187
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-196 |
8.43e-20 |
|
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: 83.90 E-value: 8.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQH-QRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSaKQIARQVAY 80
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQhspqtyqykvldyvvlgrAAHLglfgkpreedyhlaeralaqlsirhFADKIY----MQMSGGEKQLVNLAKILVQQ 156
Cdd:cd03247 80 LNQ------------------RPYL-------------------------FDTTLRnnlgRRFSGGERQRLALARILLQD 116
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2310524600 157 PQLILFDEPTSALDYGNVFKTLSLIkgLSH-QQFSIIMTTH 196
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLI--FEVlKDKTLIWITH 155
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
17-198 |
8.94e-20 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 88.40 E-value: 8.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKC--GEIFLQNKEIkqlsAKQIARQVAYVSQHS---PQTYQY 91
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP----TKQILKRTGFVTQDDilyPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 92 KVLDYVVLGRAAHlglfGKPREEDYHLAERALAQLSIRHFADKIYMQ-----MSGGEKQLVNLAKILVQQPQLILFDEPT 166
Cdd:PLN03211 159 ETLVFCSLLRLPK----SLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190
....*....|....*....|....*....|..
gi 2310524600 167 SALDYGNVFKTLSLIKGLSHQQFSIIMTTHNP 198
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMHQP 266
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-220 |
1.21e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 85.62 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAK---QIARQVAYVSQH-SPQTYQY 91
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKtvwDIREKVGIVFQNpDNQFVGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 92 KVLDYVVLGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDY 171
Cdd:PRK13640 101 TVGDDVAFG----LENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2310524600 172 GNVFKTLSLIKGLSHQ-QFSIIMTTHNPDHPMLLNEVIPNSKVAILTKSG 220
Cdd:PRK13640 177 AGKEQILKLIRKLKKKnNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-216 |
1.92e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 84.35 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQ-HQRNIplLNGIDLELKAGELLTILGANGTGKSTLLNCIAGllKPKC----GEIFLQNKEIKQLSAKQIAR 76
Cdd:COG0396 1 LEIKNLHVSvEGKEI--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG--HPKYevtsGSILLDGEDILELSPDERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 77 QVAYVSqhspqtYQY-------KVLDYVvlgRAAHlglfGKPREEDYHLAE------RALAQLSIrhfaDKIYMQ----- 138
Cdd:COG0396 77 AGIFLA------FQYpveipgvSVSNFL---RTAL----NARRGEELSAREflkllkEKMKELGL----DEDFLDryvne 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 139 -MSGGEKQLVNLAKILVQQPQLILFDEPTSALDYgNVFKTLS-LIKGLSHQQFSIIMTTHnpdHPMLLNEVIPNsKVAIL 216
Cdd:COG0396 140 gFSGGEKKRNEILQMLLLEPKLAILDETDSGLDI-DALRIVAeGVNKLRSPDRGILIITH---YQRILDYIKPD-FVHVL 214
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
14-170 |
4.65e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 86.31 E-value: 4.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 14 NIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQhSPQTYQYKV 93
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQ-EPVLFSGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 94 LDYVVlgraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYM-------QMSGGEKQLVNLAKILVQQPQLILFDEPT 166
Cdd:TIGR00958 572 RENIA------YGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTevgekgsQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
....
gi 2310524600 167 SALD 170
Cdd:TIGR00958 646 SALD 649
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-182 |
5.35e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.01 E-value: 5.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEikqlsakqiarQVAY 80
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-----------RVLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQHSpqtyqykvldYVVLGRAAHLGLFGKPREE--DYHLAErALAQLSIRHFADKIYMQ------MSGGEKQLVNLAKI 152
Cdd:COG4178 431 LPQRP----------YLPLGTLREALLYPATAEAfsDAELRE-ALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARL 499
|
170 180 190
....*....|....*....|....*....|
gi 2310524600 153 LVQQPQLILFDEPTSALDYGNVFKTLSLIK 182
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLR 529
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-240 |
5.43e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.00 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYfQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQ-VA 79
Cdd:PRK11614 5 MLSFDKVS-AHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 80 YVSQHSPQTYQYKVLDYVVLGraahlGLFGKprEEDYHLAERALAQLSIRHFADKIYM--QMSGGEKQLVNLAKILVQQP 157
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMG-----GFFAE--RDQFQERIKWVYELFPRLHERRIQRagTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 158 QLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPDHPMLLNE---VIPNSKVaILTKSGklhcgftEAILTED 234
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADrgyVLENGHV-VLEDTG-------DALLANE 228
|
....*.
gi 2310524600 235 NLRELY 240
Cdd:PRK11614 229 AVRSAY 234
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-196 |
7.12e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 81.92 E-value: 7.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQrNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEI-KQLSAKQiaRQVA 79
Cdd:PRK13540 1 MLDVIELDFDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQ--KQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 80 YVSQHSpqtyqykvldyvvlGRAAHLGLfgkpREE---DYHLAERALA------QLSIRHFADKIYMQMSGGEKQLVNLA 150
Cdd:PRK13540 78 FVGHRS--------------GINPYLTL----RENclyDIHFSPGAVGitelcrLFSLEHLIDYPCGLLSSGQKRQVALL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2310524600 151 KILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTH 196
Cdd:PRK13540 140 RLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-249 |
7.63e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.60 E-value: 7.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQR--NIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQV 78
Cdd:PRK13642 4 ILEVENLVFKYEKesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 79 AYVSQHSPQTY-QYKVLDYVVLGRAAHlglfGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQP 157
Cdd:PRK13642 84 GMVFQNPDNQFvGATVEDDVAFGMENQ----GIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 158 QLILFDEPTSALD---YGNVFKTLSLIKGLSHqqFSIIMTTHNpdhpmlLNEVIPNSKVAILtKSGKlhcgfteaILTED 234
Cdd:PRK13642 160 EIIILDESTSMLDptgRQEIMRVIHEIKEKYQ--LTVLSITHD------LDEAASSDRILVM-KAGE--------IIKEA 222
|
250
....*....|....*
gi 2310524600 235 NLRELYQTDLRLIDV 249
Cdd:PRK13642 223 APSELFATSEDMVEI 237
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-170 |
7.65e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.12 E-value: 7.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 19 NGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQ-VAYVSQHSPQTYQYKVLDYV 97
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMgVVRTFQHVRLFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 98 VLGRAAHL------GLFGKP--REEDYHLAERA---LAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPT 166
Cdd:PRK11300 102 LVAQHQQLktglfsGLLKTPafRRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
....
gi 2310524600 167 SALD 170
Cdd:PRK11300 182 AGLN 185
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-206 |
9.05e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.48 E-value: 9.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKP---KCGEIFLQNKEIkqlSAKQIARQVAYVSQHSPQTYQYKV 93
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 94 LDYVVLgrAAHLGLFGK-PREEDYHLAERALAQLSIRHFADKIYMQ------MSGGEKQLVNLAKILVQQPQLILFDEPT 166
Cdd:TIGR00955 117 REHLMF--QAHLRMPRRvTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2310524600 167 SALDYGNVFKTLSLIKGLSHQQFSIIMTTHNP--------DHPMLLNE 206
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPsselfelfDKIILMAE 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-193 |
9.44e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.07 E-value: 9.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQ-IARQVAYVS----------QH 84
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPedrkgeglvlDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 85 SpqtyqykVLD---YVVLGRAAHLGLFGKPREEDyhLAERALAQLSIR-HFADKIYMQMSGGEKQLVNLAKILVQQPQLI 160
Cdd:COG1129 346 S-------IREnitLASLDRLSRGGLLDRRRERA--LAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190
....*....|....*....|....*....|...
gi 2310524600 161 LFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIM 193
Cdd:COG1129 417 ILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIV 449
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-240 |
9.51e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.63 E-value: 9.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 21 IDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQ-VAYVSQHSPQTYQYKVLDYVVL 99
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEASIFRRLSVYDNLMA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 100 GRAAHLGLFGKPREEDyhlAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVFKTLS 179
Cdd:PRK10895 102 VLQIRDDLSAEQREDR---ANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKR 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310524600 180 LIKGLSHQQFSIIMTTHNpdhpmlLNEVIPNSKVAILTKSGKLHC-GFTEAILTEDNLRELY 240
Cdd:PRK10895 179 IIEHLRDSGLGVLITDHN------VRETLAVCERAYIVSQGHLIAhGTPTEILQDEHVKRVY 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-170 |
1.01e-18 |
|
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: 82.28 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 5 NQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQH 84
Cdd:cd03253 4 ENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 85 SP---QTYQYKVLdyvvlgraahlglFGKP---REEDYHLAERALAQLSIRHFADKiY--------MQMSGGEKQLVNLA 150
Cdd:cd03253 84 TVlfnDTIGYNIR-------------YGRPdatDEEVIEAAKAAQIHDKIMRFPDG-YdtivgergLKLSGGEKQRVAIA 149
|
170 180
....*....|....*....|
gi 2310524600 151 KILVQQPQLILFDEPTSALD 170
Cdd:cd03253 150 RAILKNPPILLLDEATSALD 169
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
7-171 |
1.68e-18 |
|
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: 81.76 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 7 LYFQHQRNIPL-LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQHS 85
Cdd:cd03252 6 VRFRYKPDGPViLDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 86 pQTYQYKVLDYVVLGRAahlglfGKPREEDYHLAERALAQLSIRHFADKiYMQM--------SGGEKQLVNLAKILVQQP 157
Cdd:cd03252 86 -VLFNRSIRDNIALADP------GMSMERVIEAAKLAGAHDFISELPEG-YDTIvgeqgaglSGGQRQRIAIARALIHNP 157
|
170
....*....|....
gi 2310524600 158 QLILFDEPTSALDY 171
Cdd:cd03252 158 RILIFDEATSALDY 171
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-206 |
1.80e-18 |
|
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: 84.41 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQHspqtyqykvld 95
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQD----------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 yVVL--GR-AAHLGLFGKPREEDYHLAeralAQLS-----IRHFADKiY--------MQMSGGEKQLVNLAKILVQQPQL 159
Cdd:COG4618 415 -VELfdGTiAENIARFGDADPEKVVAA----AKLAgvhemILRLPDG-YdtrigeggARLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2310524600 160 ILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNP------DHPMLLNE 206
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPsllaavDKLLVLRD 541
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-198 |
1.85e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.00 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNIpLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAkQIARQVAY 80
Cdd:PRK13538 1 MLEARNLACERDERI-LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 vsqhspqtyqykvldyvvLGRAA--------------HLGLFGKPREEDyhlAERALAQLSIRHFADKIYMQMSGGEKQL 146
Cdd:PRK13538 79 ------------------LGHQPgikteltalenlrfYQRLHGPGDDEA---LWEALAQVGLAGFEDVPVRQLSAGQQRR 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 147 VNLAKILVQQPQLILFDEPTSALDYGNVfKTLslikglsHQQFS--------IIMTTHNP 198
Cdd:PRK13538 138 VALARLWLTRAPLWILDEPFTAIDKQGV-ARL-------EALLAqhaeqggmVILTTHQD 189
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-170 |
2.07e-18 |
|
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: 81.51 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 15 IPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQhspQTYQYK-- 92
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQ---DVFLFNdt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 93 VLDYVVLGRaahlglFGKPREEDYHLAERALAQLSIRHFADKiY--------MQMSGGEKQLVNLAKILVQQPQLILFDE 164
Cdd:cd03251 92 VAENIAYGR------PGATREEVEEAARAANAHEFIMELPEG-YdtvigergVKLSGGQRQRIAIARALLKDPPILILDE 164
|
....*.
gi 2310524600 165 PTSALD 170
Cdd:cd03251 165 ATSALD 170
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-208 |
3.02e-18 |
|
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: 78.64 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRNiPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKeikqlsakqiarqvayv 81
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 82 sqhspqtyqykvldyvvlgraahlglfgkpreedyhlaeralaqLSIRHFAdkiymQMSGGEKQLVNLAKILVQQPQLIL 161
Cdd:cd03221 63 --------------------------------------------VKIGYFE-----QLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2310524600 162 FDEPTSALDYGNVfktLSLIKGLSHQQFSIIMTTHnpDHpMLLNEVI 208
Cdd:cd03221 94 LDEPTNHLDLESI---EALEEALKEYPGTVILVSH--DR-YFLDQVA 134
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-187 |
3.29e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.66 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIA---RQVAYVSQHSPQTY--QYK 92
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafrRDIQMVFQDSISAVnpRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 93 VLDYVvlgRAAHLGLFGKPREEDYHLAERALAQLSIR-HFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDY 171
Cdd:PRK10419 108 VREII---REPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170
....*....|....*.
gi 2310524600 172 GNVFKTLSLIKGLSHQ 187
Cdd:PRK10419 185 VLQAGVIRLLKKLQQQ 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-170 |
4.97e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.19 E-value: 4.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLqnkeikqlsAKQIarQVAYVSQHSPQ-TYQYKVL 94
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL---------GETV--KIGYFDQHQEElDPDKTVL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 95 DYVVLGR--------AAHLGLFGKPREEdyhlaeralAQLSIRHFadkiymqmSGGEKQLVNLAKILVQQPQLILFDEPT 166
Cdd:COG0488 398 DELRDGApggteqevRGYLGRFLFSGDD---------AFKPVGVL--------SGGEKARLALAKLLLSPPNVLLLDEPT 460
|
....
