|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-212 |
2.76e-105 |
|
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: 303.35 E-value: 2.76e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSGLWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFLPQR 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 82 FSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVG 161
Cdd:cd03264 81 FGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488470846 162 LDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEG 212
Cdd:cd03264 161 LDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-217 |
1.80e-83 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 248.83 E-value: 1.80e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFLPQ 80
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGeIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 RFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTV 160
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488470846 161 GLDPASRIGVRSLLGELAED-RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:COG1131 161 GLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-217 |
4.73e-69 |
|
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: 212.41 E-value: 4.73e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFLP 79
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGeITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 80 QRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPT 159
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 160 VGLDPASRIGVRSLLGELA-EDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:COG4555 161 NGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-208 |
8.10e-61 |
|
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: 188.76 E-value: 8.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFLPQ 80
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGeIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 RFSLPLHFRIRRAVEYaawargvepreccvragaaldrvglvdraddrvqslSGGMRQRLGIACAIVGDPAVLLLDEPTV 160
Cdd:cd03230 81 EPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488470846 161 GLDPASRIGVRSLLGELA-EDRTVIVSTHLLEDLQEFVSQLAVLSEGEL 208
Cdd:cd03230 125 GLDPESRREFWELLRELKkEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-217 |
5.43e-55 |
|
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: 175.77 E-value: 5.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLV--DISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFL 78
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAvdDLSLNVYKGeIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEP 158
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 159 TVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-213 |
2.89e-53 |
|
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: 171.75 E-value: 2.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRR-RRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFL 78
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFvAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKkNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQRfslPLH--FR--IRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLL 154
Cdd:COG1122 81 FQN---PDDqlFAptVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 155 LDEPTVGLDPASRIGVRSLLGEL-AEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-213 |
7.23e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 171.04 E-value: 7.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDvntiRSMVGFLP 79
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGeFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 80 QRFSLPLHFRI--RRAVEYAAWAR----GVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVL 153
Cdd:COG1121 82 QRAEVDWDFPItvRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488470846 154 LLDEPTVGLDPASRIGVRSLLGEL-AEDRTVIVSTHLLEDLQEFVSQLAVLSeGELIFEGS 213
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGP 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-212 |
5.15e-51 |
|
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: 165.40 E-value: 5.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 3 ELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDvntiRSMVGFLPQR 81
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGeFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 82 FSLPLHFRI--RRAVEYAAWARGV----EPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLL 155
Cdd:cd03235 77 RSIDRDFPIsvRDVVLMGLYGHKGlfrrLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488470846 156 DEPTVGLDPASRIGVRSLLGEL-AEDRTVIVSTHLLEDLQEFVSQLAVLsEGELIFEG 212
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-207 |
6.91e-50 |
|
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: 162.25 E-value: 6.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 3 ELEHISHRY--RRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFL 78
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGeFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQR----FSLPlhfRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLL 154
Cdd:cd03225 81 FQNpddqFFGP---TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488470846 155 LDEPTVGLDPASRIGVRSLLGELAED-RTVIVSTHLLEDLQEFVSQLAVLSEGE 207
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-213 |
1.14e-49 |
|
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: 163.29 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFL 78
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGeVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQRFSLPLHFRIRRAVEYA------AWAR-GVEPREccvRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphlgLFGRpSAEDRE---AVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488470846 152 VLLLDEPTVGLDPASRIGVRSLLGELAED--RTVIVSTHlleDLQ---EFVSQLAVLSEGELIFEGS 213
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLH---DLNlaaRYADRLVLLKDGRIVAQGP 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-212 |
2.25e-49 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 160.85 E-value: 2.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNtIRSMVGFLPQ 80
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGeIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-ALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 RFSLPLHFRIRRAVEYAAWARGVEPRECCVragaALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTV 160
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488470846 161 GLDPASRIGVRSLLGELA-EDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEG 212
Cdd:cd03268 156 GLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-237 |
3.59e-49 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 163.36 E-value: 3.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVntiRSMVGFLP 79
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGeIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED---RRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 80 QRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPT 159
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 160 VGLDPASRIGVRSLLGELAE-DRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDLESVGQKHPVRNANDAEAGYL 237
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEADGDAGWL 236
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-217 |
6.93e-49 |
|
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: 160.23 E-value: 6.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFLPQ 80
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGeIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 RFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTV 160
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 161 GLDPASRIGVRSLLGEL--AEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLkeEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-188 |
8.11e-49 |
|
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: 159.96 E-value: 8.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLV----DISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSM-- 74
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalkGVSLSIEKGEFvAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 75 ---VGFLPQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 488470846 152 VLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTH 188
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTH 199
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-188 |
5.63e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 157.90 E-value: 5.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYR----RRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS----DDVNTI 71
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGeFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslseRELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 72 R-SMVGFLPQRFSL-PlHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGD 149
Cdd:COG1136 84 RrRHIGFVFQFFNLlP-ELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488470846 150 PAVLLLDEPTVGLDPASRIGVRSLLGELAED--RTVIVSTH 188
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTH 203
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-217 |
1.65e-46 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 154.83 E-value: 1.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYR-RRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD----DVNTIRSM 74
Cdd:COG3638 2 MLELRNLSKRYPgGTPALDDVSLEIERGeFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlrgrALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 75 VGFLPQRFSLP---------LHFRIRRAVEYAAWARGVePRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACA 145
Cdd:COG3638 82 IGMIFQQFNLVprlsvltnvLAGRLGRTSTWRSLLGLF-PPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488470846 146 IVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
30-232 |
3.99e-46 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 155.63 E-value: 3.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFLPQRFSLPLHFRIRRAVEYAAWARGVEPRECC 109
Cdd:TIGR01188 23 GFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGRENLEMMGRLYGLPKDEAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 110 VRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGEL-AEDRTVIVSTH 188
Cdd:TIGR01188 103 ERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRALkEEGVTILLTTH 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488470846 189 LLEDLQEFVSQLAVLSEGELIFEGSYSDL-ESVGQKHPVRNANDA 232
Cdd:TIGR01188 183 YMEEADKLCDRIAIIDHGRIIAEGTPEELkRRLGKDTLESRPRDI 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-193 |
4.06e-44 |
|
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: 147.24 E-value: 4.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFLP 79
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGeALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 80 QRFSLPLHFRIRRAVEYAAWARGVEPREccVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPT 159
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....*
gi 488470846 160 VGLDPASRIGVRSLLGE-LAEDRTVIVSTHLLEDL 193
Cdd:COG4133 160 TALDAAGVALLAELIAAhLARGGAVLLTTHQPLEL 194
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-212 |
9.05e-43 |
|
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: 143.96 E-value: 9.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDvntIRSMVGFLPQ 80
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGeIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 RFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTV 160
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488470846 161 GLDPASRIGVRSLLGELAED-RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEG 212
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-212 |
2.35e-42 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 143.28 E-value: 2.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLV----DIS-CEFDSGLWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMV 75
Cdd:cd03266 1 MITADALTKRFRDVKKTVqavdGVSfTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 76 GFLPQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLL 155
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488470846 156 DEPTVGLDPASRIGVRSLLGEL-AEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEG 212
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-209 |
2.92e-42 |
|
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: 143.48 E-value: 2.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLRE-----PESGHFRVNGVDVSD---DVNTIR 72
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGeITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldvDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 73 SMVGFLPQRfSLPLHFRIRRAVEYAAWARGVEPRECC-VRAGAALDRVGLVDRADDRVQ--SLSGGMRQRLGIACAIVGD 149
Cdd:cd03260 81 RRVGMVFQK-PNPFPGSIYDNVAYGLRLHGIKLKEELdERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 150 PAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEFVSQLAVLSEGELI 209
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-212 |
1.04e-41 |
|
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: 140.26 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 3 ELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFLPQ 80
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGeIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 rfslplhfrirraveyaawargvepreccvragaALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTV 160
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488470846 161 GLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEG 212
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-217 |
1.27e-41 |
|
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: 141.94 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRR-RRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD----DVNTIRSMV 75
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGeFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 76 GFLPQRFSLP---------LHFRIRRAVEYAAWARGVEPRECcVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAI 146
Cdd:cd03256 81 GMIFQQFNLIerlsvlenvLSGRLGRRSTWRSLFGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488470846 147 VGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-207 |
1.58e-41 |
|
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: 139.30 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 3 ELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVN-TIRSMVGFLPQ 80
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGeIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 rfslplhfrirraveyaawargvepreccvragaaldrvglvdraddrvqsLSGGMRQRLGIACAIVGDPAVLLLDEPTV 160
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488470846 161 GLDPASRIGVRSLLGELAED-RTVIVSTHLLEDLQEFVSQLAVLSEGE 207
Cdd:cd00267 110 GLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-209 |
1.80e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 138.65 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRS-LVDISCEFDSG--LWgLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS----DDVNTIRS 73
Cdd:COG2884 1 MIRFENVSKRYPGGREaLSDVSLEIEKGefVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrlkrREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 74 MVGFLPQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVL 153
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488470846 154 LLDEPTVGLDPASRIGVRSLLGEL-AEDRTVIVSTHLLEDLQEFVSQLAVLSEGELI 209
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-195 |
2.77e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.07 E-value: 2.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRS----LVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDdvntIRSMV 75
Cdd:COG1116 7 ALELRGVSKRFPTGGGgvtaLDDVSLTVAAGEFvALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 76 GFLPQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLL 155
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488470846 156 DEPTVGLDPASRIGVRSLLGEL--AEDRTVIVSTHlleDLQE 195
Cdd:COG1116 163 DEPFGALDALTRERLQDELLRLwqETGKTVLFVTH---DVDE 201
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-188 |
5.05e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 137.82 E-value: 5.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD---DVNTIRSMVG 76
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGeVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskkDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 77 FLPQRFSLPLHFRIRRAVEYA-AWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLL 155
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLApIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190
....*....|....*....|....*....|....*
gi 488470846 156 DEPTVGLDPAsRIG-VRSLLGELAED-RTVIVSTH 188
Cdd:COG1126 161 DEPTSALDPE-LVGeVLDVMRDLAKEgMTMVVVTH 194
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-221 |
1.17e-39 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 137.97 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRR-----RRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNT----I 71
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGeFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKklkdL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 72 RSMVGFLpqrFSLPLH--FR--IRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRvqS---LSGGMRQRLGIAC 144
Cdd:TIGR04521 81 RKKVGLV---FQFPEHqlFEetVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLER--SpfeLSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 145 AIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS-------YS 215
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTprevfsdVD 235
|
....*.
gi 488470846 216 DLESVG 221
Cdd:TIGR04521 236 ELEKIG 241
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-209 |
1.98e-39 |
|
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: 135.72 E-value: 1.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDdVNTIRSMVGFLPQ 80
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGeFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-VPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 RFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTV 160
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488470846 161 GLDPASRIGVRSLLGEL--AEDRTVIVSTHLLEDLQEFVSQLAVLSEGELI 209
Cdd:cd03259 160 ALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-218 |
1.91e-38 |
|
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: 133.95 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS----DDVNTIRSMV 75
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEIlAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 76 GFLPQR---FS---------LPL--HFRIRRAveyaawargvEPREccvRAGAALDRVGLVDRADDRVQSLSGGMRQRLG 141
Cdd:COG1127 85 GMLFQGgalFDsltvfenvaFPLreHTDLSEA----------EIRE---LVLEKLELVGLPGAADKMPSELSGGMRKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 142 IACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDLE 218
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-208 |
2.41e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 132.63 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFLP 79
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGeCVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 80 QRFSLpLHFRIRRAVEYAAWARGVEPREccVRAGAALDRVGL-VDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEP 158
Cdd:COG4619 81 QEPAL-WGGTVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488470846 159 TVGLDPASRIGVRSLLGELA--EDRTVIVSTHLLEDLQEFVSQLAVLSEGEL 208
Cdd:COG4619 158 TSALDPENTRRVEELLREYLaeEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-212 |
2.83e-38 |
|
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: 133.67 E-value: 2.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGH------FRVNGVDVSDdvntIRS 73
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGeHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgERRGGEDVWE----LRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 74 MVGF----LPQRFslPLHFRIRRAVEYAAWA-----RGVEPRECcVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIAC 144
Cdd:COG1119 79 RIGLvspaLQLRF--PRDETVLDVVLSGFFDsiglyREPTDEQR-ERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 145 AIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAED--RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEG 212
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-217 |
1.02e-37 |
|
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: 139.58 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLV--DISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGF 77
Cdd:COG2274 474 IELENVSFRYPGDSPPVldNISLTIKPGeRVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQRFSLplhFR--IRRAVeyAAWARGVEP---RECCVRAGAA---------LD-RVGlvdradDRVQSLSGGMRQRLGI 142
Cdd:COG2274 554 VLQDVFL---FSgtIRENI--TLGDPDATDeeiIEAARLAGLHdfiealpmgYDtVVG------EGGSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488470846 143 ACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEfVSQLAVLSEGELIFEGSYSDL 217
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEEL 696
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-213 |
3.59e-37 |
|
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: 136.19 E-value: 3.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRS-----LVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD----DVNT 70
Cdd:COG1123 260 LLEVRNLSKRYPVRGKggvraVDDVSLTLRRGETlGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 71 IRSMVGFLPQRfslPLH-----FRIRRAVEYAAWARGVEPRECCV-RAGAALDRVGLVDRADDR-VQSLSGGMRQRLGIA 143
Cdd:COG1123 340 LRRRVQMVFQD---PYSslnprMTVGDIIAEPLRLHGLLSRAERReRVAELLERVGLPPDLADRyPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488470846 144 CAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP 488
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-217 |
9.56e-37 |
|
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: 129.24 E-value: 9.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRS----LVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD----DVNTI 71
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvtaLKDVSLSVPKGeIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 72 RSMVGFLPQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488470846 152 VLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-207 |
1.12e-36 |
|
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: 127.30 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDV---SDDVNTIRSMVGF 77
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGeIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdlEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQRFSLPLHFRIRRAVEYAawargvepreccvragaaldrvglvdraddrvqsLSGGMRQRLGIACAIVGDPAVLLLDE 157
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488470846 158 PTVGLDPASRIGVRSLLGELAED--RTVIVSTHLLEDLQEFVSQLAVLSEGE 207
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-160 |
3.06e-36 |
|
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: 125.45 E-value: 3.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 19 DISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTI-RSMVGFLPQRFSLPLHFRIRRAVEY 96
Cdd:pfam00005 3 NVSLTLNPGeILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRENLRL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488470846 97 AAWARGVEPRECCVRAGAALDRVGLVDRADDRVQ----SLSGGMRQRLGIACAIVGDPAVLLLDEPTV 160
Cdd:pfam00005 83 GLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-188 |
3.98e-36 |
|
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: 126.88 E-value: 3.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD---DVNTIRSMVGF 77
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGeVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQRFSLPLHFRIRRAVEYA-AWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLD 156
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLApIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190
....*....|....*....|....*....|...
gi 488470846 157 EPTVGLDPASRIGVRSLLGELAED-RTVIVSTH 188
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEgMTMVVVTH 193
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-225 |
4.47e-36 |
|
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: 128.00 E-value: 4.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRY----RRRRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVN-TIRSM 74
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESfGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 75 VGFLPQ--RFSLPLHFRIRRAVEYAAWARGVEPREccVRAGAALDRVGLVDR-ADDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILAEPLRIHGLPDRE--ERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488470846 152 VLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDLESvGQKHP 225
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA-GPKHP 233
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-217 |
5.59e-36 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 127.41 E-value: 5.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRY-RRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD----DVNTIRSM 74
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGeFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrgkKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 75 VGFLPQRFSL---------PLHFRIRRAVEYAAWArGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACA 145
Cdd:TIGR02315 81 IGMIFQHYNLierltvlenVLHGRLGYKPTWRSLL-GRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488470846 146 IVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-221 |
7.42e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 129.95 E-value: 7.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFLPQ 80
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGeCFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 RFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTV 160
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488470846 161 GLDPASRIGV----RSLlgeLAEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL--ESVG 221
Cdd:PRK13536 202 GLDPHARHLIwerlRSL---LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALidEHIG 265
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-217 |
7.61e-36 |
|
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: 126.85 E-value: 7.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD----DVNTIRSMVG 76
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGeILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 77 FLPQR---FS---------LPL--HFR-----IRRAVeyaawargvepRECcvragaaLDRVGLVDRADDRVQSLSGGMR 137
Cdd:cd03261 81 MLFQSgalFDsltvfenvaFPLreHTRlseeeIREIV-----------LEK-------LEAVGLRGAEDLYPAELSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 138 QRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAE--DRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYS 215
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPE 222
|
..
gi 488470846 216 DL 217
Cdd:cd03261 223 EL 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-204 |
9.18e-36 |
|
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: 126.43 E-value: 9.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLV----DISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDdvntIRSMVG 76
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaleDISLSVEEGeFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG----PGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 77 FLPQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLD 156
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488470846 157 EPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHlleDLQE--FVSQ-LAVLS 204
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETgkTVLLVTH---DIDEavFLADrVVVLS 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-213 |
2.39e-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: 131.18 E-value: 2.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYR--RRRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPE---SGHFRVNGVDVSDDVNTIRS- 73
Cdd:COG1123 4 LLEVRDLSVRYPggDVPAVDGVSLTIAPGETvALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 74 MVGFLPQRFSLPLH-FRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAV 152
Cdd:COG1123 84 RIGMVFQDPMTQLNpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488470846 153 LLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-218 |
7.56e-35 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 124.05 E-value: 7.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS-DDVNTIRSMVGflp 79
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNsVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTrKDLHKIGSLIE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 80 qrfSLPL--HFRIRRAVEYAAWARGVEPReccvRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDE 157
Cdd:TIGR03740 78 ---SPPLyeNLTARENLKVHTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488470846 158 PTVGLDPasrIGV---RSLLGELAED-RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYS---DLE 218
Cdd:TIGR03740 151 PTNGLDP---IGIqelRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVLGYQGKINkseNLE 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-212 |
7.64e-35 |
|
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: 123.04 E-value: 7.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 13 RRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPE--SGHFRVNGVDVSDDvnTIRSMVGFLPQRFSLPLHFR 89
Cdd:cd03213 21 GKQLLKNVSGKAKPGeLTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKR--SFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 90 IRRAVEYAAwargvepreccvragaaldrvglvdraddRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIG 169
Cdd:cd03213 99 VRETLMFAA-----------------------------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488470846 170 VRSLLGELAED-RTVIVSTH-LLEDLQEFVSQLAVLSEGELIFEG 212
Cdd:cd03213 150 VMSLLRRLADTgRTIICSIHqPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-212 |
1.02e-34 |
|
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: 123.98 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 4 LEHISHR-YRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGF---- 77
Cdd:cd03267 23 LKSLFKRkYREVEALKGISFTIEKGeIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVvfgq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 -------LPQRFSLPLHFRIRRaVEYAAWARGVEprECCvragAALDRVGLVDRAddrVQSLSGGMRQRLGIACAIVGDP 150
Cdd:cd03267 103 ktqlwwdLPVIDSFYLLAAIYD-LPPARFKKRLD--ELS----ELLDLEELLDTP---VRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488470846 151 AVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEG 212
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-207 |
1.15e-34 |
|
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: 122.11 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRY--RRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGF 77
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGeKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQR---FSLPLHFRIrraveyaawargvepreccvragaaldrvglvdraddrvqsLSGGMRQRLGIACAIVGDPAVLL 154
Cdd:cd03228 81 VPQDpflFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488470846 155 LDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEFvSQLAVLSEGE 207
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-217 |
1.54e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 125.69 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFLPQ 80
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGeCFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 RFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTV 160
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488470846 161 GLDPASR----IGVRSLlgeLAEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:PRK13537 168 GLDPQARhlmwERLRSL---LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-216 |
1.64e-34 |
|
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: 123.32 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGF--- 77
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGeIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIgrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 --LPQRFS---------LPLHFRIRRAVEYAAWARgvEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAI 146
Cdd:cd03219 81 fqIPRLFPeltvlenvmVAAQARTGSGLLLARARR--EEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488470846 147 VGDPAVLLLDEPTVGLDPASRIGVRSLLGELAE-DRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSD 216
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-217 |
2.19e-34 |
|
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: 129.12 E-value: 2.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRY--RRRRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGF 77
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERvAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQRFSLplhFR--IR--------RAVEYAAWArgvepreccvragaALDRVGLVDRA-------DDRV----QSLSGGM 136
Cdd:COG4987 414 VPQRPHL---FDttLRenlrlarpDATDEELWA--------------ALERVGLGDWLaalpdglDTWLgeggRRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 137 RQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLqEFVSQLAVLSEGELIFEGSYSD 216
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGTHEE 555
|
.
gi 488470846 217 L 217
Cdd:COG4987 556 L 556
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-217 |
3.21e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 125.19 E-value: 3.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLV----DISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD----DVNTI 71
Cdd:COG1135 1 MIELENLSKTFPTKGGPVtaldDVSLTIEKGeIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 72 RSMVGFLPQRFSLpLHFR-----IRRAVEYAawarGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAI 146
Cdd:COG1135 81 RRKIGMIFQHFNL-LSSRtvaenVALPLEIA----GVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488470846 147 VGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-213 |
5.33e-34 |
|
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: 129.36 E-value: 5.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 24 FDSGLWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFLPQRFSLPLHFRIRRAVEYAAWARGV 103
Cdd:TIGR01257 954 YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGR 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 104 EPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTV 183
Cdd:TIGR01257 1034 SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTI 1113
|
170 180 190
....*....|....*....|....*....|
gi 488470846 184 IVSTHLLEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:TIGR01257 1114 IMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-188 |
6.18e-34 |
|
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: 121.36 E-value: 6.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRY-RRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD----DVNTIRSMV 75
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGeFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 76 GFLPQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLL 155
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190
....*....|....*....|....*....|....
