|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-220 |
6.19e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 190.66 E-value: 6.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI---GIETKKSVAFLSD 79
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVardPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 80 GDFLDPKLTPLKAIAFYKDFF---SDFDESKALNLLKRFSVP--LKREFKALSKGMREKLQLILTLSRNASLYLFDEPVA 154
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYglpRKEARERIDELLELFGLTdaADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 155 GIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGELKKGYssLE 220
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL--LE 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-203 |
8.33e-52 |
|
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: 165.26 E-value: 8.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIG---IETKKSVAFLSD 79
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKkepEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 80 GDFLDPKLTPlkaiafykdffsdfdeskalnllkrfsvplkREFKALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPI 159
Cdd:cd03230 81 EPSLYENLTV-------------------------------RENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488135840 160 AREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKV 203
Cdd:cd03230 130 SRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-228 |
3.53e-50 |
|
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: 163.49 E-value: 3.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILN---QKIGIETKKSVAFLS 78
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 79 DGDFLDPKLTPLKAIAFYKDFFSDFDESKAL---NLLKRF--SVPLKREFKALSKGMREKLQLILTLSRNASLYLFDEPV 153
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKrieELIELLglEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488135840 154 AGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGELKKGY--SSLEVAYKERLK 228
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIgeENLEDAFVALIG 237
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
2.28e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 132.15 E-value: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLvEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKSVAFLSD- 79
Cdd:COG4152 1 ML-ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYLPEe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 80 -GdfLDPKLTPLKAIAFY---KDFFSDFDESKALNLLKRFSVP--LKREFKALSKGMREKLQLILTLSRNASLYLFDEPV 153
Cdd:COG4152 80 rG--LYPKMKVGEQLVYLarlKGLSKAEAKRRADEWLERLGLGdrANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488135840 154 AGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGELKKGY 216
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQF 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-207 |
1.33e-36 |
|
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: 127.78 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKSVAFLSDGDF 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 83 LDPKLT---PLKAIAFYKDFFSDFDESKALNLLKRFSVPLKREFK--ALSKGMREKLQLILTLSRNASLYLFDEPVAGID 157
Cdd:cd03269 81 LYPKMKvidQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRveELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488135840 158 PIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFG 207
Cdd:cd03269 161 PVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-213 |
1.87e-36 |
|
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: 127.62 E-value: 1.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSL--KALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKK---SVAFL 77
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAarqSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 SDGDFLDPKLTPLKAIAFY---KDFFSDFDESKALNLLKRFSVP--LKREFKALSKGMREKLQLILTLSRNASLYLFDEP 152
Cdd:cd03263 81 PQFDALFDELTVREHLRFYarlKGLPKSEIKEEVELLLRVLGLTdkANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488135840 153 VAGIDPIAREEIFELIASEfSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGELK 213
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-211 |
1.06e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 126.36 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGiETKKSVAFL--- 77
Cdd:COG1121 5 PAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-RARRRIGYVpqr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 --SDGDF-----------LDPKLTPLKaiafykdFFSDFDESKALNLLKRFSVP--LKREFKALSKGMREKLQLILTLSR 142
Cdd:COG1121 84 aeVDWDFpitvrdvvlmgRYGRRGLFR-------RPSRADREAVDEALERVGLEdlADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488135840 143 NASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEaKVVAFGDVGE 211
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNR-GLVAHGPPEE 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-189 |
2.12e-34 |
|
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: 121.82 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGI---ETKKSVAFL 77
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDareDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 SDGDFLDPKLTPLKAIAFYKDFF-SDFDESKALNLLKRFSVP--LKREFKALSKGMREKLQLILTLSRNASLYLFDEPVA 154
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYgLRADREAIDEALEAVGLAglADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|....*
gi 488135840 155 GIDPIAREEIFELIASEFSQNASLLVSTHLVVDVE 189
Cdd:COG4133 161 ALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA 195
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-207 |
2.28e-34 |
|
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: 121.87 E-value: 2.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 4 EIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGiETKKSVAFLS----- 78
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-KERKRIGYVPqrrsi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 79 DGDF-----------LDPKLTPLKaiafykdFFSDFDESKALNLLKRfsVPL----KREFKALSKGMREKLQLILTLSRN 143
Cdd:cd03235 80 DRDFpisvrdvvlmgLYGHKGLFR-------RLSKADKAKVDEALER--VGLselaDRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488135840 144 ASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKeAKVVAFG 207
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-207 |
6.97e-34 |
|
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: 120.76 E-value: 6.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQqFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGI---ETKKSVAFLSD 79
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKqpqKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 80 gDF-LDPKLTP---LKAIAFYKDFFSDFDESKALNLLKRfsVPL----KREFKALSKGMREKLQLILTLSRNASLYLFDE 151
Cdd:cd03264 80 -EFgVYPNFTVrefLDYIAWLKGIPSKEVKARVDEVLEL--VNLgdraKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 152 PVAGIDPIAREEIFELIaSEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFG 207
Cdd:cd03264 157 PTAGLDPEERIRFRNLL-SELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-202 |
8.82e-34 |
|
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: 118.89 E-value: 8.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 4 EIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIG----IETKKSVAFLSD 79
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAklplEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 80 gdfldpkltplkaiafykdffsdfdeskalnllkrfsvplkrefkaLSKGMREKLQLILTLSRNASLYLFDEPVAGIDPI 159
Cdd:cd00267 81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488135840 160 AREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAK 202
Cdd:cd00267 115 SRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
10-213 |
6.02e-32 |
|
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: 117.88 E-value: 6.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 10 KTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI-----------LNQKIGIeTKKSVAfls 78
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVagydvvreprkVRRSIGI-VPQYAS--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 79 dgdfLDPKLTP---LKAIAFYKDFFSDFDESKALNLLKRFSV--PLKREFKALSKGMREKLQLILTLSRNASLYLFDEPV 153
Cdd:TIGR01188 77 ----VDEDLTGrenLEMMGRLYGLPKDEAEERAEELLELFELgeAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 154 AGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGELK 213
Cdd:TIGR01188 153 TGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELK 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-204 |
1.82e-31 |
|
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: 114.24 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIG--IETKKSVAFLSDG 80
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQknIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 81 DFLDPKLTP---LKAIAFYKDfFSDFDESKALNLLKrFSVPLKREFKALSKGMREKLQLILTLSRNASLYLFDEPVAGID 157
Cdd:cd03268 81 PGFYPNLTArenLRLLARLLG-IRKKRIDEVLDVVG-LKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488135840 158 PIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVV 204
Cdd:cd03268 159 PDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-202 |
2.15e-30 |
|
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: 111.40 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 4 EIENLTKTYGSL--KALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKS----VAFL 77
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 sdgdFLDP-----KLTPLKAIAFYKDFFS---DFDESKALNLLKRF--SVPLKREFKALSKGMREKLQLILTLSRNASLY 147
Cdd:cd03225 81 ----FQNPddqffGPTVEEEVAFGLENLGlpeEEIEERVEEALELVglEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488135840 148 LFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAK 202
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-212 |
4.93e-30 |
|
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: 111.71 E-value: 4.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLN-LNYQGEVKILNQKIGIET----KKSVA 75
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERRGGEDvwelRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 FLSD--GDFLDPKLTPLKAI--AFYK-----DFFSDFDESKALNLLKRFSV-PLK-REFKALSKGMREKLQLILTLSRNA 144
Cdd:COG1119 82 LVSPalQLRFPRDETVLDVVlsGFFDsiglyREPTDEQRERARELLELLGLaHLAdRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488135840 145 SLYLFDEPVAGIDPIAREEIFELIaSEFSQN---ASLLVsTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALL-DKLAAEgapTLVLV-THHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-213 |
2.19e-29 |
|
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: 109.38 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI---GIETKKSVAFLSD 79
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrePREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 80 GDFLDPKLTPLKAIAFYKDFF---SDFDESKALNLLKRFSVPLKRE--FKALSKGMREKLQLILTLSRNASLYLFDEPVA 154
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYgvpGAERRERIDELLDFVGLLEAADrlVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 155 GIDPIAREEIFELI-ASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGELK 213
Cdd:cd03265 161 GLDPQTRAHVWEYIeKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2-207 |
4.00e-29 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 108.61 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLK----ALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILN---QKIGIETKKSV 74
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 75 AFLSDGDFLDPKLTPLKAIAFYKDFFS-DFDESKA----LNLLKRFSVPLKREFKALSKGMREKLQLILTLSRNASLYLF 149
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGlKGDELTArleeLADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488135840 150 DEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFG 207
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-212 |
4.51e-29 |
|
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: 109.36 E-value: 4.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI-GIETK---KSVAFL 77
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaSLSRRelaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 SDGDFLDPKLTPLKAIAF----YKDFFSDF---DESKALNLLKRFSV-PLK-REFKALSKGMREKLQLILTLSRNASLYL 148