gi 2310524600 167 SALD 170
Cdd:COG0488 461 NHLD 464
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-196 |
5.22e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 81.29 E-value: 5.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRN-----IPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIA 75
Cdd:PRK13633 4 MIKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 76 RQVAYVSQHSP--QTYQYKVLDYVVLGrAAHLGLfgkPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKIL 153
Cdd:PRK13633 84 RNKAGMVFQNPdnQIVATIVEEDVAFG-PENLGI---PPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2310524600 154 VQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQ-FSIIMTTH 196
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgITIILITH 203
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-236 |
6.97e-18 |
|
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: 82.57 E-value: 6.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKC--GEIFLQNKEIKQLSAKQIARQ-VAYVSQHSPQTYQYKVL 94
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 95 DYVVLGRAAHLGLFGKPREEDYHLAERALAQLSIRHFAD-KIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGN 173
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310524600 174 VFKTLSLIKGLSHQQFSIIMTTHNpdhpmlLNEVIPNSKVAILTKSGKlHCGFTEA-ILTEDNL 236
Cdd:TIGR02633 177 TEILLDIIRDLKAHGVACVYISHK------LNEVKAVCDTICVIRDGQ-HVATKDMsTMSEDDI 233
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-197 |
9.52e-18 |
|
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: 79.33 E-value: 9.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQ---RNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIflqnkEIKQLSAKQIARQ 77
Cdd:cd03266 1 MITADALTKRFRdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA-----TVDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 78 V-AYVSQHSPQTYQYKVLDyvvlGRAaHLGLFG-----KPREEDYHLAERAlAQLSIRHFADKIYMQMSGGEKQLVNLAK 151
Cdd:cd03266 76 ArRRLGFVSDSTGLYDRLT----ARE-NLEYFAglyglKGDELTARLEELA-DRLGMEELLDRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2310524600 152 ILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHN 197
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHI 195
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-196 |
1.35e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 81.69 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 4 INQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVsQ 83
Cdd:PRK10790 343 IDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV-Q 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 84 HSPQTYQYKVLDYVVLGRAAhlglfgkPREEDYHLAERA-LAQLsIRHFADKIYMQ-------MSGGEKQLVNLAKILVQ 155
Cdd:PRK10790 422 QDPVVLADTFLANVTLGRDI-------SEEQVWQALETVqLAEL-ARSLPDGLYTPlgeqgnnLSVGQKQLLALARVLVQ 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2310524600 156 QPQLILFDEPTSALDYGN---VFKTLSLIKglshQQFSIIMTTH 196
Cdd:PRK10790 494 TPQILILDEATANIDSGTeqaIQQALAAVR----EHTTLVVIAH 533
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-242 |
1.81e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 79.19 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 14 NIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGL--LKPKC---GEIFLQNKEIKQLSAKQIARQVAYVSQHSPQT 88
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEArvsGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 89 YQYKVLDYVVLGraAHLGLFGKPREEDYHLAERAL--AQL--SIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDE 164
Cdd:PRK14247 95 PNLSIFENVALG--LKLNRLVKSKKELQERVRWALekAQLwdEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 165 PTSALDYGNVFKTLSLIKGLShQQFSIIMTTHNPDHPMLLNEVipnskVAILTKSGKLHCGFTEAILT--EDNLRELYQT 242
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELK-KDMTIVLVTHFPQQAARISDY-----VAFLYKGQIVEWGPTREVFTnpRHELTEKYVT 246
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
10-198 |
1.84e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.67 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 10 QHQRNIplLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLS----AKQIARQVAYVSQHS 85
Cdd:PRK10584 20 EHELSI--LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearAKLRAKHVGFVFQSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 86 PQTYQYKVLDYVVLGRAahlgLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEP 165
Cdd:PRK10584 98 MLIPTLNALENVELPAL----LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|....
gi 2310524600 166 TSALDYGNVFKTLSLIKGLSHQQ-FSIIMTTHNP 198
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREHgTTLILVTHDL 207
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-197 |
1.88e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.31 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRNiPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCG-------EIFLQNKEIKQLSAKQI 74
Cdd:PRK14258 8 IKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEvrvegrvEFFNQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 75 ARQVAYVSQhSPQTYQYKVLDYVVLGraahLGLFG-KPREEDYHLAERAL--AQL--SIRHFADKIYMQMSGGEKQLVNL 149
Cdd:PRK14258 87 RRQVSMVHP-KPNLFPMSVYDNVAYG----VKIVGwRPKLEIDDIVESALkdADLwdEIKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2310524600 150 AKILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLS-HQQFSIIMTTHN 197
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHN 210
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-193 |
2.10e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 81.25 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 21 IDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQ-IARQVAYVSQHSPQT--YQYKVLDYV 97
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRQSSglYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 98 VLGRAAH-LGLFGKPREEDYHLaERALAQLSIR-HFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVF 175
Cdd:PRK15439 362 VCALTHNrRGFWIKPARENAVL-ERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
170
....*....|....*...
gi 2310524600 176 KTLSLIKGLSHQQFSIIM 193
Cdd:PRK15439 441 DIYQLIRSIAAQNVAVLF 458
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-208 |
2.33e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.29 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 3 KINQLYFQHQRniplLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLK----PKCgEIFLQNKEIKQlsAKQIAR-- 76
Cdd:PRK09984 9 KLAKTFNQHQA----LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGS-HIELLGRTVQR--EGRLARdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 77 -----QVAYVSQHSPQTYQYKVLDYVVLGRAAHLGLFGK-----PREEDYHlAERALAQLSIRHFADKIYMQMSGGEKQL 146
Cdd:PRK09984 82 rksraNTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTcfswfTREQKQR-ALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310524600 147 VNLAKILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQ-FSIIMTTHNPDHPMLLNEVI 208
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgITVVVTLHQVDYALRYCERI 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-207 |
3.07e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 80.74 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLkPKC---GEIF-----LQNKEIKQLSAKQIA---RQVAYVSQHSp 86
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIfegeeLQASNIRDTERAGIAiihQELALVKELS- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 87 qtyqykVLDYVVLGRA-AHLGLFGKPREedYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEP 165
Cdd:PRK13549 99 ------VLENIFLGNEiTPGGIMDYDAM--YLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2310524600 166 TSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNpdhpmlLNEV 207
Cdd:PRK13549 171 TASLTESETAVLLDIIRDLKAHGIACIYISHK------LNEV 206
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-197 |
3.23e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 78.66 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCI--AGLLKPKC---GEIFLQNKEI--KQLSAKQIARQVAYVSQHsPQTYQ 90
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVtitGSIVYNGHNIysPRTDTVDLRKEIGMVFQQ-PNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 91 YKVLDYVVLGraahLGLFG-KPREEDYHLAERALAQLSI-RHFADKIY---MQMSGGEKQLVNLAKILVQQPQLILFDEP 165
Cdd:PRK14239 100 MSIYENVVYG----LRLKGiKDKQVLDEAVEKSLKGASIwDEVKDRLHdsaLGLSGGQQQRVCIARVLATSPKIILLDEP 175
|
170 180 190
....*....|....*....|....*....|....*
gi 2310524600 166 TSALD---YGNVFKTLSLIKglshQQFSIIMTTHN 197
Cdd:PRK14239 176 TSALDpisAGKIEETLLGLK----DDYTMLLVTRS 206
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-200 |
4.21e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.00 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQlsakQIARQVAYVsqhsPQT---YQ-YKV 93
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIGYL----PEErglYPkMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 94 LDYVV-LGRaahlgLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYG 172
Cdd:COG4152 89 GEQLVyLAR-----LKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPV 163
|
170 180
....*....|....*....|....*...
gi 2310524600 173 NVFKTLSLIKGLSHQQFSIIMTTHNPDH 200
Cdd:COG4152 164 NVELLKDVIRELAAKGTTVIFSSHQMEL 191
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-197 |
5.33e-17 |
|
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: 76.74 E-value: 5.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRN----IPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKeikqlsakqiarq 77
Cdd:cd03250 1 ISVEDASFTWDSGeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 78 VAYVSQhSPQTYQYKVLDYVvlgraahlgLFGKP-REEDYHLAERALA---QLSIRHFADKIY-----MQMSGGEKQLVN 148
Cdd:cd03250 68 IAYVSQ-EPWIQNGTIRENI---------LFGKPfDEERYEKVIKACAlepDLEILPDGDLTEigekgINLSGGQKQRIS 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2310524600 149 LAKILVQQPQLILFDEPTSALDyGNVFKTL--SLIKGLSHQQFSIIMTTHN 197
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVD-AHVGRHIfeNCILGLLLNNKTRILVTHQ 187
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
21-237 |
8.52e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 78.72 E-value: 8.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 21 IDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQiaRQVAYVSQhspqtyQYKVLDYVVLG 100
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMMFQ------SYALFPHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 101 RAAHLGLFGK--PREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVFK-T 177
Cdd:PRK11607 110 QNIAFGLKQDklPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRmQ 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 178 LSLIKGLSHQQFSIIMTTHNPDHPMLLnevipNSKVAILTKSGKLHCGFTEAILTEDNLR 237
Cdd:PRK11607 190 LEVVDILERVGVTCVMVTHDQEEAMTM-----AGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-252 |
1.01e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 78.92 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 23 LELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIA----RQVAYVSQHSPQTYQYKVLDYVV 98
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 99 LGraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDygNVFKTL 178
Cdd:PRK10070 129 FG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD--PLIRTE 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310524600 179 ---SLIKGLSHQQFSIIMTTHNPDHPMLLNEvipnsKVAILTKSGKLHCGFTEAILTeDNLRELYQTDLRLIDVPEL 252
Cdd:PRK10070 203 mqdELVKLQAKHQRTIVFISHDLDEAMRIGD-----RIAIMQNGEVVQVGTPDEILN-NPANDYVRTFFRGVDISQV 273
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
18-197 |
1.29e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.13 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGL--LKPKC---GEIFLQNKEI--KQLSAKQIARQVAYVSQhSPQTYQ 90
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQ-KPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 91 YKVLDYVVLGrAAHLGLFGKPREedyhLAERALAQLSI-RHFADKIYMQ---MSGGEKQLVNLAKILVQQPQLILFDEPT 166
Cdd:PRK14243 105 KSIYDNIAYG-ARINGYKGDMDE----LVERSLRQAALwDEVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190
....*....|....*....|....*....|.
gi 2310524600 167 SALDYGNVFKTLSLIKGLShQQFSIIMTTHN 197
Cdd:PRK14243 180 SALDPISTLRIEELMHELK-EQYTIIIVTHN 209
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
21-170 |
2.26e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.76 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 21 IDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQiaRQVAYVSQhSPQTYQY-KVLDYVVL 99
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQ-SYALYPHlSVAENMSF 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310524600 100 GraahLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALD 170
Cdd:PRK11000 99 G----LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-193 |
4.24e-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: 74.01 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQ-IARQVAYVSQhspqtyqykvlDy 96
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPE-----------D- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 97 vvlgRAAHlGLFGkpreedyhlaERALAQ-LSIRHFadkiymqMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVF 175
Cdd:cd03215 84 ----RKRE-GLVL----------DLSVAEnIALSSL-------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170
....*....|....*...
gi 2310524600 176 KTLSLIKGLSHQQFSIIM 193
Cdd:cd03215 142 EIYRLIRELADAGKAVLL 159
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-197 |
5.11e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.17 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQ-HQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAY 80
Cdd:PRK11160 339 LTLNNVSFTyPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQhspqtyqyKVldYVVLGRAAHLGLFGKPREEDYHLAErALAQLSIRHFAD-----KIYM-----QMSGGEKQLVNLA 150
Cdd:PRK11160 419 VSQ--------RV--HLFSATLRDNLLLAAPNASDEALIE-VLQQVGLEKLLEddkglNAWLgeggrQLSGGEQRRLGIA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2310524600 151 KILVQQPQLILFDEPTSALDYGNVFKTLSLIkgLSH-QQFSIIMTTHN 197
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELL--AEHaQNKTVLMITHR 533
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-199 |
5.95e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 75.64 E-value: 5.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEI------KQLsaKQIARQVAYVSQHSP-QTYQ 90
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgnKNL--KKLRKKVSLVFQFPEaQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 91 YKVLDYVVLGRAAhlglFGKPREEDYHLAERALAQLSIRH-FADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSAL 169
Cdd:PRK13641 101 NTVLKDVEFGPKN----FGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190
....*....|....*....|....*....|
gi 2310524600 170 DYGNVFKTLSLIKGLSHQQFSIIMTTHNPD 199
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAGHTVILVTHNMD 206
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
12-193 |
8.40e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.51 E-value: 8.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 12 QRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKC-GEIFLQNKEIK-QLSAKQIARQVAYVS----QHS 85
Cdd:PRK13549 272 NPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKiRNPQQAIAQGIAMVPedrkRDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 86 --PQTYQYKVLDYVVLGRAAHLGLFGKPREEDYhlAERALAQLSIR--HFADKIyMQMSGGEKQLVNLAKILVQQPQLIL 161
Cdd:PRK13549 352 ivPVMGVGKNITLAALDRFTGGSRIDDAAELKT--ILESIQRLKVKtaSPELAI-ARLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190
....*....|....*....|....*....|..