gi 488470846 156 DEPTVGLDPASRIGVRSLLGEL-AEDRTVIVSTH 188
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATH 194
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-217 |
6.91e-34 |
|
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: 127.95 E-value: 6.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRY-RRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFL 78
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGeRVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQR---FSLPLHFRIRRAVEYAAWArgvEPRECCVRAGAA---------LD-RVGlvdradDRVQSLSGGMRQRLGIACA 145
Cdd:COG4988 417 PQNpylFAGTIRENLRLGRPDASDE---ELEAALEAAGLDefvaalpdgLDtPLG------EGGRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488470846 146 IVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLqEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEEL 558
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-209 |
7.26e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 124.83 E-value: 7.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDdVNTIRSMVGFLP 79
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGeFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG-LPPEKRNVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 80 QRFSL-PlHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEP 158
Cdd:COG3842 84 QDYALfP-HLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488470846 159 TVGLDPASRIGVRSLLGELAEDR--TVIVSTHlleDLQEFVS---QLAVLSEGELI 209
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELgiTFIYVTH---DQEEALAladRIAVMNDGRIE 215
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-213 |
7.68e-34 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 122.54 E-value: 7.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRR--RRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDD--VNTIRSMVG 76
Cdd:TIGR04520 1 IEVENVSFSYPEseKPALKNVSLSIEKGEFvAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEenLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 77 FLpqrFSLPLHFRIRRAVEY-AAWA---RGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAV 152
Cdd:TIGR04520 81 MV---FQNPDNQFVGATVEDdVAFGlenLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488470846 153 LLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHlleDLQEFVS--QLAVLSEGELIFEGS 213
Cdd:TIGR04520 158 IILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITH---DMEEAVLadRVIVMNKGKIVAEGT 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-193 |
1.00e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 120.03 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 10 RYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGvdvsddvntiRSMVGFLPQRFSLP--L 86
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGsLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----------GARVAYVPQRSEVPdsL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 87 HFRIRRAVEYAAWAR----GVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGL 162
Cdd:NF040873 71 PLTVRDLVAMGRWARrglwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|..
gi 488470846 163 DPASRIGVRSLLGELAED-RTVIVSTHLLEDL 193
Cdd:NF040873 151 DAESRERIIALLAEEHARgATVVVVTHDLELV 182
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-212 |
1.07e-33 |
|
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: 120.86 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 19 DISCEFDSGLWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTI-----RSMVGFLPQRFSLPLHFRIRRA 93
Cdd:cd03297 16 KIDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqQRKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 94 VEYAAwaRGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSL 173
Cdd:cd03297 96 LAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488470846 174 LGELAED--RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEG 212
Cdd:cd03297 174 LKQIKKNlnIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-212 |
3.88e-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: 119.53 E-value: 3.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLV----DISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD----DVNTI 71
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkaldDVSFSIKKGETlGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsrrLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 72 RSMVGFLPQ--RFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLV---DRADDRVQSLSGGMRQRLGIACAI 146
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488470846 147 VGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEG 212
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-213 |
4.89e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 120.12 E-value: 4.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFL 78
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGkITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQRFSLPLHFRIRRAVEY------AAWAR-GVEPREccvRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYgrspwlSLWGRlSAEDNA---RVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488470846 152 VLLLDEPTVGLDPASRIGVRSLLGEL-AEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-216 |
2.09e-32 |
|
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: 118.60 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS----DDVN------ 69
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGeIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglppHRIArlgiar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 70 ---TIRsmvgfLPQRFS------LPLHFRIRRAVEYAA---WARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMR 137
Cdd:COG0411 84 tfqNPR-----LFPELTvlenvlVAAHARLGRGLLAALlrlPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 138 QRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHlleDLqEFVSQLA----VLSEGELIFE 211
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEH---DM-DLVMGLAdrivVLDFGRVIAE 234
|
....*
gi 488470846 212 GSYSD 216
Cdd:COG0411 235 GTPAE 239
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-209 |
2.51e-32 |
|
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: 116.97 E-value: 2.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 3 ELEHISHRYRRRRSLVD-ISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDdvNTIRSMVGFLPQ 80
Cdd:cd03226 1 RIENISFSYKKGTEILDdLSLDLYAGEIiALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA--KERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 R-----FS----LPLHFRIRRAVEYAAWARGVepreccvragaaLDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:cd03226 79 DvdyqlFTdsvrEELLLGLKELDAGNEQAETV------------LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 152 VLLLDEPTVGLDPASRIGVRSLLGELA-EDRTVIVSTHLLEDLQEFVSQLAVLSEGELI 209
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-221 |
6.04e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 118.23 E-value: 6.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRR-----RRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD---DVNTIR 72
Cdd:PRK13637 3 IKIENLTHIYMEgtpfeKKALDNVNIEIEDGEFvGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 73 SMVGFLpqrFSLPLH--FR--IRRAVEYAAWARGVEPRECCVRAGAALDRVGLvDRADDRVQS---LSGGMRQRLGIACA 145
Cdd:PRK13637 83 KKVGLV---FQYPEYqlFEetIEKDIAFGPINLGLSEEEIENRVKRAMNIVGL-DYEDYKDKSpfeLSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 146 IVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSD------- 216
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREvfkevet 238
|
....*
gi 488470846 217 LESVG 221
Cdd:PRK13637 239 LESIG 243
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-209 |
8.07e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 119.10 E-value: 8.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFLPQ 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGeLVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 RFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTV 160
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488470846 161 GLDPASRIGVRSLLGELAED--RTVIVSTHLLEDLQEFVSQLAVLSEGELI 209
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDElgGTTVFVTHDQEEALELADRVVVMNQGRIE 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-208 |
4.16e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 117.48 E-value: 4.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD------DVntirS 73
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGeFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDlppkdrNI----A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 74 MVgflPQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVL 153
Cdd:COG3839 79 MV---FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 154 LLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHlleDLQE---FVSQLAVLSEGEL 208
Cdd:COG3839 156 LLDEPLSNLDAKLRVEMRAEIKRLHRRLgtTTIYVTH---DQVEamtLADRIAVMNDGRI 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-217 |
1.17e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 113.65 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD---DVNTIRSMVG 76
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGeVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 77 FLPQRFSLPLHFRirrAVEYAAWA----RGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAV 152
Cdd:PRK09493 81 MVFQQFYLFPHLT---ALENVMFGplrvRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488470846 153 LLLDEPTVGLDPASRIGVRSLLGELAED-RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-213 |
1.21e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.10 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD----DVNTIRSMv 75
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGeVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspaELARRRAV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 76 gfLPQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIV------GD 149
Cdd:PRK13548 81 --LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 150 PAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHlleDLQ---EFVSQLAVLSEGELIFEGS 213
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLH---DLNlaaRYADRIVLLHQGRLVADGT 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-212 |
1.94e-30 |
|
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: 112.30 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRY--RRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGF 77
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGeKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQRFSL-------------PLH--FRIRRAVEYAawargveprecCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGI 142
Cdd:cd03245 83 VPQDVTLfygtlrdnitlgaPLAddERILRAAELA-----------GVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 143 ACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQeFVSQLAVLSEGELIFEG 212
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-217 |
2.57e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 117.96 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRS-LVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFL 78
Cdd:COG1132 340 IEFENVSFSYPGDRPvLKDISLTIPPGeTVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQRFSLpLHFRIRRAVEYAA-WARGVEPRECCVRAGAA---------LD-RVGlvdradDRVQSLSGGMRQRLGIACAIV 147
Cdd:COG1132 420 PQDTFL-FSGTIRENIRYGRpDATDEEVEEAAKAAQAHefiealpdgYDtVVG------ERGVNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 148 GDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEfVSQLAVLSEGELIFEGSYSDL 217
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEEL 561
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-237 |
2.90e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 112.16 E-value: 2.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRslVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIR--SMvgf 77
Cdd:COG3840 1 MLRLDDLTYRYGDFP--LRFDLTIAAGERvAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERpvSM--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQRFSLPLHFRIRRAVeyaawARGVEP-----RECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAV 152
Cdd:COG3840 76 LFQENNLFPHLTVAQNI-----GLGLRPglkltAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 153 LLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDLESvgqkhpvRNAN 230
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLD-------GEPP 223
|
....*..
gi 488470846 231 DAEAGYL 237
Cdd:COG3840 224 PALAAYL 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-217 |
8.68e-30 |
|
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: 111.28 E-value: 8.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDdVNTIRSMVGFLPQ 80
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGeLVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD-VPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 RFSLPLHFRIRRAVEYAAWARGVEPR----ECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLD 156
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488470846 157 EPTVGLDPASRIGVRSLLGELAED---RTVIVsTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDElhvTTVFV-THDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-213 |
1.53e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 110.98 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD----DVNTIRsmv 75
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGeLTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwspwELARRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 76 GFLPQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIA-------CAIVG 148
Cdd:COG4559 78 AVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLArvlaqlwEPVDG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 149 DPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR-TVIVSTHlleDLQ---EFVSQLAVLSEGELIFEGS 213
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLARRGgGVVAVLH---DLNlaaQYADRILLLHQGRLVAQGT 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
31-209 |
2.64e-29 |
|
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: 110.81 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS----DDVNTIR----SMVgFlpQRFSLPLHFRIRRAVEYAAWARG 102
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamsrKELRELRrkkiSMV-F--QSFALLPHRTVLENVAFGLEVQG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 103 VEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAED-- 180
Cdd:cd03294 132 VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElq 211
|
170 180 190
....*....|....*....|....*....|..
gi 488470846 181 RTVIVSTHlleDLQEFV---SQLAVLSEGELI 209
Cdd:cd03294 212 KTIVFITH---DLDEALrlgDRIAIMKDGRLV 240
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-213 |
2.69e-29 |
|
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: 110.08 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLV-DISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFL 78
Cdd:cd03295 1 IEFENVTKRYGGGKKAVnNLNLEIAKGeFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDR--ADDRVQSLSGGMRQRLGIACAIVGDPAVLLLD 156
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488470846 157 EPTVGLDPASRIGVRSLLGELAED--RTVIVSTHlleDLQEFV---SQLAVLSEGELIFEGS 213
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQElgKTIVFVTH---DIDEAFrlaDRIAIMKNGEIVQVGT 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-244 |
3.26e-29 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 115.22 E-value: 3.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDV--NTIRSMVGFL 78
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGcMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARhrRAVCPRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQRF--SLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLD 156
Cdd:NF033858 82 PQGLgkNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 157 EPTVGLDPASRIGVRSLLGELAEDR---TVIVSTHLLEDLQEFvSQLAVLSEGELIFEGSYSDL-ESVGqkhpvrnANDA 232
Cdd:NF033858 162 EPTTGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELlARTG-------ADTL 233
|
250
....*....|..
gi 488470846 233 EAGYLTLLGEAA 244
Cdd:NF033858 234 EAAFIALLPEEK 245
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-212 |
4.10e-29 |
|
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: 109.28 E-value: 4.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 14 RRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPE---SGHFRVNGVDVSDDvnTIRSMVGFLPQRFSLPLHFR 89
Cdd:cd03234 20 ARILNDVSLHVESGqVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPD--QFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 90 IRRAVEYAAWARGVEPRECCVR----AGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPA 165
Cdd:cd03234 98 VRETLTYTAILRLPRKSSDAIRkkrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488470846 166 SRIGVRSLLGELA-EDRTVIVSTHL-LEDLQEFVSQLAVLSEGELIFEG 212
Cdd:cd03234 178 TALNLVSTLSQLArRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-217 |
5.48e-29 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 109.24 E-value: 5.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLV--DISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGF 77
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlrDISLDIPAGeTVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQRFSLpLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRV-----GLVDRADDRVQSLSGGMRQRLGIACAIVGDPAV 152
Cdd:cd03251 81 VSQDVFL-FNDTVAENIAYGRPGATREEVEEAARAANAHEFImelpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488470846 153 LLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEfVSQLAVLSEGELIFEGSYSDL 217
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-217 |
1.05e-28 |
|
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: 108.40 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSM--VGFL 78
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGeIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQRFSLplhFR-------IRRAVEYaawaRGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:cd03218 81 PQEASI---FRkltveenILAVLEI----RGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488470846 152 VLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVST-HLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
16-226 |
1.20e-28 |
|
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: 108.19 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 16 SLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDdVNTIRSMVGFLPQRFSLPLHFRIRRAV 94
Cdd:cd03299 14 KLKNVSLEVERGDYfVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN-LPPEKRDISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 95 EYAAWARGVE----PREccVRAGAALDRVG-LVDRaddRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIG 169
Cdd:cd03299 93 AYGLKKRKVDkkeiERK--VLEIAEMLGIDhLLNR---KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 170 VRSLLGELAE--DRTVIVSTHLLEDLQEFVSQLAVLSEGELIfegSYSDLESVgQKHPV 226
Cdd:cd03299 168 LREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLI---QVGKPEEV-FKKPK 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-223 |
1.28e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 109.33 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYR--RRRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDD-VNTIRSMVGF 77
Cdd:PRK13635 6 IRVEHISFRYPdaATYALKDVSFSVYEGEWvAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQ----RFslpLHFRIRRAVEYAAWARGVePRECCV-RAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAV 152
Cdd:PRK13635 86 VFQnpdnQF---VGATVQDDVAFGLENIGV-PREEMVeRVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488470846 153 LLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHlleDLQE--FVSQLAVLSEGELIFEGSYSDLESVGQK 223
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITH---DLDEaaQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-215 |
3.39e-28 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 107.41 E-value: 3.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNG--VDVSDDVNT-----IRS 73
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGeTLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqFDFSQKPSEkairlLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 74 MVGFLPQRFSLPLHFRIRR-AVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAV 152
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMEnLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488470846 153 LLLDEPTVGLDPASRIGVRSLLGELAEDR-TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYS 215
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-217 |
5.20e-28 |
|
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: 106.59 E-value: 5.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 5 EHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSM--VGFLPQR 81
Cdd:TIGR04406 5 ENLIKSYKKRKVVNDVSLSVKSGeIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARlgIGYLPQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 82 FSLplhFR-------IRRAVEYAAWARGVEPREccvRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLL 154
Cdd:TIGR04406 85 ASI---FRkltveenIMAVLEIRKDLDRAEREE---RLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488470846 155 LDEPTVGLDPASRIGVRSLLGELAEDRT-VIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:TIGR04406 159 LDEPFAGVDPIAVGDIKKIIKHLKERGIgVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-188 |
7.28e-28 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 105.98 E-value: 7.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLV----DISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS----DDVNTI 71
Cdd:COG4181 8 IIELRGLTKTVGTGAGELtilkGISLEVEAGeSVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldeDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 72 RS-MVGFLPQRF------------SLPLHFRIRRaveyaawargvEPREccvRAGAALDRVGLVDRADDRVQSLSGGMRQ 138
Cdd:COG4181 88 RArHVGFVFQSFqllptltalenvMLPLELAGRR-----------DARA---RARALLERVGLGHRLDHYPAQLSGGEQQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488470846 139 RLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTH 188
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTH 205
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-206 |
7.46e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 106.87 E-value: 7.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRY----RRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDV----SDdvnti 71
Cdd:COG4525 3 MLTVRHVSVRYpgggQPQPALQDVSLTIESGeFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgAD----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 72 RSMV----GFLPQRfslplhfRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIV 147
Cdd:COG4525 78 RGVVfqkdALLPWL-------NVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488470846 148 GDPAVLLLDEPTVGLDPASRIGVRSLLGELAED--RTVIVSTHLLEDLQEFVSQLAVLSEG 206
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQELLLDVWQRtgKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-209 |
1.25e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 105.89 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEF-DSGLWGLLGPNGAGKSTLLSILATLRE--PE---SGHFRVNGVDVSD---DVNTIR 72
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIpENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIYDpdvDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 73 SMVGFLPQRfSLPLHFRIRRAVEYAAWARGVEPR-ECCVRAGAALDRVGL---V-DRADDRVQSLSGGMRQRLGIACAIV 147
Cdd:COG1117 92 RRVGMVFQK-PNPFPKSIYDNVAYGLRLHGIKSKsELDEIVEESLRKAALwdeVkDRLKKSALGLSGGQQQRLCIARALA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488470846 148 GDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHlleDLQEF--VSQ-LAVLSEGELI 209
Cdd:COG1117 171 VEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTH---NMQQAarVSDyTAFFYLGELV 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-212 |
1.39e-27 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 103.93 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLV--DISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFL 78
Cdd:cd03247 1 LSINNVSFSYPEQEQQVlkNLSLELKQGeKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQRfslPLHFrirraveyaawargvepreccvrAGAALDRVGLvdraddrvqSLSGGMRQRLGIACAIVGDPAVLLLDEP 158
Cdd:cd03247 81 NQR---PYLF-----------------------DTTLRNNLGR---------RFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488470846 159 TVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLqEFVSQLAVLSEGELIFEG 212
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGI-EHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-217 |
1.59e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 106.36 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRR-RRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS-DDVNTIRSMVGFL 78
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGsKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 -----PQRFSLPlhfrIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVL 153
Cdd:PRK13647 85 fqdpdDQVFSST----VWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488470846 154 LLDEPTVGLDPASRIGVRSLLGEL-AEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-193 |
1.86e-27 |
|
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: 109.68 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVD-ISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFL 78
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRpVSFTVPPGeRVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQR---FSLPLHFRIRRAVEYAAWArgvEPRECCVRAGAA-LDRV---GLVDRADDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:TIGR02857 402 PQHpflFAGTIAENIRLARPDASDA---EIREALERAGLDeFVAAlpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488470846 152 VLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDL 193
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALA 520
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-188 |
1.93e-27 |
|
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: 104.64 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD----DVNTirSMVg 76
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGeFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlppkDRDI--AMV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 77 FlpQRFSLPLHFRIRRAVEYAAWARGVEPRECC--VRAGAALDRVG-LVDRaddRVQSLSGGMRQRLGIACAIVGDPAVL 153
Cdd:cd03301 78 F--QNYALYPHMTVYDNIAFGLKLRKVPKDEIDerVREVAELLQIEhLLDR---KPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 488470846 154 LLDEPTVGLDPASRIGVRSLLGELAE--DRTVIVSTH 188
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTH 189
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-213 |
2.29e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.17 E-value: 2.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFL 78
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGgITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQRFSLPLHFRIRRAVEYAAW--ARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLD 156
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFpySKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488470846 157 EPTVGLDPASRIGVRSLLGELAED--RTVIVSTHlleDLQeFVSQLA----VLSEGELIFEGS 213
Cdd:COG4604 161 EPLNNLDMKHSVQMMKLLRRLADElgKTVVIVLH---DIN-FASCYAdhivAMKDGRVVAQGT 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-206 |
4.20e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 106.71 E-value: 4.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSdDVNTIRSMVGFLPQ 80
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGqMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS-RLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 RFSLplhFRIRRAVEYAAWARGVEPREccVRAGAA---------LDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:PRK10851 82 HYAL---FRHMTVFDNIAFGLTVLPRR--ERPNAAaikakvtqlLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488470846 152 VLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEG 206
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-206 |
5.28e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 104.40 E-value: 5.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDvNTIRSMV---- 75
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGeLLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP-GAERGVVfqne 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 76 GFLPQRfslplhfRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLL 155
Cdd:PRK11248 80 GLLPWR-------NVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488470846 156 DEPTVGLDPASRIGVRSLLGELAED--RTVIVSTHLLEDLQEFVSQLAVLSEG 206
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-215 |
6.13e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 103.94 E-value: 6.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRV--NGVDVSDDVN-----TIRS 73
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGeTLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFSKTPSdkairELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 74 MVGFLPQRFSLPLHFRIRR-AVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAV 152
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQnLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488470846 153 LLLDEPTVGLDPASRIGVRSLLGELAEDR-TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYS 215
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-188 |
1.07e-26 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 107.89 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLV----DISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTI--- 71
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVevlkGISLDIYAGeMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADALaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 72 -RSMVGFLPQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDP 150
Cdd:PRK10535 84 rREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 488470846 151 AVLLLDEPTVGLDPASRIGVRSLLGELAED-RTVIVSTH 188
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTH 202
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-217 |
1.40e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.05 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYR-----RRRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-----DVN 69
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYtALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStskqkEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 70 TIRSMVGFLpqrFSLP----LHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQ-SLSGGMRQRLGIAC 144
Cdd:PRK13643 81 PVRKKVGVV---FQFPesqlFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488470846 145 AIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAED-RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-217 |
1.68e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.67 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYR-----RRRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-----DVNT 70
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYtAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 71 IRSMVGFLPQrFSLPLHFR--IRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQ-SLSGGMRQRLGIACAIV 147
Cdd:PRK13649 83 IRKKVGLVFQ-FPESQLFEetVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPfELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488470846 148 GDPAVLLLDEPTVGLDPASRIGVRSLLGELAED-RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-217 |
2.78e-26 |
|
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: 101.93 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD------DVNTIrsm 74
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGeFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpphkrPVNTV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 75 vgFlpQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLL 154
Cdd:cd03300 78 --F--QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488470846 155 LDEPTVGLDPASRigvRSLLGELAE--DR---TVIVSTHlleDLQEFVS---QLAVLSEGELIFEGSYSDL 217
Cdd:cd03300 154 LDEPLGALDLKLR---KDMQLELKRlqKElgiTFVFVTH---DQEEALTmsdRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-217 |
2.93e-26 |
|
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: 101.85 E-value: 2.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRS---LVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVG 76
Cdd:cd03249 1 IEFKNVSFRYPSRPDvpiLKGLSLTIPPGkTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 77 FLPQRfslPLHF--RIRRAVEYAAWARGVEPRECCVRAGAALDRV-GLVDRADDRV----QSLSGGMRQRLGIACAIVGD 149
Cdd:cd03249 81 LVSQE---PVLFdgTIAENIRYGKPDATDEEVEEAAKKANIHDFImSLPDGYDTLVgergSQLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488470846 150 PAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEfVSQLAVLSEGELIFEGSYSDL 217
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDEL 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-216 |
2.99e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 104.11 E-value: 2.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLV----DISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDV----SDDVNTI 71
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIhalnNVSLHIPAGeIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 72 RSMVGFLPQRFSLpLHFR-----IRRAVEYAAWARgvepRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAI 146
Cdd:PRK11153 81 RRQIGMIFQHFNL-LSSRtvfdnVALPLELAGTPK----AEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488470846 147 VGDPAVLLLDEPTVGLDPASrigVRSLLGELAE-DR----TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSD 216
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPAT---TRSILELLKDiNRelglTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
18-206 |
4.42e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.54 E-value: 4.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 18 VDISCEfDSGLWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFLPQRFSLPLHFRIRRAVEY 96
Cdd:PRK09536 22 VDLSVR-EGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlSARAASRRVASVPQDTSLSFEFDVRQVVEM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 97 ------AAWARGVEPRECCVRAgaALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGV 170
Cdd:PRK09536 101 grtphrSRFDTWTETDRAAVER--AMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRT 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 488470846 171 RSLLGELAED-RTVIVSTHLLEDLQEFVSQLAVLSEG 206
Cdd:PRK09536 179 LELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-213 |
7.35e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.87 E-value: 7.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDvntirSM----- 74
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGeIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-----PMhkrar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 75 --VGFLPQRFSLplhFR-------IRRAVEYaawaRGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACA 145
Cdd:COG1137 78 lgIGYLPQEASI---FRkltvednILAVLEL----RKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 146 IVGDPAVLLLDEPTVGLDPasrIGVrsllgelaedrtvivsthllEDLQEFVSQLA------------------------ 201
Cdd:COG1137 151 LATNPKFILLDEPFAGVDP---IAV--------------------ADIQKIIRHLKergigvlitdhnvretlgicdray 207
|
250
....*....|..