Cdd:COG1120 81 PQEPPAPFGLTVRELVALgrypHLGLFGRPsaeDREAVEEALERTGLeHLAdRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488135840 149 FDEPVAGIDPIAREEIFELIASEF-SQNASLLVSTHlvvDvekyLNSA-------IFLKEAKVVAFGDVGEL 212
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLH---D----LNLAaryadrlVLLKDGRIVAQGPPEEV 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-212 |
7.34e-29 |
|
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: 108.19 E-value: 7.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTY-GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKS----VAFL 77
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 sdgdFLDP-----KLTPLKAIAFY-KDFFSDFDE--SKALNLLKRFSVP--LKREFKALSKGMREKLQLILTLSRNASLY 147
Cdd:COG1122 81 ----FQNPddqlfAPTVEEDVAFGpENLGLPREEirERVEEALELVGLEhlADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488135840 148 LFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-202 |
1.43e-27 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 103.42 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGietkksvaflsDGDF 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT-----------DLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 83 LDPKLTPLKAIAFyKDFfsdfdeskalNLLKRFSVPLKREFkALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIARE 162
Cdd:cd03229 70 ELPPLRRRIGMVF-QDF----------ALFPHLTVLENIAL-GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488135840 163 EIFELIASEFSQ-NASLLVSTHLVVDVEKYLNSAIFLKEAK 202
Cdd:cd03229 138 EVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-204 |
1.27e-26 |
|
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: 102.65 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 4 EIENLTKTYGSLK-ALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKS-------VA 75
Cdd:cd03256 2 EVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrrqIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 FLSDGDFLDPKLTPLKAI--------AFYKDFFSDFDES---KALNLLKRFSVpLKREFK---ALSKGMREKLQLILTLS 141
Cdd:cd03256 82 MIFQQFNLIERLSVLENVlsgrlgrrSTWRSLFGLFPKEekqRALAALERVGL-LDKAYQradQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 142 RNASLYLFDEPVAGIDPIAREEIFEL---IASEFsqNASLLVSTHLVVDVEKYLNSAIFLKEAKVV 204
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLlkrINREE--GITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-207 |
1.37e-26 |
|
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: 100.97 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 4 EIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKSVAflsdgdfl 83
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 84 dpkltplKAIAFykdffsdfdeskALNLLKRFSV-PLK-REFKALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAR 161
Cdd:cd03214 73 -------RKIAY------------VPQALELLGLaHLAdRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488135840 162 EEIFELIASEF-SQNASLLVSTHlvvdvekYLNSA-------IFLKEAKVVAFG 207
Cdd:cd03214 134 IELLELLRRLArERGKTVVMVLH-------DLNLAaryadrvILLKDGRIVAQG 180
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-207 |
1.66e-26 |
|
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: 101.44 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIET--KKSVAFLSDG 80
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPpeRRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 81 DFLDPKLTPLKAIAF-YKDFFSDFDE--SKALNLLKRF--SVPLKREFKALSKGMREKLQLILTLSRNASLYLFDEPVAG 155
Cdd:cd03259 81 YALFPHLTVAENIAFgLKLRGVPKAEirARVRELLELVglEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 156 IDPIAREEIFELIASEFSQN-ASLLVSTHlvvDVEKYLNSA---IFLKEAKVVAFG 207
Cdd:cd03259 161 LDAKLREELREELKELQRELgITTIYVTH---DQEEALALAdriAVMNEGRIVQVG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-154 |
2.67e-25 |
|
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: 96.56 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 18 LDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIET----KKSVAFLSDGDFLDPKLTPLKAI 93
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDErkslRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 94 AFY---KDFFSDFDESKALNLLKRFS------VPLKREFKALSKGMREKLQLILTLSRNASLYLFDEPVA 154
Cdd:pfam00005 81 RLGlllKGLSKREKDARAEEALEKLGlgdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-214 |
4.62e-25 |
|
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: 98.34 E-value: 4.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIG---------IETKKS 73
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseaelyrLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 74 VAFLSDGDFLDpkLTPLKAIAFYKDFFSDFDES--KALNLLKRFSVPLKREFKA----LSKGMREKLQLILTLSRNASLY 147
Cdd:cd03261 81 MLFQSGALFDS--LTVFENVAFPLREHTRLSEEeiREIVLEKLEAVGLRGAEDLypaeLSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488135840 148 LFDEPVAGIDPIAREEIFELIAS-EFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGELKK 214
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-198 |
1.07e-24 |
|
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: 96.77 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGS----LKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIgIETKKSVAFLS 78
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-TGPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 79 DGDFLDPKLTPLKAIAF-YKDFFSDFDESK--ALNLLKRfsVPLKrEF-----KALSKGMREKLQLILTLSRNASLYLFD 150
Cdd:cd03293 80 QQDALLPWLTVLDNVALgLELQGVPKAEARerAEELLEL--VGLS-GFenaypHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488135840 151 EPVAGIDPIAREEIFELIASEFSQN--ASLLVsTHlvvDVEKylnsAIFL 198
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETgkTVLLV-TH---DIDE----AVFL 198
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-204 |
2.34e-24 |
|
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: 95.79 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 4 EIENLTKTYG-SLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGI-ETKKSVAFLSDgd 81
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAkERRKSIGYVMQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 82 flDPkltplkaiafYKDFFSD--FDE------------SKALNLLKRFSVPLKREF--KALSKGMREKLQLILTLSRNAS 145
Cdd:cd03226 79 --DV----------DYQLFTDsvREElllglkeldagnEQAETVLKDLDLYALKERhpLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488135840 146 LYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHlvvDVE---KYLNSAIFLKEAKVV 204
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITH---DYEflaKVCDRVLLLANGAIV 205
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-212 |
3.38e-24 |
|
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: 96.19 E-value: 3.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 5 IENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIG-----IETKKSVAFLSD 79
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDIThlpmhERARLGIGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 80 GDFLDPKLT---PLKAI-AFYKDFFSDFDESKALNLLKRFSVPLKREFKA--LSKGMREKLQLILTLSRNASLYLFDEPV 153
Cdd:TIGR04406 84 EASIFRKLTveeNIMAVlEIRKDLDRAEREERLEALLEEFQISHLRDNKAmsLSGGERRRVEIARALATNPKFILLDEPF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488135840 154 AGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:TIGR04406 164 AGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-152 |
4.51e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 4.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVkilnqKIGIETKksVAFLS-DG 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-----KLGETVK--IGYFDqHQ 387
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488135840 81 DFLDPKLTPLKAIAfykDFFSDFDESKALNLLKRFSVPLKREFK---ALSKGMREKLQLILTLSRNASLYLFDEP 152
Cdd:COG0488 388 EELDPDKTVLDELR---DGAPGGTEQEVRGYLGRFLFSGDDAFKpvgVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-214 |
1.00e-23 |
|
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: 94.66 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIgietkksvaflsdgd 81
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDI--------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 82 fldpkltplkaiafykdffSDFDESKALNLLKRFSV-------------------PLkREFKALSKGM-----REKLQLi 137
Cdd:COG1127 70 -------------------TGLSEKELYELRRRIGMlfqggalfdsltvfenvafPL-REHTDLSEAEirelvLEKLEL- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 138 LTLSRNASLY-------------------------LFDEPVAGIDPIAREEIFELIAS---EFsqNASLLVSTHLVVDVE 189
Cdd:COG1127 129 VGLPGAADKMpselsggmrkrvalaralaldpeilLYDEPTAGLDPITSAVIDELIRElrdEL--GLTSVVVTHDLDSAF 206
|
250 260
....*....|....*....|....*
gi 488135840 190 KYLNSAIFLKEAKVVAFGDVGELKK 214
Cdd:COG1127 207 AIADRVAVLADGKIIAEGTPEELLA 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-212 |
2.78e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 95.26 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI---GIETKKSVAFLSD 79
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpsrARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 80 GDFLDPKLTPLKAIAFYKDFF--SDFDESKALNLLKRFSvplKREFKA------LSKGMREKLQLILTLSRNASLYLFDE 151
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFglSAAAARALVPPLLEFA---KLENKAdakvgeLSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488135840 152 PVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-198 |
9.30e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 92.85 E-value: 9.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTY----GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI-GIETKKSVA 75
Cdd:COG1116 6 PALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVtGPGPDRGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 FLSDGdfLDPKLTPLKAIAF---YKDFFSDFDESKALNLLKRfsVPLKrEF-----KALSKGMREKLQLILTLSRNASLY 147
Cdd:COG1116 86 FQEPA--LLPWLTVLDNVALgleLRGVPKAERRERARELLEL--VGLA-GFedaypHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488135840 148 LFDEPVAGIDPIAREEIFELIASEFSQN--ASLLVsTHlvvDVEKylnsAIFL 198
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLWQETgkTVLFV-TH---DVDE----AVFL 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-212 |
9.66e-23 |
|
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: 95.74 E-value: 9.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTY-----GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKSVA- 75
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRe 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 ------------FLSdgdfLDPKLTPLKAIAF----YKDFFSDFDESKALNLLKRfsVPLKREFK-----ALSKGMRekl 134
Cdd:COG1123 340 lrrrvqmvfqdpYSS----LNPRMTVGDIIAEplrlHGLLSRAERRERVAELLER--VGLPPDLAdryphELSGGQR--- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 135 QLIL---TLSRNASLYLFDEPVAGIDPIAREEIFELIAS---EFsqNASLLVSTHlvvD---VEKYLNSAIFLKEAKVVA 205
Cdd:COG1123 411 QRVAiarALALEPKLLILDEPTSALDVSVQAQILNLLRDlqrEL--GLTYLFISH---DlavVRYIADRVAVMYDGRIVE 485
|
....*..
gi 488135840 206 FGDVGEL 212
Cdd:COG1123 486 DGPTEEV 492
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-183 |
9.84e-23 |
|
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: 91.80 E-value: 9.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTY----GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKSV--- 74
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 75 ----------AFLSdgdfLDPKLTPLKAIA----FYKDFFSDFDESKALnLLKRFSVPLKREFK-----ALSKGMREKLQ 135
Cdd:cd03257 81 rkeiqmvfqdPMSS----LNPRMTIGEQIAeplrIHGKLSKKEARKEAV-LLLLVGVGLPEEVLnryphELSGGQRQRVA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488135840 136 LILTLSRNASLYLFDEPVAGIDPIAREEIFEL---IASEFsqNASLLVSTH 183
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLlkkLQEEL--GLTLLFITH 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-183 |
1.20e-22 |
|
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: 90.13 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGS--LKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI-GIETK---KSVAF 76
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLrDLDLEslrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 77 LSDGDFLdpkltplkaiafykdffsdFDESKALNLlkrfsvplkrefkaLSKGMREKLQLILTLSRNASLYLFDEPVAGI 156
Cdd:cd03228 81 VPQDPFL-------------------FSGTIRENI--------------LSGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180
....*....|....*....|....*..