gi 2310524600 162 FDEPTSALDYGNVFKTLSLIKGLSHQQFSIIM 193
Cdd:PRK13549 429 LDEPTRGIDVGAKYEIYKLINQLVQQGVAIIV 460
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-196 |
9.47e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.42 E-value: 9.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLkPKCGEIFLQNKEIKQLSAKQIARQVAYVSQhSPQTYQYKVLD 95
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQ-NPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 YVVLGRaahlglfgkPREEDYHLaERALAQLSIRHFADK--------IYMQM---SGGEKQLVNLAKILVQQPQLILFDE 164
Cdd:PRK11174 442 NVLLGN---------PDASDEQL-QQALENAWVSEFLPLlpqgldtpIGDQAaglSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190
....*....|....*....|....*....|..
gi 2310524600 165 PTSALDYGNVFKTLSLIKGLSHQQfSIIMTTH 196
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASRRQ-TTLMVTH 542
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-208 |
1.04e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.04 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQN-------KEIKQLsaKQIARQVAYVSQHSP-QTY 89
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEV--KRLRKEIGLVFQFPEyQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 90 QYKVLDYVVLGrAAHLGlfgKPREEDYHLAERALAQLSI-RHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSA 168
Cdd:PRK13645 105 QETIEKDIAFG-PVNLG---ENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2310524600 169 L------DYGNVFKTLSlikglSHQQFSIIMTTHNPDHPM-LLNEVI 208
Cdd:PRK13645 181 LdpkgeeDFINLFERLN-----KEYKKRIIMVTHNMDQVLrIADEVI 222
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-197 |
1.12e-15 |
|
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: 74.33 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 26 KAGELLTILGANGTGKSTLLNCIAGLLKPKCG---------EIF-------LQNKEIKQLSAK-QIARQVAYVSQhSPQT 88
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILdefrgseLQNYFTKLLEGDvKVIVKPQYVDL-IPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 89 YQYKVLDyvVLGRAAHLGLFgkpreedyhlaERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSA 168
Cdd:cd03236 103 VKGKVGE--LLKKKDERGKL-----------DELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180
....*....|....*....|....*....
gi 2310524600 169 LDYGNVFKTLSLIKGLSHQQFSIIMTTHN 197
Cdd:cd03236 170 LDIKQRLNAARLIRELAEDDNYVLVVEHD 198
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-204 |
1.23e-15 |
|
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: 72.19 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEikqlsakqiarQVAYV 81
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-----------DLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 82 SQHSpqtyqykvldYVVLGRaahlglfgkpreedyhLAEralaQLsirhfadkIY---MQMSGGEKQLVNLAKILVQQPQ 158
Cdd:cd03223 70 PQRP----------YLPLGT----------------LRE----QL--------IYpwdDVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2310524600 159 LILFDEPTSALDYGNVFKTLSLIKGLShqqFSIIMTTHNPD----HPMLL 204
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKELG---ITVISVGHRPSlwkfHDRVL 158
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-260 |
1.25e-15 |
|
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: 76.59 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIkQLSAKQIARQVAYVSQHSPQTYQYKVLD 95
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 YVVLgraaHLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALD-YGNV 174
Cdd:TIGR01257 1023 HILF----YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDpYSRR 1098
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 175 FKTLSLIKGLSHQqfSIIMTTHNPDHPMLLNEvipnsKVAILTKsGKLHCGFTEAILTEDNLRELYQTDLRLIDVPELQR 254
Cdd:TIGR01257 1099 SIWDLLLKYRSGR--TIIMSTHHMDEADLLGD-----RIAIISQ-GRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQR 1170
|
....*.
gi 2310524600 255 KICAIT 260
Cdd:TIGR01257 1171 GGCEGT 1176
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-170 |
1.30e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 75.26 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQiaRQVAY 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQH---SPQTYQYKVLDYvvlgraahlGL--FGKPREEdyhLAER---ALAQLSIRHFADKIYMQMSGGEKQLVNLAKI 152
Cdd:PRK11650 81 VFQNyalYPHMSVRENMAY---------GLkiRGMPKAE---IEERvaeAARILELEPLLDRKPRELSGGQRQRVAMGRA 148
|
170
....*....|....*...
gi 2310524600 153 LVQQPQLILFDEPTSALD 170
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLD 166
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-196 |
1.84e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 75.54 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQ-IARQVAYVSQHSPQTYQYKVLDY 96
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 97 VVLGRAAHLGLFgKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVFK 176
Cdd:PRK10982 94 MWLGRYPTKGMF-VDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNH 172
|
170 180
....*....|....*....|
gi 2310524600 177 TLSLIKGLSHQQFSIIMTTH 196
Cdd:PRK10982 173 LFTIIRKLKERGCGIVYISH 192
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-195 |
1.97e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.59 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 19 NGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSA-KQIARQVAYVSQHSPQT--------- 88
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITESRRDNgffpnfsia 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 89 YQYKVLDYVVLGR-AAHLGLFGKPREEDYHLAERALAQLSIrHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTS 167
Cdd:PRK09700 360 QNMAISRSLKDGGyKGAMGLFHEVDEQRTAENQRELLALKC-HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180
....*....|....*....|....*...
gi 2310524600 168 ALDYGNVFKTLSLIKGLSHQQFSIIMTT 195
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLADDGKVILMVS 466
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-197 |
2.07e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 73.53 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGL--LKPKC---GEIFLQNKEI--KQLSAKQIARQVAYVSQHS---PQ 87
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGEDIydPDVDVVELRRRVGMVFQKPnpfPK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 88 TyqykVLDYVVLGraahLGLFG-KPREEDYHLAERALaqlsiRHFA------DKIY---MQMSGGEKQLVNLAKILVQQP 157
Cdd:COG1117 107 S----IYDNVAYG----LRLHGiKSKSELDEIVEESL-----RKAAlwdevkDRLKksaLGLSGGQQQRLCIARALAVEP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2310524600 158 QLILFDEPTSALDYGNVFKTLSLIKGLShQQFSIIMTTHN 197
Cdd:COG1117 174 EVLLMDEPTSALDPISTAKIEELILELK-KDYTIVIVTHN 212
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
17-197 |
3.16e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.84 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIflqnkeikqlsAKQIARQVAYVSQ--HSPQTYQYKVL 94
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQklYLDTTLPLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 95 DYVVLgraahlglfgKPREEDYHLAErALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNV 174
Cdd:PRK09544 88 RFLRL----------RPGTKKEDILP-ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|....
gi 2310524600 175 FKTLSLIKGLSHQ-QFSIIMTTHN 197
Cdd:PRK09544 157 VALYDLIDQLRRElDCAVLMVSHD 180
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-170 |
3.19e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 74.00 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIA---RQVAYVSQHSpqtyqYKVL 94
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRplrRRMQMVFQDP-----YASL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 95 D-----YVVLGRAahLGLFG-KPREEdyhLAERALAQLSI----RHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDE 164
Cdd:COG4608 109 NprmtvGDIIAEP--LRIHGlASKAE---RRERVAELLELvglrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDE 183
|
....*.
gi 2310524600 165 PTSALD 170
Cdd:COG4608 184 PVSALD 189
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-196 |
4.46e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.44 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQ-VAYVSQHSPQTYQYKVLDY 96
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 97 VVLGRAAHLGLFGKPREEDYHLAERA---LAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGN 173
Cdd:PRK09700 101 LYIGRHLTKKVCGVNIIDWREMRVRAammLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKE 180
|
170 180
....*....|....*....|...
gi 2310524600 174 VFKTLSLIKGLSHQQFSIIMTTH 196
Cdd:PRK09700 181 VDYLFLIMNQLRKEGTAIVYISH 203
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
11-171 |
5.26e-15 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 74.39 E-value: 5.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 11 HQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQHSpQTYQ 90
Cdd:TIGR01846 466 APDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQEN-VLFS 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 91 YKVLDYVVLGRAahlglfGKPREEDYHLAERALAQ---LSIRHFADKIYMQ----MSGGEKQLVNLAKILVQQPQLILFD 163
Cdd:TIGR01846 545 RSIRDNIALCNP------GAPFEHVIHAAKLAGAHdfiSELPQGYNTEVGEkganLSGGQRQRIAIARALVGNPRILIFD 618
|
....*...
gi 2310524600 164 EPTSALDY 171
Cdd:TIGR01846 619 EATSALDY 626
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
20-196 |
6.05e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 72.27 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 20 GIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNK-----EIKQLSAKQ---IAR-QVAYVSQHSPQTYQ 90
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAErrrLLRtEWGFVHQHPRDGLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 91 YKV---------LdyVVLGrAAHlglFGKPREEdyhlAERALAQLSIRhfADKI---YMQMSGGEKQLVNLAKILVQQPQ 158
Cdd:PRK11701 104 MQVsaggnigerL--MAVG-ARH---YGDIRAT----AGDWLERVEID--AARIddlPTTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 2310524600 159 LILFDEPTSALDYGNVFKTLSLIKGLSHQ-QFSIIMTTH 196
Cdd:PRK11701 172 LVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTH 210
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-197 |
6.26e-15 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 74.13 E-value: 6.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 20 GIDLELKagelLTILGANGTGKSTLLNCIAGLLKPKCGEIFLqnkeikqlSAKQiarQVAYVSQH---------SPQTYQ 90
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVFR--------SAKV---RMAVFSQHhvdgldlssNPLLYM 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 91 YKVLDYVVLGR-AAHLGLFGKPReedyHLAERALAQLSirhfadkiymqmsGGEKQLVNLAKILVQQPQLILFDEPTSAL 169
Cdd:PLN03073 596 MRCFPGVPEQKlRAHLGSFGVTG----NLALQPMYTLS-------------GGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
170 180
....*....|....*....|....*...
gi 2310524600 170 DYGNVfktLSLIKGLSHQQFSIIMTTHN 197
Cdd:PLN03073 659 DLDAV---EALIQGLVLFQGGVLMVSHD 683
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-188 |
6.60e-15 |
|
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: 71.14 E-value: 6.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 13 RNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKC---GEIFLQNKEIKQLsAKQIARQVAYVSqhspqty 89
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEF-AEKYPGEIIYVS------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 90 qykvldyvvlgraahlglfgkprEEDYHLAERALAQL---SIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPT 166
Cdd:cd03233 90 -----------------------EEDVHFPTLTVRETldfALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180
....*....|....*....|..
gi 2310524600 167 SALDYGNVFKTLSLIKGLSHQQ 188
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADVL 168
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
13-196 |
1.13e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 70.65 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 13 RN-IPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQlsaKQIARQVAYVSqHSPQTYQy 91
Cdd:PRK13543 21 RNeEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYLG-HLPGLKA- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 92 kvlDYVVLGRAAHL-GLFG-KPREedyhLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSAL 169
Cdd:PRK13543 96 ---DLSTLENLHFLcGLHGrRAKQ----MPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
170 180
....*....|....*....|....*..
gi 2310524600 170 DYGNVFKTLSLIKGLSHQQFSIIMTTH 196
Cdd:PRK13543 169 DLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-198 |
1.19e-14 |
|
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: 70.35 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIA-----GLLKpkcGEIFLQNKEIKqlsaKQIARQVAYVSQ---HSPQ 87
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktaGVIT---GEILINGRPLD----KNFQRSTGYVEQqdvHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 88 TYQYKVLDYVVLGRAahlglfgkpreedyhlaeralaqLSIRHfadkiymqmsggeKQLVNLAKILVQQPQLILFDEPTS 167
Cdd:cd03232 94 LTVREALRFSALLRG-----------------------LSVEQ-------------RKRLTIGVELAAKPSILFLDEPTS 137
|
170 180 190
....*....|....*....|....*....|.
gi 2310524600 168 ALDYGNVFKTLSLIKGLSHQQFSIIMTTHNP 198
Cdd:cd03232 138 GLDSQAAYNIVRFLKKLADSGQAILCTIHQP 168
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-210 |
1.56e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.21 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQhQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAG-----LLKpkcGEIFLQNKEIKQLSAKQIA 75
Cdd:CHL00131 7 ILEIKNLHAS-VNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykILE---GDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 76 RQVAYVSqhspqtYQYKV-------LDYVVLGRAAHLGLFGKPREEDYHLAERALAQLSI----RHFADK-IYMQMSGGE 143
Cdd:CHL00131 83 HLGIFLA------FQYPIeipgvsnADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLvgmdPSFLSRnVNEGFSGGE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310524600 144 KQLVNLAKILVQQPQLILFDEPTSALDYgNVFKTLSL-IKGLSHQQFSIIMTTHnpdHPMLLNEVIPN 210
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDI-DALKIIAEgINKLMTSENSIILITH---YQRLLDYIKPD 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-238 |
1.69e-14 |
|
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: 72.55 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 13 RNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKC-GEIFLQNKEIKQLS-AKQIARQVAYVSQHS----- 85
Cdd:TIGR02633 271 PHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFeGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkrhgi 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 86 -PQTYQYKVLDYVVLGRAAHLGLFGKPREEDyhLAERALAQLSIRHFA-DKIYMQMSGGEKQLVNLAKILVQQPQLILFD 163
Cdd:TIGR02633 351 vPILGVGKNITLSVLKSFCFKMRIDAAAELQ--IIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310524600 164 EPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNpdhpmlLNEVIPNSKVAILTKSGKLHCGFTEAILTEDNLRE 238
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSE------LAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQVLA 497
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-222 |
1.69e-14 |
|
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: 72.53 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGL---------------LKPKCGEIFLQNKEIKQLSA----------- 71
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgriiyhvaLCEKCGYVERPSKVGEPCPVcggtlepeevd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 72 ---------KQIARQVAYVSQHSPQTYQYK-VLDYVVlgRAAHLglFGKPREEDYHLAERALAQLSIRHFADKIYMQMSG 141
Cdd:TIGR03269 96 fwnlsdklrRRIRKRIAIMLQRTFALYGDDtVLDNVL--EALEE--IGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 142 GEKQLVNLAKILVQQPQLILFDEPTSALDYgnvfKTLSLI-----KGLSHQQFSIIMTTHNPdhpmllnEVIPN-SKVAI 215
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDP----QTAKLVhnaleEAVKASGISMVLTSHWP-------EVIEDlSDKAI 240
|
....*..