gi 488470846 202 VLSEGELIFEGS 213
Cdd:COG1137 208 IISEGKVLAEGT 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
13-213 |
7.38e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 105.51 E-value: 7.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 13 RRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPE---SGHFRVNGVDVsdDVNTIRSMVGFLpQRFSLPL-- 86
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGeLLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI--DAKEMRAISAYV-QQDDLFIpt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 87 -----------HFRIRRAVEYaawargVEPREccvRAGAALDRVGLVDRAD------DRVQSLSGGMRQRLGIACAIVGD 149
Cdd:TIGR00955 114 ltvrehlmfqaHLRMPRRVTK------KEKRE---RVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488470846 150 PAVLLLDEPTVGLDPASRIGVRSLLGELAED-RTVIVSTHL-LEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKgKTIICTIHQpSSELFELFDKIILMAEGRVAYLGS 250
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-217 |
8.35e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 105.29 E-value: 8.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLV--DISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGF 77
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVlkGLSLQIKAGeKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQR---FSLPLHFRIRRAVEYAAWARGVEpreccvragaALDRVGLVDRADDRV----------QSLSGGMRQRLGIAC 144
Cdd:PRK11160 419 VSQRvhlFSATLRDNLLLAAPNASDEALIE----------VLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488470846 145 AIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEFvSQLAVLSEGELIFEGSYSDL 217
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQEL 560
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-213 |
1.23e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.22 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLV--DISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDD-VNTIRSMVG 76
Cdd:PRK13632 7 MIKVENVSFSYPNSENNAlkNVSFEINEGEYvAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 77 FLpqrFSLPLHFRIRRAVEyAAWARGVEPRecCVRAGA-------ALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGD 149
Cdd:PRK13632 87 II---FQNPDNQFIGATVE-DDIAFGLENK--KVPPKKmkdiiddLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488470846 150 PAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHlleDLQEFV--SQLAVLSEGELIFEGS 213
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITH---DMDEAIlaDKVIVFSEGKLIAQGK 225
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
1.70e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 101.70 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRR----------RSLV-----------DISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFR 58
Cdd:COG4586 1 IIEVENLSKTYRVYekepglkgalKGLFrreyreveavdDISFTIEPGeIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 59 VNGVDVSDDVNTIRSMVGF-LPQR----FSLPLH--FRIRRAVeYaawarGVEPRECCVRAGAALDRVGLVDRADDRVQS 131
Cdd:COG4586 81 VLGYVPFKRRKEFARRIGVvFGQRsqlwWDLPAIdsFRLLKAI-Y-----RIPDAEYKKRLDELVELLDLGELLDTPVRQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 132 LSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELI 209
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
....*...
gi 488470846 210 FEGSYSDL 217
Cdd:COG4586 235 YDGSLEEL 242
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-188 |
3.14e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.44 E-value: 3.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDD---------VNT 70
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGeVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 71 IRSMVGFLPQRFSL-PLHFRIRRAVEYAAWARGvEPRECCV-RAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVG 148
Cdd:PRK11264 83 LRQHVGFVFQNFNLfPHRTVLENIIEGPVIVKG-EPKEEATaRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488470846 149 DPAVLLLDEPTVGLDPASRIGVRSLLGELAED-RTVIVSTH 188
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTH 202
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-213 |
5.82e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 99.71 E-value: 5.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYR-----RRRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRV------NGVDvSDDVN 69
Cdd:PRK13634 3 ITFQKVEHRYQyktpfERRALYDVNVSIPSGSYvAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKK-NKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 70 TIRSMVGFLpqrFSLPLHFRIRRAVE----YAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQ-SLSGGMRQRLGIAC 144
Cdd:PRK13634 82 PLRKKVGIV---FQFPEHQLFEETVEkdicFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488470846 145 AIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARYADQIVVMHKGTVFLQGT 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-217 |
7.60e-25 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 102.49 E-value: 7.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRY--RRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGF 77
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGeTVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQRFSLplhFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQS--------LSGGMRQRLGIACAIVGD 149
Cdd:TIGR02203 411 VSQDVVL---FNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTpigengvlLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488470846 150 PAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEfVSQLAVLSEGELIFEGSYSDL 217
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNEL 554
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-217 |
9.85e-25 |
|
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: 98.07 E-value: 9.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYR-RRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFL 78
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGkKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQRFSLpLHFRIRRAVEYAAW-ARGVEPRECCVRAGAALDRVGLVDRADDRVQS----LSGGMRQRLGIACAIVGDPAVL 153
Cdd:cd03253 81 PQDTVL-FNDTIGYNIRYGRPdATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488470846 154 LLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHlleDLQEFVS--QLAVLSEGELIFEGSYSDL 217
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAH---RLSTIVNadKIIVLKDGRIVERGTHEEL 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
1.03e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 98.67 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRS--LVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS-DDVNTIRSMVG 76
Cdd:PRK13648 7 IIVFKNVSFQYQSDASftLKDVSFNIPKGQWtSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITdDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 77 FLpqrFSLPLHFRIRRAVEYAAwARGVE----PRECCVR-AGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:PRK13648 87 IV---FQNPDNQFVGSIVKYDV-AFGLEnhavPYDEMHRrVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488470846 152 VLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHlleDLQEFV--SQLAVLSEGELIFEGSYSDLESVGQ 222
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITH---DLSEAMeaDHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-208 |
1.14e-24 |
|
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: 96.13 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRY--RRRRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGF 77
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESlAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQRFSLplhFrirraveyaawargvepreccvrAGAALDRVglvdraddrvqsLSGGMRQRLGIACAIVGDPAVLLLDE 157
Cdd:cd03246 81 LPQDDEL---F-----------------------SGSIAENI------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488470846 158 PTVGLDPASRIGVRSLLGEL-AEDRTVIVSTHLLEDLQEfVSQLAVLSEGEL 208
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-209 |
1.24e-24 |
|
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: 95.57 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSddvntirsmvgflpq 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGeVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 rFSLPLHfrirraveyaAWARGVEpreccvragaaldrvglvdraddRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTV 160
Cdd:cd03216 66 -FASPRD----------ARRAGIA-----------------------MVYQLSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488470846 161 GLDPASRIGVRSLLGEL-AEDRTVIVSTHLLEDLQEFVSQLAVLSEGELI 209
Cdd:cd03216 112 ALTPAEVERLFKVIRRLrAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-217 |
1.24e-24 |
|
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: 97.30 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRS-LVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFL 78
Cdd:cd03254 3 IEFENVNFSYDEKKPvLKDINFSIKPGeTVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQR---FSLPLHFRIRRAVEYaawARGVEPRECCVRAGAA--LDRV--GLVDRADDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:cd03254 83 LQDtflFSGTIMENIRLGRPN---ATDEEVIEAAKEAGAHdfIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488470846 152 VLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQeFVSQLAVLSEGELIFEGSYSDL 217
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIK-NADKILVLDDGKIIEEGTHDEL 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
31-208 |
1.36e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 96.85 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSmVGFLPQRFSLPLHFRIRRAVeyaawARGVEP----- 105
Cdd:TIGR01277 29 IMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP-VSMLFQENNLFAHLTVRQNI-----GLGLHPglkln 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 106 RECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAE--DRTV 183
Cdd:TIGR01277 103 AEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSerQRTL 182
|
170 180
....*....|....*....|....*
gi 488470846 184 IVSTHLLEDLQEFVSQLAVLSEGEL 208
Cdd:TIGR01277 183 LMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-208 |
1.77e-24 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 96.87 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRR-RRSLVDISCEFDSGLWGLL-GPNGAGKSTLLSILATLREPESGHFRVNGVDVS----DDVNTIRSM 74
Cdd:PRK10908 1 MIRFEHVSKAYLGgRQALQGVTFHMRPGEMAFLtGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 75 VGFLPQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLL 154
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488470846 155 LDEPTVGLDPASRIGVRSLLGELAE-DRTVIVSTHLLEDLQEFVSQLAVLSEGEL 208
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
2.86e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 97.61 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRR-RRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNG--VDVS-DDVNTIRSMV 75
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGeVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSrKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 76 GFL-----PQRFSLPLHfrirRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDP 150
Cdd:PRK13636 85 GMVfqdpdNQLFSASVY----QDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 151 AVLLLDEPTVGLDPASRIGVRSLLGELAE--DRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSdlESVGQKHPVRN 228
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK--EVFAEKEMLRK 238
|
..
gi 488470846 229 AN 230
Cdd:PRK13636 239 VN 240
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-213 |
3.17e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.47 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRY------RRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNT--I 71
Cdd:PRK13633 4 MIKCKNVSYKYesneesTEKLALDDVNLEVKKGeFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwdI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 72 RSMVGFLpqrFSLPLHFRIRRAVE----YAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIV 147
Cdd:PRK13633 84 RNKAGMV---FQNPDNQIVATIVEedvaFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488470846 148 GDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEfVSQLAVLSEGELIFEGS 213
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVE-ADRIIVMDSGKVVMEGT 227
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-208 |
4.33e-24 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 95.88 E-value: 4.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVD----ISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDV----SDDVNTI 71
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRvlkgVSLSIGKGeIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLsklsSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 72 RSM-VGFLPQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDP 150
Cdd:TIGR02211 81 RNKkLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 151 AVLLLDEPTVGLDPASRIGVRSLLGEL-AEDRT-VIVSTHLLEdLQEFVSQLAVLSEGEL 208
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELnRELNTsFLVVTHDLE-LAKKLDRVLEMKDGQL 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
31-213 |
5.77e-24 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 97.56 E-value: 5.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSmVGFLPQRFSLPLHFRIRRAVEYAAWARGVEPRECCV 110
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRH-INMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 111 RAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASR----IGVRSLLGELAedRTVIVS 186
Cdd:TIGR01187 80 RVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRdqmqLELKTIQEQLG--ITFVFV 157
|
170 180
....*....|....*....|....*..
gi 488470846 187 THLLEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
28-218 |
6.48e-24 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 95.69 E-value: 6.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 28 LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDvntiRSMVGFLPQRFSLPLHFRIrrAVEYA---------A 98
Cdd:TIGR03771 8 LLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKG----WRHIGYVPQRHEFAWDFPI--SVAHTvmsgrtghiG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 99 WARgvEPRECCVRA-GAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGEL 177
Cdd:TIGR03771 82 WLR--RPCVADFAAvRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIEL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488470846 178 AEDRTVIV-STHLLEDLQEFVSQLaVLSEGELIFEGSYSDLE 218
Cdd:TIGR03771 160 AGAGTAILmTTHDLAQAMATCDRV-VLLNGRVIADGTPQQLQ 200
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-217 |
7.34e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.40 E-value: 7.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 4 LEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFLPQR 81
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGkVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 82 FSLPLHFRIRRAVE------YAAWAR-GVEPREccvRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLL 154
Cdd:PRK10575 94 LPAAEGMTVRELVAigrypwHGALGRfGAADRE---KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488470846 155 LDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-244 |
7.70e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 99.65 E-value: 7.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRY-RRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFL 78
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGqTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQR---FSLPLHFRIRRAVEYAAWArgvEPRECCVRAgAALDRV-----GLVDRADDRVQSLSGGMRQRLGIACAIVGDP 150
Cdd:PRK13657 415 FQDaglFNRSIEDNIRVGRPDATDE---EMRAAAERA-QAHDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 151 AVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEfVSQLAVLSEGELIFEGSYSDLESVGQkhpvRNAN 230
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVARGG----RFAA 565
|
250
....*....|....
gi 488470846 231 DAEAGYLTLLGEAA 244
Cdd:PRK13657 566 LLRAQGMLQEDERR 579
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-212 |
1.04e-23 |
|
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: 94.48 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRslVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSmVGFLPQ 80
Cdd:cd03298 1 VRLDKIRFSYGEQP--MHFDLTFAQGeITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP-VSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 RFSLPLHFRIRRAVeyaawARGVEPR-----ECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLL 155
Cdd:cd03298 78 ENNLFAHLTVEQNV-----GLGLSPGlkltaEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 156 DEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEG 212
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
30-188 |
2.09e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 98.27 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDV-SDDVNTiRSMVGFLPQRFSL----------PLHfrirraveyaa 98
Cdd:NF033858 296 GFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdAGDIAT-RRRVGYMSQAFSLygeltvrqnlELH----------- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 99 wAR--GVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGE 176
Cdd:NF033858 364 -ARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIE 442
|
170
....*....|....
gi 488470846 177 LA-EDR-TVIVSTH 188
Cdd:NF033858 443 LSrEDGvTIFISTH 456
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-233 |
2.20e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.08 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATL----REPESgHFRVNGVDV------SDDVN 69
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGeMVALLGPSGSGKSTLLRHLSGLitgdKSAGS-HIELLGRTVqregrlARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 70 TIRSMVGFLPQRFSLPLHFRIRRAVEYAAWARGVEPRECCV--------RAGAALDRVGLVDRADDRVQSLSGGMRQRLG 141
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSwftreqkqRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 142 IACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDLES 219
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDN 242
|
250
....*....|....
gi 488470846 220 VGQKHPVRNANDAE 233
Cdd:PRK09984 243 ERFDHLYRSINRVE 256
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
30-188 |
2.22e-23 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 93.26 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS---DDVNTIRSMVGFLPQRFSLPLHF-RIRRAVEYAAWARGVEP 105
Cdd:TIGR01166 22 ALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysrKGLLERRQRVGLVFQDPDDQLFAaDVDQDVAFGPLNLGLSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 106 RECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGEL-AEDRTVI 184
Cdd:TIGR01166 102 AEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAILRRLrAEGMTVV 181
|
....
gi 488470846 185 VSTH 188
Cdd:TIGR01166 182 ISTH 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-219 |
3.73e-23 |
|
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: 98.16 E-value: 3.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 29 WGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFLPQRFSLPLHFRIRRAVEYAAWARGVEPREC 108
Cdd:TIGR01257 1968 FGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEI 2047
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 109 CVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDP-ASRIGVRSLLGELAEDRTVIVST 187
Cdd:TIGR01257 2048 EKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPqARRMLWNTIVSIIREGRAVVLTS 2127
|
170 180 190
....*....|....*....|....*....|..
gi 488470846 188 HLLEDLQEFVSQLAVLSEGELIFEGSYSDLES 219
Cdd:TIGR01257 2128 HSMEECEALCTRLAIMVKGAFQCLGTIQHLKS 2159
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
6.64e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.99 E-value: 6.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRR-RRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNT---IRSMV 75
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGeMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSlleVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 76 GFL-----PQRFSlPlhfRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDP 150
Cdd:PRK13639 81 GIVfqnpdDQLFA-P---TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 151 AVLLLDEPTVGLDPASRIGVRSLLGEL-AEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDLESvgQKHPVRNA 229
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS--DIETIRKA 234
|
.
gi 488470846 230 N 230
Cdd:PRK13639 235 N 235
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-163 |
8.04e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.40 E-value: 8.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD------DVNTIrsm 74
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGeFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpaenrHVNTV--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 75 vgFlpQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLL 154
Cdd:PRK09452 92 --F--QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
....*....
gi 488470846 155 LDEPTVGLD 163
Cdd:PRK09452 168 LDESLSALD 176
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-216 |
9.48e-23 |
|
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: 9.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVnGVDVSddvntirsmVGFLP 79
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGdRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK---------IGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 80 Q-RFSLPLHfriRRAVEY-AAWARGVEPREccVRagAALDRVGLV-DRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLD 156
Cdd:COG0488 385 QhQEELDPD---KTVLDElRDGAPGGTEQE--VR--GYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488470846 157 EPTVGLDPASRigvRSLLGELAE-DRTVIVSTHlleD---LQEFVSQLAVLSEGELI-FEGSYSD 216
Cdd:COG0488 458 EPTNHLDIETL---EALEEALDDfPGTVLLVSH---DryfLDRVATRILEFEDGGVReYPGGYDD 516
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-219 |
1.17e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 92.34 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSGLwGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSmVGFLPQ 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFDLTVERGERV-AILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP-VSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 RFSLPLHFRIRRAVeyaawARGVEP-------RECCVRAGAalDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVL 153
Cdd:PRK10771 79 ENNLFSHLTVAQNI-----GLGLNPglklnaaQREKLHAIA--RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488470846 154 LLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDLES 219
Cdd:PRK10771 152 LLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
25-213 |
1.32e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.13 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 25 DSGLWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNT-IRSMVGFLPQRFSLPLHFRIRRAVeyaawARGV 103
Cdd:PRK10253 32 DGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGLLAQNATTPGDITVQELV-----ARGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 104 EP---------RECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLL 174
Cdd:PRK10253 107 YPhqplftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488470846 175 GELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:PRK10253 187 SELNREKgyTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-217 |
2.38e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.03 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 25 DSGLWGLLGPNGAGKSTLLSILATLREPESGHFRVNGV------DVSD-DVNTIRSMVGFLPQRFSLPLHFRIRRAVEYA 97
Cdd:PRK14246 35 NNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQiDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 98 AWARGV-EPRECCVRAGAALDRVGLVDRADDRVQS----LSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRS 172
Cdd:PRK14246 115 LKSHGIkEKREIKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488470846 173 LLGELAEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:PRK14246 195 LITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-217 |
3.49e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.17 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYR--RRRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPES---GHFRVNGVDV-SDDVNTIRSM 74
Cdd:PRK13640 6 VEFKHVSFTYPdsKKPALNDISFSIPRGSWtALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLtAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 75 VGFLpqrFSLPLHFRIRRAVE----YAAWARGVePRECCVR-AGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGD 149
Cdd:PRK13640 86 VGIV---FQNPDNQFVGATVGddvaFGLENRAV-PRPEMIKiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 150 PAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDlQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDE-ANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-217 |
6.55e-22 |
|
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: 90.62 E-value: 6.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYR--RRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGF 77
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGeVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQRfSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALD-----RVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAV 152
Cdd:cd03252 81 VLQE-NVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDfiselPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488470846 153 LLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEfVSQLAVLSEGELIFEGSYSDL 217
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-190 |
9.66e-22 |
|
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: 93.19 E-value: 9.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRY-RRRRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFL 78
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERvAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQRFSLpLHFRIRRAVEYAAwaRGVEPREccvrAGAALDRVGLVDRADDRV-----------QSLSGGMRQRLGIACAIV 147
Cdd:TIGR02868 415 AQDAHL-FDTTVRENLRLAR--PDATDEE----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488470846 148 GDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLL 190
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-193 |
1.56e-21 |
|
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: 90.88 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLV----DISCEFDSG--LwGLLGPNGAGKSTL-LSILATLREP--ESGHFRVNGVDVSD----D 67
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVkavdGVSFDVRRGetL-GLVGESGSGKSTLaRAILGLLPPPgiTSGEILFDGEDLLKlsekE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 68 VNTIR----SMVgflpqrF-----SL-PLhFRIRRAVEYAAWA-RGVEPRECCVRAGAALDRVGLvDRADDRVQS----L 132
Cdd:COG0444 80 LRKIRgreiQMI------FqdpmtSLnPV-MTVGDQIAEPLRIhGGLSKAEARERAIELLERVGL-PDPERRLDRypheL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488470846 133 SGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHlleDL 193
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITH---DL 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-185 |
1.89e-21 |
|
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: 89.03 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRY-------RRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLL-SILATLRePESGHFRVN----GVDVSD- 66
Cdd:COG4778 4 LLEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGeCVALTGPSGAGKSTLLkCIYGNYL-PDSGSILVRhdggWVDLAQa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 67 DVNTI----RSMVGFLPQrFslpLHFRIRRA----VEYAAWARGVEPRECCVRAGAALDRVGLvdraDDRVQSL-----S 133
Cdd:COG4778 83 SPREIlalrRRTIGYVSQ-F---LRVIPRVSaldvVAEPLLERGVDREEARARARELLARLNL----PERLWDLppatfS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488470846 134 GGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIV 185
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-213 |
1.92e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.05 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRR-RRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD--DVNTIRSMVG 76
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYiGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfsKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 77 FLpqrFSLPLHFRIRRAVEyAAWARGVE-----PRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:PRK13644 81 IV---FQNPETQFVGRTVE-EDLAFGPEnlclpPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488470846 152 VLLLDEPTVGLDPASRIGVRSLLGELAED-RTVIVSTHLLEDLQEfVSQLAVLSEGELIFEGS 213
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
10-217 |
2.36e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 89.64 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 10 RYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS--------------DDVNTIRSM 74
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGdVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 75 VGFLPQRFSLPLHFRIRRAV-EYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQS-LSGGMRQRLGIACAIVGDPAV 152
Cdd:PRK10619 94 LTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488470846 153 LLLDEPTVGLDPASRIGVRSLLGELAED-RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
31-188 |
2.38e-21 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 89.47 E-value: 2.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPESGHFRVNGVDV------------SDD--VNTIRSMVGFLPQRFSLPLHFRIRRAV-E 95
Cdd:COG4598 39 IIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgelvpADRrqLQRIRTRLGMVFQSFNLWSHMTVLENViE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 96 YAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPasrigvrSLLG 175
Cdd:COG4598 119 APVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP-------ELVG 191
|
170 180
....*....|....*....|.