gi 488135840 157 DPIAREEIFELIAsEFSQNASLLVSTH 183
Cdd:cd03228 128 DPETEALILEALR-ALAKGKTVIVIAH 153
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-209 |
1.44e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 92.49 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTY-GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKSVAFLSDGD 81
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 82 FLDPKLTPLKAIAFYKDFFSDFD-ESKALNLLKRFSVPLK----REFKA-----LSKGMREKLQLILTLSRNASLYLFDE 151
Cdd:PRK13647 85 FQDPDDQVFSSTVWDDVAFGPVNmGLDKDEVERRVEEALKavrmWDFRDkppyhLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488135840 152 PVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDV 209
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-190 |
2.75e-22 |
|
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: 90.85 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTY----------GSLK-----------ALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI 61
Cdd:cd03267 1 IEVSNLSKSYrvyskepgliGSLKslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 62 L-----NQKIGIETKKSVAFLSDGDfLDPKLTPLKAIAFYKDFFsDFDESKALNLLKRFSVPLKRE------FKALSKGM 130
Cdd:cd03267 81 AglvpwKRRKKFLRRIGVVFGQKTQ-LWWDLPVIDSFYLLAAIY-DLPPARFKKRLDELSELLDLEelldtpVRQLSLGQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488135840 131 REKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQ-NASLLVSTHLVVDVEK 190
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEA 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-212 |
1.07e-21 |
|
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: 89.14 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIgieTK--------KSV 74
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI---TKlpmhkrarLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 75 AFLSDGDFLDPKLT---PLKAIAFYKDFFSDFDESKALNLLKRFSVPLKREFKA--LSKGMREKLQLILTLSRNASLYLF 149
Cdd:cd03218 78 GYLPQEASIFRKLTveeNILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKAssLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488135840 150 DEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-183 |
1.71e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.01 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLnlnYQ---GEVKILNQKigietkksVAFL 77
Cdd:COG3845 4 PALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGL---YQpdsGEILIDGKP--------VRIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 SDGD------------F-LDPKLTPLKAIAFY----KDFFSDFDE--SKALNLLKR--FSVPLKREFKALSKGMREKLQL 136
Cdd:COG3845 73 SPRDaialgigmvhqhFmLVPNLTVAENIVLGleptKGGRLDRKAarARIRELSERygLDVDPDAKVEDLSVGEQQRVEI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488135840 137 ILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTH 183
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITH 199
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-212 |
2.09e-21 |
|
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: 88.39 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQ-----GEVKILNQKIG------IETK 71
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYdldvdvLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 72 KSVAFLsdgdFLDPklTPLKA-----IAF------YKDffSDFDESKALNLLKRfsVPLKREFK------ALSKGMREKL 134
Cdd:cd03260 81 RRVGMV----FQKP--NPFPGsiydnVAYglrlhgIKL--KEELDERVEEALRK--AALWDEVKdrlhalGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488135840 135 QLILTLSRNASLYLFDEPVAGIDPIAREEIFELIAsEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIA-ELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-212 |
5.25e-21 |
|
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: 90.73 E-value: 5.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTY--GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGL---NLNYQGEVK-----ILNQKIGIETK 71
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLldgrdLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 72 K-SVAFLSDGDFLDPkLTPLKAIAF---YKDFFSDFDESKALNLLKRfsVPLKREFKA----LSKGMREKLQLILTLSRN 143
Cdd:COG1123 84 RiGMVFQDPMTQLNP-VTVGDQIAEaleNLGLSRAEARARVLELLEA--VGLERRLDRyphqLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 144 ASLYLFDEPVAGIDPIAREEIFELIASEFSQ-NASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-183 |
6.12e-21 |
|
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: 85.56 E-value: 6.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLnlnYQ---GEVKILNQKigietkksVAFLSD 79
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGL---YKpdsGEILVDGKE--------VSFASP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 80 GDFLDpkltplKAIAF-YKdffsdfdeskalnllkrfsvplkrefkaLSKGMREKLQLILTLSRNASLYLFDEPVAGIDP 158
Cdd:cd03216 70 RDARR------AGIAMvYQ----------------------------LSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180
....*....|....*....|....*
gi 488135840 159 IAREEIFELIASEFSQNASLLVSTH 183
Cdd:cd03216 116 AEVERLFKVIRRLRAQGVAVIFISH 140
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-183 |
1.50e-20 |
|
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: 86.00 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGS----LKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIgieTKKSVAFLS 78
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDI---SKLSEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 79 D------G----DF-LDPKLTPLKAIA---FYKDFFSDFDESKALNLLKRFSVPLKREFKA--LSKGMREKLQLILTLSR 142
Cdd:cd03255 78 AfrrrhiGfvfqSFnLLPDLTALENVElplLLAGVPKKERRERAEELLERVGLGDRLNHYPseLSGGQQQRVAIARALAN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488135840 143 NASLYLFDEPVAGIDPIAREEIFELIASEFSQ-NASLLVSTH 183
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTH 199
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3-207 |
1.64e-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: 86.05 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTY-------GSLK---------------ALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVK 60
Cdd:cd03220 1 IELENVSKSYptykggsSSLKklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 61 IlnqkigieTKKSVAFLSDGDFLDPKLT--------------PLKAIAFYKDFFSDFDEskalnLLKRFSVPLKRefkaL 126
Cdd:cd03220 81 V--------RGRVSSLLGLGGGFNPELTgreniylngrllglSRKEIDEKIDEIIEFSE-----LGDFIDLPVKT----Y 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 127 SKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAF 206
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
.
gi 488135840 207 G 207
Cdd:cd03220 224 G 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-207 |
1.74e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.96 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIE---TKKSVAFL 77
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARarlARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 SDGDFLDPKLTPLKAIAFYKDFF--SDFDESKALNLLKRFSvplKREFKA------LSKGMREKLQLILTLSRNASLYLF 149
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFgmSTREIEAVIPSLLEFA---RLESKAdarvsdLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488135840 150 DEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFG 207
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-183 |
7.74e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.77 E-value: 7.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIET-KKSVAFLSD 79
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvAEACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 80 GDFLDPKLTPLKAIAFYKDFFSDfDESKALNLLKRFSVP--LKREFKALSKGMREKLQLILTLSRNASLYLFDEPVAGID 157
Cdd:PRK13539 81 RNAMKPALTVAENLEFWAAFLGG-EELDIAAALEAVGLAplAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....*.
gi 488135840 158 PIAREEIFELIASEFSQNASLLVSTH 183
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-170 |
9.56e-20 |
|
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: 84.03 E-value: 9.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 4 EIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIgieTKKSVA-------- 75
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI---TGLPPHeiarlgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 --------FlsdgdfldPKLTPLK-----AIAFYKDFFSDFDES--------KALNLLKRFSVPLKREFKA--LSKGMRE 132
Cdd:cd03219 79 rtfqiprlF--------PELTVLEnvmvaAQARTGSGLLLARARreereareRAEELLERVGLADLADRPAgeLSYGQQR 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 488135840 133 KLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIAS 170
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRE 188
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-207 |
1.47e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.79 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 6 ENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGI-----ETKKSVAFLSDG 80
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlplhaRARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 81 DFLDPKLTP----LKAIAFYKDFFSDFDESKALNLLKRFSVPLKREF--KALSKGMREKLQLILTLSRNASLYLFDEPVA 154
Cdd:PRK10895 87 ASIFRRLSVydnlMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSmgQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488135840 155 GIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFG 207
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHG 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-213 |
1.80e-19 |
|
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: 83.25 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 4 EIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIgieTKKS--------VA 75
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI---TGLPpheraragIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 FLSDGDFLDPKLTPLK--AIAFYKDFFSDFDESKAlNLLKRFsvPLKREFKA-----LSKGMREKLQLILTLSRNASLYL 148
Cdd:cd03224 79 YVPEGRRIFPELTVEEnlLLGAYARRRAKRKARLE-RVYELF--PRLKERRKqlagtLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488135840 149 FDEPVAGIDPIAREEIFELIASEFSQNASLLVsthlvvdVEKYLNSA-------IFLKEAKVVAFGDVGELK 213
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDEGVTILL-------VEQNARFAleiadraYVLERGRVVLEGTAAELL 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-219 |
2.24e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.21 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTY-------GSLK---------------ALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLnlnYQ---G 57
Cdd:COG1134 5 IEVENVSKSYrlyhepsRSLKelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGI---LEptsG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 58 EVKIlnqkigietKKSVAFLSD-GDFLDPKLT--------------PLKAIAFYKDFFSDFDEskalnlLKRFsvpLKRE 122
Cdd:COG1134 82 RVEV---------NGRVSALLElGAGFHPELTgreniylngrllglSRKEIDEKFDEIVEFAE------LGDF---IDQP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 123 FKALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPI----AREEIFELIAsefsQNASLLVSTHLVVDVEKYLNSAIFL 198
Cdd:COG1134 144 VKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRE----SGRTVIFVSHSMGAVRRLCDRAIWL 219
|
250 260
....*....|....*....|.
gi 488135840 199 KEAKVVAFGDVGELKKGYSSL 219
Cdd:COG1134 220 EKGRLVMDGDPEEVIAAYEAL 240
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-183 |
2.32e-19 |
|
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: 82.41 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 4 EIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVkILNQKIGIETK----KSVAFLSD 79
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV-RWNGTPLAEQRdephENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 80 GDFLDPKLTPLKAIAFYKDFFSD-----FDESKALNLLKRFSVPlkreFKALSKGMREKLQLI-LTLSRnASLYLFDEPV 153
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGaqrtiEDALAAVGLTGFEDLP----AAQLSAGQQRRLALArLWLSR-RPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 488135840 154 AGIDPIAREEIFELIASEFSQNASLLVSTH 183
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-164 |
4.19e-19 |
|
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: 82.39 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIET--KKSVAFLS 78
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPvqERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 79 DGDFLDPKLTPLKAIAF---YKDFFSDFDES----KALNLLK--RFSVPLKREFKALSKGMREKLQLILTLSRNASLYLF 149
Cdd:cd03296 81 QHYALFRHMTVFDNVAFglrVKPRSERPPEAeiraKVHELLKlvQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170
....*....|....*
gi 488135840 150 DEPVAGIDPIAREEI 164
Cdd:cd03296 161 DEPFGALDAKVRKEL 175
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-169 |
5.93e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.00 E-value: 5.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIgieT--------KK 72
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI---ThlpmhkraRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 73 SVAFLsdgdfldP-------KLT---PLKAIAFYKDFFSDFDESKALNLLKRFSVPLKREFKA--LSKGMREKLQLILTL 140
Cdd:COG1137 79 GIGYL-------PqeasifrKLTvedNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAysLSGGERRRVEIARAL 151
|
170 180
....*....|....*....|....*....
gi 488135840 141 SRNASLYLFDEPVAGIDPIAREEIFELIA 169
Cdd:COG1137 152 ATNPKFILLDEPFAGVDPIAVADIQKIIR 180
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-207 |
1.06e-18 |
|
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: 80.05 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYG--SLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI---LNQKIGIETKKSVAFL 77
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLdgvPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 SDGDFLdpkltplkaiafykdffsdFDESKALNLLKRFSvplkrefkalsKGMREKLQLILTLSRNASLYLFDEPVAGID 157
Cdd:cd03247 81 NQRPYL-------------------FDTTLRNNLGRRFS-----------GGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488135840 158 PIAREEIFELIAsEFSQNASLLVSTHLVVDVEkYLNSAIFLKEAKVVAFG 207
Cdd:cd03247 131 PITERQLLSLIF-EVLKDKTLIWITHHLTGIE-HMDKILFLENGKIIMQG 178
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-223 |
1.55e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 83.64 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILnqkigietkksvaflsDGDF 82
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVL----------------GGDM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 83 LDPK----LTPlkAIAF---------YK--------DFFSD-FDESKA------LNLLK-----RFsvpLKREFKALSKG 129
Cdd:NF033858 66 ADARhrraVCP--RIAYmpqglgknlYPtlsvfenlDFFGRlFGQDAAerrrriDELLRatglaPF---ADRPAGKLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 130 MREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNA--SLLVST----------HLVVdvekylnsaif 197
Cdd:NF033858 141 MKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgmSVLVATaymeeaerfdWLVA----------- 209
|
250 260
....*....|....*....|....*...
gi 488135840 198 LKEAKVVAFGDVGELKK--GYSSLEVAY 223
Cdd:NF033858 210 MDAGRVLATGTPAELLArtGADTLEAAF 237
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-61 |
1.87e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 82.45 E-value: 1.87e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI 61
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL 64
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-51 |
2.02e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 82.50 E-value: 2.02e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGL 51
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGL 51
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-184 |
2.15e-18 |
|
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: 79.84 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 4 EIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGI---ETKKSVAFLSDG 80
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFqrdSIARGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 81 DFLDPKLTPLKAIAFYKDFFSDFDESKAL---NLLKRFSVPlkreFKALSKGMREKLQLILTLSRNASLYLFDEPVAGID 157
Cdd:cd03231 82 PGIKTTLSVLENLRFWHADHSDEQVEEALarvGLNGFEDRP----VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180
....*....|....*....|....*..