gi 2310524600 216 LTKSGKL 222
Cdd:TIGR03269 241 WLENGEI 247
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-170 |
2.97e-14 |
|
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: 72.08 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYV 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 82 SQhSPQTYQYKVLDYVVLGraahlglfGKPREEDyhlaERALAQLSIRHFADKI-YMQM-------------SGGEKQLV 147
Cdd:TIGR01193 554 PQ-EPYIFSGSILENLLLG--------AKENVSQ----DEIWAACEIAEIKDDIeNMPLgyqtelseegssiSGGQKQRI 620
|
170 180
....*....|....*....|...
gi 2310524600 148 NLAKILVQQPQLILFDEPTSALD 170
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLD 643
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-199 |
3.12e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.82 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRNIPL----LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEI------KQLsa 71
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkknKKL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 72 KQIARQVAYVSQ---HspQTYQYKVLDYVVLGRAAhlglFGKPREEDYHLAERALAQLSIRH-FADKIYMQMSGGEKQLV 147
Cdd:PRK13634 81 KPLRKKVGIVFQfpeH--QLFEETVEKDICFGPMN----FGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310524600 148 NLAKILVQQPQLILFDEPTSALD-YG-----NVFKTLSLIKGLshqqfSIIMTTHNPD 199
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDpKGrkemmEMFYKLHKEKGL-----TTVLVTHSME 207
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-170 |
4.66e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.67 E-value: 4.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINqlyFQHQRNIPLLNgIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLqNKEIKQLSAKQIA----- 75
Cdd:PRK11144 1 MLELN---FKQQLGDLCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVL-NGRVLFDAEKGIClppek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 76 RQVAYVSQHSPQTYQYKV---LDYVVlgraahlglfgkpREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKI 152
Cdd:PRK11144 76 RRIGYVFQDARLFPHYKVrgnLRYGM-------------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRA 142
|
170
....*....|....*...
gi 2310524600 153 LVQQPQLILFDEPTSALD 170
Cdd:PRK11144 143 LLTAPELLLMDEPLASLD 160
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-240 |
8.02e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 69.31 E-value: 8.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFqHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLL-----KPKC-GEIFLQNKEIKQLSAKQI 74
Cdd:PRK14246 10 VFNISRLYL-YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydsKIKVdGKVLYFGKDIFQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 75 ARQVAYVSQHSPQTYQYKVLDYVVLGRAAHlGLfgKPREEDYHLAERALAQLSI-RHFADKI---YMQMSGGEKQLVNLA 150
Cdd:PRK14246 89 RKEVGMVFQQPNPFPHLSIYDNIAYPLKSH-GI--KEKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 151 KILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLShQQFSIIMTTHNPDHPMLLNEVipnskVAILTKSGKLHCGFTEAI 230
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELK-NEIAIVIVSHNPQQVARVADY-----VAFLYNGELVEWGSSNEI 239
|
250
....*....|..
gi 2310524600 231 LT--EDNLRELY 240
Cdd:PRK14246 240 FTspKNELTEKY 251
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-170 |
8.09e-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: 70.48 E-value: 8.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKcGEIFLQNKEIKQLSAKQIA---RQVAYVSQH-----SPqty 89
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRALRplrRRMQVVFQDpfgslSP--- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 90 QYKVLDYVVLGRAAH-LGLFGKPREEdyhLAERALAQLSI-RHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTS 167
Cdd:COG4172 378 RMTVGQIIAEGLRVHgPGLSAAERRA---RVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
...
gi 2310524600 168 ALD 170
Cdd:COG4172 455 ALD 457
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-224 |
9.38e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.81 E-value: 9.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQ-RNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEiflqnkeiKQLSAKQIARQVA 79
Cdd:TIGR01257 1937 ILRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGD--------ATVAGKSILTNIS 2008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 80 YVSQHSPQTYQYKVLDYVVLGRAaHLGLF----GKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQ 155
Cdd:TIGR01257 2009 DVHQNMGYCPQFDAIDDLLTGRE-HLYLYarlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310524600 156 QPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPDHPMLLnevipNSKVAILTKsGKLHC 224
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEAL-----CTRLAIMVK-GAFQC 2150
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-171 |
1.14e-13 |
|
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: 68.29 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQhSPQTYQYKVld 95
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQ-DPVLFSGTI-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 yvvlgrAAHLGLFGKPREEDYHLA-ERALAQLSIRHFADKIYMQM-------SGGEKQLVNLAKILVQQPQLILFDEPTS 167
Cdd:cd03244 95 ------RSNLDPFGEYSDEELWQAlERVGLKEFVESLPGGLDTVVeeggenlSVGQRQLLCLARALLRKSKILVLDEATA 168
|
....
gi 2310524600 168 ALDY 171
Cdd:cd03244 169 SVDP 172
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-197 |
1.40e-13 |
|
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: 68.13 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 13 RNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLqNKEIKQLSAKQIARQVAYV-SQHSPQTYQY 91
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV-AGLVPWKRRKKFLRRIGVVfGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 92 KVLDYVVLGRAAHlglfgkpREEDYHLAERaLAQLS----IRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTS 167
Cdd:cd03267 111 PVIDSFYLLAAIY-------DLPPARFKKR-LDELSelldLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190
....*....|....*....|....*....|....
gi 2310524600 168 ALDygnVFKTLSLIKGL----SHQQFSIIMTTHN 197
Cdd:cd03267 183 GLD---VVAQENIRNFLkeynRERGTTVLLTSHY 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-196 |
1.65e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 15 IPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQiARQVA-YVSQHSPQTY-QYK 92
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-AHQLGiYLVPQEPLLFpNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 93 VLDYVvlgraahlgLFGKPREEDyhlAERALAQLsIRHFADKIYMQMSGG-----EKQLVNLAKILVQQPQLILFDEPTS 167
Cdd:PRK15439 103 VKENI---------LFGLPKRQA---SMQKMKQL-LAALGCQLDLDSSAGslevaDRQIVEILRGLMRDSRILILDEPTA 169
|
170 180
....*....|....*....|....*....
gi 2310524600 168 ALDYGNVFKTLSLIKGLSHQQFSIIMTTH 196
Cdd:PRK15439 170 SLTPAETERLFSRIRELLAQGVGIVFISH 198
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-196 |
1.89e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.09 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 13 RNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQlSAKQIARQVAYVSQHSPQTYQYK 92
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 93 VLD-YVVLGRaahlgLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDY 171
Cdd:PRK13536 131 VREnLLVFGR-----YFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180
....*....|....*....|....*
gi 2310524600 172 GNVFKTLSLIKGLSHQQFSIIMTTH 196
Cdd:PRK13536 206 HARHLIWERLRSLLARGKTILLTTH 230
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
2-196 |
2.64e-13 |
|
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: 66.97 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQ---- 77
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrys 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 78 VAYVSQhSPQTYQYKVLDYVVLGRAahlglFGKPREEDYHLAERALAQLSIRHFADKIY-----MQMSGGEKQLVNLAKI 152
Cdd:cd03290 81 VAYAAQ-KPWLLNATVEENITFGSP-----FNKQRYKAVTDACSLQPDIDLLPFGDQTEigergINLSGGQRQRICVARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2310524600 153 LVQQPQLILFDEPTSALD--YGNVFKTLSLIKGLSHQQFSIIMTTH 196
Cdd:cd03290 155 LYQNTNIVFLDDPFSALDihLSDHLMQEGILKFLQDDKRTLVLVTH 200
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-197 |
4.67e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.43 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKP-----KCGEIFLQNKEI-KQLSAKQIARQVAYVSQHsPQTYQ 90
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfNYRDVLEFRRRVGMLFQR-PNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 91 YKVLDYVVLGRAAHLGLfgkPREEDYHLAERALAQLSI-----RHFADKIYmQMSGGEKQLVNLAKILVQQPQLILFDEP 165
Cdd:PRK14271 115 MSIMDNVLAGVRAHKLV---PRKEFRGVAQARLTEVGLwdavkDRLSDSPF-RLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190
....*....|....*....|....*....|..
gi 2310524600 166 TSALDYGNVFKTLSLIKGLShQQFSIIMTTHN 197
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLA-DRLTVIIVTHN 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
17-196 |
8.47e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 66.75 E-value: 8.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQlSAKQIARQVAYVSQHSPQTYQYKVLD- 95
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVPQFDNLDPDFTVREn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 YVVLGRaahlgLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVF 175
Cdd:PRK13537 101 LLVFGR-----YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARH 175
|
170 180
....*....|....*....|.
gi 2310524600 176 KTLSLIKGLSHQQFSIIMTTH 196
Cdd:PRK13537 176 LMWERLRSLLARGKTILLTTH 196
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-218 |
1.15e-12 |
|
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: 65.13 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQhspqtyqykvlD 95
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQ-----------D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 YVVLGRAAHLGL--FGKPREEDYHLAeralaqLSIRHFADkiymQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYgn 173
Cdd:cd03369 91 PTLFSGTIRSNLdpFDEYSDEEIYGA------LRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDY-- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2310524600 174 vfKTLSLIKGLSHQQFS---IIMTTHNpdhpmlLNEVIPNSKVAILTK 218
Cdd:cd03369 159 --ATDALIQKTIREEFTnstILTIAHR------LRTIIDYDKILVMDA 198
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-197 |
1.30e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.04 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTllnciAGL----LKPKCGEIFLQNKEIKQLSAKQ---IARQVAYVSQ--HSPQT 88
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKST-----TGLallrLINSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQdpNSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 89 YQYKVLDYVVLG-RAAHLGLFGKPREEDY--HLAERALAQLSiRHfadKIYMQMSGGEKQLVNLAKILVQQPQLILFDEP 165
Cdd:PRK15134 377 PRLNVLQIIEEGlRVHQPTLSAAQREQQViaVMEEVGLDPET-RH---RYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190
....*....|....*....|....*....|...
gi 2310524600 166 TSALDYGNVFKTLSLIKGLSHQ-QFSIIMTTHN 197
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKhQLAYLFISHD 485
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-170 |
1.43e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 67.12 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLqnkeikqlsAKQIarQVAYVSQHSpqtyqykvLDY 96
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGI--KLGYFAQHQ--------LEF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 97 VvlgRAAHlglfgKPREEDYHLAERALAQlSIRHF-------ADKIY---MQMSGGEKQLVNLAKILVQQPQLILFDEPT 166
Cdd:PRK10636 388 L---RADE-----SPLQHLARLAPQELEQ-KLRDYlggfgfqGDKVTeetRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
....
gi 2310524600 167 SALD 170
Cdd:PRK10636 459 NHLD 462
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
9-170 |
1.54e-12 |
|
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: 66.77 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 9 FQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVsqhsPQt 88
Cdd:COG5265 365 FGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIV----PQ- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 89 yqykvlDYVvlgraahlgLF----------GKP---REEDYHLAEraLAQLS--IRHFADKiY--------MQMSGGEKQ 145
Cdd:COG5265 440 ------DTV---------LFndtiayniayGRPdasEEEVEAAAR--AAQIHdfIESLPDG-YdtrvgergLKLSGGEKQ 501
|
170 180
....*....|....*....|....*
gi 2310524600 146 LVNLAKILVQQPQLILFDEPTSALD 170
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALD 526
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-172 |
1.86e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.59 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQ-VAY 80
Cdd:COG3845 258 LEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQhSPQTY----QYKVLDYVVLGRA-----AHLGLFGKPREEDYhlAERALAQLSIRhfADKIYM---QMSGGEKQLVN 148
Cdd:COG3845 338 IPE-DRLGRglvpDMSVAENLILGRYrrppfSRGGFLDRKAIRAF--AEELIEEFDVR--TPGPDTparSLSGGNQQKVI 412
|
170 180
....*....|....*....|....