gi 488470846 176 E-------LAED-RTVIVSTH 188
Cdd:COG4598 192 EvlkvmrdLAEEgRTMLVVTH 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-217 |
2.69e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.20 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 25 DSGLWGLLGPNGAGKSTLLSILATLRE--PE---SGHFRVNGVDVSD-DVNTIRSMVGFLpqrFSLP------------- 85
Cdd:PRK14247 28 DNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKmDVIELRRRVQMV---FQIPnpipnlsifenva 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 86 LHFRIRRAVEyaawargvEPRECCVRAGAALDRVGLVDRADDRVQ----SLSGGMRQRLGIACAIVGDPAVLLLDEPTVG 161
Cdd:PRK14247 105 LGLKLNRLVK--------SKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARALAFQPEVLLADEPTAN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488470846 162 LDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:PRK14247 177 LDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-217 |
2.82e-21 |
|
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: 90.93 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELeHISHRYRRRRSLVDISCEfDSGLWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTI-----RSMV 75
Cdd:COG4148 2 MLEV-DFRLRRGGFTLDVDFTLP-GRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIflpphRRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 76 GFLPQRFSLPLHFRIRRAVEYAAWARGVEPReccvraGAALDRV-------GLVDRaddRVQSLSGGMRQRLGIACAIVG 148
Cdd:COG4148 80 GYVFQEARLFPHLSVRGNLLYGRKRAPRAER------RISFDEVvellgigHLLDR---RPATLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488470846 149 DPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRT--VIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:COG4148 151 SPRLLLMDEPLAALDLARKAEILPYLERLRDELDipILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-213 |
4.36e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.21 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRS----------------------LVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHF 57
Cdd:COG1134 4 MIEVENVSKSYRLYHEpsrslkelllrrrrtrreefwaLKDVSFEVERGeSVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 58 RVNGvdvsddvnTIRSM----VGFLPQrFSLplhfriRRAVEYAAWARGVEPREccVRagAALDRV----GLVDRADDRV 129
Cdd:COG1134 84 EVNG--------RVSALlelgAGFHPE-LTG------RENIYLNGRLLGLSRKE--ID--EKFDEIvefaELGDFIDQPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 130 QSLSGGMRQRLGIACAIVGDPAVLLLDEPT-VGlDPASRIGVRSLLGELAED-RTVIVSTHLLEDLQEFVSQLAVLSEGE 207
Cdd:COG1134 145 KTYSSGMRARLAFAVATAVDPDILLVDEVLaVG-DAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
....*.
gi 488470846 208 LIFEGS 213
Cdd:COG1134 224 LVMDGD 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-217 |
4.87e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 91.23 E-value: 4.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRY--RRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGF 77
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGkTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQRFSLplhFR--IRRAVEYAA---WARgvEPRECCVRAGAALDRVGLVDRADDRV-----QSLSGGMRQRLGIACAIV 147
Cdd:PRK11176 422 VSQNVHL---FNdtIANNIAYARteqYSR--EQIEEAARMAYAMDFINKMDNGLDTVigengVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 148 GDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLqEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTI-EKADEILVVEDGEIVERGTHAEL 565
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-216 |
5.43e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 5.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 4 LEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNgvdvsddvNTIRsmVGFLPQRF 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGdRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP--------KGLR--IGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 83 SLPLHFRIRRAV------------EY-AAWARGVEPRECCV-------------------RAGAALDRVGLVDRADDR-V 129
Cdd:COG0488 71 PLDDDLTVLDTVldgdaelraleaELeELEAKLAEPDEDLErlaelqeefealggweaeaRAEEILSGLGFPEEDLDRpV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 130 QSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLgeLAEDRTVIVSTHlleD---LQEFVSQLAVLSEG 206
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL--KNYPGTVLVVSH---DryfLDRVATRILELDRG 225
|
250
....*....|.
gi 488470846 207 ELI-FEGSYSD 216
Cdd:COG0488 226 KLTlYPGNYSA 236
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-224 |
5.53e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 89.07 E-value: 5.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRR-----RRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDD-----VNT 70
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGkYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 71 IRSMVGFLpqrFSLP----LHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLvdRADDRVQS---LSGGMRQRLGIA 143
Cdd:PRK13646 83 VRKRIGMV---FQFPesqlFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGF--SRDVMSQSpfqMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 144 CAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAED--RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS----YSDL 217
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSpkelFKDK 237
|
....*..
gi 488470846 218 ESVGQKH 224
Cdd:PRK13646 238 KKLADWH 244
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-213 |
7.28e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.97 E-value: 7.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 17 LVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLrEPESGHFRVNGVDVSD-DVNTIRSMVGFLPQR----FSLPLHfri 90
Cdd:COG4138 12 LGPISAQVNAGeLIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDwSAAELARHRAYLSQQqsppFAMPVF--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 91 rravEYAA--WARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIV-------GDPAVLLLDEPTVG 161
Cdd:COG4138 88 ----QYLAlhQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488470846 162 LDPASRIGVRSLLGELAED-RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:COG4138 164 LDVAQQAALDRLLRELCQQgITVVMSSHDLNHTLRHADRVWLLKQGKLVASGE 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-209 |
1.06e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.59 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 27 GLWGLLGPNGAGKSTLLSILATLRE--PES---GHFRVNGVDV-SDDVNTIR-----SMVGFLPQRFS-LPLHFRIRRAV 94
Cdd:PRK14267 31 GVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIySPDVDPIEvrrevGMVFQYPNPFPhLTIYDNVAIGV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 95 EYAAWARGVEprECCVRAGAALDRVGLVDRADDRVQ----SLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGV 170
Cdd:PRK14267 111 KLNGLVKSKK--ELDERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKI 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 488470846 171 RSLLGELAEDRTVIVSTHLLEDLQEFVSQLAVLSEGELI 209
Cdd:PRK14267 189 EELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-217 |
1.11e-20 |
|
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: 86.72 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSddvntirsmvgflpq 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGeIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 rfSLPLHFRIRRAVEY-------------------AAWARGVEPREccvragAALDRV-----GLVDRADDRVQSLSGGM 136
Cdd:cd03224 66 --GLPPHERARAGIGYvpegrrifpeltveenlllGAYARRRAKRK------ARLERVyelfpRLKERRKQLAGTLSGGE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 137 RQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGEL-AEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYS 215
Cdd:cd03224 138 QQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELrDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAA 217
|
..
gi 488470846 216 DL 217
Cdd:cd03224 218 EL 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-212 |
1.28e-20 |
|
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: 86.82 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 10 RYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSddvnTIRSMVGFLPQrfslplhF 88
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGeRIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS----LLGLGGGFNPE-------L 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 89 RIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPT-VGlDPASR 167
Cdd:cd03220 100 TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLaVG-DAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488470846 168 IGVRSLLGELAED-RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEG 212
Cdd:cd03220 179 EKCQRRLRELLKQgKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-213 |
1.91e-20 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 86.01 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRR--RRSLVDISCEFDSGL-WGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGF 77
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEkVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQ---------RFSL-PLH----FRIRRAVEyaawargveprECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIA 143
Cdd:cd03244 83 IPQdpvlfsgtiRSNLdPFGeysdEELWQALE-----------RVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 144 CAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEFvSQLAVLSEGELIFEGS 213
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDS 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-209 |
2.54e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 86.37 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEF-DSGLWGLLGPNGAGKSTLLSILATLRE--PE---SGHFRVNGVDV----SDDVNt 70
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFyPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIysprTDTVD- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 71 IRSMVGFLPQRFSlPLHFRIRRAVEYAAWARGV-------EPRECCVRAGAALDRVGlvDRADDRVQSLSGGMRQRLGIA 143
Cdd:PRK14239 84 LRKEIGMVFQQPN-PFPMSIYENVVYGLRLKGIkdkqvldEAVEKSLKGASIWDEVK--DRLHDSALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488470846 144 CAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEFVSQLAVLSEGELI 209
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-208 |
3.15e-20 |
|
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: 85.60 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRS---LVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDD----VNTIRS 73
Cdd:cd03248 12 VKFQNVTFAYPTRPDtlvLQDVSFTLHPGeVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYehkyLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 74 MVGFLPQRFSlplhfriRRAVEYAAWARGVEPRECCVRAGAALD--------RVGLVDRADDRVQSLSGGMRQRLGIACA 145
Cdd:cd03248 92 LVGQEPVLFA-------RSLQDNIAYGLQSCSFECVKEAAQKAHahsfiselASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488470846 146 IVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEfVSQLAVLSEGEL 208
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
13-208 |
3.56e-20 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 88.94 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 13 RRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFLPQRFSLplhFRI 90
Cdd:TIGR01842 330 KKPTLRGISFSLQAGeALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwDRETFGKHIGYLPQDVEL---FPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 91 RRAVEYAAWARGVEPR---ECCVRAGAALDRVGLVDRAD----DRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLD 163
Cdd:TIGR01842 407 TVAENIARFGENADPEkiiEAAKLAGVHELILRLPDGYDtvigPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488470846 164 PASRIGVRSLLGEL-AEDRTVIVSTHLLEDLQEfVSQLAVLSEGEL 208
Cdd:TIGR01842 487 EEGEQALANAIKALkARGITVVVITHRPSLLGC-VDKILVLQDGRI 531
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-217 |
3.88e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.72 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 5 EHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS--DDVNTIRSMVGFLPQR 81
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGeIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 82 FSLplhfrIRRAVEYAAWARGVEPRECCV------RAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLL 155
Cdd:PRK10895 87 ASI-----FRRLSVYDNLMAVLQIRDDLSaeqredRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488470846 156 DEPTVGLDPASRIGVRSLLGELAEDRT-VIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLgVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-219 |
6.01e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.92 E-value: 6.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPESGhFRVNGvDV---------SDDVNTIRSMVGFLPQRFSlPLHFRIRRAVEYAAWAR 101
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSG-YRYSG-DVllggrsifnYRDVLEFRRRVGMLFQRPN-PFPMSIMDNVLAGVRAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 102 GVEPR-ECCVRAGAALDRVGLVDRADDRVQS----LSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGE 176
Cdd:PRK14271 129 KLVPRkEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS 208
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488470846 177 LAEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDLES 219
Cdd:PRK14271 209 LADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-213 |
7.64e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.62 E-value: 7.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDiSCEFDSGL---WGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS-DDVNTIRSMVG 76
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALN-NINFIAPRnsrIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 77 FLPQR-----FSLPlhfrIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:PRK13652 82 LVFQNpddqiFSPT----VEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488470846 152 VLLLDEPTVGLDPASRIGVRSLLGELAED--RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGT 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-224 |
1.03e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.65 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYR-----RRRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDV-----SDDVNT 70
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFvALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 71 IRSMVGFLPQrFSLPLHFR--IRRAVEYAAWARGVEPRECCVRAGAALDRVGL-VDRADDRVQSLSGGMRQRLGIACAIV 147
Cdd:PRK13641 83 LRKKVSLVFQ-FPEAQLFEntVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 148 GDPAVLLLDEPTVGLDPASRIGVRSLLGEL-AEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS----YSDLESVgQ 222
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASpkeiFSDKEWL-K 240
|
..
gi 488470846 223 KH 224
Cdd:PRK13641 241 KH 242
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-217 |
1.42e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 85.93 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDdvNTIRS----MVg 76
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGtMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH--RSIQQrdicMV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 77 FlpQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLD 156
Cdd:PRK11432 84 F--QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488470846 157 EPTVGLDPASRIGVRSLLGELaEDRTVIVSTHLLEDLQE-F-VS-QLAVLSEGELIFEGSYSDL 217
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIREL-QQQFNITSLYVTHDQSEaFaVSdTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-213 |
1.49e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.67 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 19 DISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFLPQR--------------FS 83
Cdd:PRK13631 44 NISYTFEKNkIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKiknfkelrrrvsmvFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 84 LPLH--FR--IRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQ-SLSGGMRQRLGIACAIVGDPAVLLLDEP 158
Cdd:PRK13631 124 FPEYqlFKdtIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILIFDEP 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488470846 159 TVGLDPA-SRIGVRSLLGELAEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:PRK13631 204 TAGLDPKgEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-194 |
1.50e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.10 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 17 LVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMV-----GFLPQRFSLPLHFRI 90
Cdd:PRK11629 25 LHNVSFSIGEGeMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqklGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 91 RRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGV 170
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180
....*....|....*....|....*.
gi 488470846 171 RSLLGEL--AEDRTVIVSTHlleDLQ 194
Cdd:PRK11629 185 FQLLGELnrLQGTAFLVVTH---DLQ 207
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-213 |
1.78e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 86.24 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 19 DISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNT-----IRSMVGFLPQRFSLPLHFRIRR 92
Cdd:PRK10070 46 DASLAIEEGeIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrevRRKKIAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 93 AVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRS 172
Cdd:PRK10070 126 NTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488470846 173 LLGEL--AEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:PRK10070 206 ELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-195 |
3.80e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.01 E-value: 3.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRY---RRRRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS-DDVNTIRSMV 75
Cdd:PRK13650 4 IIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWlSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 76 GFLpqrFSLPLHFRIRRAVE----YAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:PRK13650 84 GMV---FQNPDNQFVGATVEddvaFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488470846 152 VLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHlleDLQE 195
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITH---DLDE 203
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-218 |
4.05e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 84.37 E-value: 4.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRR-----RSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDD-------- 67
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFiAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 68 -----------------VNTIRSMVGFLPQrFSLPLHFR--IRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDR 128
Cdd:PRK13651 83 vleklviqktrfkkikkIKEIRRRVGVVFQ-FAEYQLFEqtIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 129 VQ-SLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAED-RTVIVSTHLLEDLQEFVSQLAVLSEG 206
Cdd:PRK13651 162 SPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
250
....*....|...
gi 488470846 207 ELIFEG-SYSDLE 218
Cdd:PRK13651 242 KIIKDGdTYDILS 254
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-192 |
4.18e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 82.14 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPE---SGHFRVNGVDVsDDVNTIRSMVG 76
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGeILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRL-TALPAEQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 77 FLPQRFSLPLHFRIRRAVEYAAwARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLD 156
Cdd:COG4136 80 ILFQDDLLFPHLSVGENLAFAL-PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 488470846 157 EPTVGLDPASRIGVRSLLGELAEDR---TVIVsTHLLED 192
Cdd:COG4136 159 EPFSKLDAALRAQFREFVFEQIRQRgipALLV-THDEED 196
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
30-233 |
6.68e-19 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 84.40 E-value: 6.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLlSILATLREPESGHFRVNGVDVSDDVNTIRSMVGF-LPQRFSLPLHFRIRRAVEYAAWARGVEPREC 108
Cdd:NF000106 43 GVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*hRPVR*GRRESFSGRENLYMIGR*LDLSRKDA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 109 CVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAED-RTVIVST 187
Cdd:NF000106 122 RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488470846 188 HLLEDLQEFVSQLAVLSEGELIFEGSYSDLESV--GQKHPVRNANDAE 233
Cdd:NF000106 202 QYMEEAEQLAHELTVIDRGRVIADGKVDELKTKvgGRTLQIRPAHAAE 249
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-226 |
1.48e-18 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 82.16 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYR---------RRRSLVDISCEFDSGL-WGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS----D 66
Cdd:TIGR02769 2 LLEVRDVTHTYRtgglfgakqRAPVLTNVSLSIEEGEtVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqldrK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 67 DVNTIRSMVGFLPQrfSLPLHFRIRRAVEyaaWARGvEP---------RECCVRAGAALDRVGL-VDRADDRVQSLSGGM 136
Cdd:TIGR02769 82 QRRAFRRDVQLVFQ--DSPSAVNPRMTVR---QIIG-EPlrhltsldeSEQKARIAELLDMVGLrSEDADKLPRQLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 137 RQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAED--RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSY 214
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfgTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDV 235
|
250
....*....|..
gi 488470846 215 SDLESVgqKHPV 226
Cdd:TIGR02769 236 AQLLSF--KHPA 245
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-213 |
2.05e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.59 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFD-SGLWGLLGPNGAGKSTLLSILATLREPESGHFRVNG--VDVSD-DVNTIRSMVG 76
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSlSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKrGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 77 FLPQRFSLPLHFR-IRRAVEYAAWARGVEPRECCVRAGAALDrvgLVDRADDR---VQSLSGGMRQRLGIACAIVGDPAV 152
Cdd:PRK13638 81 TVFQDPEQQIFYTdIDSDIAFSLRNLGVPEAEITRRVDEALT---LVDAQHFRhqpIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488470846 153 LLLDEPTVGLDPASRIGVRSLLGEL-AEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-219 |
2.57e-18 |
|
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: 82.47 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 27 GLWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-----DVNTIRSMVGFLPQRFSLPLHFRIRRAVEYAAWAr 101
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgiFLPPEKRRIGYVFQEARLFPHLSVRGNLRYGMKR- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 102 gVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAE-- 179
Cdd:TIGR02142 103 -ARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAef 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488470846 180 DRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDLES 219
Cdd:TIGR02142 182 GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-215 |
2.85e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 81.24 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCE-FDSGLWGLLGPNGAGKSTLLSILATLREPEsGHFRVNG---------VDVSDDVNTI 71
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEiYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnqniYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 72 R---SMVGFLPQRFSLPLHFRIRRAVEYAAWARGVEPR---ECCVRAGAALDRVGlvDRADDRVQSLSGGMRQRLGIACA 145
Cdd:PRK14258 87 RrqvSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDdivESALKDADLWDEIK--HKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488470846 146 IVGDPAVLLLDEPTVGLDPASRIGVRSLL--GELAEDRTVIVSTHLLEdlqefvsQLAVLSEGELIFEGSYS 215
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLH-------QVSRLSDFTAFFKGNEN 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-217 |
3.36e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 83.23 E-value: 3.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRS---LVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVG 76
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDvpvLKGLTFTLHPGeVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 77 FLPQRfslPLHFR--IRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRV-----QSLSGGMRQRLGIACAIVGD 149
Cdd:TIGR00958 559 LVGQE---PVLFSgsVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEvgekgSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 150 PAVLLLDEPTVGLDPAsrigVRSLLGEL--AEDRTVIVSTHLLEDLQEfVSQLAVLSEGELIFEGSYSDL 217
Cdd:TIGR00958 636 PRVLILDEATSALDAE----CEQLLQESrsRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-217 |
4.45e-18 |
|
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: 80.03 E-value: 4.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSddvntirsmvgflp 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGeIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 80 qrfSLPLHFRIRRAVEYAAWARGV--------------EPRECCVRAGAALDRVG-----LVDRADDRVQSLSGGMRQRL 140
Cdd:COG0410 69 ---GLPPHRIARLGIGYVPEGRRIfpsltveenlllgaYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 141 GIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVsthLLEdlQ--EFVSQLA----VLSEGELIFEGSY 214
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTIL---LVE--QnaRFALEIAdrayVLERGRIVLEGTA 220
|
...