gi 488135840 158 PIAREEIFELIASEFSQNASLLVSTHL 184
Cdd:cd03231 158 KAGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-164 |
3.34e-18 |
|
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: 79.61 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI-GIETKK-SVAFLSDG 80
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtDLPPKDrDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 81 DFLDPKLT-------PLKAIAFYKDffsDFDE--SKALNLLkRFSVPLKREFKALSKGMREKLQLILTLSRNASLYLFDE 151
Cdd:cd03301 81 YALYPHMTvydniafGLKLRKVPKD---EIDErvREVAELL-QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170
....*....|...
gi 488135840 152 PVAGIDPIAREEI 164
Cdd:cd03301 157 PLSNLDAKLRVQM 169
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-212 |
3.62e-18 |
|
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: 82.57 E-value: 3.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLK--ALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI----LNQkIGIET-KKSVA 75
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidLRQ-IDPASlRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 FLSDGDFL------------DPKLTPLKAIAFYKDF-FSDFdeskALNLLKRFSVPLKREFKALSKGMREKLQLILTLSR 142
Cdd:COG2274 553 VVLQDVFLfsgtirenitlgDPDATDEEIIEAARLAgLHDF----IEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488135840 143 NASLYLFDEPVAGIDPIAREEIFELIAsEFSQNASLLVSTH---LVVDVEKylnsAIFLKEAKVVAFGDVGEL 212
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLR-RLLKGRTVIIIAHrlsTIRLADR----IIVLDKGRIVEDGTHEEL 696
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-212 |
3.65e-18 |
|
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: 82.50 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTY-GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKS----VAFL 77
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrrqIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 SDGDFLdPKLTpLKA-IAFYKdffSDFDESKALNLLKRfsVPLKREFKALSKGMREKL-------------QLILT--LS 141
Cdd:COG4988 417 PQNPYL-FAGT-IREnLRLGR---PDASDEELEAALEA--AGLDEFVAALPDGLDTPLgeggrglsggqaqRLALAraLL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488135840 142 RNASLYLFDEPVAGIDPIAREEIFELIAsEFSQNASLLVSTH---LVVDVEKylnsAIFLKEAKVVAFGDVGEL 212
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALR-RLAKGRTVILITHrlaLLAQADR----ILVLDDGRIVEQGTHEEL 558
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-168 |
4.01e-18 |
|
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: 80.08 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLnlnYQ---GEVKILNQKIgieTKKS---- 73
Cdd:COG0411 3 PLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF---YRptsGRILFDGRDI---TGLPphri 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 74 -------------------------VAFLS--DGDFLDPKLTPLKAIAFYKDffsdfDESKALNLLKRFSVPLKREFKA- 125
Cdd:COG0411 77 arlgiartfqnprlfpeltvlenvlVAAHArlGRGLLAALLRLPRARREERE-----ARERAEELLERVGLADRADEPAg 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488135840 126 -LSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELI 168
Cdd:COG0411 152 nLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELI 195
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-183 |
4.74e-18 |
|
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: 82.33 E-value: 4.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTY-GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI-GIETK---KSVAFL 77
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLaDADADswrDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 SDGDFLDPKlTPLKAIAFYKDFFSDFDESKALNL--LKRF--SVPLKREFKA------LSKGMREKLQLILTLSRNASLY 147
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLARPDASDAEIREALERagLDEFvaALPQGLDTPIgeggagLSGGQAQRLALARAFLRDAPLL 480
|
170 180 190
....*....|....*....|....*....|....*.
gi 488135840 148 LFDEPVAGIDPIAREEIFELIAsEFSQNASLLVSTH 183
Cdd:TIGR02857 481 LLDEPTAHLDAETEAEVLEALR-ALAQGRTVLLVTH 515
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-167 |
6.73e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 80.89 E-value: 6.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI-GIETKK-SVAFLsdg 80
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtDLPPKDrNIAMV--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 81 dF----LDPKLT-------PLKAIAFYKDffsDFDE-----SKALN---LLKRFsvPlkrefKALSKGMREKLQLILTLS 141
Cdd:COG3839 81 -FqsyaLYPHMTvyeniafPLKLRKVPKA---EIDRrvreaAELLGledLLDRK--P-----KQLSGGQRQRVALGRALV 149
|
170 180 190
....*....|....*....|....*....|
gi 488135840 142 RNASLYLFDEPVAGIDP----IAREEIFEL 167
Cdd:COG3839 150 REPKVFLLDEPLSNLDAklrvEMRAEIKRL 179
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-205 |
6.76e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 78.93 E-value: 6.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGS----LKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIgieTKKSVAFL 77
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI---SSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 SD------G----DF-LDPKLTPLKAIAF---YKDFFSDFDESKALNLLKRFSVPLKREFKA--LSKGMReklQ------ 135
Cdd:COG1136 81 ARlrrrhiGfvfqFFnLLPELTALENVALpllLAGVSRKERRERARELLERVGLGDRLDHRPsqLSGGQQ---Qrvaiar 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 136 -LIltlsRNASLYLFDEPVAGIDPIAREEIFEL---IASEfsQNASLLVSTHlvvDVE--KYLNSAIFLKEAKVVA 205
Cdd:COG1136 158 aLV----NRPKLILADEPTGNLDSKTGEEVLELlreLNRE--LGTTIVMVTH---DPElaARADRVIRLRDGRIVS 224
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
2-183 |
1.72e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 77.30 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIET---KKSVAFLS 78
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLctyQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 79 DGDFLDPKLTpLKAIAFYKDFFSdfdeSKAL---NLLKRFSVPLKREFKA--LSKGMREKLQLILTLSRNASLYLFDEPV 153
Cdd:PRK13540 81 HRSGINPYLT-LRENCLYDIHFS----PGAVgitELCRLFSLEHLIDYPCglLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|
gi 488135840 154 AGIDPIAREEIFELIASEFSQNASLLVSTH 183
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-203 |
1.91e-17 |
|
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: 77.45 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTY-GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKSVAFL--SD 79
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 80 G----DF-LDPKLTPLKAIAFYKDFFsdfdESKALNLLKRFSVPL--------KREFKA-LSKGMREKLQLILTLSRNAS 145
Cdd:cd03292 81 GvvfqDFrLLPDRNVYENVAFALEVT----GVPPREIRKRVPAALelvglshkHRALPAeLSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488135840 146 LYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKV 203
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-207 |
3.75e-17 |
|
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: 76.44 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKT------YGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGL--NLNYQGEVKILNQKIGIET-KKS 73
Cdd:cd03213 4 LSFRNLTVTvksspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSfRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 74 VAFLSDGDFLDPKLTPLKAIAFykdffsdfdeskALNLlkrfsvplkrefKALSKGMREKLQLILTLSRNASLYLFDEPV 153
Cdd:cd03213 84 IGYVPQDDILHPTLTVRETLMF------------AAKL------------RGLSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488135840 154 AGIDPIAREEIFELIASEFSQNASLLVSTH-LVVDVEKYLNSAIFLKEAKVVAFG 207
Cdd:cd03213 140 SGLDSSSALQVMSLLRRLADTGRTIICSIHqPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-211 |
3.81e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGI----ETKKSVAF 76
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlssrQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 77 LsdgdfldPK--LTPlKAIAFYKdfFSDFDESKALNLLKRFSVPLK-----------------REFKALSKGMREKLQLI 137
Cdd:PRK11231 81 L-------PQhhLTP-EGITVRE--LVAYGRSPWLSLWGRLSAEDNarvnqameqtrinhladRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488135840 138 LTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGE 211
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-208 |
4.79e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.20 E-value: 4.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGS-----LKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKIL--NQKIGIETKKS 73
Cdd:PRK13651 1 MQIKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkDEKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 74 VAFLSDGDFLDPKLTPLKAI-------------AFYKDFFSDFDE-----------------SKALNLLKRFSVP---LK 120
Cdd:PRK13651 81 EKVLEKLVIQKTRFKKIKKIkeirrrvgvvfqfAEYQLFEQTIEKdiifgpvsmgvskeeakKRAAKYIELVGLDesyLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 121 REFKALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKE 200
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
....*...
gi 488135840 201 AKVVAFGD 208
Cdd:PRK13651 241 GKIIKDGD 248
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-164 |
1.60e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.18 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGI--ETKKSVAFLSD 79
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvpPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 80 GDFLDPKLTPLKAIAF--------YKDFFSDFDESKALNLLKRFSvplKREFKALSKGMREKLQLILTLSRNASLYLFDE 151
Cdd:PRK11607 99 SYALFPHMTVEQNIAFglkqdklpKAEIASRVNEMLGLVHMQEFA---KRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170
....*....|...
gi 488135840 152 PVAGIDPIAREEI 164
Cdd:PRK11607 176 PMGALDKKLRDRM 188
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-212 |
3.82e-16 |
|
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: 74.25 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI-GIET----KKSVA 75
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItGLPPhriaRLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 FLSDGDFLDPKLTP---LKAIAFYKDFFSDFDESKALnLLKRFsvPLKREFKA-----LSKGmrEklQLILTLSR----N 143
Cdd:COG0410 82 YVPEGRRIFPSLTVeenLLLGAYARRDRAEVRADLER-VYELF--PRLKERRRqragtLSGG--E--QQMLAIGRalmsR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 144 ASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVsthlvvdVEKYLNSA-------IFLKEAKVVAFGDVGEL 212
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILL-------VEQNARFAleiadraYVLERGRIVLEGTAAEL 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-212 |
5.41e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.02 E-value: 5.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLvEIENLTKTYGSLKAldNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIgieTKKS-----VA 75
Cdd:COG3840 1 ML-RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL---TALPpaerpVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 FLSDGDFLDPKLTPLKAIAF-----YKdfFSDFDESKALNLLKRFSVP--LKREFKALSKGMREKLQLILTLSRNASLYL 148
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGLglrpgLK--LTAEQRAQVEQALERVGLAglLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488135840 149 FDEPVAGIDPIAREEIFEL---IASEfsQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLvdeLCRE--RGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
2-198 |
7.08e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.97 E-value: 7.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI-GIETKKSVAFLSDG 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVeGPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 81 dfLDPKLTPLKAIAF---YKDFFSDFDESKALNLLKRfsVPL----KREFKALSKGMREKLQLILTLSRNASLYLFDEPV 153
Cdd:PRK11248 81 --LLPWRNVQDNVAFglqLAGVEKMQRLEIAHQMLKK--VGLegaeKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488135840 154 AGIDPIAREEIFELIASEFSQNAS-LLVSTHlvvDVEKylnsAIFL 198
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQETGKqVLLITH---DIEE----AVFM 195
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-181 |
8.10e-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: 71.33 E-value: 8.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKIL-NQKIGIetkksvaflsdgd 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGsTVKIGY------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 82 fldpkltplkaiafykdffsdfdeskalnllkrfsvplkreFKALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAR 161
Cdd:cd03221 68 -----------------------------------------FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI 106
|
170 180
....*....|....*....|
gi 488135840 162 EEIFELIaSEFsQNASLLVS 181
Cdd:cd03221 107 EALEEAL-KEY-PGTVILVS 124
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-152 |
1.06e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.10 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 5 IENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQkigietkKSVAFLSDGDFLD 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-------LRIGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 85 PKLTPL----------------------------KAIAFYKDFFSDFD-------ESKALNLLKRF---SVPLKREFKAL 126
Cdd:COG0488 74 DDLTVLdtvldgdaelraleaeleeleaklaepdEDLERLAELQEEFEalggweaEARAEEILSGLgfpEEDLDRPVSEL 153
|
170 180
....*....|....*....|....*.