gi 2310524600 149 LAKILVQQPQLILFDEPTSALDYG 172
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLDVG 436
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-59 |
1.95e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.10 E-value: 1.95e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEI 59
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-196 |
2.13e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQ-IARQVAYVSQHSPQTYQYKVLDY 96
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 97 VVLGRAAHLGLFGKPREedyhLAERALAQLSirHFADKIYMQ-----MSGGEKQLVNLAKILVQQPQLILFDEPTSALDY 171
Cdd:PRK11288 100 LYLGQLPHKGGIVNRRL----LNYEAREQLE--HLGVDIDPDtplkyLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180
....*....|....*....|....*
gi 2310524600 172 GNVFKTLSLIKGLSHQQFSIIMTTH 196
Cdd:PRK11288 174 REIEQLFRVIRELRAEGRVILYVSH 198
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-198 |
2.98e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.29 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKP---KCGEIFLQNKEIKqlsaKQIARQVAYVSQ---HSPQTYQ 90
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLD----SSFQRSIGYVQQqdlHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 91 YKVLDY-VVLGRAAHLglfgkPREEDYHLAERALAQLSIRHFADKIYMQMSGG----EKQLVNLAKILVQQPQLILF-DE 164
Cdd:TIGR00956 854 RESLRFsAYLRQPKSV-----SKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKLLLFlDE 928
|
170 180 190
....*....|....*....|....*....|....
gi 2310524600 165 PTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNP 198
Cdd:TIGR00956 929 PTSGLDSQTAWSICKLMRKLADHGQAILCTIHQP 962
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
16-170 |
3.22e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.68 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEI-FLQNKEI---KQLSAKQIARQVA---YVSQHSpqt 88
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIgyyAQDHAYDFENDLTlfdWMSQWR--- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 89 yQYKVLDYVV---LGRAahlgLFGkprEEDYHLAERALaqlsirhfadkiymqmSGGEKQLVNLAKILVQQPQLILFDEP 165
Cdd:PRK15064 410 -QEGDDEQAVrgtLGRL----LFS---QDDIKKSVKVL----------------SGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
....*
gi 2310524600 166 TSALD 170
Cdd:PRK15064 466 TNHMD 470
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-197 |
3.62e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.13 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 19 NGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPK---CGEIFLQNKEIKQLSAKQI----ARQVAYVSQhSPQT--- 88
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELnklrAEQISMIFQ-DPMTsln 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 89 -YQyKVLDYVVLGRAAHLGLfgkPREEDYHLAERALAQLSIRHFADKIYM---QMSGGEKQLVNLAKILVQQPQLILFDE 164
Cdd:PRK09473 112 pYM-RVGEQLMEVLMLHKGM---SKAEAFEESVRMLDAVKMPEARKRMKMyphEFSGGMRQRVMIAMALLCRPKLLIADE 187
|
170 180 190
....*....|....*....|....*....|....
gi 2310524600 165 PTSALDYGNVFKTLSLIKGLSHQ-QFSIIMTTHN 197
Cdd:PRK09473 188 PTTALDVTVQAQIMTLLNELKREfNTAIIMITHD 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-185 |
3.96e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 25 LKAGELLTILGANGTGKSTLLNCIAGLLKPKCG---------EIF-------LQNKeIKQLSAKQI--ARQVAYVSQhSP 86
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeepswdEVLkrfrgteLQNY-FKKLYNGEIkvVHKPQYVDL-IP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 87 QTYQYKVLDyvVLGRAAHLGLFgkpREedyhLAERalaqLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPT 166
Cdd:PRK13409 174 KVFKGKVRE--LLKKVDERGKL---DE----VVER----LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170
....*....|....*....
gi 2310524600 167 SALDYGNVFKTLSLIKGLS 185
Cdd:PRK13409 241 SYLDIRQRLNVARLIRELA 259
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-196 |
4.00e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.58 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 25 LKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEI-----------FLQNKEI----KQLSAKQIarQVAyvsqHSPQtY 89
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGTELqdyfKKLANGEI--KVA----HKPQ-Y 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 90 QYKVLDYV------VLGRAAHLGLFGkpreedyHLAERalaqLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFD 163
Cdd:COG1245 169 VDLIPKVFkgtvreLLEKVDERGKLD-------ELAEK----LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|...
gi 2310524600 164 EPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTH 196
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
16-193 |
5.36e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQ-IARQVAYVSQHSPQtyqykvl 94
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRKR------- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 95 DYVVLGRA-------AHLGLFGKPREEDYHLAERALAQLSIRHF------ADKIYMQMSGGEKQLVNLAKILVQQPQLIL 161
Cdd:PRK10762 339 DGLVLGMSvkenmslTALRYFSRAGGSLKHADEQQAVSDFIRLFniktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190
....*....|....*....|....*....|..
gi 2310524600 162 FDEPTSALDYGNVFKTLSLIKGLSHQQFSIIM 193
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQFKAEGLSIIL 450
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-198 |
8.11e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 63.32 E-value: 8.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKC-----GEIFLQNKEI--KQLSAKQIARQVAYVSQHSPQTY 89
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 90 QYKVLDYVVLGraAHLGLFGKPREEDYHLAERALAQLSI-RHFADKIY---MQMSGGEKQLVNLAKILVQQPQLILFDEP 165
Cdd:PRK14267 99 HLTIYDNVAIG--VKLNGLVKSKKELDERVEWALKKAALwDEVKDRLNdypSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190
....*....|....*....|....*....|...
gi 2310524600 166 TSALDYGNVFKTLSLIKGLShQQFSIIMTTHNP 198
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELK-KEYTIVLVTHSP 208
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-169 |
1.28e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKqiARQVAYVS---QHSPQTYQYKVL 94
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK--SSQEAGIGiihQELNLIPQLTIA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310524600 95 DYVVLGRAaHLGLFGKPR-EEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSAL 169
Cdd:PRK10762 98 ENIFLGRE-FVNRFGRIDwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-170 |
1.96e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.44 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQhspqtyqykvlD 95
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQ-----------D 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 YVVLGRAAHLGL-FGKP---REEDYHLAERALAQLSIRHFADKIYM-------QMSGGEKQLVNLAKILVQQPQLILFDE 164
Cdd:PRK13657 418 AGLFNRSIEDNIrVGRPdatDEEMRAAAERAQAHDFIERKPDGYDTvvgergrQLSGGERQRLAIARALLKDPPILILDE 497
|
....*.
gi 2310524600 165 PTSALD 170
Cdd:PRK13657 498 ATSALD 503
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-234 |
2.38e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.81 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNkeikqlsakqiarQVAYVSQHS---PQTYQYK 92
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAwiqNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 93 VLdyvvlgraahlglFGKPREEDYHL----AERALAQLSIRHFADKIYM-----QMSGGEKQLVNLAKILVQQPQLILFD 163
Cdd:TIGR00957 719 IL-------------FGKALNEKYYQqvleACALLPDLEILPSGDRTEIgekgvNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310524600 164 EPTSALD-------YGNVFKTLSLIKGLSHqqfsiIMTTHNPDHpmllnevIPNSKVAILTKSGKL-HCGFTEAILTED 234
Cdd:TIGR00957 786 DPLSAVDahvgkhiFEHVIGPEGVLKNKTR-----ILVTHGISY-------LPQVDVIIVMSGGKIsEMGSYQELLQRD 852
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-170 |
2.45e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.51 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLK--PKCGEIFLQNKEIKQLSAkqiarqvayvsqhspqtyqykV 93
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGREAS---------------------L 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 94 LDYVvlgraahlglfgkPREEDYHLAERAL-------AQLSIRHFAdkiymQMSGGEKQLVNLAKILVQQPQLILFDEPT 166
Cdd:COG2401 103 IDAI-------------GRKGDFKDAVELLnavglsdAVLWLRRFK-----ELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
....
gi 2310524600 167 SALD 170
Cdd:COG2401 165 SHLD 168
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-197 |
2.68e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.19 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLY--FQHQRNI-PLLNGIDLELKAGELLTILGANGTGKS-TLLNCIAGLLKPKC----GEIFLQNK-------- 64
Cdd:PRK15134 5 LLAIENLSvaFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGEsllhaseq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 65 EIKQLSAKQIAR--QVAYVSQ---HSPQTYQYKVLdyvvlgrAAHLGLFGKP-REEDYHLAERalaqLSIRHFADKIY-- 136
Cdd:PRK15134 85 TLRGVRGNKIAMifQEPMVSLnplHTLEKQLYEVL-------SLHRGMRREAaRGEILNCLDR----VGIRQAAKRLTdy 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310524600 137 -MQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQ-QFSIIMTTHN 197
Cdd:PRK15134 154 pHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHN 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-170 |
2.83e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.26 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 24 ELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIflqNKEIKqlsakqiarqVAYVSQHSPQTYQYKVLDYvvLGRAA 103
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLK----------ISYKPQYISPDYDGTVEEF--LRSAN 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310524600 104 HLGLFGKPREEDyhLAERalaqLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALD 170
Cdd:COG1245 427 TDDFGSSYYKTE--IIKP----LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-170 |
4.48e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.65 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 12 QRNIplLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQnKEIKqlsakqiarqVAYVSQhSPQTYQY 91
Cdd:TIGR03719 17 KKEI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGIK----------VGYLPQ-EPQLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 92 K-VLDYVVLGRAAHLGL----------FGKPREE-DYHLAERALAQLSIRH-----FADKIYMQM--------------- 139
Cdd:TIGR03719 83 KtVRENVEEGVAEIKDAldrfneisakYAEPDADfDKLAAEQAELQEIIDAadawdLDSQLEIAMdalrcppwdadvtkl 162
|
170 180 190
....*....|....*....|....*....|.
gi 2310524600 140 SGGEKQLVNLAKILVQQPQLILFDEPTSALD 170
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-170 |
5.10e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.26 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNkeikqlsakqiARQVAYVSQH----SPQTYQYK 92
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE-----------TVKLAYVDQSrdalDPNKTVWE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 93 V----LDYVVLGRA-----AHLGLFGkpreedyhlaeralaqlsirhF--AD--KIYMQMSGGEKQLVNLAKILVQQPQL 159
Cdd:TIGR03719 406 EisggLDIIKLGKReipsrAYVGRFN---------------------FkgSDqqKKVGQLSGGERNRVHLAKTLKSGGNV 464
|
170
....*....|.
gi 2310524600 160 ILFDEPTSALD 170
Cdd:TIGR03719 465 LLLDEPTNDLD 475
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
15-170 |
5.61e-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: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 15 IPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKE----IKQLSAKQIARQVAYVSQHSPQTYQ 90
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDewvdMTKPGPDGRGRAKRYIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 91 Y---KVLDYvvLGRAAHLGL---FGKpREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDE 164
Cdd:TIGR03269 377 YphrTVLDN--LTEAIGLELpdeLAR-MKAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDE 453
|
....*.
gi 2310524600 165 PTSALD 170
Cdd:TIGR03269 454 PTGTMD 459
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-170 |
6.78e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAgllkpkcGEIFLQNKEIkqlsakQIARQ--VAYVSQHSPQTYQYKV 93
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDDGRI------IYEQDliVARLQQDPPRNVEGTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 94 LDYVVLG---RAAHLglfgkpreEDYH---------LAERALAQLS-----IRHF-------------------ADKIYM 137
Cdd:PRK11147 84 YDFVAEGieeQAEYL--------KRYHdishlvetdPSEKNLNELAklqeqLDHHnlwqlenrinevlaqlgldPDAALS 155
|
170 180 190
....*....|....*....|....*....|...
gi 2310524600 138 QMSGGEKQLVNLAKILVQQPQLILFDEPTSALD 170
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-170 |
7.37e-11 |
|
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: 60.50 E-value: 7.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAG-----ELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEikqlsakqiarqVAYVSQHSPQTYQYK 92
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT------------VSYKPQYIKADYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 93 VLDYvvlgraahlgLFGKPR---EEDYHLAErALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSAL 169
Cdd:cd03237 78 VRDL----------LSSITKdfyTHPYFKTE-IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
.
gi 2310524600 170 D 170
Cdd:cd03237 147 D 147
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
9-170 |
7.81e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.13 E-value: 7.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 9 FQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLS---AKQIARQVAYVSQhS 85
Cdd:PRK11308 22 FKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQ-N 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 86 PqtyqYKVLDyvvlgraahlglfgkPR-------EE------DYHLAERA------LAQLSIR-HFADKiYMQM-SGGEK 144
Cdd:PRK11308 101 P----YGSLN---------------PRkkvgqilEEpllintSLSAAERRekalamMAKVGLRpEHYDR-YPHMfSGGQR 160
|
170 180
....*....|....*....|....*.