gi 488470846 215 SDL 217
Cdd:COG0410 221 AEL 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-209 |
5.29e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.38 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVsddvnTIRS------ 73
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGeIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-----RIRSprdaia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 74 ----MVgflPQRFSL----------------PLHFRIRRAveyAAWARgvepreccVRagAALDRVGL-VDrADDRVQSL 132
Cdd:COG3845 80 lgigMV---HQHFMLvpnltvaenivlglepTKGGRLDRK---AARAR--------IR--ELSERYGLdVD-PDAKVEDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 133 SGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPAsriGVRSLLGEL----AEDRTVIVSTHLLEDLQEFVSQLAVLSEGEL 208
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVLTPQ---EADELFEILrrlaAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
.
gi 488470846 209 I 209
Cdd:COG3845 220 V 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-217 |
5.68e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.37 E-value: 5.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDvNTIRSM---VG 76
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGeVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFR-SPRDAQaagIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 77 FLPQRFSL---------------PLHF-RIRRAVEYAawargvepreccvRAGAALDRVGLVDRADDRVQSLSGGMRQRL 140
Cdd:COG1129 83 IIHQELNLvpnlsvaeniflgrePRRGgLIDWRAMRR-------------RARELLARLGLDIDPDTPVGDLSVAQQQLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 141 GIACAIVGDPAVLLLDEPTVGLDPAsriGVRSLLG---ELAED-RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSD 216
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTER---EVERLFRiirRLKAQgVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAE 226
|
.
gi 488470846 217 L 217
Cdd:COG1129 227 L 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
31-188 |
8.95e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.76 E-value: 8.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDvnTIRSMVGFLPQRFSLPLHFRIRRAVEYaaWARGVEPRECCV 110
Cdd:PRK13539 33 LTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDP--DVAEACHYLGHRNAMKPALTVAENLEF--WAAFLGGEELDI 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 111 RAgaALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPAS-RIGVRSLLGELAEDRTVIVSTH 188
Cdd:PRK13539 109 AA--ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAvALFAELIRAHLAQGGIVIAATH 185
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
32-188 |
9.03e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.83 E-value: 9.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 32 LGPNGAGKSTLLSILATLREPESGhFRVNG---------VDVSDDVNTIRSMVGFLPQRFSlPLHFRIRRAVEYAAWARG 102
Cdd:PRK14243 42 IGPSGCGKSTILRCFNRLNDLIPG-FRVEGkvtfhgknlYAPDVDPVEVRRRIGMVFQKPN-PFPKSIYDNIAYGARING 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 103 V-----EPRECCVRAGAALDRVGlvDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGEL 177
Cdd:PRK14243 120 YkgdmdELVERSLRQAALWDEVK--DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL 197
|
170
....*....|.
gi 488470846 178 AEDRTVIVSTH 188
Cdd:PRK14243 198 KEQYTIIIVTH 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-198 |
1.88e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 78.95 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 4 LEHISHRYRRRRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMvgFLPQRF 82
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFvAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLM--FQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 83 sLPLhfriRRAVEYAAWARGVEPREccvRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGL 162
Cdd:PRK11247 93 -LPW----KKVIDNVGLGLKGQWRD---AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 488470846 163 DPASRIGVRSLLGELAEDR--TVIVSTHlleDLQEFVS 198
Cdd:PRK11247 165 DALTRIEMQDLIESLWQQHgfTVLLVTH---DVSEAVA 199
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
31-188 |
1.89e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.28 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSM-----VGFLPQRFSLPLHFRIRRAVEYAAWARGVEP 105
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlrakhVGFVFQSFMLIPTLNALENVELPALLRGESS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 106 RECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TV 183
Cdd:PRK10584 121 RQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTL 200
|
....*
gi 488470846 184 IVSTH 188
Cdd:PRK10584 201 ILVTH 205
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
31-221 |
4.05e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.89 E-value: 4.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLS-ILATLrePESGHFRVNGVDVSD-DVNTIRSMVGFLPQRFSLPlHFRIRRAVEYA-AWARGVEPRE 107
Cdd:PRK11174 381 LVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIELRElDPESWRKHLSWVGQNPQLP-HGTLRDNVLLGnPDASDEQLQQ 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 108 CCVRAGAA--LDRV--GLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTV 183
Cdd:PRK11174 458 ALENAWVSefLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTT 537
|
170 180 190
....*....|....*....|....*....|....*...
gi 488470846 184 IVSTHLLEDLQEfVSQLAVLSEGELIFEGSYSDLESVG 221
Cdd:PRK11174 538 LMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
30-206 |
4.09e-17 |
|
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: 79.79 E-value: 4.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFLPQRFSLplhFR--IRRAVeyaawAR--GVE 104
Cdd:COG4618 362 GVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGYLPQDVEL---FDgtIAENI-----ARfgDAD 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 105 PReccvRAGAALDRVGLVD-----------RADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSL 173
Cdd:COG4618 434 PE----KVVAAAKLAGVHEmilrlpdgydtRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAA 509
|
170 180 190
....*....|....*....|....*....|....
gi 488470846 174 LGELAED-RTVIVSTHLLEDLQEfVSQLAVLSEG 206
Cdd:COG4618 510 IRALKARgATVVVITHRPSLLAA-VDKLLVLRDG 542
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
31-188 |
4.81e-17 |
|
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: 77.12 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDvnTIRSMVGFlpQRFSLPLHFRIRR----AVEYAAWARGVEPR 106
Cdd:TIGR01184 16 LIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEP--GPDRMVVF--QNYSLLPWLTVREnialAVDRVLPDLSKSER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 107 ECCVRAGAALdrVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVI 184
Cdd:TIGR01184 92 RAIVEEHIAL--VGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEHrvTVL 169
|
....
gi 488470846 185 VSTH 188
Cdd:TIGR01184 170 MVTH 173
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-211 |
6.11e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.43 E-value: 6.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRR-----RRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRS- 73
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFvTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 74 ---------MVGFLP---------------QRFSLPLHFRIRRAVEYaawargvepRECCvragAALDRvGLVDRADDRV 129
Cdd:COG1101 81 yigrvfqdpMMGTAPsmtieenlalayrrgKRRGLRRGLTKKRRELF---------RELL----ATLGL-GLENRLDTKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 130 QSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGE 207
Cdd:COG1101 147 GLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
....
gi 488470846 208 LIFE 211
Cdd:COG1101 227 IILD 230
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-217 |
6.16e-17 |
|
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: 79.40 E-value: 6.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRY-RRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFL 78
Cdd:TIGR01193 474 IVINDVSYSYgYGSNILSDISLTIKMNsKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQRfslPLHF-------------------RIRRAVEYAAWARGVEPREccvragaaldrVGLVDRADDRVQSLSGGMRQR 139
Cdd:TIGR01193 554 PQE---PYIFsgsilenlllgakenvsqdEIWAACEIAEIKDDIENMP-----------LGYQTELSEEGSSISGGQKQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488470846 140 LGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELaEDRTVIVSTHLLEdLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-188 |
1.04e-16 |
|
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: 75.47 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 14 RRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFLPQRFSLP------- 85
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEAlQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKpelsale 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 86 -LHF--RIRRAVEYAAWArgvepreccvragaALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGL 162
Cdd:TIGR01189 93 nLHFwaAIHGGAQRTIED--------------ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180 190
....*....|....*....|....*....|.
gi 488470846 163 DPAsriGVRsLLGELAEDRT-----VIVSTH 188
Cdd:TIGR01189 159 DKA---GVA-LLAGLLRAHLarggiVLLTTH 185
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-177 |
1.18e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.69 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGvdvsddvntiRSMVGFLP 79
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGkILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----------KLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 80 QRF----SLPL----HFRIRRAVEYAawargvepreccvRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:PRK09544 74 QKLyldtTLPLtvnrFLRLRPGTKKE-------------DILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180
....*....|....*....|....*.
gi 488470846 152 VLLLDEPTVGLDPASRIGVRSLLGEL 177
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQL 166
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-201 |
2.03e-16 |
|
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: 73.64 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSGlW--GLLGPNGAGKSTLLSILATLREPESGHfrvngVDVSDDVNtirsmVGFLP 79
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPG-DriGLVGRNGAGKSTLLKLIAGELEPDEGI-----VTWGSTVK-----IGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 80 QrfslplhfrirraveyaawargvepreccvragaaldrvglvdraddrvqsLSGGMRQRLGIACAIVGDPAVLLLDEPT 159
Cdd:cd03221 70 Q---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488470846 160 VGLDPASRIGVRSLLGELaeDRTVIVSTHlleDlQEFVSQLA 201
Cdd:cd03221 99 NHLDLESIEALEEALKEY--PGTVILVSH---D-RYFLDQVA 134
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-209 |
2.88e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.80 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSdDVNTIRSMVGFLP 79
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGeIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-HVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 80 QRFSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPT 159
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488470846 160 VGLDPASRIGVRSLLGELAE--DRTVIVSTHLLEDLQEFVSQLAVLSEGELI 209
Cdd:PRK11607 178 GALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-188 |
3.13e-16 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 74.20 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 13 RRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPE--SGHFRVNGVDVSDdvnTIRSMVGFLPQrfsLPLHF- 88
Cdd:cd03232 19 KRQLLNNISGYVKPGtLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK---NFQRSTGYVEQ---QDVHSp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 89 --RIRRAVEYAAWARGvepreccvragaaldrvglvdraddrvqsLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPAS 166
Cdd:cd03232 93 nlTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180
....*....|....*....|...
gi 488470846 167 RIGVRSLLGELAED-RTVIVSTH 188
Cdd:cd03232 144 AYNIVRFLKKLADSgQAILCTIH 166
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-218 |
3.87e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.13 E-value: 3.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS--DDVNTIRSMVGF 77
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGeIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQRFSLPLHFRI-------RRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDP 150
Cdd:PRK09700 85 IYQELSVIDELTVlenlyigRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 151 AVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVS-THLLEDLQEFVSQLAVLSEGELIFEGSYSDLE 218
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYiSHKLAEIRRICDRYTVMKDGSSVCSGMVSDVS 233
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
31-196 |
3.94e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.30 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNtiRSMVGFLPQRFSLPLHFRIrrAVE---------YAAWAR 101
Cdd:PRK15056 38 LVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ--KNLVAYVPQSEEVDWSFPV--LVEdvvmmgrygHMGWLR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 102 GVEPRECcVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGEL-AED 180
Cdd:PRK15056 114 RAKKRDR-QIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrDEG 192
|
170
....*....|....*.
gi 488470846 181 RTVIVSTHLLEDLQEF 196
Cdd:PRK15056 193 KTMLVSTHNLGSVTEF 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-188 |
6.31e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.98 E-value: 6.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSGLWGLL-GPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFL 78
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQRfslPLHF--RIRRAVEYAAWARGVEPRECCVRAGaaLDRVGLVDRA-DDRVQSLSGGMRQRLGIACAIVGDPAVLLL 155
Cdd:PRK10247 87 AQT---PTLFgdTVYDNLIFPWQIRNQQPDPAIFLDD--LERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 488470846 156 DEPTVGLDPASRIGVRSLLGELAEDRTVIV--STH 188
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVlwVTH 196
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-217 |
7.16e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 76.40 E-value: 7.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYR-RRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDdVN--TIRSMVGF 77
Cdd:COG5265 358 VRFENVSFGYDpERPILKGVSFEVPAGkTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRD-VTqaSLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQR---FSLPLHFRIR--------RAVEYAAwargvepreccvRAgAALDR--VGLVDRADDRVQS----LSGGMRQRL 140
Cdd:COG5265 437 VPQDtvlFNDTIAYNIAygrpdaseEEVEAAA------------RA-AQIHDfiESLPDGYDTRVGErglkLSGGEKQRV 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488470846 141 GIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEfVSQLAVLSEGELIFEGSYSDL 217
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAEL 579
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-188 |
1.43e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 75.23 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLV-DISCEFDSGLWGLL-GPNGAGKSTLLSILATLREPESGHFRVNGVDvsddvntiRSMvgFL 78
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLeDLSLSLKPGERLLItGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA--------RVL--FL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQRFSLPLHfRIRRAVEYAAWARGVEPRECCvragAALDRVGL---VDRADDRV---QSLSGGMRQRLGIACAIVGDPAV 152
Cdd:COG4178 432 PQRPYLPLG-TLREALLYPATAEAFSDAELR----EALEAVGLghlAERLDEEAdwdQVLSLGEQQRLAFARLLLHKPDW 506
|
170 180 190
....*....|....*....|....*....|....*.
gi 488470846 153 LLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTH 188
Cdd:COG4178 507 LFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-217 |
3.37e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 72.82 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRR---RSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS-DDVNTIRSMV 75
Cdd:PRK13642 4 ILEVENLVFKYEKEsdvNQLNGVSFSITKGEWvSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 76 GFLpqrFSLPLHFRIRRAVE----YAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:PRK13642 84 GMV---FQNPDNQFVGATVEddvaFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 152 VLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHlleDLQEFVS--QLAVLSEGELIFEGSYSDL 217
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITH---DLDEAASsdRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
31-206 |
3.52e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 71.76 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFLPQRFSLPLHFRirrAVEYAAWARGVEPRECCV 110
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLS---VLENLRFWHADHSDEQVE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 111 RAgaaLDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLL-GELAEDRTVIVSTHL 189
Cdd:cd03231 108 EA---LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMaGHCARGGMVVLTTHQ 184
|
170
....*....|....*..
gi 488470846 190 leDLQEFVSQLAVLSEG 206
Cdd:cd03231 185 --DLGLSEAGARELDLG 199
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
33-188 |
7.41e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.75 E-value: 7.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 33 GPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSmVGFLPQRFSLPLHFRIRRAVEYAAWARGVEPRECCVRA 112
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG-VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRV 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488470846 113 GAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAE--DRTVIVSTH 188
Cdd:PRK11000 115 NQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTH 192
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-226 |
8.08e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.64 E-value: 8.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYR---------RRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD---- 66
Cdd:PRK10419 3 LLNVSGLSHHYAhgglsgkhqHQTVLNNVSLSLKSGeTVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 67 -------DVNTI--RSMVGFLPQRfslplhfRIRRAV-EYAAWARGVEPRECCVRAGAALDRVGLVDR-ADDRVQSLSGG 135
Cdd:PRK10419 83 qrkafrrDIQMVfqDSISAVNPRK-------TVREIIrEPLRHLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 136 MRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAE--DRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
250
....*....|...
gi 488470846 214 YSDLESVgqKHPV 226
Cdd:PRK10419 236 VGDKLTF--SSPA 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-220 |
1.01e-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: 72.91 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLR--EPESGH---------------------- 56
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGeVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRiiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 57 -----------FRVNGVDVSDDVN-TIRSMVGFLPQR-FSLPLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGLVD 123
Cdd:TIGR03269 81 pcpvcggtlepEEVDFWNLSDKLRrRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 124 RADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLA 201
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....*....
gi 488470846 202 VLSEGELIFEGSYSDLESV 220
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVAV 259
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
2-213 |
1.10e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.12 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRrrrsLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLRePESGHFRVNGVDVSD-DVNTIRSMVGFLP 79
Cdd:PRK03695 1 MQLNDVAVSTR----LGPLSAEVRAGeILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwSAAELARHRAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 80 QR----FSLPLHfrirravEYAAWARGVEPRECCVRagAALDRV----GLVDRADDRVQSLSGGMRQRLGIACAI----- 146
Cdd:PRK03695 76 QQqtppFAMPVF-------QYLTLHQPDKTRTEAVA--SALNEVaealGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwp 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 147 VGDPA--VLLLDEPTVGLDPASRIGVRSLLGELAED-RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:PRK03695 147 DINPAgqLLLLDEPMNSLDVAQQAALDRLLSELCQQgIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGR 216
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
30-217 |
1.41e-14 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 70.48 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKS-TLLSILATLrEPE----SGHFRVNGVDVSDdvNTIRS----------MVGFLPQrFSLPLHFR--IRR 92
Cdd:TIGR02770 16 ALVGESGSGKSlTCLAILGLL-PPGltqtSGEILLDGRPLLP--LSIRGrhiatimqnpRTAFNPL-FTMGNHAIetLRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 93 AVEYAAWARGvepreccvRAGAALDRVGLVDRAddRVQS-----LSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASR 167
Cdd:TIGR02770 92 LGKLSKQARA--------LILEALEAVGLPDPE--EVLKkypfqLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488470846 168 IGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:TIGR02770 162 ARVLKLLRELRQLFgtGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEI 213
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-221 |
2.55e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.83 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPES--GHFRVNGVDVSddvNTIRSMVGFLPQRFSLPLHFRIRRAVEYAAWAR---GVEP 105
Cdd:PLN03211 99 VLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT---KQILKRTGFVTQDDILYPHLTVRETLVFCSLLRlpkSLTK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 106 RECCVRAGAALDRVGLVD-----RADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAED 180
Cdd:PLN03211 176 QEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK 255
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488470846 181 -RTVIVSTHLLED--LQEFVSQLaVLSEGELIFEGSYSD----LESVG 221
Cdd:PLN03211 256 gKTIVTSMHQPSSrvYQMFDSVL-VLSEGRCLFFGKGSDamayFESVG 302
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-188 |
4.29e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.81 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSGL-WGLLGPNGAGKSTLLSILaTLREPES--------GHFRVNGVDVSDdvntIR 72
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEhWQIVGPNGAGKSTLLSLI-TGDHPQGysndltlfGRRRGSGETIWD----IK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 73 SMVGFLPQrfSLPLHFRIRRAVE-------------YAAwargVEPRECcVRAGAALDRVGLVDR-ADDRVQSLSGGmRQ 138
Cdd:PRK10938 336 KHIGYVSS--SLHLDYRVSTSVRnvilsgffdsigiYQA----VSDRQQ-KLAQQWLDILGIDKRtADAPFHSLSWG-QQ 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488470846 139 RLG-IACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGEL-AEDRT--VIVSTH 188
Cdd:PRK10938 408 RLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLiSEGETqlLFVSHH 461
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-212 |
6.16e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.18 E-value: 6.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 5 EHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESG--HFRVNGVDVSDdVNTI---------R 72
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGeVLGIVGESGSGKTTLLNALSARLAPDAGevHYRMRDGQLRD-LYALseaerrrllR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 73 SMVGFLPQrfslplHFR--IRRAVeyAAWARGVEP------------REccvRAGAALDRVGL-VDRADDRVQSLSGGMR 137
Cdd:PRK11701 89 TEWGFVHQ------HPRdgLRMQV--SAGGNIGERlmavgarhygdiRA---TAGDWLERVEIdAARIDDLPTTFSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 138 QRLGIACAIVGDPAVLLLDEPTVGLDPASRIG----VRSLLGELaeDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEG 212
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARlldlLRGLVREL--GLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-218 |
6.58e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 69.65 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRR-----RSLVDISCEF-DSGLWGLLGPNGAGKSTLLSILATLREPESGHFRVN------GVDVSDDVN 69
Cdd:PRK13645 7 IILDNVSYTYAKKtpfefKALNNTSLTFkKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 70 TIRSMVGFLpqrFSLPLH--FR--IRRAVEYAAWARGVEPRECCVRAGAALDRVGLVDRADDRVQ-SLSGGMRQRLGIAC 144
Cdd:PRK13645 87 RLRKEIGLV---FQFPEYqlFQetIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 145 AIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAED--RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS----YSDLE 218
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSpfeiFSNQE 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-209 |
7.66e-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: 70.22 E-value: 7.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRY----RRRRSLVD-ISCE-FDSGLWGLLGPNGAGKSTLLSILATLREPESG--HFRVNG--VDVS----D 66
Cdd:TIGR03269 279 IIKVRNVSKRYisvdRGVVKAVDnVSLEvKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVGDewVDMTkpgpD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 67 DVNTIRSMVGFLPQRFSLPLHfriRRAVEYAAWARGVE-PRECCVR-AGAALDRVGLVDRADDRV-----QSLSGGMRQR 139
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPH---RTVLDNLTEAIGLElPDELARMkAVITLKMVGFDEEKAEEIldkypDELSEGERHR 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488470846 140 LGIACAIVGDPAVLLLDEPTVGLDPASRIGV-RSLLGELAE-DRTVIVSTHLLEDLQEFVSQLAVLSEGELI 209
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVtHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-209 |
7.72e-14 |
|
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: 68.21 E-value: 7.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRR--RSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSddvntirsmvgfl 78
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGeKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 pqrfSLPLHfRIRRAVeyaawarGVEPRECCVRAGAALDRVGLVDRADD-------RVQS----LSGGMRQRLGIACAIV 147
Cdd:cd03369 74 ----TIPLE-DLRSSL-------TIIPQDPTLFSGTIRSNLDPFDEYSDeeiygalRVSEgglnLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488470846 148 GDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEFvSQLAVLSEGELI 209
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-207 |
1.18e-13 |
|
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: 67.49 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 17 LVDISCEFDSG-LWGLLGPNGAGKSTLLS-ILATLrEPESGHFRVNGvdvsddvntirsMVGFLPQ-------------R 81
Cdd:cd03250 21 LKDINLEVPKGeLVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPG------------SIAYVSQepwiqngtireniL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 82 FSLPL-HFRIRRAVEyaawargvepreCCvragaALDR------------VGlvdradDRVQSLSGGMRQRLGIACAIVG 148
Cdd:cd03250 88 FGKPFdEERYEKVIK------------AC-----ALEPdleilpdgdlteIG------EKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488470846 149 DPAVLLLDEPTVGLDP--ASRIGVRSLLGELAEDRTVIVSTHLLEDLQEfVSQLAVLSEGE 207
Cdd:cd03250 145 DADIYLLDDPLSAVDAhvGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
31-212 |
1.67e-13 |
|
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: 66.90 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPE---SGHFRVNGVDVSDDVNTIRSMVGFLPQRFSLPLHFRIRRAVEYAAWARGvepre 107
Cdd:cd03233 38 VLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETLDFALRCKG----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 108 ccvragaaldrvglvdraDDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELA--EDRTVIV 185
Cdd:cd03233 113 ------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMAdvLKTTTFV 174
|
170 180 190
....*....|....*....|....*....|
gi 488470846 186 SthLL---EDLQEFVSQLAVLSEGELIFEG 212
Cdd:cd03233 175 S--LYqasDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
30-213 |
1.91e-13 |
|
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: 68.94 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKS-TLLSILATLREP---ESGHFRVNGVDVSD----DVNTIR----SMVgflpqrF-----SL-PLHfRIR 91
Cdd:COG4172 40 ALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGlserELRRIRgnriAMI------FqepmtSLnPLH-TIG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 92 RAV-EYAAWARGVEPRECCVRAGAALDRVGLVDrADDRVQS----LSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPAS 166
Cdd:COG4172 113 KQIaEVLRLHRGLSGAAARARALELLERVGIPD-PERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTV 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488470846 167 RIGVRSLLGELAEDR--TVIVSTHlleDL---QEFVSQLAVLSEGELIFEGS 213
Cdd:COG4172 192 QAQILDLLKDLQRELgmALLLITH---DLgvvRRFADRVAVMRQGEIVEQGP 240
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
33-164 |
2.29e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.80 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 33 GPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTirSMVGFLPQRFSLPLHFRIRRAVEYAAWARGVEPRECcvrA 112
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS--RFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQM---P 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 488470846 113 GAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDP 164
Cdd:PRK13543 119 GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
30-208 |
2.29e-13 |
|
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: 66.30 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVsddvnTIRSmvgflpqrfslplhfrirraveyaawargvePRECc 109
Cdd:cd03215 30 GIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV-----TRRS-------------------------------PRDA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 110 VRAGAAL---DR--VGLVDRADDR-----VQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAE 179
Cdd:cd03215 73 IRAGIAYvpeDRkrEGLVLDLSVAenialSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD 152
|
170 180 190
....*....|....*....|....*....|
gi 488470846 180 D-RTVIVSTHLLEDLQEFVSQLAVLSEGEL 208
Cdd:cd03215 153 AgKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-207 |
2.53e-13 |
|
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: 67.43 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 25 DSGLWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS--------DDVNTIRSMvgflpqrfslpLHFRIRRAVEY 96
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikaDYEGTVRDL-----------LSSITKDFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 97 AAWARGVepreccvragaaLDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGE 176
Cdd:cd03237 93 PYFKTEI------------AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180 190
....*....|....*....|....*....|....*
gi 488470846 177 LAE--DRTVIVSTHlleD--LQEFVSQLAVLSEGE 207
Cdd:cd03237 161 FAEnnEKTAFVVEH---DiiMIDYLADRLIVFEGE 192
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-188 |
4.19e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.98 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 19 DISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS---DDVNTIRSMVGFLPQ-----------RFS 83
Cdd:PRK13538 19 GLSFTLNAGeLVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrDEYHQDLLYLGHQPGikteltalenlRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 84 LPLHFRIRRAveyAAWargvepreccvragAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLD 163
Cdd:PRK13538 99 QRLHGPGDDE---ALW--------------EALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180
....*....|....*....|....*....