gi 488135840 127 SKGMREKLQLILTLSRNASLYLFDEP 152
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-168 |
1.09e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.05 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLnlnYQ---GEVKILNQKIGIETKK----- 72
Cdd:COG1129 3 PLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGV---YQpdsGEILLDGEPVRFRSPRdaqaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 73 ---------------SVA---FLSD----GDFLDPKLTplkaiafykdffsdfdESKALNLLKRF--SVPLKREFKALSK 128
Cdd:COG1129 80 giaiihqelnlvpnlSVAeniFLGReprrGGLIDWRAM----------------RRRARELLARLglDIDPDTPVGDLSV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488135840 129 GMReklQLIL---TLSRNASLYLFDEPVAGIDPIAREEIFELI 168
Cdd:COG1129 144 AQQ---QLVEiarALSRDARVLILDEPTASLTEREVERLFRII 183
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3-207 |
1.43e-15 |
|
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: 72.53 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKAldNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIE--TKKSVAFLSDG 80
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAppADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 81 DFLDPKLTPLKAIAFYKD---FFSDFDESKALNLLKRFSVP--LKREFKALSKGMREKLQLILTLSRNASLYLFDEPVAG 155
Cdd:cd03298 79 NNLFAHLTVEQNVGLGLSpglKLTAEDRQAIEVALARVGLAglEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488135840 156 IDPIAREEIFELIASEFSQNA-SLLVSTHLVVDVEKYLNSAIFLKEAKVVAFG 207
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-220 |
2.04e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.16 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTY--GS---LKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI-------------- 61
Cdd:PRK13637 1 MSIKIENLTHIYmeGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditdkkvklsd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 62 LNQKIGI-----------ET-KKSVAF------LSDGDFLDPKLTPLKAIAFYKDFFSDfdeskalnllkrfsvplKREF 123
Cdd:PRK13637 81 IRKKVGLvfqypeyqlfeETiEKDIAFgpinlgLSEEEIENRVKRAMNIVGLDYEDYKD-----------------KSPF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 124 KaLSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIAS--EFSQNASLLVStHLVVDVEKYLNSAIFLKEA 201
Cdd:PRK13637 144 E-LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVS-HSMEDVAKLADRIIVMNKG 221
|
250
....*....|....*....
gi 488135840 202 KVVAFGDVGELKKGYSSLE 220
Cdd:PRK13637 222 KCELQGTPREVFKEVETLE 240
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-61 |
2.62e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.42 E-value: 2.62e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI 61
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLV 60
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
8-187 |
2.65e-15 |
|
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: 72.44 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 8 LTKTYGSLKaLDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILN-------QKIGIETKKSVAflsdg 80
Cdd:cd03237 6 MKKTLGEFT-LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtvsykpQYIKADYEGTVR----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 81 DFLDPKLTPLKAIAFYKdffsdfdeSKALNLLKRFSVpLKREFKALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIA 160
Cdd:cd03237 80 DLLSSITKDFYTHPYFK--------TEIAKPLQIEQI-LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
170 180 190
....*....|....*....|....*....|.
gi 488135840 161 ReeifeLIASE----FSQNASllvSTHLVVD 187
Cdd:cd03237 151 R-----LMASKvirrFAENNE---KTAFVVE 173
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-218 |
3.06e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.20 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTY----------GSLK-----------ALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI 61
Cdd:COG4586 2 IEVENLSKTYrvyekepglkGALKglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 62 LNQkigIETKKSVAFLSDGDF-------LDPKLTP------LKAIafY----KDFFSDFDE-SKALNLLKRFSVPLKRef 123
Cdd:COG4586 82 LGY---VPFKRRKEFARRIGVvfgqrsqLWWDLPAidsfrlLKAI--YripdAEYKKRLDElVELLDLGELLDTPVRQ-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 124 kaLSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIAsEFSQ--NASLLVSTHLVVDVEKYLNSAIFLKEA 201
Cdd:COG4586 155 --LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLK-EYNRerGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
250
....*....|....*..
gi 488135840 202 KVVAFGDVGELKKGYSS 218
Cdd:COG4586 232 RIIYDGSLEELKERFGP 248
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-216 |
3.11e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.94 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYG-----SLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIET----- 70
Cdd:PRK13641 1 MSIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 71 -----KKSVAFlsdgDFLDPKL---TPLKAIAF-YKDF-FSDFD-ESKALNLLKRFSVPL----KREFKaLSKGMREKLQ 135
Cdd:PRK13641 81 kklrkKVSLVF----QFPEAQLfenTVLKDVEFgPKNFgFSEDEaKEKALKWLKKVGLSEdlisKSPFE-LSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 136 LILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVA-------FGD 208
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKhaspkeiFSD 235
|
....*...
gi 488135840 209 VGELKKGY 216
Cdd:PRK13641 236 KEWLKKHY 243
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-222 |
4.56e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 71.95 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLK--ALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKIL------------------ 62
Cdd:PRK13632 8 IKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDgitiskenlkeirkkigi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 63 ------NQKIGIETKKSVAFLSDGDFLDPKltPLKAIAFykdffsdfDESKALNLLKRfsvpLKREFKALSKGMREKLQL 136
Cdd:PRK13632 88 ifqnpdNQFIGATVEDDIAFGLENKKVPPK--KMKDIID--------DLAKKVGMEDY----LDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 137 ILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVS-THlvvDVEKYLNS--AIFLKEAKVVAFGDVGELK 213
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTH---DMDEAILAdkVIVFSEGKLIAQGKPKEIL 230
|
....*....
gi 488135840 214 KGYSSLEVA 222
Cdd:PRK13632 231 NNKEILEKA 239
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-214 |
4.83e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.11 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI---------GIETKK 72
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrsrlyTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 73 SVAFLSDGDFLDpkLTPLKAIAFYKDFFSDFDES--KALNLLKRFSVPLKREFK----ALSKGMREKLQLILTLSRNASL 146
Cdd:PRK11831 87 SMLFQSGALFTD--MNVFDNVAYPLREHTQLPAPllHSTVMMKLEAVGLRGAAKlmpsELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488135840 147 YLFDEPVAGIDPIAREEIFELIaSEFsqNASL----LVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGELKK 214
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLI-SEL--NSALgvtcVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-164 |
5.50e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.81 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIG-IETK-KSVAFLS 78
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSrLHARdRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 79 DGDFLDPKLTPLKAIAF-------YKDFFSDFDESKALNLLKRFSVP-LKREFKA-LSKGMREKLQLILTLSRNASLYLF 149
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFgltvlprRERPNAAAIKAKVTQLLEMVQLAhLADRYPAqLSGGQKQRVALARALAVEPQILLL 160
|
170
....*....|....*
gi 488135840 150 DEPVAGIDPIAREEI 164
Cdd:PRK10851 161 DEPFGALDAQVRKEL 175
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-183 |
6.30e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 73.51 E-value: 6.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTY--GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIgiET-----KKSVA 75
Cdd:TIGR01257 929 VCVKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETnldavRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 FLSDGDFLDPKLTPLKAIAFYKDFFSDFDESKALNL---LKRFSVPLKR--EFKALSKGMREKLQLILTLSRNASLYLFD 150
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMeamLEDTGLHHKRneEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190
....*....|....*....|....*....|...
gi 488135840 151 EPVAGIDPIAREEIFELIAsEFSQNASLLVSTH 183
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLL-KYRSGRTIIMSTH 1118
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-212 |
9.33e-15 |
|
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: 70.69 E-value: 9.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGS----LKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKSVA-- 75
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 ------------FLSDGDFLDPKLTPLKaIAFYKDffsDFDESKALNLLKRFSVPLKREF--KALSKGMREKLQLILTLS 141
Cdd:cd03258 81 rrrigmifqhfnLLSSRTVFENVALPLE-IAGVPK---AEIEERVLELLELVGLEDKADAypAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488135840 142 RNASLYLFDEPVAGIDPIAREEIFEL---IASEFsqNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALlrdINREL--GLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
2-207 |
1.12e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 71.30 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYG-----SLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILN--------QKIGI 68
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 69 ETKKSVAFLSDgdFLDPKL---TPLKAIAF-YKDFFSDFDESKALNLLKRFSVPLKREFKA-----LSKGMREKLQLILT 139
Cdd:PRK13643 81 PVRKKVGVVFQ--FPESQLfeeTVLKDVAFgPQNFGIPKEKAEKIAAEKLEMVGLADEFWEkspfeLSGGQMRRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488135840 140 LSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFG 207
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-167 |
1.16e-14 |
|
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: 70.34 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI-GIETKK---SVAFLS 78
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDItNLPPHKrpvNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 79 DGDFldPKLTPLKAIAF---YKDFFSDFDESKALNLLK--RFSVPLKREFKALSKGMREKLQLILTLSRNASLYLFDEPV 153
Cdd:cd03300 81 YALF--PHLTVFENIAFglrLKKLPKAEIKERVAEALDlvQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170
....*....|....*
gi 488135840 154 AGIDPIAREEI-FEL 167
Cdd:cd03300 159 GALDLKLRKDMqLEL 173
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-157 |
1.74e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.89 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI--------LNQ-KIGIETKKS 73
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklayVDQsRDALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 74 V-AFLSDG-DFLDPKLTPLKAIAFYKDF-FSDFDESKALnllkrfsvplkrefKALSKGMREKLQLILTLSRNASLYLFD 150
Cdd:TIGR03719 403 VwEEISGGlDIIKLGKREIPSRAYVGRFnFKGSDQQKKV--------------GQLSGGERNRVHLAKTLKSGGNVLLLD 468
|
....*..
gi 488135840 151 EPVAGID 157
Cdd:TIGR03719 469 EPTNDLD 475
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-168 |
2.19e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 71.39 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGL--NLNYQGEV-----KILNQKIGIETKKSV 74
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIywsgsPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 75 AFLSDGDFLDPKLTPLKAIAF-----YKDFFSDFDES--KALNLLKRFSV---PLKREFKALSKGMREKLQLILTLSRNA 144
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLgneitLPGGRMAYNAMylRAKNLLRELQLdadNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180
....*....|....*....|....