gi 2310524600 145 QLVNLAKILVQQPQLILFDEPTSALD 170
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALD 186
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-197 |
1.07e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.10 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRniPLLNGIDLELKAGELLTILGANGTGKStlLNCIA--GLLKP----KCGEIFLQNKEIkqLSAKQIA 75
Cdd:PRK10418 5 IELRNIALQAAQ--PLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAalGILPAgvrqTAGRVLLDGKPV--APCALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 76 RQVAYVSQHSPQTYQykvldyVVLGRAAH----LGLFGKPREEDYHLAERALAQLSIRHFADKIY-MQMSGGEKQLVNLA 150
Cdd:PRK10418 79 RKIATIMQNPRSAFN------PLHTMHTHaretCLALGKPADDATLTAALEAVGLENAARVLKLYpFEMSGGMLQRMMIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2310524600 151 KILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQ-FSIIMTTHN 197
Cdd:PRK10418 153 LALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRaLGMLLVTHD 200
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-197 |
1.16e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.41 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 4 INQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKP-----KCGEIFLQNK-----EIKQLSAKQ 73
Cdd:PRK10261 18 LNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQagglvQCDKMLLRRRsrqviELSEQSAAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 74 IAR----QVAYVSQHsPQTYQ---YKVLDYVVLGRAAHLGLfgkPREEDYHLAERALAQLSI---RHFADKIYMQMSGGE 143
Cdd:PRK10261 98 MRHvrgaDMAMIFQE-PMTSLnpvFTVGEQIAESIRLHQGA---SREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2310524600 144 KQLVNLAKILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQ-QFSIIMTTHN 197
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHD 228
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-233 |
1.76e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQ-HQRNIPLLNgiDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVA 79
Cdd:PRK10938 3 SLQISQGTFRlSDTKTLQLP--SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 80 yvsqhspQTYQYKVLDYVVLGRAAhlglFGKPREE-------DYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKI 152
Cdd:PRK10938 81 -------DEWQRNNTDMLSPGEDD----TGRTTAEiiqdevkDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 153 LVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIImtthnpdhpMLLN--EVIPN--SKVAILTKSGKLHCGFTE 228
Cdd:PRK10938 150 LMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLV---------LVLNrfDEIPDfvQFAGVLADCTLAETGERE 220
|
....*
gi 2310524600 229 AILTE 233
Cdd:PRK10938 221 EILQQ 225
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-165 |
2.71e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.39 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQhQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSakqiaRQVAY 80
Cdd:PRK11831 7 LVDMRGVSFT-RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMS-----RSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 -VSQHSPQTYQYKVL--DYVVLGRAAHlglfgkPREEDYHLAER--------ALAQLSIRHFADKIYMQMSGGEKQLVNL 149
Cdd:PRK11831 81 tVRKRMSMLFQSGALftDMNVFDNVAY------PLREHTQLPAPllhstvmmKLEAVGLRGAAKLMPSELSGGMARRAAL 154
|
170
....*....|....*.
gi 2310524600 150 AKILVQQPQLILFDEP 165
Cdd:PRK11831 155 ARAIALEPDLIMFDEP 170
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-185 |
3.23e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 59.33 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 5 NQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQ---IARQVAYV 81
Cdd:PRK15079 24 KQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwraVRSDIQMI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 82 SQH-----SP------------QTYQYKVLDYVVLGRA----AHLGLfgkpreedyhlaeraLAQLSIR--HfadkiymQ 138
Cdd:PRK15079 104 FQDplaslNPrmtigeiiaeplRTYHPKLSRQEVKDRVkammLKVGL---------------LPNLINRypH-------E 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2310524600 139 MSGGEKQLVNLAKILVQQPQLILFDEPTSALDYG------NVFKTLSLIKGLS 185
Cdd:PRK15079 162 FSGGQCQRIGIARALILEPKLIICDEPVSALDVSiqaqvvNLLQQLQREMGLS 214
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-170 |
4.10e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 9 FQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIA----GLLKPKCGEIF---LQNKEIKqlsaKQIARQVAYV 81
Cdd:TIGR00956 68 FRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITydgITPEEIK----KHYRGDVVYN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 82 SQ---HSPQTYQYKVLDYVVLGRAAHLGLFGKPREEdY--HLAERALAQLSIRH-----FADKIYMQMSGGEKQLVNLAK 151
Cdd:TIGR00956 144 AEtdvHFPHLTVGETLDFAARCKTPQNRPDGVSREE-YakHIADVYMATYGLSHtrntkVGNDFVRGVSGGERKRVSIAE 222
|
170
....*....|....*....
gi 2310524600 152 ILVQQPQLILFDEPTSALD 170
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLD 241
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-59 |
6.53e-10 |
|
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: 57.54 E-value: 6.53e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEI 59
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV 79
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
20-199 |
8.39e-10 |
|
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: 56.21 E-value: 8.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 20 GIDLELKAGELLTILGANGTGKSTLLNCIAgllkpkcgeiflqnkeikqlsakqiarqvayvsqhspqtyqykvldYVVL 99
Cdd:cd03227 13 PNDVTFGEGSLTIITGPNGSGKSTILDAIG----------------------------------------------LALG 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 100 GRAAHLGLFGKPREEDYHLAERALAQLSIrhfadkiyMQMSGGEKQLVNLAKIL----VQQPQLILFDEPTSALDYGNVF 175
Cdd:cd03227 47 GAQSATRRRSGVKAGCIVAAVSAELIFTR--------LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQ 118
|
170 180
....*....|....*....|....
gi 2310524600 176 KTLSLIKGLSHQQFSIIMTTHNPD 199
Cdd:cd03227 119 ALAEAILEHLVKGAQVIVITHLPE 142
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-197 |
9.29e-10 |
|
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: 58.54 E-value: 9.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQL--YF-QHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKC----GEIFLQNKEIKQLSAKQ 73
Cdd:COG4172 6 LLSVEDLsvAFgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpsGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 74 IAR----QVAYVSQhSPQTY---QYKVLDYVVLGRAAHLGLFGKPREEdyhlaeRALAQLS---IRHFADKI--Y-MQMS 140
Cdd:COG4172 86 LRRirgnRIAMIFQ-EPMTSlnpLHTIGKQIAEVLRLHRGLSGAAARA------RALELLErvgIPDPERRLdaYpHQLS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310524600 141 GGEKQLVNLAKILVQQPQLILFDEPTSALDygnVfkT-----LSLIKGLshQQ---FSIIMTTHN 197
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALD---V--TvqaqiLDLLKDL--QRelgMALLLITHD 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
17-170 |
9.94e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 9.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIflqnkEIKQlsakqiARQVAYVSQH----SPQTYQYK 92
Cdd:PRK11819 339 LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-----KIGE------TVKLAYVDQSrdalDPNKTVWE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 93 V----LDYVVLGRA-----AHLGLFGkpreedyhlaeralaqlsirhF--AD--KIYMQMSGGEKQLVNLAKILVQQPQL 159
Cdd:PRK11819 408 EisggLDIIKVGNReipsrAYVGRFN---------------------FkgGDqqKKVGVLSGGERNRLHLAKTLKQGGNV 466
|
170
....*....|.
gi 2310524600 160 ILFDEPTSALD 170
Cdd:PRK11819 467 LLLDEPTNDLD 477
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-170 |
1.34e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.21 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLqnkeikqlsakqIARQVAYVSQHSpQTYQYKVLD 95
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVS-WIFNATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 YVvlgraahlgLFGKPREEDYHlaERALAQLSIRHFADKIY-----------MQMSGGEKQLVNLAKILVQQPQLILFDE 164
Cdd:PLN03130 698 NI---------LFGSPFDPERY--ERAIDVTALQHDLDLLPggdlteigergVNISGGQKQRVSMARAVYSNSDVYIFDD 766
|
....*.
gi 2310524600 165 PTSALD 170
Cdd:PLN03130 767 PLSALD 772
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-164 |
2.79e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.90 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIkqlsakQIARQVAYV 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV------TAEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 82 SQHSPQTYQYKVLDYVvlgraahLGLFGKPREEDyhLAERALAQLSIRH---FAD-KIY-MQMSGGEKQLVNLAKILVQQ 156
Cdd:PRK10522 397 KLFSAVFTDFHLFDQL-------LGPEGKPANPA--LVEKWLERLKMAHkleLEDgRISnLKLSKGQKKRLALLLALAEE 467
|
....*...
gi 2310524600 157 PQLILFDE 164
Cdd:PRK10522 468 RDILLLDE 475
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
2-199 |
3.39e-09 |
|
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: 54.64 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYfqhQRNIpllNGIDLELKAGELLTILGANGTGKSTLLNciagllkpKCGEIFLQNKEIKQLSaKQIARQVAYV 81
Cdd:cd03238 1 LTVSGAN---VHNL---QNLDVSIPLNVLVVVTGVSGSGKSTLVN--------EGLYASGKARLISFLP-KFSRNKLIFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 82 SQhspqtyqykvldyvvLGRAAHLGLfgkpreeDYHLAERALAQLSirhfadkiymqmsGGEKQLVNLAKILVQQPQ--L 159
Cdd:cd03238 66 DQ---------------LQFLIDVGL-------GYLTLGQKLSTLS-------------GGELQRVKLASELFSEPPgtL 110
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2310524600 160 ILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPD 199
Cdd:cd03238 111 FILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
33-170 |
3.44e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 33 ILGANGTGKSTLLNCIAGLLKPKCGEIFLQnKEIKqlsakqiarqVAYVSQHSPQTYQYKVLDYVVLGRAAHLGL----- 107
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGIK----------VGYLPQEPQLDPEKTVRENVEEGVAEVKAAldrfn 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 108 -----FGKPREE-DYHLAERALAQLSIRHfAD------KIYMQM---------------SGGEKQLVNLAKILVQQPQLI 160
Cdd:PRK11819 107 eiyaaYAEPDADfDALAAEQGELQEIIDA-ADawdldsQLEIAMdalrcppwdakvtklSGGERRRVALCRLLLEKPDML 185
|
170
....*....|
gi 2310524600 161 LFDEPTSALD 170
Cdd:PRK11819 186 LLDEPTNHLD 195
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-170 |
4.33e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.91 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPkcgeiflqnkeiKQLSAKQIARQVAYVSQhSPQTYQYKVLD 95
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH------------AETSSVVIRGSVAYVPQ-VSWIFNATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 YVVLGRAAHLGLFGK-----PREEDYHL-AERALAQLSIRHfadkiyMQMSGGEKQLVNLAKILVQQPQLILFDEPTSAL 169
Cdd:PLN03232 698 NILFGSDFESERYWRaidvtALQHDLDLlPGRDLTEIGERG------VNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
.
gi 2310524600 170 D 170
Cdd:PLN03232 772 D 772
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-214 |
4.68e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.28 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 14 NIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSA-KQIARQVAYVSQHSPQTYQYK 92
Cdd:PRK10982 260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAnEAINHGFALVTEERRSTGIYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 93 VLDY----VVLGRAAHLGLFG----KPREEDYHLAERALAQLSIRHFADkiYMQMSGGEKQLVNLAKILVQQPQLILFDE 164
Cdd:PRK10982 340 YLDIgfnsLISNIRNYKNKVGlldnSRMKSDTQWVIDSMRVKTPGHRTQ--IGSLSGGNQQKVIIGRWLLTQPEILMLDE 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2310524600 165 PTSALDYGNVFKTLSLIKGLSHQQFSIIMTThnPDHPMLLN-----EVIPNSKVA 214
Cdd:PRK10982 418 PTRGIDVGAKFEIYQLIAELAKKDKGIIIIS--SEMPELLGitdriLVMSNGLVA 470
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-196 |
5.07e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.18 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQHQRNiPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKC--GEIFLQNKEIKQLSAKQIARQV 78
Cdd:PRK09580 1 MLSIKDLHVSVEDK-AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVtgGTVEFKGKDLLELSPEDRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 79 AYVSqhspqtYQYKVldyVVLGRAAHLGLFGKPREEDYHLAERALAQLSIRHF-ADKI-YMQM-------------SGGE 143
Cdd:PRK09580 80 IFMA------FQYPV---EIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLmEEKIaLLKMpedlltrsvnvgfSGGE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2310524600 144 KQLVNLAKILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTH 196
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-225 |
6.00e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.49 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQhspqtyqykvlDY 96
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQ-----------DP 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 97 VVLGRAAHLGL--FGKPREEDYHLA-ERALAQLSIRHFADKIYMQ-------MSGGEKQLVNLAKILVQQPQLILFDEPT 166
Cdd:TIGR00957 1370 VLFSGSLRMNLdpFSQYSDEEVWWAlELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310524600 167 SALDygnvFKTLSLIKGLSHQQF---SIIMTTHNpdhpmlLNEVIPNSKVAILTKSGKLHCG 225
Cdd:TIGR00957 1450 AAVD----LETDNLIQSTIRTQFedcTVLTIAHR------LNTIMDYTRVIVLDKGEVAEFG 1501
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-197 |
6.62e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 55.48 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 13 RNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEI-------FLQNKEikqlsakqIARQVAYV---- 81
Cdd:COG4586 33 REVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrvlgyvpFKRRKE--------FARRIGVVfgqr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 82 SQ---HSPqtyqykVLDYVVLGRAahlgLFGKPREE-DYHLAEraLAQ-LSIRHFADKIYMQMSGGEKQLVNLAKILVQQ 156
Cdd:COG4586 105 SQlwwDLP------AIDSFRLLKA----IYRIPDAEyKKRLDE--LVElLDLGELLDTPVRQLSLGQRMRCELAAALLHR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2310524600 157 PQLILFDEPTSALDygnVF---KTLSLIKGLSHQ-QFSIIMTTHN 197
Cdd:COG4586 173 PKILFLDEPTIGLD---VVskeAIREFLKEYNRErGTTILLTSHD 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-170 |
7.71e-09 |
|
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: 55.25 E-value: 7.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIflqnkeikqlsaKQIARqVAYVSQHSpqtyqykvld 95
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI------------KHSGR-ISFSSQFS---------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 YVVLGRAAHLGLFGKPREEDYHLAERALAQLS--IRHFADKIY-------MQMSGGEKQLVNLAKILVQQPQLILFDEPT 166
Cdd:cd03291 108 WIMPGTIKENIIFGVSYDEYRYKSVVKACQLEedITKFPEKDNtvlgeggITLSGGQRARISLARAVYKDADLYLLDSPF 187
|
....