gi 488470846 164 PAsriGVRSLLGELAE--DR--TVIVSTH 188
Cdd:PRK13538 162 KQ---GVARLEALLAQhaEQggMVILTTH 187
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-225 |
1.10e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.04 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRR----RRSLVDISCEFDSG-LWGLLGPNGAGKS-TLLSILATLREPE----SGHFRVNGVDVSD-DVN 69
Cdd:PRK15134 5 LLAIENLSVAFRQqqtvRTVVNDVSLQIEAGeTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHaSEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 70 TIRSMVG------FLPQRFSL-PLHFRIRRAVEYAAWARGVEPRECCVRAGAALDRVGL---VDRADDRVQSLSGGMRQR 139
Cdd:PRK15134 85 TLRGVRGnkiamiFQEPMVSLnPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 140 LGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAE--DRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
....*...
gi 488470846 218 ESVGQkHP 225
Cdd:PRK15134 245 FSAPT-HP 251
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-195 |
1.20e-12 |
|
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: 67.24 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 14 RRSLVDISCEFDSGLW-GLLGPNGAGKSTLLSILATLREPEsGHFRVNGVDV-SDDVNTIRSMVGFLPQR-FSLPLHFRi 90
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRvGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWnSVTLQTWRKAFGVIPQKvFIFSGTFR- 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 91 RRAVEYAAW--------ARGVEPRECCVRAGAALDRVgLVDRAddrvQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGL 162
Cdd:TIGR01271 1310 KNLDPYEQWsdeeiwkvAEEVGLKSVIEQFPDKLDFV-LVDGG----YVLSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
170 180 190
....*....|....*....|....*....|...
gi 488470846 163 DPASRIGVRSLLGELAEDRTVIVSTHLLEDLQE 195
Cdd:TIGR01271 1385 DPVTLQIIRKTLKQSFSNCTVILSEHRVEALLE 1417
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
31-171 |
1.28e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.41 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPESGHF-----RVNGVDVSD-DVntirSMVgFlpQRFSLPLHFRIRRAVEYAAWARGVE 104
Cdd:PRK11650 35 LVGPSGCGKSTLLRMVAGLERITSGEIwiggrVVNELEPADrDI----AMV-F--QNYALYPHMSVRENMAYGLKIRGMP 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488470846 105 PRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVR 171
Cdd:PRK11650 108 KAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMR 174
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-220 |
1.53e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 3 ELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDV--SDDVNTIRS------ 73
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGqVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfASTTAALAAgvaiiy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 74 ---------------MVGFLPQRFSLplhfrirraveyaawargVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQ 138
Cdd:PRK11288 86 qelhlvpemtvaenlYLGQLPHKGGI------------------VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 139 RLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGEL-AEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIfeGSYSDL 217
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELrAEGRVILYVSHRMEEIFALCDAITVFKDGRYV--ATFDDM 225
|
...
gi 488470846 218 ESV 220
Cdd:PRK11288 226 AQV 228
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-193 |
1.73e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.37 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGhfRVNGVDVSDDV------------------NTIRS-----MVGFLPQRFSLPL 86
Cdd:PRK13409 103 GILGPNGIGKTTAVKILSGELIPNLG--DYEEEPSWDEVlkrfrgtelqnyfkklynGEIKVvhkpqYVDLIPKVFKGKV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 87 HFRIRRAVEyaawaRGVepreccvrAGAALDRVGL---VDRaddRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLD 163
Cdd:PRK13409 181 RELLKKVDE-----RGK--------LDEVVERLGLeniLDR---DISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190
....*....|....*....|....*....|
gi 488470846 164 PASRIGVRSLLGELAEDRTVIVSTHlleDL 193
Cdd:PRK13409 245 IRQRLNVARLIRELAEGKYVLVVEH---DL 271
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
31-185 |
2.03e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 65.01 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPESGHFRVNG----------------VDVSDDVNTIRSM---------------VGFLP 79
Cdd:PRK11300 36 LIGPNGAGKTTVFNCLTGFYKPTGGTILLRGqhieglpghqiarmgvVRTFQHVRLFREMtvienllvaqhqqlkTGLFS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 80 QRFSLPlhfRIRRAveyaawargvePRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPT 159
Cdd:PRK11300 116 GLLKTP---AFRRA-----------ESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180
....*....|....*....|....*.
gi 488470846 160 VGLDPASRIGVRSLLGELAEDRTVIV 185
Cdd:PRK11300 182 AGLNPKETKELDELIAELRNEHNVTV 207
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-209 |
4.07e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.04 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 3 ELEHIShryrRRRSLVDISceFDS------GLWGLLGpngAGKSTLLSILATLREPESGHFRVNGVDVsdDVNTIRSM-- 74
Cdd:COG1129 258 EVEGLS----VGGVVRDVS--FSVrageilGIAGLVG---AGRTELARALFGADPADSGEIRLDGKPV--RIRSPRDAir 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 75 --VGFLP---QRFSLPLHFRIRR-----AVEYAAWARGVEPRECCVRAGAALDRVGL-VDRADDRVQSLSGGMRQRLGIA 143
Cdd:COG1129 327 agIAYVPedrKGEGLVLDLSIREnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLA 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488470846 144 CAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAED-RTVIVSTHLLEDLQEFVSQLAVLSEGELI 209
Cdd:COG1129 407 KWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEgKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-190 |
9.94e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 62.77 E-value: 9.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESG-------------HFRVNGVD------VSDDVNTIR--SMVGFLPQRFSLPLHF 88
Cdd:cd03236 30 GLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeildEFRGSELQnyftklLEGDVKVIVkpQYVDLIPKAVKGKVGE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 89 RIRRAVEyaawaRGVEPRECcvragAALDRVGLVDRAddrVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRI 168
Cdd:cd03236 110 LLKKKDE-----RGKLDELV-----DQLELRHVLDRN---IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|...
gi 488470846 169 GVRSLLGELAED-RTVIVSTHLL 190
Cdd:cd03236 177 NAARLIRELAEDdNYVLVVEHDL 199
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-193 |
1.03e-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: 64.04 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATL---------REPE--------SG-----HFRvngvDVSDdvNTIRS-----MVGFLPQRF 82
Cdd:COG1245 103 GILGPNGIGKSTALKILSGElkpnlgdydEEPSwdevlkrfRGtelqdYFK----KLAN--GEIKVahkpqYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 83 SLPLHFRIRRAVEyaawaRGVepreccvrAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGL 162
Cdd:COG1245 177 KGTVRELLEKVDE-----RGK--------LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190
....*....|....*....|....*....|..
gi 488470846 163 DPASRIGVRSLLGELAE-DRTVIVSTHlleDL 193
Cdd:COG1245 244 DIYQRLNVARLIRELAEeGKYVLVVEH---DL 272
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-212 |
1.08e-11 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 62.93 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESG--HFRVNG--------VDVSDDVN 69
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGeVLGIVGESGSGKSTLLGCLAGRLAPDHGtaTYIMRSgaelelyqLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 70 TIRSMVGFLPQRFSLPLHFRIRRAVEYAAWARGVEPRECC-VRAGAA--LDRVGL-VDRADDRVQSLSGGMRQRLGIACA 145
Cdd:TIGR02323 83 LMRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGnIRATAQdwLEEVEIdPTRIDDLPRAFSGGMQQRLQIARN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 146 IVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDR--TVIVSTHLLEDLQEFVSQLAVLSEGELIFEG 212
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLglAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
36-211 |
1.31e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.51 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 36 GAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSM-VGFLPQ---------RFSLPLHFRIRRAVEYAAWARGVe 104
Cdd:COG3845 294 GNGQSELAEALAGLRPPASGSIRLDGEDITGlSPRERRRLgVAYIPEdrlgrglvpDMSVAENLILGRYRRPPFSRGGF- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 105 preccVRAGAALDRV-GLVDR-------ADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGE 176
Cdd:COG3845 373 -----LDRKAIRAFAeELIEEfdvrtpgPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE 447
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488470846 177 LAEDRT--VIVSthllEDLQEFVS---QLAVLSEGELIFE 211
Cdd:COG3845 448 LRDAGAavLLIS----EDLDEILAlsdRIAVMYEGRIVGE 483
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-229 |
1.55e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.20 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD--DVNTIRSMVGF 77
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGeIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQR---FSlplhfriRRAVEY-----AAWARGVEPRECCVRAGAALDRvgLVDRADDRVQSLSGGMRQRLGIACAIVGD 149
Cdd:PRK11614 85 VPEGrrvFS-------RMTVEEnlamgGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 150 PAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVsthLLEDLQEFVSQLA----VLSEGELIFEGSYSDLESvgqKHP 225
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIF---LVEQNANQALKLAdrgyVLENGHVVLEDTGDALLA---NEA 229
|
....
gi 488470846 226 VRNA 229
Cdd:PRK11614 230 VRSA 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
30-163 |
3.26e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 62.06 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD----DVNTIRS---MVgflpqrF-----SLPLHFRIRRAVEYA 97
Cdd:COG4608 48 GLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGlsgrELRPLRRrmqMV------FqdpyaSLNPRMTVGDIIAEP 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 98 AWARGVEPR-ECCVRAGAALDRVGLvdRAD--DRV-QSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLD 163
Cdd:COG4608 122 LRIHGLASKaERRERVAELLELVGL--RPEhaDRYpHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-231 |
3.40e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.74 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSL---VDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNT--IRSMV 75
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVeiyKDLNFTLTEGkTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLkwWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 76 GFLPQRfslPLHFR--IRRAVEYAAWA-------------------RGVEPRECCVRAGA--------ALDRVGLV---- 122
Cdd:PTZ00265 463 GVVSQD---PLLFSnsIKNNIKYSLYSlkdlealsnyynedgndsqENKNKRNSCRAKCAgdlndmsnTTDSNELIemrk 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 123 ---------------------------DRADDRVQS----LSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVR 171
Cdd:PTZ00265 540 nyqtikdsevvdvskkvlihdfvsalpDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488470846 172 SLLGELA--EDRTVIVSTHLLEDLQeFVSQLAVLSEGElifEGSYSDLESVGQKhPVRNAND 231
Cdd:PTZ00265 620 KTINNLKgnENRITIIIAHRLSTIR-YANTIFVLSNRE---RGSTVDVDIIGED-PTKDNKE 676
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-215 |
3.57e-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: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 14 RRSLVDISCEFDSGL-WGLLGPNGAGKSTLLSILATLREPESGHFRVngvdvSDDVNtirsmVGFLPQRFSLPLHFRIRR 92
Cdd:TIGR03719 18 KEILKDISLSFFPGAkIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-----QPGIK-----VGYLPQEPQLDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 93 AVE----------------YAAWARGVEPRECCVRAGAAL----DRVGL------VDRA---------DDRVQSLSGGMR 137
Cdd:TIGR03719 88 NVEegvaeikdaldrfneiSAKYAEPDADFDKLAAEQAELqeiiDAADAwdldsqLEIAmdalrcppwDADVTKLSGGER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 138 QRLGIACAIVGDPAVLLLDEPTVGLDPASrigVRSLLGELAE-DRTVIVSTH---LLEDLQEFVSQlavLSEGELI-FEG 212
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQEyPGTVVAVTHdryFLDNVAGWILE---LDRGRGIpWEG 241
|
...
gi 488470846 213 SYS 215
Cdd:TIGR03719 242 NYS 244
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
31-217 |
4.61e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 60.96 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRS----MVGFLP-------QRFSLPLHFRIRRAVEYAAW 99
Cdd:PRK15112 44 IIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqrirMIFQDPstslnprQRISQILDFPLRLNTDLEPE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 100 ARGvepreccVRAGAALDRVGLV-DRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELA 178
Cdd:PRK15112 124 QRE-------KQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQ 196
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488470846 179 EDRTV--IVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDL 217
Cdd:PRK15112 197 EKQGIsyIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-217 |
1.50e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.50 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRR-RRSLVDISCEFDS-GLWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVS-------------- 65
Cdd:PRK10790 341 IDIDNVSFAYRDdNLVLQNINLSVPSrGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSslshsvlrqgvamv 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 66 --DDVNTIRSMVG--FLPQRFSLPLHFRIRRAVEYAAWARGVEPreccvragaaldrvGLVDRADDRVQSLSGGMRQRLG 141
Cdd:PRK10790 421 qqDPVVLADTFLAnvTLGRDISEEQVWQALETVQLAELARSLPD--------------GLYTPLGEQGNNLSVGQKQLLA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488470846 142 IACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEfVSQLAVLSEGELIFEGSYSDL 217
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-217 |
1.69e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.73 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLV--DISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGF 77
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLVlrHINVTIHGGeKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKiGLHDLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQR---FSLPLHFRIRRAVEYAA----WARGVEPRECCVRAGAAldrvGLVDRADDRVQSLSGGMRQRLGIACAIVGDP 150
Cdd:TIGR00957 1365 IPQDpvlFSGSLRMNLDPFSQYSDeevwWALELAHLKTFVSALPD----KLDHECAEGGENLSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488470846 151 AVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVSTHLLEDLQEFvSQLAVLSEGELIFEGSYSDL 217
Cdd:TIGR00957 1441 KILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-219 |
2.02e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.39 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDV----SDDVNTIRSMV 75
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGkITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 76 GFLPQRFSLplhFRIRRAVEYAAWARGVEPR--ECCVRAGA--ALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:PRK11831 87 SMLFQSGAL---FTDMNVFDNVAYPLREHTQlpAPLLHSTVmmKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 152 VLLLDEPTVGLDPASRIGVRSLLGEL--AEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDLES 219
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
26-220 |
2.44e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.50 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 26 SGLWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTI-----RSMVGFLPQRFSLPLHFRIRRAVEYaawa 100
Cdd:PRK11144 24 QGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppeKRRIGYVFQDARLFPHYKVRGNLRY---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 101 rGVEPreccVRAGAALDRVGLVDRAD--DRV-QSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLD-PASRiGVRSLLGE 176
Cdd:PRK11144 100 -GMAK----SMVAQFDKIVALLGIEPllDRYpGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKR-ELLPYLER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488470846 177 LAED-RTVIV-STHLLEDLQEFVSQLAVLSEGELIfegSYSDLESV 220
Cdd:PRK11144 174 LAREiNIPILyVSHSLDEILRLADRVVVLEQGKVK---AFGPLEEV 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
30-213 |
2.67e-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: 59.70 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLsiLATLR-EPESGHFRVNGVDVSDdvntiRSMVGFLPQR------F-----SLPLHFRIRRAVE-- 95
Cdd:COG4172 316 GLVGESGSGKSTLG--LALLRlIPSEGEIRFDGQDLDG-----LSRRALRPLRrrmqvvFqdpfgSLSPRMTVGQIIAeg 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 96 YAAWARGVEPRECCVRAGAALDRVGLVDRADDR-VQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLdpasrigvrsll 174
Cdd:COG4172 389 LRVHGPGLSAAERRARVAEALEEVGLDPAARHRyPHEFSGGQRQRIAIARALILEPKLLVLDEPTSAL------------ 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 175 gelaeDRTV---IVSthLLEDLQE-------FVS-----------QLAVLSEGELIFEGS 213
Cdd:COG4172 457 -----DVSVqaqILD--LLRDLQRehglaylFIShdlavvralahRVMVMKDGKVVEQGP 509
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-208 |
4.24e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 18 VDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVG--FLP---QRFSLPLHFRIR 91
Cdd:PRK15439 280 RNISLEVRAGeILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvYLPedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 92 RAV------EYAAWARGVEPRECCVRAGAALdrvGL-VDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDP 164
Cdd:PRK15439 360 WNVcalthnRRGFWIKPARENAVLERYRRAL---NIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488470846 165 ASRIGVRSLLGELAEDRTVIVstHLLEDLQEFV---SQLAVLSEGEL 208
Cdd:PRK15439 437 SARNDIYQLIRSIAAQNVAVL--FISSDLEEIEqmaDRVLVMHQGEI 481
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
30-217 |
4.25e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 59.34 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRS---MVGFLPQRFSLPLHFRI--------RRAVEYA 97
Cdd:PRK10789 345 GICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSrlaVVSQTPFLFSDTVANNIalgrpdatQQEIEHV 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 98 AwargvepRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGEL 177
Cdd:PRK10789 425 A-------RLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQW 497
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488470846 178 AEDRTVIVSTHLLEDLQEfVSQLAVLSEGELIFEGSYSDL 217
Cdd:PRK10789 498 GEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQL 536
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-194 |
4.55e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.66 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 7 ISHRYRRRRSLVDISCEFDSGLWGLL-GPNGAGKSTLLSIL--ATLREPESGHFRVNGVDVSDDVNTIRSmvgfLPQRFS 83
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIvGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFGREASLIDA----IGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 84 LPLhfrirrAVEyaawargvepreccvragaALDRVGLVD----RAddRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPT 159
Cdd:COG2401 112 FKD------AVE-------------------LLNAVGLSDavlwLR--RFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488470846 160 VGLDPA-SRIGVRSlLGELAEDR--TVIVSTH---LLEDLQ 194
Cdd:COG2401 165 SHLDRQtAKRVARN-LQKLARRAgiTLVVATHhydVIDDLQ 204
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
85-226 |
4.64e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.17 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 85 PLHFRIRRAVEYAAwARGVEPREccVRAGAALDRVGLVDraDDRVQSL-----SGGMRQRLGIACAIVGDPAVLLLDEPT 159
Cdd:PRK10418 94 PLHTMHTHARETCL-ALGKPADD--ATLTAALEAVGLEN--AARVLKLypfemSGGMLQRMMIALALLCEAPFIIADEPT 168
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 160 VGLDPASRIGVRSLLGELAEDRT--VIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDLESVGQkHPV 226
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK-HAV 236
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
54-188 |
5.46e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 54 SGHFRVNGVDVSD----DVNTIRSMVGFLPQRFSLPLHFRIRRAVEYAAwargvepRECCVRAG--AALDRV--GLVDRA 125
Cdd:PTZ00265 1276 SGKILLDGVDICDynlkDLRNLFSIVSQEPMLFNMSIYENIKFGKEDAT-------REDVKRACkfAAIDEFieSLPNKY 1348
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 126 DDRV----QSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAE--DRTVIVSTH 188
Cdd:PTZ00265 1349 DTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAH 1417
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-221 |
5.90e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHfrvngVDVSDDVNtirsmVGFLPQ 80
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGeRLAIIGENGVGKTTLLRTLVGELEPDSGT-----VKWSENAN-----IGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 RFSLplHFRIRRAV-EYAAWARGVEPRECCVRAgaALDRvgLVDRADD---RVQSLSGGMRQRLGIACAIVGDPAVLLLD 156
Cdd:PRK15064 390 DHAY--DFENDLTLfDWMSQWRQEGDDEQAVRG--TLGR--LLFSQDDikkSVKVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488470846 157 EPTVGLDPASrigVRSLlgELAEDR---TVIVSTHlleDlQEFVSQLAV----LSEGELI-FEGSYSD-LESVG 221
Cdd:PRK15064 464 EPTNHMDMES---IESL--NMALEKyegTLIFVSH---D-REFVSSLATriieITPDGVVdFSGTYEEyLRSQG 528
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
111-229 |
1.40e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.06 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 111 RAGAALDRVGLVD---RADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELA--EDRTVIV 185
Cdd:PRK11022 130 RAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqkENMALVL 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 488470846 186 STHLLEDLQEFVSQLAVLSEGELIFEGSYSDLESvGQKHPVRNA 229
Cdd:PRK11022 210 ITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR-APRHPYTQA 252
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
31-221 |
1.41e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 56.61 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILA--TLREPESGHFRVNGVDVSDDVNTIRSMVG-FL----PQRFS-LPLHFRIRRAVEyaawARG 102
Cdd:COG0396 31 IMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSPDERARAGiFLafqyPVEIPgVSVSNFLRTALN----ARR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 103 VEP---RECCVRAGAALDRVGLVDRADDR-V-QSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLD-PASRI---GVRSL 173
Cdd:COG0396 107 GEElsaREFLKLLKEKMKELGLDEDFLDRyVnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDiDALRIvaeGVNKL 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488470846 174 LGelaEDRTVIVSTH---LLEDLQ-EFVSqlaVLSEGELIFEGSYS---DLESVG 221
Cdd:COG0396 187 RS---PDRGILIITHyqrILDYIKpDFVH---VLVDGRIVKSGGKElalELEEEG 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-208 |
2.17e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 12 RRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDD------------VNTIRSMVGFL 78
Cdd:PRK09700 274 RDRKKVRDISFSVCRGeILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRspldavkkgmayITESRRDNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 79 PQrFSLPLHFRIRRAVEYAAW--ARG-VEPRECCVRAGAALDRVGL-VDRADDRVQSLSGGMRQRLGIACAIVGDPAVLL 154
Cdd:PRK09700 354 PN-FSIAQNMAISRSLKDGGYkgAMGlFHEVDEQRTAENQRELLALkCHSVNQNITELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488470846 155 LDEPTVGLDPASRIGVRSLLGELAEDRTVI--VSTHLLEdLQEFVSQLAVLSEGEL 208
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDGKVIlmVSSELPE-IITVCDRIAVFCEGRL 487
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
13-212 |
3.31e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.78 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 13 RRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPE--SGHFRVNGVDVSDDvnTIRSMVGFLPQRFSLPLHFR 89
Cdd:PLN03140 892 RLQLLREVTGAFRPGvLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQE--TFARISGYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 90 IRRAVEYAAWAR---GVEPRECCVRAGAALDRVGLVDRADDRV-----QSLSGGMRQRLGIACAIVGDPAVLLLDEPTVG 161
Cdd:PLN03140 970 VRESLIYSAFLRlpkEVSKEEKMMFVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488470846 162 LDP-ASRIGVRSLLGELAEDRTVIVSTHLLE-DLQEFVSQLAVLSE-GELIFEG 212
Cdd:PLN03140 1050 LDArAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRgGQVIYSG 1103
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-207 |
4.08e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGhfrvngvDVSDDVNtirsmVGFLPQRfslplhfrIRRAVEyaawargVEPRECC 109
Cdd:PRK13409 369 GIVGPNGIGKTTFAKLLAGVLKPDEG-------EVDPELK-----ISYKPQY--------IKPDYD-------GTVEDLL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 110 VRAGAALD----------RVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAE 179
Cdd:PRK13409 422 RSITDDLGssyykseiikPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAE 501
|
170 180 190
....*....|....*....|....*....|..