gi 488135840 145 SLYLFDEPVAGIDPIAREEIFELI 168
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDII 184
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-212 |
2.98e-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: 70.99 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTY-----GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVK---------------- 60
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewvdmtkpgpd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 61 ----------ILNQKIGIETKKSV-AFLSDGDFLD-PK-LTPLKAIAFYKdfFSDFDESKALNLLKRFSvplkrefKALS 127
Cdd:TIGR03269 359 grgrakryigILHQEYDLYPHRTVlDNLTEAIGLElPDeLARMKAVITLK--MVGFDEEKAEEILDKYP-------DELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 128 KGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELI-ASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAF 206
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
....*.
gi 488135840 207 GDVGEL 212
Cdd:TIGR03269 510 GDPEEI 515
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-213 |
3.02e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 70.53 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAG--KTTLLKILAGLN--------LNYQGEVKILNQKIG----I 68
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDagrrpwrf*TWCANRRALRRTIG*hrpV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 69 ETKKSVAFLSDGDfldpkltpLKAIAFYKDFFSDFDESKALNLLKRFSV--PLKREFKALSKGMREKLQLILTL-SRNAS 145
Cdd:NF000106 94 R*GRRESFSGREN--------LYMIGR*LDLSRKDARARADELLERFSLteAAGRAAAKYSGGMRRRLDLAASMiGRPAV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488135840 146 LYLfDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGELK 213
Cdd:NF000106 166 LYL-DEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-183 |
3.19e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.10 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 4 EIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQkigietkkSVAFLSDGDFL 83
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ--------EMRFASTTAAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 84 D-------------PKLT----------PLKaiafykdfFSDFDESK----ALNLLKRFSV------PLKRefkaLSKGM 130
Cdd:PRK11288 78 AagvaiiyqelhlvPEMTvaenlylgqlPHK--------GGIVNRRLlnyeAREQLEHLGVdidpdtPLKY----LSIGQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488135840 131 REKLQLILTLSRNASLYLFDEPVAGIDpiARE--EIFELIASEFSQNASLLVSTH 183
Cdd:PRK11288 146 RQMVEIAKALARNARVIAFDEPTSSLS--AREieQLFRVIRELRAEGRVILYVSH 198
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-183 |
3.19e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 68.93 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTY-GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKSVAFL--SD 79
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 80 G----DF-LDPKLT-------PLKAIafYKDffSDFDESKALNLLKRFsvplkrefkalskGMREKL-QLILTLS----- 141
Cdd:COG2884 82 GvvfqDFrLLPDRTvyenvalPLRVT--GKS--RKEIRRRVREVLDLV-------------GLSDKAkALPHELSggeqq 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488135840 142 ---------RNASLYLFDEPVAGIDPIAREEIFELIAsEFSQN-ASLLVSTH 183
Cdd:COG2884 145 rvaiaralvNRPELLLADEPTGNLDPETSWEIMELLE-EINRRgTTVLIATH 195
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-212 |
3.38e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 69.65 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 12 YGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEV----KILN-QKIGI-ETKKSVAFLsdgdFLDP 85
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgKPLDySKRGLlALRQQVATV----FQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 86 KLTplkaiAFYKDFFSDF------------------DESKALNLLKRFSvplKREFKALSKGMREKLQLILTLSRNASLY 147
Cdd:PRK13638 87 EQQ-----IFYTDIDSDIafslrnlgvpeaeitrrvDEALTLVDAQHFR---HQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 148 LFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHlVVDVEKYLNSAIF-LKEAKVVAFGDVGEL 212
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSH-DIDLIYEISDAVYvLRQGQILTHGAPGEV 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-208 |
3.89e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 69.27 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQ----------KIGIET 70
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpsdKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 71 KKSVAFLSDGDFLDPKLT--------PLKAIAFYKdffsdfDESK--ALNLLKRfsvpLKREFKA------LSKGMREKL 134
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTvqqnlieaPCRVLGLSK------DQALarAEKLLER----LRLKPYAdrfplhLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488135840 135 QLILTLSRNASLYLFDEPVAGIDPIAREEIFELIaSEFSQNA-SLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGD 208
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVSII-RELAETGiTQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-184 |
4.21e-14 |
|
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: 70.47 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTY-GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI----LNQKIGIETKKSVAFL 77
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdgvpVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 SDgdflDPKL---TPLKAIAFYKDFFSDFDESKAL------NLLKR----FSVPLKREFKALSKGMREKLQLILTLSRNA 144
Cdd:TIGR02868 415 AQ----DAHLfdtTVRENLRLARPDATDEELWAALervglaDWLRAlpdgLDTVLGEGGARLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488135840 145 SLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHL 184
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-222 |
6.11e-14 |
|
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: 68.52 E-value: 6.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKaLDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVkILNQKiGIET----KKSVAFLS 78
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI-LLNGK-DITNlppeKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 79 DGDFLDPKLTPLKAIAF---YKDFFSDFDESKALNLLKRFSVP--LKREFKALSKGMREKLQLILTLSRNASLYLFDEPV 153
Cdd:cd03299 78 QNYALFPHMTVYKNIAYglkKRKVDKKEIERKVLEIAEMLGIDhlLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488135840 154 AGIDPIAREEIFELIA---SEFsqNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGELKKGYSSLEVA 222
Cdd:cd03299 158 SALDVRTKEKLREELKkirKEF--GVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVA 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
2-183 |
7.07e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.52 E-value: 7.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGietKKSVAFLSDGD 81
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR---RQRDEYHQDLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 82 FL------DPKLTPLKAIAFY---KDFFSDFDESKAL---NLLKRFSVPLKRefkaLSKGMREKLQLI-LTLSrNASLYL 148
Cdd:PRK13538 78 YLghqpgiKTELTALENLRFYqrlHGPGDDEALWEALaqvGLAGFEDVPVRQ----LSAGQQRRVALArLWLT-RAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*
gi 488135840 149 FDEPVAGIDPIAREEIFELIASEFSQNASLLVSTH 183
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-198 |
7.59e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 68.74 E-value: 7.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLK----ALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI-GIETKKSVA 75
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtGPGADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 FLSDGdfLDPKLTPLKAIAF---YKDFFSDFDESKALNLLKRfsVPL----KREFKALSKGMREKLQLILTLSRNASLYL 148
Cdd:COG4525 82 FQKDA--LLPWLNVLDNVAFglrLRGVPKAERRARAEELLAL--VGLadfaRRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488135840 149 FDEPVAGIDPIAREEIFELIASEFSQ-NASLLVSTHlvvDVEKylnsAIFL 198
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRtGKGVFLITH---SVEE----ALFL 201
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2-212 |
1.02e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.81 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGE-----VKILNQKIGIETKKSVAF 76
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdgLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 77 LSDGDF-LDPKLTPLKAIAF----YKDFFSDFDESKALNLLKRfsVPLKREF----KALSKGMREKLQLILTLSRNASLY 147
Cdd:PRK09493 81 MVFQQFyLFPHLTALENVMFgplrVRGASKEEAEKQARELLAK--VGLAERAhhypSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488135840 148 LFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-225 |
1.15e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.38 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI---GIETKKSVAFLSD 79
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdagDIATRRRVGYMSQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 80 GdfldpkltplkaiafykdfFSDFDE-SKALNLL---KRFSVP----------LKREFK----------ALSKGMREKLQ 135
Cdd:NF033858 347 A-------------------FSLYGElTVRQNLElhaRLFHLPaaeiaarvaeMLERFDladvadalpdSLPLGIRQRLS 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 136 L---------ILTLsrnaslylfDEPVAGIDPIAREEIFELIAsEFS--QNASLLVSTHlvvdvekylnsaiFLKEA--- 201
Cdd:NF033858 408 LavavihkpeLLIL---------DEPTSGVDPVARDMFWRLLI-ELSreDGVTIFISTH-------------FMNEAerc 464
|
250 260 270
....*....|....*....|....*....|....*...
gi 488135840 202 ---------KVVAFGDVGEL--KKGYSSLE---VAYKE 225
Cdd:NF033858 465 drislmhagRVLASDTPAALvaARGAATLEeafIAYLE 502
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-157 |
1.21e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.45 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKaLDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGL----NLNYQGEVKIL--NQKIGIETKKSVA 75
Cdd:PRK13409 340 LVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVlkpdEGEVDPELKISykPQYIKPDYDGTVE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 FLsdgdfldpkltpLKAIAfyKDFFSDFDESkalNLLKRFSVP--LKREFKALSKGMREKLQLILTLSRNASLYLFDEPV 153
Cdd:PRK13409 419 DL------------LRSIT--DDLGSSYYKS---EIIKPLQLErlLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
....
gi 488135840 154 AGID 157
Cdd:PRK13409 482 AHLD 485
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-189 |
1.28e-13 |
|
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: 66.68 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 16 KALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIG------IETKKSVAFLsdgdFLDPKLTp 89
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysrkglLERRQRVGLV----FQDPDDQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 90 lkaiAFYKDFFSDF-----------DE-----SKALNLLKrFSVPLKREFKALSKGMREKLQLILTLSRNASLYLFDEPV 153
Cdd:TIGR01166 81 ----LFAADVDQDVafgplnlglseAEverrvREALTAVG-ASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 488135840 154 AGIDPIAREEIFELIASEFSQNASLLVSTHlvvDVE 189
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVISTH---DVD 188
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-67 |
1.50e-13 |
|
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: 67.46 E-value: 1.50e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTY----GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIG 67
Cdd:COG4181 8 IIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF 77
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
2-212 |
1.74e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.91 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTY-GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGI----ETKKSVAF 76
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenirEVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 77 L---SDGDFLDPklTPLKAIAFYKDFFSdFDE-------SKALNLLKrFSVPLKREFKALSKGMREKLQLILTLSRNASL 146
Cdd:PRK13652 83 VfqnPDDQIFSP--TVEQDIAFGPINLG-LDEetvahrvSSALHMLG-LEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488135840 147 YLFDEPVAGIDPIAREEIFELIaSEFSQNASLLV--STHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFL-NDLPETYGMTVifSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-183 |
2.22e-13 |
|
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: 65.70 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 4 EIENLTKTYGSLKA--LDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIgietkKSVAFLSDGD 81
Cdd:cd03246 2 EVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI-----SQWDPNELGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 82 FL-----DPKLtplkaiafykdffsdFDESKALNLlkrfsvplkrefkaLSKGMREKLQLILTLSRNASLYLFDEPVAGI 156
Cdd:cd03246 77 HVgylpqDDEL---------------FSGSIAENI--------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180
....*....|....*....|....*..