gi 2310524600 167 SALD 170
Cdd:cd03291 188 GYLD 191
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-214 |
8.22e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 8.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLkPKC---GEIFLQNKE-----IKQLSAKQIA---RQVAYVSQHSp 86
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVcrfkdIRDSEALGIViihQELALIPYLS- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 87 qtyqykVLDYVVLGRA-AHLGLFGkpREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEP 165
Cdd:NF040905 95 ------IAENIFLGNErAKRGVID--WNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2310524600 166 TSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNpdhpmlLNEVipnSKVA 214
Cdd:NF040905 167 TAALNEEDSAALLDLLLELKAQGITSIIISHK------LNEI---RRVA 206
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-234 |
1.36e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.37 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQhSPQTYQYKVld 95
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQ-SPVLFSGTV-- 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 yvvlgrAAHLGLFGKPREED-YHLAERALAQLSIRHFADKIYMQMS-GGE------KQLVNLAKILVQQPQLILFDEPTS 167
Cdd:PLN03232 1327 ------RFNIDPFSEHNDADlWEALERAHIKDVIDRNPFGLDAEVSeGGEnfsvgqRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 168 ALDygnvFKTLSLIKGLSHQQF---SIIMTTHNpdhpmlLNEVIPNSKVAILTKSGKLHCGFTEAILTED 234
Cdd:PLN03232 1401 SVD----VRTDSLIQRTIREEFkscTMLVIAHR------LNTIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-170 |
1.49e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.02 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 2 LKINQLYFQHQ-RNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAY 80
Cdd:PRK11176 342 IEFRNVTFTYPgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 81 VSQhspQTYQYK--VLDYVVLGRAAHLGlfgkpREEDYHLAERALAQLSIR---HFADKIY----MQMSGGEKQLVNLAK 151
Cdd:PRK11176 422 VSQ---NVHLFNdtIANNIAYARTEQYS-----REQIEEAARMAYAMDFINkmdNGLDTVIgengVLLSGGQRQRIAIAR 493
|
170 180
....*....|....*....|
gi 2310524600 152 ILVQQ-PQLILfDEPTSALD 170
Cdd:PRK11176 494 ALLRDsPILIL-DEATSALD 512
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-170 |
1.89e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 24 ELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIflqNKEIKqlsakqiarqVAYvsqhSPqtyQYKVLDY-----VV 98
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELK----------ISY----KP---QYIKPDYdgtveDL 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310524600 99 LGRAAhlglfgkpreEDYH-------LAERalaqLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALD 170
Cdd:PRK13409 421 LRSIT----------DDLGssyykseIIKP----LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
25-170 |
2.02e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.64 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 25 LKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQHS-----PQTYQYKVLDYVVL 99
Cdd:PRK15112 36 LREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstslnPRQRISQILDFPLR 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310524600 100 graAHLGLFGKPREEDYHLAERalaQLSIRHFADKIYMQM-SGGEKQLVNLAKILVQQPQLILFDEPTSALD 170
Cdd:PRK15112 116 ---LNTDLEPEQREKQIIETLR---QVGLLPDHASYYPHMlAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
4-170 |
2.03e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 54.33 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 4 INQLYFQHQRNiPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQ 83
Cdd:PRK10789 318 IRQFTYPQTDH-PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 84 hSPQTYQYKVLDYVVLGRAahlglfGKPREEDYHLAERA--------LAQLSIRHFADKIYMqMSGGEKQLVNLAKILVQ 155
Cdd:PRK10789 397 -TPFLFSDTVANNIALGRP------DATQQEIEHVARLAsvhddilrLPQGYDTEVGERGVM-LSGGQKQRISIARALLL 468
|
170
....*....|....*
gi 2310524600 156 QPQLILFDEPTSALD 170
Cdd:PRK10789 469 NAEILILDDALSAVD 483
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-66 |
3.55e-08 |
|
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: 53.65 E-value: 3.55e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2310524600 21 IDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEI 66
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-170 |
1.21e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAG-----------LLKPK--CGEIFLqnkeikqlsakQIARQVAYVS 82
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRrgSGETIW-----------DIKKHIGYVS 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 83 QHSPQTYQYK--VLDYVVLGRAAHLGLFGKPREEDYHLAERALAQLSI-RHFADKIYMQMSGGEKQLVNLAKILVQQPQL 159
Cdd:PRK10938 343 SSLHLDYRVStsVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIdKRTADAPFHSLSWGQQRLALIVRALVKHPTL 422
|
170
....*....|.
gi 2310524600 160 ILFDEPTSALD 170
Cdd:PRK10938 423 LILDEPLQGLD 433
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-169 |
1.61e-07 |
|
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: 51.67 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 14 NIPLL--NGIDL------ELKAGELLTILGANGTGKSTLLNCIAGL--------LKPKCGEIFLqnkeIKQ---LSAKQI 74
Cdd:TIGR00954 456 NIPLVtpNGDVLieslsfEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFY----VPQrpyMTLGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 75 ARQVAYvsQHSPQTYQYK---------VLDYVVLGraahlglfgkpreedyHLAERALAQLSIRHFADkiymQMSGGEKQ 145
Cdd:TIGR00954 532 RDQIIY--PDSSEDMKRRglsdkdleqILDNVQLT----------------HILEREGGWSAVQDWMD----VLSGGEKQ 589
|
170 180
....*....|....*....|....
gi 2310524600 146 LVNLAKILVQQPQLILFDEPTSAL 169
Cdd:TIGR00954 590 RIAMARLFYHKPQFAILDECTSAV 613
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-170 |
2.26e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.45 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIflqnkeikqlsakqiaRQVAYVSqHSPQTyqykvlD 95
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----------------KHSGRIS-FSPQT------S 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 YVVLGRAAHLGLFGKPREEDYHLAERALAQLS--IRHFA--DKIYM-----QMSGGEKQLVNLAKILVQQPQLILFDEPT 166
Cdd:TIGR01271 497 WIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEedIALFPekDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPF 576
|
....
gi 2310524600 167 SALD 170
Cdd:TIGR01271 577 THLD 580
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-193 |
2.43e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 21 IDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIAR-----------QVAYVSQHSpqty 89
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRagimlcpedrkAEGIIPVHS---- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 90 qykVLDYVVLG-RAAHL--GLFGKPREEDyHLAERALAQLSIRH-FADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEP 165
Cdd:PRK11288 348 ---VADNINISaRRHHLraGCLINNRWEA-ENADRFIRSLNIKTpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180
....*....|....*....|....*...
gi 2310524600 166 TSALDYGNVFKTLSLIKGLSHQQFSIIM 193
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAAQGVAVLF 451
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-170 |
2.61e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFlqnkeikqlsakqIARQVAYVSQhspqtyQYKVLDY 96
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------------AERSIAYVPQ------QAWIMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 97 VVLGraaHLGLFGKPREEDYHLAERA------LAQLS--IRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSA 168
Cdd:PTZ00243 736 TVRG---NILFFDEEDAARLADAVRVsqleadLAQLGggLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
..
gi 2310524600 169 LD 170
Cdd:PTZ00243 813 LD 814
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-170 |
3.75e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 13 RNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIAR---------QVAYVSQ 83
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAlrrdiqfifQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 84 HSPQTYQYKVLDYVvlgRAAHLGLFGKPREEDYHLAERalAQLSIRHfADKIYMQMSGGEKQLVNLAKILVQQPQLILFD 163
Cdd:PRK10261 415 DPRQTVGDSIMEPL---RVHGLLPGKAAAARVAWLLER--VGLLPEH-AWRYPHEFSGGQRQRICIARALALNPKVIIAD 488
|
....*..
gi 2310524600 164 EPTSALD 170
Cdd:PRK10261 489 EAVSALD 495
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-203 |
4.51e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.68 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKcGEIFLQNKEIKQLSAKQIARQVAYVSQhspqtyqyKVLDY 96
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQ--------KVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 97 VvlgraahlGLFGK--------PREEDYHLAERALAQLSIRHFADKIYMQM-------SGGEKQLVNLAKILVQQPQLIL 161
Cdd:TIGR01271 1305 S--------GTFRKnldpyeqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLvdggyvlSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2310524600 162 FDEPTSALDYgnvfKTLSLIKGLSHQQFS---IIMTTHNPDhPML 203
Cdd:TIGR01271 1377 LDEPSAHLDP----VTLQIIRKTLKQSFSnctVILSEHRVE-ALL 1416
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-189 |
6.74e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSA-KQIARQVAYVsqhsPQ-----TYQ- 90
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHrRAVCPRIAYM----PQglgknLYPt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 91 ---YKVLDYvvLGRaahlgLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTS 167
Cdd:NF033858 93 lsvFENLDF--FGR-----LFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 165
|
170 180
....*....|....*....|..
gi 2310524600 168 ALDygnvfktlslikGLSHQQF 189
Cdd:NF033858 166 GVD------------PLSRRQF 175
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
17-196 |
9.64e-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: 48.70 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKcGEIFLQNKEIKQLSAKQIARQVAYVSQhspqtyqyKVLDY 96
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQ--------KVFIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 97 VVLGRAaHLGLFGK-PREEDYHLAERALAQLSIRHFADKIYMQM-------SGGEKQLVNLAKILVQQPQLILFDEPTSA 168
Cdd:cd03289 90 SGTFRK-NLDPYGKwSDEEIWKVAEEVGLKSVIEQFPGQLDFVLvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
170 180 190
....*....|....*....|....*....|.
gi 2310524600 169 LDYgnvfKTLSLIKGLSHQQFS---IIMTTH 196
Cdd:cd03289 169 LDP----ITYQVIRKTLKQAFAdctVILSEH 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-184 |
1.20e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 28 GELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKeikqlsakqiaRQVAYVSQH----SPQTyqyKVLDYVVLGRAa 103
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK-----------LEVAYFDQHraelDPEK---TVMDNLAEGKQ- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 104 HLGLFGKPReedyHlaerALAQLSIRHFADKIYMQ----MSGGEKQLVNLAKILVQQPQLILFDEPTSALDygnvFKTLS 179
Cdd:PRK11147 410 EVMVNGRPR----H----VLGYLQDFLFHPKRAMTpvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDLD----VETLE 477
|
....*
gi 2310524600 180 LIKGL 184
Cdd:PRK11147 478 LLEEL 482
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-173 |
1.62e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 1 MLKINQLYFQ-HQRNIPLLNgidLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIarqvA 79
Cdd:PRK13541 1 MLSLHQLQFNiEQKNLFDLS---ITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC----T 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 80 YVSQHSPQTYQYKVLDYVVLGraahlglfgkprEEDYHLAER---ALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQ 156
Cdd:PRK13541 74 YIGHNLGLKLEMTVFENLKFW------------SEIYNSAETlyaAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQ 141
|
170
....*....|....*..
gi 2310524600 157 PQLILFDEPTSALDYGN 173
Cdd:PRK13541 142 SDLWLLDEVETNLSKEN 158
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-202 |
3.38e-06 |
|
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: 45.83 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 28 GELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQhspqtyqykvldyvvlgraahlgl 107
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGK------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 108 fgkpreedyhlaeralaqlsirhfadkiYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVF------KTLSLI 181
Cdd:smart00382 58 ----------------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAllllleELRLLL 109
|
170 180
....*....|....*....|.
gi 2310524600 182 KGLSHQQFSIIMTTHNPDHPM 202
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLG 130
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-170 |
3.94e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.81 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 21 IDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKqlsAKQIA--RQVAYVSQ----HSPQT-YQYKV 93
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDIAtrRRVGYMSQafslYGELTvRQNLE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 94 LdyvvlgraaHLGLFGKPREEdyhLAER---ALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALD 170
Cdd:NF033858 362 L---------HARLFHLPAAE---IAARvaeMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
16-170 |
4.18e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKE-IKQLSAKQIARQvayvsqhspqtyQYKVL 94
Cdd:PRK15064 15 PLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNErLGKLRQDQFAFE------------EFTVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 95 DYVVLG--------------------------RAAHL-GLFGkprEEDYHLAE-RA---LAQLSI---RHFAdkiYM-QM 139
Cdd:PRK15064 83 DTVIMGhtelwevkqerdriyalpemseedgmKVADLeVKFA---EMDGYTAEaRAgelLLGVGIpeeQHYG---LMsEV 156
|
170 180 190
....*....|....*....|....*....|.