gi 488470846 180 DR--TVIVSTHlleD--LQEFVSQLAVLSEGE 207
Cdd:PRK13409 502 EReaTALVVDH---DiyMIDYISDRLMVFEGE 530
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-213 |
6.28e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILAT----LREPESGHFRVNGVDVSDDVNTIRSMVGFLPQrfsLPLHF---RIRRAVEYAAWARGV 103
Cdd:TIGR00956 92 VLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGITPEEIKKHYRGDVVYNAE---TDVHFphlTVGETLDFAARCKTP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 104 EPRECCV--------RAGAALDRVGL-----VDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGV 170
Cdd:TIGR00956 169 QNRPDGVsreeyakhIADVYMATYGLshtrnTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEF 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488470846 171 RSLLGELAE--DRTVIVSTHLL-EDLQEFVSQLAVLSEGELIFEGS 213
Cdd:TIGR00956 249 IRALKTSANilDTTPLVAIYQCsQDAYELFDKVIVLYEGYQIYFGP 294
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
33-180 |
1.02e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.59 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 33 GPNGAGKSTLLSILATLREPESGHFRVNGVDVSD----DVNTIRSMVGFLPQR--FSL-PlhfriRRAVEY--------- 96
Cdd:PRK11308 48 GESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpeAQKLLRQKIQIVFQNpyGSLnP-----RKKVGQileepllin 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 97 ----AAwargvEPREccvRAGAALDRVGLVDRADDRVQSL-SGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVR 171
Cdd:PRK11308 123 tslsAA-----ERRE---KALAMMAKVGLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVL 194
|
....*....
gi 488470846 172 SLLGELAED 180
Cdd:PRK11308 195 NLMMDLQQE 203
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-219 |
1.24e-08 |
|
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: 55.30 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 17 LVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGvdvsddvntirsMVGFLPQrFSLPLHFRIRRAVE 95
Cdd:TIGR01271 442 LKNISFKLEKGqLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQ-TSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 96 YaawarGVEPRE----CCVRAGAALDRVGLVDRADDRVQ-----SLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPAS 166
Cdd:TIGR01271 509 F-----GLSYDEyrytSVIKACQLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488470846 167 RIGV-RSLLGELAEDRTVIVSTHLLEDLQEfVSQLAVLSEGELIFEGSYSDLES 219
Cdd:TIGR01271 584 EKEIfESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQA 636
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
23-188 |
1.39e-08 |
|
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: 53.38 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 23 EFDSGLWGLLGPNGAGKSTLL-SILATLrepeSGHFRVNgvdvSDDVNTIRSMVGFLPQRFSLPLHFRIRRAVEYAawar 101
Cdd:cd03240 19 EFFSPLTLIVGQNGAGKTTIIeALKYAL----TGELPPN----SKGGAHDPKLIREGEVRAQVKLAFENANGKKYT---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 102 gveprecCVRAGAALDRVGLVDRAD------DRVQSLSGGMRQ------RLGIACAIVGDPAVLLLDEPTVGLDPASRIG 169
Cdd:cd03240 87 -------ITRSLAILENVIFCHQGEsnwpllDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEE 159
|
170 180
....*....|....*....|....
gi 488470846 170 -----VRSLLGElaEDRTVIVSTH 188
Cdd:cd03240 160 slaeiIEERKSQ--KNFQLIVITH 181
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-212 |
1.39e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.79 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGhfrvngvDVSDDVNtirsmVGFLPQR----FSLPLHFRIRRAVEYA-----AWA 100
Cdd:COG1245 370 GIVGPNGIGKTTFAKILAGVLKPDEG-------EVDEDLK-----ISYKPQYispdYDGTVEEFLRSANTDDfgssyYKT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 101 RGVEPreccvragAALDRvgLVDRaddRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAE- 179
Cdd:COG1245 438 EIIKP--------LGLEK--LLDK---NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEn 504
|
170 180 190
....*....|....*....|....*....|....*.
gi 488470846 180 -DRTVIVSTH--LLEDLqefvsqlavLSEGELIFEG 212
Cdd:COG1245 505 rGKTAMVVDHdiYLIDY---------ISDRLMVFEG 531
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-217 |
1.39e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVG--F 77
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGeVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiyL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQR--------------FSLPLHFRIRRAVEyaawargveprECCVRAGAALD---RVGLVDRADDR-VQSLSGGMRqr 139
Cdd:PRK15439 91 VPQEpllfpnlsvkenilFGLPKRQASMQKMK-----------QLLAALGCQLDldsSAGSLEVADRQiVEILRGLMR-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 140 lgiacaivgDPAVLLLDEPTVGLDPA------SRIgvRSLlgeLAEDRTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:PRK15439 158 ---------DSRILILDEPTASLTPAeterlfSRI--REL---LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
....
gi 488470846 214 YSDL 217
Cdd:PRK15439 224 TADL 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-188 |
1.47e-08 |
|
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: 52.54 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLV-DISCEFDSGLWGLL-GPNGAGKSTLLSILATLREPESGHfrvngVDVSDDVNTIrsmvgFLP 79
Cdd:cd03223 1 IELENLSLATPDGRVLLkDLSFEIKPGDRLLItGPSGTGKSSLFRALAGLWPWGSGR-----IGMPEGEDLL-----FLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 80 QRFSLPLHfRIRRAVEYAaWargvepreccvragaaldrvglvdradDRVqsLSGGMRQRLGIACAIVGDPAVLLLDEPT 159
Cdd:cd03223 71 QRPYLPLG-TLREQLIYP-W---------------------------DDV--LSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170 180 190
....*....|....*....|....*....|
gi 488470846 160 VGLDPASRIGVRSLL-GELAedrTVIVSTH 188
Cdd:cd03223 120 SALDEESEDRLYQLLkELGI---TVISVGH 146
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-218 |
2.11e-08 |
|
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: 54.17 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEF-DSGLWGLLGPNGAGKSTLLSILATLREPESGHFRVNG------VDVS----DDVNT 70
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLpPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGEtvklayVDQSrdalDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 71 IrsmvgflpqrfslplhfrirraveyaaWARgvepreccVRAGAALDRVGLVD---RA------------DDRVQSLSGG 135
Cdd:TIGR03719 403 V---------------------------WEE--------ISGGLDIIKLGKREipsRAyvgrfnfkgsdqQKKVGQLSGG 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 136 MRQRLGIACAIVGDPAVLLLDEPTVGLDPASrigVRSL---LGELAEDRTVI---------VSTHLledlqefvsqLAVL 203
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLDVET---LRALeeaLLNFAGCAVVIshdrwfldrIATHI----------LAFE 514
|
250
....*....|....*.
gi 488470846 204 SEGELI-FEGSYSDLE 218
Cdd:TIGR03719 515 GDSHVEwFEGNFSEYE 530
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
27-188 |
2.30e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 27 GLWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDVNTIRSMVGFLPQRFSLPLHFRIRRA----VEYAAWARG 102
Cdd:PRK13540 28 GLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENclydIHFSPGAVG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 103 VEPRECCVRAGAALD-RVGLvdraddrvqsLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASrigVRSLLGELAEDR 181
Cdd:PRK13540 108 ITELCRLFSLEHLIDyPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS---LLTIITKIQEHR 174
|
170
....*....|.
gi 488470846 182 ----TVIVSTH 188
Cdd:PRK13540 175 akggAVLLTSH 185
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
31-213 |
2.53e-08 |
|
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: 52.53 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPE--SGHFRVNGVDVSDdvntirsmvgflpqrfsLPLHFRIRRAVeYAAWARGVEprec 108
Cdd:cd03217 31 LMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITD-----------------LPPEERARLGI-FLAFQYPPE---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 109 cvragaaLDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLD-PASRIGVRSLLGELAEDRTVIVST 187
Cdd:cd03217 89 -------IPGVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDiDALRLVAEVINKLREEGKSVLIIT 161
|
170 180 190
....*....|....*....|....*....|
gi 488470846 188 H---LLEDLQ-EFVSqlaVLSEGELIFEGS 213
Cdd:cd03217 162 HyqrLLDYIKpDRVH---VLYDGRIVKSGD 188
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
30-215 |
3.21e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGHFRvngvdVSDDVNtirsmVGFLPQRFSLPLHFRIRRAVE-------------- 95
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEAR-----PAPGIK-----VGYLPQEPQLDPEKTVRENVEegvaevkaaldrfn 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 96 --YAAWArgvEPR----ECCVRAG---AALDRVGL------VDRA---------DDRVQSLSGGMRQRLGIACAIVGDPA 151
Cdd:PRK11819 107 eiYAAYA---EPDadfdALAAEQGelqEIIDAADAwdldsqLEIAmdalrcppwDAKVTKLSGGERRRVALCRLLLEKPD 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 152 VLLLDEPTVGLDPASrigVRSLLGELAE-DRTVIVSTH---LLEDLQEFVSQlavLSEGELI-FEGSYS 215
Cdd:PRK11819 184 MLLLDEPTNHLDAES---VAWLEQFLHDyPGTVVAVTHdryFLDNVAGWILE---LDRGRGIpWEGNYS 246
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
111-213 |
3.70e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.56 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 111 RAGAALDRVGLVDRADDRVQS-LSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTV--IVST 187
Cdd:PRK15134 404 QVIAVMEEVGLDPETRHRYPAeFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFIS 483
|
90 100
....*....|....*....|....*.
gi 488470846 188 HLLEDLQEFVSQLAVLSEGELIFEGS 213
Cdd:PRK15134 484 HDLHVVRALCHQVIVLRQGEVVEQGD 509
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
30-195 |
3.85e-08 |
|
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: 52.55 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPEsGHFRVNGVDVsddvNTI-----RSMVGFLPQR---FSLPLhfriRRAVE-YAAW- 99
Cdd:cd03289 34 GLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSW----NSVplqkwRKAFGVIPQKvfiFSGTF----RKNLDpYGKWs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 100 -------ARGVEPRECCVRAGAALDRVgLVDRAddrvQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRS 172
Cdd:cd03289 105 deeiwkvAEEVGLKSVIEQFPGQLDFV-LVDGG----CVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRK 179
|
170 180
....*....|....*....|...
gi 488470846 173 LLGELAEDRTVIVSTHLLEDLQE 195
Cdd:cd03289 180 TLKQAFADCTVILSEHRIEAMLE 202
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
133-190 |
5.96e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.42 E-value: 5.96e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 133 SGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAED--RTVIVSTHLL 190
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDL 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
132-213 |
7.56e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 132 LSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRT--VIVSTHLLEDLQEFVSQLAVLSEGELI 209
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
....
gi 488470846 210 FEGS 213
Cdd:PRK10261 249 ETGS 252
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
102-219 |
1.06e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 102 GVEPRECCVRAGAALDRVGLVDRaddRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELA-ED 180
Cdd:PRK10938 109 EVKDPARCEQLAQQFGITALLDR---RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHqSG 185
|
90 100 110
....*....|....*....|....*....|....*....
gi 488470846 181 RTVIVSTHLLEDLQEFVSQLAVLSEGELIFEGSYSDLES 219
Cdd:PRK10938 186 ITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
30-220 |
1.26e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.97 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGHFRVNGvdvsdDVNTIRSMVGFLPQRFSLplhfrirRAVEYAAWARGVEPRECC 109
Cdd:PRK13546 54 GLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----EVSVIAISAGLSGQLTGI-------ENIEFKMLCMGFKRKEIK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 110 VRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEP-TVGLDPASRIGVRSLLGELAEDRTVIVSTH 188
Cdd:PRK13546 122 AMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCLDKIYEFKEQNKTIFFVSH 201
|
170 180 190
....*....|....*....|....*....|..
gi 488470846 189 LLEDLQEFVSQLAVLSEGELifeGSYSDLESV 220
Cdd:PRK13546 202 NLGQVRQFCTKIAWIEGGKL---KDYGELDDV 230
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-221 |
1.35e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 14 RRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSilATLREPESghfrvngvdVSDDVNTIRSMVGFLPQ------------ 80
Cdd:PLN03130 630 RPTLSNINLDVPVGsLVAIVGSTGEGKTSLIS--AMLGELPP---------RSDASVVIRGTVAYVPQvswifnatvrdn 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 81 -RFSLPLH-FRIRRAVEYAAWARGVEpreccVRAGAALDRVGlvdradDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEP 158
Cdd:PLN03130 699 iLFGSPFDpERYERAIDVTALQHDLD-----LLPGGDLTEIG------ERGVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488470846 159 TVGLDP--ASRIGVRSLLGELAEDRTVIVSTHLledlqEFVSQ---LAVLSEGELIFEGSYSDLESVG 221
Cdd:PLN03130 768 LSALDAhvGRQVFDKCIKDELRGKTRVLVTNQL-----HFLSQvdrIILVHEGMIKEEGTYEELSNNG 830
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
14-189 |
2.02e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 14 RRSLVDISCEF-DSGLWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSddvNTIRSMVGFLPQRFSLPLHFRIRR 92
Cdd:PRK13541 13 QKNLFDLSITFlPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN---NIAKPYCTYIGHNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 93 AVEYaaWARGVEPRECCVragAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRS 172
Cdd:PRK13541 90 NLKF--WSEIYNSAETLY---AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN 164
|
170
....*....|....*...
gi 488470846 173 LLGELAED-RTVIVSTHL 189
Cdd:PRK13541 165 LIVMKANSgGIVLLSSHL 182
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-217 |
2.15e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.60 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATlREPESGhfRVNGVDVSDDVN---------- 69
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGrVTALLGRNGAGKSTLLKALAG-DLTGGG--APRGARVTGDVTlngeplaaid 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 70 --TIRSMVGFLPQRFSLPLHFRIRRAVEYA----AWARGVEPRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIA 143
Cdd:PRK13547 78 apRLARLRAVLPQAAQPAFAFSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 144 CAI---------VGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRT--VIVSTHLLEDLQEFVSQLAVLSEGELIFEG 212
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
....*
gi 488470846 213 SYSDL 217
Cdd:PRK13547 238 APADV 242
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-187 |
2.22e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATlrepesghfRVN-GVDVSDDVntirsMVGFLPQRFSLP----------LHFR---IRRAVEY 96
Cdd:TIGR00956 794 LMGASGAGKTTLLNVLAE---------RVTtGVITGGDR-----LVNGRPLDSSFQrsigyvqqqdLHLPtstVRESLRF 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 97 AAWARgvEPRECCVR-----AGAALDRVGLVDRADDRV----QSLSGGMRQRLGIACAIVGDPAVLL-LDEPTVGLDPAS 166
Cdd:TIGR00956 860 SAYLR--QPKSVSKSekmeyVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
170 180
....*....|....*....|.