gi 488135840 157 DPIAREEIFELIASEFSQNASLLVSTH 183
Cdd:cd03246 128 DVEGERALNQAIAALKAAGATRIVIAH 154
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-185 |
2.37e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.01 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 5 IENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNqkigietkksvAFLSDGD--- 81
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT-----------APLAEARedt 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 82 ---FLDPKLTPLKAI---------AFYKDffsdfdesKALNLLKrfSVPLKREFK----ALSKGMREKLQLILTLSRNAS 145
Cdd:PRK11247 84 rlmFQDARLLPWKKVidnvglglkGQWRD--------AALQALA--AVGLADRANewpaALSGGQKQRVALARALIHRPG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488135840 146 LYLFDEPVAGIDPIAREEIFELIASEFSQNA-SLLVSTHLV 185
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQHGfTVLLVTHDV 194
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-64 |
2.48e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.10 E-value: 2.48e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQ 64
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR 64
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-66 |
2.76e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 2.76e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGL--NLNYQGEVKILNQKI 66
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEEL 71
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-64 |
2.90e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 67.06 E-value: 2.90e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488135840 1 MLvEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQ 64
Cdd:COG4559 1 ML-EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR 63
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-157 |
3.36e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 67.89 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKaLDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGL----NLNYQGEVKIL--NQKIGIETKKSVA 75
Cdd:COG1245 341 LVEYPDLTKSYGGFS-LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVlkpdEGEVDEDLKISykPQYISPDYDGTVE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 flsdgDFLDPKLTPlkaiafykdffsDFDESKALN-LLKRFSVP--LKREFKALSKGMREKLQLILTLSRNASLYLFDEP 152
Cdd:COG1245 420 -----EFLRSANTD------------DFGSSYYKTeIIKPLGLEklLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
....*
gi 488135840 153 VAGID 157
Cdd:COG1245 483 SAHLD 487
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-183 |
4.61e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.34 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLN-----LNYQGEVKILNQKI------GIET 70
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlipgFRVEGKVTFHGKNLyapdvdPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 71 KKSVAFLsdgdFLDPKLTP---LKAIAF------YKdffSDFDE--SKALN---LLKRFSVPLKREFKALSKGMREKLQL 136
Cdd:PRK14243 90 RRRIGMV----FQKPNPFPksiYDNIAYgaringYK---GDMDElvERSLRqaaLWDEVKDKLKQSGLSLSGGQQQRLCI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488135840 137 ILTLSRNASLYLFDEPVAGIDPIAREEIFELIaSEFSQNASLLVSTH 183
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELM-HELKEQYTIIIVTH 208
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-218 |
5.68e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.21 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLN-----LNYQGEVKILNQKIgIETKKSVAFL 77
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNeleseVRVEGRVEFFNQNI-YERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 S---DGDFLDPKLTPL----------KAIAFY-KDFFSDFDES--KALNLLKRFSVPLKREFKALSKGMREKLQLILTLS 141
Cdd:PRK14258 87 RrqvSMVHPKPNLFPMsvydnvaygvKIVGWRpKLEIDDIVESalKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 142 RNASLYLFDEPVAGIDPIAREEIFELIAS-EFSQNASLLVSTHLVVDVEKYLNSAIFLK--EAKVVAFGDVGELKKGYSS 218
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSlRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnENRIGQLVEFGLTKKIFNS 246
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-207 |
5.72e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 66.31 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGS-----LKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETK---- 71
Cdd:PRK13649 1 MGINLQNVSYTYQAgtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 72 ----KSVAFLSDgdFLDPKL---TPLKAIAF-YKDFFSDFDESKALNLLKRFSVPLKREFKA-----LSKGMREKLQLIL 138
Cdd:PRK13649 81 kqirKKVGLVFQ--FPESQLfeeTVLKDVAFgPQNFGVSQEEAEALAREKLALVGISESLFEknpfeLSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488135840 139 TLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFG 207
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-183 |
7.29e-13 |
|
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: 65.24 E-value: 7.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETK------KSVAF 76
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKninelrQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 77 LSDGDFLDPKLTPLKAI--AFYKDFFSDFDES--KALNLLKRFSVPLKREFKA--LSKGMREKLQLILTLSRNASLYLFD 150
Cdd:cd03262 81 VFQQFNLFPHLTVLENItlAPIKVKGMSKAEAeeRALELLEKVGLADKADAYPaqLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190
....*....|....*....|....*....|...
gi 488135840 151 EPVAGIDPIAREEIFELIASEFSQNASLLVSTH 183
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-212 |
7.30e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.13 E-value: 7.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKIL--------------NQKIGI 68
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIyhvalcekcgyverPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 69 ETKKSVAFLS--DGDFLDP------KLTPLKAIAFYKDFFSDFDES---------------------KALNLLKRFSVP- 118
Cdd:TIGR03269 81 PCPVCGGTLEpeEVDFWNLsdklrrRIRKRIAIMLQRTFALYGDDTvldnvlealeeigyegkeavgRAVDLIEMVQLSh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 119 ----LKREfkaLSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFE-LIASEFSQNASLLVSTHLVVDVEKYLN 193
Cdd:TIGR03269 161 rithIARD---LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250
....*....|....*....
gi 488135840 194 SAIFLKEAKVVAFGDVGEL 212
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEV 256
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-212 |
7.93e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 66.02 E-value: 7.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGS-LKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIG------IETKKSV 74
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkglMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 75 AFLsdgdFLDPKlTPLKAIAFYKDFF---------SDFDESKALNLLKRFSV-PLK-REFKALSKGMREKLQLILTLSRN 143
Cdd:PRK13636 85 GMV----FQDPD-NQLFSASVYQDVSfgavnlklpEDEVRKRVDNALKRTGIeHLKdKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 144 ASLYLFDEPVAGIDPIAREEIFELIASEFSQ-NASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-203 |
1.53e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.03 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGL---NLNYQGEVKILNQ------KIGIETKK 72
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRtvqregRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 73 SVA---FLSDGDFLDPKLTPLKAI--------AFYK---DFFSDFDESKALNLLKRFSVP--LKREFKALSKGMREKLQL 136
Cdd:PRK09984 84 SRAntgYIFQQFNLVNRLSVLENVligalgstPFWRtcfSWFTREQKQRALQALTRVGMVhfAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488135840 137 ILTLSRNASLYLFDEPVAGIDPIAREEIFELIaSEFSQN--ASLLVSTHLVVDVEKYLNSAIFLKEAKV 203
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTL-RDINQNdgITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-212 |
1.71e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.01 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 6 ENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKSVA----FLSDGD 81
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVArrigLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 82 FLDPKLTPLKAIAF----YKDFFSDF---DESKALNLLKRFSVP--LKREFKALSKGMREKLQLILTLSRNASLYLFDEP 152
Cdd:PRK10253 91 TTPGDITVQELVARgrypHQPLFTRWrkeDEEAVTKAMQATGIThlADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488135840 153 VAGIDPIAREEIFELIaSEFS--QNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:PRK10253 171 TTWLDISHQIDLLELL-SELNreKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-152 |
1.79e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.91 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVkilnqKIGiETKKsVAFLSDG-D 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-----KIG-ETVK-LAYVDQSrD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 82 FLDPKLTPLKAIafykdffsdfdeSKALNLLK--RFSVP----LKR-EFK---------ALSKGMREKLQLILTLSRNAS 145
Cdd:PRK11819 398 ALDPNKTVWEEI------------SGGLDIIKvgNREIPsrayVGRfNFKggdqqkkvgVLSGGERNRLHLAKTLKQGGN 465
|
....*..
gi 488135840 146 LYLFDEP 152
Cdd:PRK11819 466 VLLLDEP 472
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-66 |
3.73e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.58 E-value: 3.73e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI 66
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI 78
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
16-208 |
4.62e-12 |
|
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: 63.08 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 16 KALDNISLKLP---KQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI-------LNQKIGIET-KKSVAFLSDGDFLD 84
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdSRKKINLPPqQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 85 PKLTPLKAIAF-YKDFFSDFDESKALNLLKRFSVP--LKREFKALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAR 161
Cdd:cd03297 88 PHLNVRENLAFgLKRKRNREDRISVDELLDLLGLDhlLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488135840 162 EEI---FELIASEFSQnASLLVsTHLVVDVEkYLNSAIFLKEAKVVAFGD 208
Cdd:cd03297 168 LQLlpeLKQIKKNLNI-PVIFV-THDLSEAE-YLADRIVVMEDGRLQYIG 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-215 |
4.90e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.57 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLvEIENLTKTYGS-----LKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIgieTKKSV- 74
Cdd:COG1101 1 ML-ELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV---TKLPEy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 75 ---AFLSDgDFLDPK------LTPLK--AIAF---------------YKDFFSDFDESKALNLLKRfsvpLKREFKALSK 128
Cdd:COG1101 77 kraKYIGR-VFQDPMmgtapsMTIEEnlALAYrrgkrrglrrgltkkRRELFRELLATLGLGLENR----LDTKVGLLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 129 GMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFEL---IASEfsQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVA 205
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELtekIVEE--NNLTTLMVTHNMEQALDYGNRLIMMHEGRIIL 229
|
250
....*....|.
gi 488135840 206 fgDV-GELKKG 215
Cdd:COG1101 230 --DVsGEEKKK 238
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-212 |
5.80e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.58 E-value: 5.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 7 NLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLN-----LNYQGEV-----KILNQKIGIETKKSVAF 76
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVllggrSIFNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 77 LsdgdFLDPKLTPLKAIafykdffsdfdeSKALNLLKRFSVPLKREFKA-------------------------LSKGMR 131
Cdd:PRK14271 106 L----FQRPNPFPMSIM------------DNVLAGVRAHKLVPRKEFRGvaqarltevglwdavkdrlsdspfrLSGGQQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 132 EKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIASeFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGE 211
Cdd:PRK14271 170 QLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS-LADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQ 248
|
.