gi 2310524600 140 SGGEKQLVNLAKILVQQPQLILFDEPTSALD 170
Cdd:PRK15064 157 APGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-170 |
7.81e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.76 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGllkPKCGEIFLQNKEIKQLSAKQ--IARQVAYVSQ---HSPQTYQY 91
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRISGFPKKQetFARISGYCEQndiHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 92 KVLDYvvlgrAAHLGLFGK-PREEDYHLAERALAQLSIRHFADKIY-----MQMSGGEKQLVNLAKILVQQPQLILFDEP 165
Cdd:PLN03140 972 ESLIY-----SAFLRLPKEvSKEEKMMFVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
....*
gi 2310524600 166 TSALD 170
Cdd:PLN03140 1047 TSGLD 1051
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
139-199 |
9.16e-06 |
|
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: 46.54 E-value: 9.16e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310524600 139 MSGGEKQLVNLAKIL---VQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPD 199
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLD 893
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-222 |
1.01e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 16 PLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQhSPQTYQYKVld 95
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQ-APVLFSGTV-- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 96 yvvlgrAAHLGLFGKPREED-YHLAERALAQLSIRHFADKIYMQMS-GGE------KQLVNLAKILVQQPQLILFDEPTS 167
Cdd:PLN03130 1330 ------RFNLDPFNEHNDADlWESLERAHLKDVIRRNSLGLDAEVSeAGEnfsvgqRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310524600 168 ALDYGnvfkTLSLIKGLSHQQF---SIIMTTHNpdhpmlLNEVIPNSKVAILtKSGKL 222
Cdd:PLN03130 1404 AVDVR----TDALIQKTIREEFkscTMLIIAHR------LNTIIDCDRILVL-DAGRV 1450
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-197 |
1.64e-05 |
|
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: 44.10 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 24 ELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQnkeikqlsakqiARQVAYvsqhspqtyqykvldyvvlgraa 103
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD------------GITPVY----------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 104 hlglfgKPReedyhlaeralaqlsirhfadkiYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVFKTLSLIKG 183
Cdd:cd03222 66 ------KPQ-----------------------YIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170
....*....|....*
gi 2310524600 184 LS-HQQFSIIMTTHN 197
Cdd:cd03222 117 LSeEGKKTALVVEHD 131
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
3-198 |
1.67e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 44.99 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 3 KINQLYFQHQRNIPllnGIDLELKAGELLTIL-GANGTGKSTLLNCIAGLL---------------------KPKCGEIF 60
Cdd:COG3950 2 RIKSLTIENFRGFE---DLEIDFDNPPRLTVLvGENGSGKTTLLEAIALALsgllsrlddvkfrkllirngeFGDSAKLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 61 L-----------QNKEIKQLSAKQIARQVAYVSQHSPQTYQYKVLDYVVLGRAAHLGLFGKPREEDYHLAERALAQL--- 126
Cdd:COG3950 79 LyygtsrllldgPLKKLERLKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVREALNKLlpd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 127 --------------SIRHFADKIYM-QMSGGEKQLVNLA--------------KILVQQPQLILFDEP---------TSA 168
Cdd:COG3950 159 fkdiridrdpgrlvILDKNGEELPLnQLSDGERSLLALVgdlarrlaelnpalENPLEGEGIVLIDEIdlhlhpkwqRRI 238
|
250 260 270
....*....|....*....|....*....|
gi 2310524600 169 LDygnvfktlSLIKGLSHQQFsiIMTTHNP 198
Cdd:COG3950 239 LP--------DLRKIFPNIQF--IVTTHSP 258
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-193 |
2.14e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 6 QLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKE-IKQLSAKQIARQVAYVSQh 84
Cdd:PTZ00265 389 RFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnLKDINLKWWRSKIGVVSQ- 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 85 SP-------------QTYQYKVLDYV---------------------VLGRAAHLGLFGKPREED--------------- 115
Cdd:PTZ00265 468 DPllfsnsiknnikySLYSLKDLEALsnyynedgndsqenknkrnscRAKCAGDLNDMSNTTDSNeliemrknyqtikds 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 116 --YHLAERALAQLSIRHFADKIYM-------QMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGN---VFKTLSLIKG 183
Cdd:PTZ00265 548 evVDVSKKVLIHDFVSALPDKYETlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSeylVQKTINNLKG 627
|
250
....*....|
gi 2310524600 184 lSHQQFSIIM 193
Cdd:PTZ00265 628 -NENRITIII 636
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-59 |
2.33e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.27 E-value: 2.33e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEI 59
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
14-198 |
3.84e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 43.60 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 14 NIPLLNGID-LELKAGelLTIL-GANGTGKSTLLNCIAGllkpKCGeiflqnkeikqLSAKQIARQVAYVSQHSPQTyqy 91
Cdd:COG3910 23 NLPAVRNLEgLEFHPP--VTFFvGENGSGKSTLLEAIAV----AAG-----------FNPEGGSKNFRFSTRESESA--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 92 kvL-DYVVLGRAahlglFGKP------REEDYH-----LAERALAQLSI-RHFADKIYMQMSGGE--KQLVNlAKIlvQQ 156
Cdd:COG3910 83 --LgEYLRLSRG-----LPKPrdgfflRAESFFnvatyLDELAAEGPGIlDSYGGRSLHEQSHGEsfLALFE-NRF--RG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2310524600 157 PQLILFDEPTSALDYGNVFKTLSLIKGL--SHQQFsiIMTTHNP 198
Cdd:COG3910 153 NGLYLLDEPEAALSPSRQLALLALIHDLvrEGSQF--IIATHSP 194
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-199 |
4.11e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 57 GEIFLQNKEIKQLSAKQIARQVAYVSQHsPQTYQYKVLDYVVLGRAahlglfGKPREEdyhlAERALAQLSIRHFADKIY 136
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQE-PMLFNMSIYENIKFGKE------DATRED----VKRACKFAAIDEFIESLP 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 137 MQ-----------MSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGN---VFKTLSLIKG--------LSHQQFSI--- 191
Cdd:PTZ00265 1346 NKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSeklIEKTIVDIKDkadktiitIAHRIASIkrs 1425
|
170
....*....|
gi 2310524600 192 --IMTTHNPD 199
Cdd:PTZ00265 1426 dkIVVFNNPD 1435
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
136-198 |
4.99e-05 |
|
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: 43.92 E-value: 4.99e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310524600 136 YMQMSGGEKQLVNLAKILVQQPQ---LILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNP 198
Cdd:pfam13304 234 AFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSP 299
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
21-197 |
5.83e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.58 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 21 IDLELKAGELLTILGANGTGKSTLLNCIAGLL----KPKCGEIFLQNKEIKQLSAKQ----IARQVAYVSQhSPQTY--- 89
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKErrnlVGAEVAMIFQ-DPMTSlnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 90 QYKVLDYVVLGRAAHLGLFGKPREEdyhlaeRA---LAQLSIRHFADKIYM---QMSGGEKQLVNLAKILVQQPQLILFD 163
Cdd:PRK11022 105 CYTVGFQIMEAIKVHQGGNKKTRRQ------RAidlLNQVGIPDPASRLDVyphQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190
....*....|....*....|....*....|....*
gi 2310524600 164 EPTSALDYGNVFKTLSLIKGLSHQ-QFSIIMTTHN 197
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKeNMALVLITHD 213
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
137-205 |
9.07e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 9.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310524600 137 MQMSGGEKQLVNLAKIL----VQQPQLILFDEPTSALDYGNVFKTLSLIKGLShQQFSIIMTTHNPdhPMLLN 205
Cdd:pfam02463 1076 DLLSGGEKTLVALALIFaiqkYKPAPFYLLDEIDAALDDQNVSRVANLLKELS-KNAQFIVISLRE--EMLEK 1145
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-198 |
1.26e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 1.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310524600 137 MQMSGGEKQLVNLA---KILVQQPQ-LILFDEPTSALDYGNVFKTLSLIKGLSHQ-QFSIImtTHNP 198
Cdd:TIGR02168 1088 SLLSGGEKALTALAllfAIFKVKPApFCILDEVDAPLDDANVERFANLLKEFSKNtQFIVI--THNK 1152
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-199 |
1.31e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 17 LLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKeikqlsakqiaRQVAYVSQHSPQTYQyKVLDY 96
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN-----------WQLAWVNQETPALPQ-PALEY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 97 VVLG----RAAHLGLFGKPREEDYH----------------LAERALAQLSIRHFADKIYMQ----MSGGEKQLVNLAKI 152
Cdd:PRK10636 84 VIDGdreyRQLEAQLHDANERNDGHaiatihgkldaidawtIRSRAASLLHGLGFSNEQLERpvsdFSGGWRMRLNLAQA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2310524600 153 LVQQPQLILFDEPTSALDYGNVfktLSLIKGLSHQQFSIIMTTHNPD 199
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLDLDAV---IWLEKWLKSYQGTLILISHDRD 207
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
3-241 |
2.25e-04 |
|
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: 41.91 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 3 KINQLYFQHQRNIpllNGIDLELKAGeLLTILGANGTGKSTLLNCIAGLLKPKCG-----EIFLQNKEIKQLSA------ 71
Cdd:COG3593 2 KLEKIKIKNFRSI---KDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSrkfdeEDFYLGDDPDLPEIeieltf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 72 ----KQIARQVAYVSQHSPQTYQYKVLDYV---VLGRA-AHLGLFGKPREEDYHLaERALAQLSIRHFADKIYMQMSG-- 141
Cdd:COG3593 78 gsllSRLLRLLLKEEDKEELEEALEELNEElkeALKALnELLSEYLKELLDGLDL-ELELSLDELEDLLKSLSLRIEDgk 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 142 ---------GEKQLV--NLAKILVQ-----QPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPDhpmLLN 205
Cdd:COG3593 157 elpldrlgsGFQRLIllALLSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPH---LLS 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 2310524600 206 EViPNSKVAILTKSGKLHCGFTEAILTEDNLRELYQ 241
Cdd:COG3593 234 EV-PLENIRRLRRDSGGTTSTKLIDLDDEDLRKLLR 268
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
139-197 |
3.01e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 40.53 E-value: 3.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310524600 139 MSGGEKQLVNLAKIL-VQQ----PqLILFDEPTSALDYGNVFKTLSLIKGLSHQ-QFSIImtTHN 197
Cdd:cd03278 114 LSGGEKALTALALLFaIFRvrpsP-FCVLDEVDAALDDANVERFARLLKEFSKEtQFIVI--THR 175
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-193 |
4.10e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 8 YFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPK--CGEIFLQNKEIkQLS--AKQIARQVAYVSQ 83
Cdd:NF040905 266 YHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRniSGTVFKDGKEV-DVStvSDAIDAGLAYVTE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 84 HSpQTYQYKVLDYVV-------LGRAAHLGLFGKPREedYHLAERALAQLSIR-HFADKIYMQMSGGEKQLVNLAKILVQ 155
Cdd:NF040905 345 DR-KGYGLNLIDDIKrnitlanLGKVSRRGVIDENEE--IKVAEEYRKKMNIKtPSVFQKVGNLSGGNQQKVVLSKWLFT 421
|
170 180 190
....*....|....*....|....*....|....*...
gi 2310524600 156 QPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIM 193
Cdd:NF040905 422 DPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIV 459
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-59 |
8.15e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.80 E-value: 8.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2310524600 18 LNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEI 59
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
138-199 |
9.19e-04 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 39.55 E-value: 9.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 138 QMSGGEKQLVNLAKILVQQ-----PqLILFDEPTSALDygNVFKTL--SLIKGLSHQ-QFsiIMTTHNPD 199
Cdd:cd03272 158 QLSGGQKSLVALALIFAIQkcdpaP-FYLFDEIDAALD--AQYRTAvaNMIKELSDGaQF--ITTTFRPE 222
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
10-196 |
1.18e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 39.72 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 10 QHQRNIPLLNGIDLELKAGELLTILGANGTG--KSTLLNCIAGllkPKCGEiflQNKEIKQLSAKQIARQVAyVSQHSP- 86
Cdd:NF000106 21 KHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGR---RPWRF*TWCANRRALRRT-IG*HRPv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 87 -----QTYQYKVLDYVVlGRAAHLGlfgkpREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLIL 161
Cdd:NF000106 94 r*grrESFSGRENLYMI-GR*LDLS-----RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167
|
170 180 190
....*....|....*....|....*....|....*
gi 2310524600 162 FDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTH 196
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQ 202
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
33-199 |
1.91e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 38.36 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 33 ILGANGTGKSTLLNCI-AGLLkpkcGEIFLQNKEIKQLSakQIARQVAyvsqhspqtyqykVLDYVVLGraahlglFGKP 111
Cdd:cd03240 27 IVGQNGAGKTTIIEALkYALT----GELPPNSKGGAHDP--KLIREGE-------------VRAQVKLA-------FENA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524600 112 REEDYHlAERALAQLSIRHF-----ADKIYMQM----SGGEKQLVNLAKIL-------VQQPQLILfDEPTSALDYGNVF 175
Cdd:cd03240 81 NGKKYT-ITRSLAILENVIFchqgeSNWPLLDMrgrcSGGEKVLASLIIRLalaetfgSNCGILAL-DEPTTNLDEENIE 158
|
170 180
....*....|....*....|....*.
gi 2310524600 176 KTLS-LIKGLSHQ-QFSIIMTTHNPD 199
Cdd:cd03240 159 ESLAeIIEERKSQkNFQLIVITHDEE 184
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-197 |
2.43e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 2.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310524600 139 MSGGEKQLVNLAKIL---VQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHN 197
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHN 871
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
138-182 |
2.74e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.87 E-value: 2.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310524600 138 QMSGGEKQLVNLA------KILVQ-------QPQLILfDEPTSALDYGNVFKTLSLIK 182
Cdd:PRK02224 781 QLSGGERALFNLSlrcaiyRLLAEgiegdapLPPLIL-DEPTVFLDSGHVSQLVDLVE 837
|
|
| |