gi 488470846 167 RIGVRSLLGELAEDRTVIVST 187
Cdd:TIGR00956 938 AWSICKLMRKLADHGQAILCT 958
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
31-215 |
2.23e-07 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 50.34 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILA--TLREPESGHFRVNGVDVSDDVNTIRSMVG-FLPqrFSLPLH-------FRIRRAVEYAAWA 100
Cdd:TIGR01978 31 IMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQDLLELEPDERARAGlFLA--FQYPEEipgvsnlEFLRSALNARRSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 101 RGVEP---RECCVRAGAALDRVGLVDRADDRvqSL----SGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSL 173
Cdd:TIGR01978 109 RGEEPldlLDFEKLLKEKLALLDMDEEFLNR--SVnegfSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEG 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488470846 174 LGELA-EDRTVIVSTH---LLEDLQ-EFVSqlaVLSEGELIFEGSYS 215
Cdd:TIGR01978 187 INRLRePDRSFLIITHyqrLLNYIKpDYVH---VLLDGRIVKSGDVE 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-219 |
2.92e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD----DVNTIRSMVGFLPQRFSLPLHFRIRRAVEY---AAWarg 102
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgltDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHndaDLW--- 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 103 veprECCVRA--GAALDR--VGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELA 178
Cdd:PLN03232 1343 ----EALERAhiKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEF 1418
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488470846 179 EDRTVIVSTHLLEDLQEfVSQLAVLSEGELIFEGSYSDLES 219
Cdd:PLN03232 1419 KSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
2-207 |
3.06e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.11 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFDSGLWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSddvntirsmvgFLPQR 81
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-----------YKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 82 FSLplhfrirraveyaawargvepreccvragaaldrvglvdraddrvqslSGGMRQRLGIACAIVGDPAVLLLDEPTVG 161
Cdd:cd03222 70 IDL------------------------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAY 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488470846 162 LDPASRIGVRSLLGELAE--DRTVIVSTHLLEDLqEFVSQLAVLSEGE 207
Cdd:cd03222 102 LDIEQRLNAARAIRRLSEegKKTALVVEHDLAVL-DYLSDRIHVFEGE 148
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-219 |
7.76e-07 |
|
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: 49.08 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 17 LVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGvdvsddvntirsMVGFLPQrFSLPLHFRIRRAVE 95
Cdd:cd03291 53 LKNINLKIEKGeMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------------RISFSSQ-FSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 96 YaawarGVEPRE----CCVRAGAALDRVGLVDRADDRVQ-----SLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPAS 166
Cdd:cd03291 120 F-----GVSYDEyrykSVVKACQLEEDITKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488470846 167 RIGV-RSLLGELAEDRTVIVSTHLLEDLQEfVSQLAVLSEGELIFEGSYSDLES 219
Cdd:cd03291 195 EKEIfESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELQS 247
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-217 |
2.30e-06 |
|
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: 48.40 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 28 LWGLLGPNGAGKSTLLSILATLREPESGHFrvngvdvsddvnTIRSMVGFLPQR-------------FSLPLHFRIRRAV 94
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAEMDKVEGHV------------HMKGSVAYVPQQawiqndslrenilFGKALNEKYYQQV 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 95 EYAawargvepreCCVRAGAALDRVGlvDRAD--DRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDP-------A 165
Cdd:TIGR00957 734 LEA----------CALLPDLEILPSG--DRTEigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhvgkhifE 801
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488470846 166 SRIGVRSLLgelaEDRTVIVSTHLLEDLQEfVSQLAVLSEGELIFEGSYSDL 217
Cdd:TIGR00957 802 HVIGPEGVL----KNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQEL 848
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
20-216 |
2.57e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 20 ISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHfrvngvdVSDDVNTirsMVGFLPQ-RFSLPlHFRIRRAV--- 94
Cdd:PRK15064 20 ISVKFGGGnRYGLIGANGCGKSTFMKILGGDLEPSAGN-------VSLDPNE---RLGKLRQdQFAFE-EFTVLDTVimg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 95 EYAAWARGVEpRECC------------------------------VRAGAALDRVGL-VDRADDRVQSLSGGMRQRLGIA 143
Cdd:PRK15064 89 HTELWEVKQE-RDRIyalpemseedgmkvadlevkfaemdgytaeARAGELLLGVGIpEEQHYGLMSEVAPGWKLRVLLA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488470846 144 CAIVGDPAVLLLDEPTVGLDPASrigVRSLLGELAE-DRTVIVSTHLLEDLQEFVSQLAVLSEGEL-IFEGSYSD 216
Cdd:PRK15064 168 QALFSNPDILLLDEPTNNLDINT---IRWLEDVLNErNSTMIIISHDRHFLNSVCTHMADLDYGELrVYPGNYDE 239
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-234 |
3.92e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 16 SLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATlrepESGHFRVNGVDvsddvntIRSMVGFLPQrFSLPLHFRIRRAV 94
Cdd:PLN03232 632 TLSDINLEIPVGsLVAIVGGTGEGKTSLISAMLG----ELSHAETSSVV-------IRGSVAYVPQ-VSWIFNATVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 95 EYAAwarGVEPReccvRAGAALDRVGLVDRAD-----------DRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLD 163
Cdd:PLN03232 700 LFGS---DFESE----RYWRAIDVTALQHDLDllpgrdlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488470846 164 P-ASRIGVRSLLGELAEDRTVIVSTHLLEDLQEfVSQLAVLSEGELIFEGSYSDLESVGQ--KHPVRNANDAEA 234
Cdd:PLN03232 773 AhVAHQVFDSCMKDELKGKTRVLVTNQLHFLPL-MDRIILVSEGMIKEEGTFAELSKSGSlfKKLMENAGKMDA 845
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
128-232 |
6.37e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 6.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 128 RVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLgeLAEDRTVIVSTHLLEDLQEFVSQLAVLSEGE 207
Cdd:PLN03073 341 ATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSHAREFLNTVVTDILHLHGQK 418
|
90 100
....*....|....*....|....*.
gi 488470846 208 LI-FEGSYSDLESVGQKHpVRNANDA 232
Cdd:PLN03073 419 LVtYKGDYDTFERTREEQ-LKNQQKA 443
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
129-208 |
7.51e-06 |
|
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: 46.36 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 129 VQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAED--RTVIVSTHLLEDLQeFVSQLAVLSEG 206
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEgvAIIVVSSELAEVLG-LSDRVLVIGEG 479
|
..
gi 488470846 207 EL 208
Cdd:TIGR02633 480 KL 481
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-195 |
7.99e-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: 44.67 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGHFrvngvdVSDDVNTIRsmvgflpqrfslplhfrirraveyaawargveprecc 109
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGV------IYIDGEDIL------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 110 vragAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELA-------EDRT 182
Cdd:smart00382 43 ----EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllkseKNLT 118
|
170
....*....|...
gi 488470846 183 VIVSTHLLEDLQE 195
Cdd:smart00382 119 VILTTNDEKDLGP 131
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
31-215 |
9.61e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.55 E-value: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPE--SGHFRVNGVDVSDDVNTIRSMVG-FLPqrFSLPL-------HFRIRRAVEYAAWA 100
Cdd:PRK09580 32 IMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLELSPEDRAGEGiFMA--FQYPVeipgvsnQFFLQTALNAVRSY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 101 RGVEPreccvragaaLDRVGLVDRADDRVQSL---------------SGGMRQRLGIACAIVGDPAVLLLDEPTVGLD-P 164
Cdd:PRK09580 110 RGQEP----------LDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDiD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488470846 165 ASRI---GVRSLLGelaEDRTVIVSTH---LLEDLQ-EFVSqlaVLSEGELIFEGSYS 215
Cdd:PRK09580 180 ALKIvadGVNSLRD---GKRSFIIVTHyqrILDYIKpDYVH---VLYQGRIVKSGDFT 231
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-190 |
1.15e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 1 MIELEHISHRYRRRRSLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHfrvngVDVSDDVNtirsmVGFLP 79
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGsRIGLLGRNGAGKSTLIKLLAGELAPVSGE-----IGLAKGIK-----LGYFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 80 QRfslPLHFriRRAVEYAA--WARgVEPRECCVRAGAALDRVGLV-DRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLD 156
Cdd:PRK10636 382 QH---QLEF--LRADESPLqhLAR-LAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180 190
....*....|....*....|....*....|....*.
gi 488470846 157 EPTVGLDPASRIGVRSLLGELaEDRTVIVS--THLL 190
Cdd:PRK10636 456 EPTNHLDLDMRQALTEALIDF-EGALVVVShdRHLL 490
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
131-206 |
1.33e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 1.33e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488470846 131 SLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELA-EDRTVIVSTHLLEDLQEFVSQLAVLSEG 206
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-163 |
1.84e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISceFD---SGLWGLLGPNGAGKSTLLSILATLREPESGHFRVnG-------VD-------- 63
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLS--FSlppGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GetvklayVDqsrdaldp 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 64 -------VSDDVNTIRsmVGflpqRFSLPlhfriRRAveYAAW--ARGvepreccvragaaldrvglvdrADD--RVQSL 132
Cdd:PRK11819 402 nktvweeISGGLDIIK--VG----NREIP-----SRA--YVGRfnFKG----------------------GDQqkKVGVL 446
|
170 180 190
....*....|....*....|....*....|.
gi 488470846 133 SGGMRQRLGIACAIVGDPAVLLLDEPTVGLD 163
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-163 |
2.66e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRRSLVDISCEFD---SGLWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGF 77
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEispSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 78 LPQR---FSLPLHFRIRRAVEYA---AWargvepreccvragAALDRVGLVDRA-------DDRV----QSLSGGMRQRL 140
Cdd:PLN03130 1318 IPQApvlFSGTVRFNLDPFNEHNdadLW--------------ESLERAHLKDVIrrnslglDAEVseagENFSVGQRQLL 1383
|
170 180
....*....|....*....|...
gi 488470846 141 GIACAIVGDPAVLLLDEPTVGLD 163
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVD 1406
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
128-208 |
2.69e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.53 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 128 RVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAED--RTVIVSTHLLEDLQefVS-QLAVLS 204
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQgvAIIVISSELPEVLG--LSdRVLVMH 479
|
....
gi 488470846 205 EGEL 208
Cdd:PRK13549 480 EGKL 483
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
125-163 |
3.79e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 3.79e-05
10 20 30
....*....|....*....|....*....|....*....
gi 488470846 125 ADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLD 163
Cdd:PRK11147 150 PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
128-191 |
4.90e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.35 E-value: 4.90e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 128 RVQsLSGGMRQRLGIA-----CAIVGDPaVLLLDEPTVGLDPASRIGVRSLLGELA-EDRTVIVSTHLLE 191
Cdd:cd03227 75 RLQ-LSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPE 142
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
30-165 |
5.45e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDV-SDDVNTIRSMVGFLPQRfslPLHF--RIRRAVEYAAWARGVEpr 106
Cdd:PTZ00243 1340 GIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIgAYGLRELRRQFSMIPQD---PVLFdgTVRQNVDPFLEASSAE-- 1414
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488470846 107 eccvrAGAALDRVGLVDRA-------DDRVQ----SLSGGMRQRLGIACAIVG-DPAVLLLDEPTVGLDPA 165
Cdd:PTZ00243 1415 -----VWAALELVGLRERVasesegiDSRVLeggsNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPA 1480
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-216 |
6.02e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 17 LVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGhfrvngvdvsdDVNTIRSmVGFLPQRF--------SLPLH 87
Cdd:PTZ00243 676 LRDVSVSVPRGkLTVVLGATGSGKSTLLQSLLSQFEISEG-----------RVWAERS-IAYVPQQAwimnatvrGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 88 FRIRRAveyAAWARGVepRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDP--A 165
Cdd:PTZ00243 744 FDEEDA---ARLADAV--RVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhvG 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488470846 166 SRIGVRSLLGELAeDRTVIVSTHLLE--DLQEFVsqlAVLSEGELIFEGSYSD 216
Cdd:PTZ00243 819 ERVVEECFLGALA-GKTRVLATHQVHvvPRADYV---VALGDGRVEFSGSSAD 867
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
2-43 |
8.10e-05 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 42.10 E-value: 8.10e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 488470846 2 IELEHIshryrrrRSLVDISCEFDSGLWGLLGPNGAGKSTLL 43
Cdd:pfam13476 1 LTIENF-------RSFRDQTIDFSKGLTLITGPNGSGKTTIL 35
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-188 |
9.53e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.04 E-value: 9.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 2 IELEHISHRYRRRR-SLVDISCEFDSG-LWGLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSDDvntirSMVGFLp 79
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGeLLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE-----QPEDYR- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 80 QRFSlplhfrirrAVEYAAW-------ARGVEPRECCVRAGaaLDRVGLVDR---ADDRVQ--SLSGGMRQRLGIACAIV 147
Cdd:PRK10522 397 KLFS---------AVFTDFHlfdqllgPEGKPANPALVEKW--LERLKMAHKlelEDGRISnlKLSKGQKKRLALLLALA 465
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488470846 148 GDPAVLLLDEPTVGLDPA-SRIGVRSLLGELAE-DRTVIVSTH 188
Cdd:PRK10522 466 EERDILLLDEWAADQDPHfRREFYQVLLPLLQEmGKTIFAISH 508
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
30-209 |
1.07e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.20 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD-DVNTIRSMVGFL---PQRFSLPLHFRI---RRAVEYAAW-AR 101
Cdd:cd03288 51 GICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlPLHTLRSRLSIIlqdPILFSGSIRFNLdpeCKCTDDRLWeAL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 102 GVEPRECCVRA-GAALDRVglvdrADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAED 180
Cdd:cd03288 131 EIAQLKNMVKSlPGGLDAV-----VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD 205
|
170 180
....*....|....*....|....*....
gi 488470846 181 RTVIVSTHLLEDLQEfVSQLAVLSEGELI 209
Cdd:cd03288 206 RTVVTIAHRVSTILD-ADLVLVLSRGILV 233
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
30-177 |
1.61e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 42.00 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGHFRVNGVDVSD----DVNTIRSMVGFLPQRFSLPLHFRIRRAVEYAAWARGVEP 105
Cdd:PRK15079 51 GVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmkddEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHP 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488470846 106 R----ECCVRAGAALDRVGLVDRADDRV-QSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGEL 177
Cdd:PRK15079 131 KlsrqEVKDRVKAMMLKVGLLPNLINRYpHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQL 207
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
126-227 |
1.86e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 126 DDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAE--DRTVIVSthLLEDLQE---FVSQL 200
Cdd:PLN03140 331 DEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHltEATVLMS--LLQPAPEtfdLFDDI 408
|
90 100 110
....*....|....*....|....*....|.
gi 488470846 201 AVLSEGELIFEGSYSDL----ESVGQKHPVR 227
Cdd:PLN03140 409 ILLSEGQIVYQGPRDHIleffESCGFKCPER 439
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
15-188 |
2.91e-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: 41.53 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 15 RSLVDISCEFDSGLWGLLGPNGAGKSTLLSILATLREPESGHfRVNGVD--VSDDVN--------TIRSMVGFLPQRFSL 84
Cdd:COG3593 12 RSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSR-KFDEEDfyLGDDPDlpeieielTFGSLLSRLLRLLLK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 85 PLHF-----------------------RIRRAVEYAAWARGVE--PRECCVRAGAALDRVGLVDRADDRVQSLSGGMRQR 139
Cdd:COG3593 91 EEDKeeleealeelneelkealkalneLLSEYLKELLDGLDLEleLSLDELEDLLKSLSLRIEDGKELPLDRLGSGFQRL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488470846 140 LGIACAIV-------GDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRT-VIVSTH 188
Cdd:COG3593 171 ILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNqVIITTH 227
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-193 |
3.65e-04 |
|
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: 40.39 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 16 SLVDISCEFDSG-LWGLLGPNGAGKSTLLsiLATLREPESGHFRVNGVDVSDDVNTI-------RSMVGFLPQR------ 81
Cdd:cd03290 16 TLSNINIRIPTGqLTMIVGQVGCGKSSLL--LAILGEMQTLEGKVHWSNKNESEPSFeatrsrnRYSVAYAAQKpwllna 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 82 -------FSLPLHFRIRRAVEYAawargvepreCCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLL 154
Cdd:cd03290 94 tveenitFGSPFNKQRYKAVTDA----------CSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488470846 155 LDEPTVGLDP--ASRIGVRSLLGELAED-RTVIVSTHLLEDL 193
Cdd:cd03290 164 LDDPFSALDIhlSDHLMQEGILKFLQDDkRTLVLVTHKLQYL 205
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
126-163 |
4.00e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.14 E-value: 4.00e-04
10 20 30
....*....|....*....|....*....|....*...
gi 488470846 126 DDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLD 163
Cdd:PRK10762 390 EQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
131-188 |
4.83e-04 |
|
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: 40.45 E-value: 4.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488470846 131 SLSGGMRQRLGIACAIVGD---PAVLLLDEPTVGLDPASRIGVRSLLGELAEDRT-VIVSTH 188
Cdd:pfam13304 236 ELSDGTKRLLALLAALLSAlpkGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTH 297
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
130-212 |
5.03e-04 |
|
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: 39.61 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 130 QSLSGGMRQRLGIACAIVGDP--AVLLLDEPTVGLDPasrIGVRSLLGELAEDR----TVIVSTHLLEDLQE-----FVS 198
Cdd:cd03238 86 STLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQ---QDINQLLEVIKGLIdlgnTVILIEHNLDVLSSadwiiDFG 162
|
90
....*....|....
gi 488470846 199 QLAVLSEGELIFEG 212
Cdd:cd03238 163 PGSGKSGGKVVFSG 176
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
31-180 |
5.13e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.99 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPESGHFRVNG--VDVSDD--VNTIRSMVGFLPQR------------FSLPLHFRIRRAV 94
Cdd:PRK10261 355 LVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPgkLQALRRDIQFIFQDpyasldprqtvgDSIMEPLRVHGLL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 95 EYAAWARgvepreccvRAGAALDRVGLV-DRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSL 173
Cdd:PRK10261 435 PGKAAAA---------RVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINL 505
|
....*..
gi 488470846 174 LGELAED 180
Cdd:PRK10261 506 LLDLQRD 512
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-212 |
6.53e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.70 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 31 LLGPNGAGKSTLLSILATLREPESGHFR-----------------------------------VNGVDvsddvntiRSMV 75
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGQLQADSGRIHcgtklevayfdqhraeldpektvmdnlaegkqevmVNGRP--------RHVL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 76 GFLpQRFSLPlhfrirraveyaawargvePReccvragaaldrvglvdRADDRVQSLSGGMRQRLGIACAIVGDPAVLLL 155
Cdd:PRK11147 422 GYL-QDFLFH-------------------PK-----------------RAMTPVKALSGGERNRLLLARLFLKPSNLLIL 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 156 DEPTVGLDpasrIGVRSLLGELAEDR--TVIVSTHlleDLQeFVSQLAVLSegeLIFEG 212
Cdd:PRK11147 465 DEPTNDLD----VETLELLEELLDSYqgTVLLVSH---DRQ-FVDNTVTEC---WIFEG 512
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
30-218 |
6.54e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.54 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 30 GLLGPNGAGKSTLLSILATLREPESGHFR---------VNGVDVSDDVNTIRSMVGflPQRFSLPLHFRIRRAVEY---- 96
Cdd:PRK10636 31 GLVGKNGCGKSTLLALLKNEISADGGSYTfpgnwqlawVNQETPALPQPALEYVID--GDREYRQLEAQLHDANERndgh 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 97 ------------AAWArgvepreccVRAGAA--LDRVGLVDRADDR-VQSLSGGMRQRLGIACAIVGDPAVLLLDEPTVG 161
Cdd:PRK10636 109 aiatihgkldaiDAWT---------IRSRAAslLHGLGFSNEQLERpVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNH 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488470846 162 LDPASRIGVRSLLGELAEdrTVIVSTHLLEDLQEFVSQLAVLsEGELIFE--GSYSDLE 218
Cdd:PRK10636 180 LDLDAVIWLEKWLKSYQG--TLILISHDRDFLDPIVDKIIHI-EQQSLFEytGNYSSFE 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-208 |
1.84e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 39.12 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 27 GLWGLLGpngAGKSTLLSILATLREPESGHFRVNG--VDVSDDVNTIRSMVGFLPQ-RFS---LPLHfRIRRAVEYAAwa 100
Cdd:PRK11288 283 GLFGLVG---AGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRAGIMLCPEdRKAegiIPVH-SVADNINISA-- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 101 rgvepRECCVRAGAALDRVGLVDRADDRVQS--------------LSGGMRQRlgiacAIVG-----DPAVLLLDEPTVG 161
Cdd:PRK11288 357 -----RRHHLRAGCLINNRWEAENADRFIRSlniktpsreqlimnLSGGNQQK-----AILGrwlseDMKVILLDEPTRG 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488470846 162 LDPASRIGVRSLLGELAED-RTVIVSThllEDLQEfVSQLA----VLSEGEL 208
Cdd:PRK11288 427 IDVGAKHEIYNVIYELAAQgVAVLFVS---SDLPE-VLGVAdrivVMREGRI 474
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
32-188 |
2.35e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 38.76 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 32 LGPNGAGkstLLSILATLREPESGHFRvngvdvsddvntirsmvgflpqrfslplhfRIRRAVEYAA-WARGVEPREccv 110
Cdd:COG4637 192 LAPDGSN---LAAVLATLRETHPERFE------------------------------RILEALRDAFpGFEDIEVEP--- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 111 rAGAALDRVGLVDRADDRVQS---LSGGMRQRLGIACAIV--GDPAVLLLDEPTVGLDPaSRIG-VRSLLGELAEDRTVI 184
Cdd:COG4637 236 -DEDGRVLLEFREKGLDRPFPareLSDGTLRFLALLAALLspRPPPLLCIEEPENGLHP-DLLPaLAELLREASERTQVI 313
|
....
gi 488470846 185 VSTH 188
Cdd:COG4637 314 VTTH 317
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-43 |
4.16e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 37.30 E-value: 4.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 488470846 2 IELEHIsHRYRRRRSLvdiscEFDSGLWGLLGPNGAGKSTLL 43
Cdd:COG0419 5 LRLENF-RSYRDTETI-----DFDDGLNLIVGPNGAGKSTIL 40
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
106-199 |
5.99e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.46 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 106 RECCVRAGAALDRVGLVDRADDRVQSLSGGMRQRLGIACAIVGDPAVLLLDEPTvgldpASrigvrslLGElaEDrtviv 185
Cdd:NF040905 114 NETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT-----AA-------LNE--ED----- 174
|
90
....*....|....
gi 488470846 186 STHLLEDLQEFVSQ 199
Cdd:NF040905 175 SAALLDLLLELKAQ 188
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
31-49 |
6.52e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 36.90 E-value: 6.52e-03
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
15-50 |
6.98e-03 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 37.06 E-value: 6.98e-03
10 20 30
....*....|....*....|....*....|....*....
gi 488470846 15 RSLVDISCEFDSGLWGLLGPNGAGKSTLL---SILATLR 50
Cdd:COG1195 11 RNYESLELEFSPGINVLVGPNGQGKTNLLeaiYLLATGR 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
122-205 |
8.71e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 37.05 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488470846 122 VDRADDR---VQSLSGGMR-Q-----RLGIACAIVGDPAVLLLDEPTVGLDPASRIGVRSLLGELAEDRTVIVST---HL 189
Cdd:COG4717 546 VDTEDGRtrpVEELSRGTReQlylalRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGRQVIYFTcheEL 625
|
90
....*....|....*.
gi 488470846 190 LEDLQEFVSQLAVLSE 205
Cdd:COG4717 626 VELFQEEGAHVIELES 641
|
|
| |