gi 488135840 212 L 212
Cdd:PRK14271 249 L 249
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-204 |
5.88e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 63.65 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYG-----SLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETK---- 71
Cdd:PRK13646 1 MTIRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 72 ----KSVAFLSDgdFLDPKL---TPLKAIAF-YKDFFSDFDESK--ALNLLKRFSVP---LKREFKALSKGMREKLQLIL 138
Cdd:PRK13646 81 rpvrKRIGMVFQ--FPESQLfedTVEREIIFgPKNFKMNLDEVKnyAHRLLMDLGFSrdvMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488135840 139 TLSRNASLYLFDEPVAGIDPIAREEIFELIAS-EFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVV 204
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlQTDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-158 |
6.27e-12 |
|
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: 62.67 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 14 SLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNY---QGEVKILNQKIGIET-KKSVAFLSDGDFLDPKLTP 89
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQfQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488135840 90 LKAIAFYKDF-----FSDF-----DESKALNLLKRFSVPLKReFKALSKGMREKLQLILTLSRNASLYLFDEPVAGIDP 158
Cdd:cd03234 99 RETLTYTAILrlprkSSDAirkkrVEDVLLRDLALTRIGGNL-VKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-183 |
6.59e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 6.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 22 SLKLPKQ-QFIGLLGPNGAGKTTLLKILAGL---NL-NYQGEV---KILNQKIGIETKKSVAFLSDGDfLDPKLTP--LK 91
Cdd:PRK13409 92 GLPIPKEgKVTGILGPNGIGKTTAVKILSGElipNLgDYEEEPswdEVLKRFRGTELQNYFKKLYNGE-IKVVHKPqyVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 92 AIAFY-----KDFFSDFDESKALN-LLKRFSVP--LKREFKALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREE 163
Cdd:PRK13409 171 LIPKVfkgkvRELLKKVDERGKLDeVVERLGLEniLDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLN 250
|
170 180
....*....|....*....|
gi 488135840 164 IFELIaSEFSQNASLLVSTH 183
Cdd:PRK13409 251 VARLI-RELAEGKYVLVVEH 269
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-183 |
7.62e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.92 E-value: 7.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI-----------LNQKIGIET 70
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIggnpcarltpaKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 71 KKSVAFLsdgdFldPKLTPLKAIAFYKDFFSDfDESKALNLLKRFSVPLKREFKA--LSKGMREKLQLILTLSRNASLYL 148
Cdd:PRK15439 91 VPQEPLL----F--PNLSVKENILFGLPKRQA-SMQKMKQLLAALGCQLDLDSSAgsLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190
....*....|....*....|....*....|....*
gi 488135840 149 FDEPVAGIDPIAREEIFELIASEFSQNASLLVSTH 183
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAQGVGIVFISH 198
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
2-168 |
8.97e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.59 E-value: 8.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI-GIET----KKSVAF 76
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItDWQTakimREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 77 LSDGDFLDPKLTPLKAIAFyKDFFSDFDE-----SKALNLLKRFSVPLKREFKALSKGMREKLQLILTLSRNASLYLFDE 151
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAM-GGFFAERDQfqeriKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170
....*....|....*..
gi 488135840 152 PVAGIDPIAREEIFELI 168
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTI 180
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-193 |
9.36e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.28 E-value: 9.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 18 LDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKSV--AFLSDGDFLDPKltplkaiaf 95
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLidAIGRKGDFKDAV--------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 96 ykdffsdfdesKALNLLKRFSVPL-KREFKALSKGMREKLQLILTLSRNASLYLFDEPVAGIDP-IAReeIFELIASEFS 173
Cdd:COG2401 117 -----------ELLNAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRqTAK--RVARNLQKLA 183
|
170 180
....*....|....*....|..
gi 488135840 174 QNA--SLLVSTHlVVDVEKYLN 193
Cdd:COG2401 184 RRAgiTLVVATH-HYDVIDDLQ 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-68 |
1.04e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 1.04e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488135840 7 NLTKTYGSLKA-LDNISLklpkqQF-----IGLLGPNGAGKTTLLKILAGLNLNYQGEVKIL-NQKIGI 68
Cdd:PRK11819 11 RVSKVVPPKKQiLKDISL-----SFfpgakIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKVGY 74
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-224 |
1.17e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 62.72 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 5 IENLTKTYG-----SLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI--GIETKKSVAFL 77
Cdd:PRK13645 9 LDNVSYTYAkktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 SDG-----DFLDPKL---TPLKAIAFYK-DFFSDFDES--KALNLLKRFSVP---LKREFKALSKGMREKLQLILTLSRN 143
Cdd:PRK13645 89 RKEiglvfQFPEYQLfqeTIEKDIAFGPvNLGENKQEAykKVPELLKLVQLPedyVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 144 ASLYLFDEPVAGIDPIAREE---IFELIASEfsQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGELkkgYSSLE 220
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDfinLFERLNKE--YKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI---FSNQE 243
|
....
gi 488135840 221 VAYK 224
Cdd:PRK13645 244 LLTK 247
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-212 |
1.17e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.46 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI----------LNQKIGI--ET 70
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarsLSQQKGLirQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 71 KKSVAFLSDGDFLDPKLTPLKAI----AFYKDFFSDFDESKALNLLKRFSVPLKREF--KALSKGMREKLQLILTLSRNA 144
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIiegpVIVKGEPKEEATARARELLAKVGLAGKETSypRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488135840 145 SLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-207 |
2.27e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.40 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGL-NLN----YQGEVKILNQKI------GIETK 71
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlELNeearVEGEVRLFGRNIyspdvdPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 72 KSVAFLSDGDFLDPKLTPLKAIAFYKDFFSDFDESKALNllKRFSVPLKR-----EFK--------ALSKGMREKLQLIL 138
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELD--ERVEWALKKaalwdEVKdrlndypsNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488135840 139 TLSRNASLYLFDEPVAGIDPIAREEIFELIAsEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFG 207
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLF-ELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
2-212 |
2.70e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 61.63 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTY-GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIG------IETKKSV 74
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkkslLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 75 AFL---SDGDFLDPklTPLKAIAFykdffsdfdesKALNL-------LKRFSVPLKR------EFKA---LSKGMREKLQ 135
Cdd:PRK13639 81 GIVfqnPDDQLFAP--TVEEDVAF-----------GPLNLglskeevEKRVKEALKAvgmegfENKPphhLSGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488135840 136 LILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-212 |
4.14e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQkigietkksvaflsDGD 81
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI--------------NYN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 82 FLDPKLTPLKAIAFYKDFFSDFDE-----------------------------SKALNLLKRfsVPLKREFKA----LSK 128
Cdd:PRK09700 71 KLDHKLAAQLGIGIIYQELSVIDEltvlenlyigrhltkkvcgvniidwremrVRAAMMLLR--VGLKVDLDEkvanLSI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 129 GMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGD 208
Cdd:PRK09700 149 SHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGM 228
|
....
gi 488135840 209 VGEL 212
Cdd:PRK09700 229 VSDV 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-61 |
4.24e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 61.66 E-value: 4.24e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI 61
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI 65
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-157 |
4.58e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 61.40 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI------------LNQKIG- 67
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagddvealsaraASRRVAs 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 68 IETKKSVAFLSDGDFL-----DPKLTPLkaiafykDFFSDFDESKALNLLKRFSVP--LKREFKALSKGMREKLQLILTL 140
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVvemgrTPHRSRF-------DTWTETDRAAVERAMERTGVAqfADRPVTSLSGGERQRVLLARAL 154
|
170
....*....|....*..
gi 488135840 141 SRNASLYLFDEPVAGID 157
Cdd:PRK09536 155 AQATPVLLLDEPTASLD 171
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-216 |
5.51e-11 |
|
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: 61.95 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYG--SLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGI---ETKKSVAF 76
Cdd:TIGR01257 1937 ILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTnisDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 77 LSDGDFLDPKLTPLKAIAFYKDFFSDFDES---------KALNLlkrfSVPLKREFKALSKGMREKLQLILTLSRNASLY 147
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYLYARLRGVPAEEiekvanwsiQSLGL----SLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488135840 148 LFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGELKKGY 216
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKF 2161
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-138 |
8.01e-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: 61.10 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 7 NLTKTYGSLKA-LDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI-LNQKIGietkksvaFLSDGDFLD 84
Cdd:TIGR03719 9 RVSKVVPPKKEiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKVG--------YLPQEPQLD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 488135840 85 PKLTPL----KAIAFYKDFFSDFDESKAlnllkRFSVPlKREFKALSKGMrEKLQLIL 138
Cdd:TIGR03719 81 PTKTVRenveEGVAEIKDALDRFNEISA-----KYAEP-DADFDKLAAEQ-AELQEII 131
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-212 |
9.03e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 59.93 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNY-----QGEVKILNQKIG----IETKKS 73
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFkmdvIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 74 VAFLSDGDFLDPKLTPLKAIAFYKDFFSDFDESKALNLLKRFSVP---LKREFK--------ALSKGMREKLQLILTLSR 142
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEkaqLWDEVKdrldapagKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 143 NASLYLFDEPVAGIDPIAREEIFELIAsEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFL-ELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
2-168 |
9.58e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.74 E-value: 9.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQ-KIGIETKKSvaflsdg 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlRIGYVPQKL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 81 dFLDPKLtPLKAIAFY--------KDFFSDFDESKALNLLKRfsvPLKRefkaLSKGMREKLQLILTLSRNASLYLFDEP 152
Cdd:PRK09544 77 -YLDTTL-PLTVNRFLrlrpgtkkEDILPALKRVQAGHLIDA---PMQK----LSGGETQRVLLARALLNRPQLLVLDEP 147
|
170
....*....|....*.
gi 488135840 153 VAGIDPIAREEIFELI 168
Cdd:PRK09544 148 TQGVDVNGQVALYDLI 163
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
35-183 |
1.09e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.09 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 35 GPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGI-ETKKSVAFLSDGDFLDPKLTPLKAIAFYKDFFSDFDE---SKALN 110
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKqmpGSALA 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488135840 111 L--LKRFSVPLKREfkaLSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTH 183
Cdd:PRK13543 124 IvgLAGYEDTLVRQ---LSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-192 |
1.28e-10 |
|
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: 58.96 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGS--LKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQ---KIGIET-KKSVAF 76
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdisTIPLEDlRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 77 LSDgdflDPKLTpLKAIAFYKDFFSDFDESKALNLLKrfsvpLKREFKALSKGMREKLQLILTLSRNASLYLFDEPVAGI 156
Cdd:cd03369 87 IPQ----DPTLF-SGTIRSNLDPFDEYSDEEIYGALR-----VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASI 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 488135840 157 DPIAREEIFELIASEFSqNASLLVSTH---LVVDVEKYL 192
Cdd:cd03369 157 DYATDALIQKTIREEFT-NSTILTIAHrlrTIIDYDKIL 194
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-212 |
1.41e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.29 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 18 LDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI----------LNQKIGIETKKSVAFLSDGDFLDPKL 87
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdgkvlyfgkdIFQIDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 88 T-------PLKA--IAFYKDFFSDFDES-KALNLLKRFSVPLKREFKALSKGMREKLQLILTLSRNASLYLFDEPVAGID 157
Cdd:PRK14246 106 SiydniayPLKShgIKEKREIKKIVEEClRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488135840 158 PIAREEIFELIaSEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:PRK14246 186 IVNSQAIEKLI-TELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-168 |
2.14e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.65 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTygslKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIET-----KKSVAF 76
Cdd:COG1129 256 VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSprdaiRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 77 LS-----DGDFLDpkltplKAIAfykdffsdfdESKALNLLKRFS----VPLKREfKALSKGMREKL--------QLILT 139
Cdd:COG1129 332 VPedrkgEGLVLD------LSIR----------ENITLASLDRLSrgglLDRRRE-RALAEEYIKRLriktpspeQPVGN 394
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488135840 140 LS--------------RNASLYLFDEPVAGIDPIAREEIFELI 168
Cdd:COG1129 395 LSggnqqkvvlakwlaTDPKVLILDEPTRGIDVGAKAEIYRLI 437
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-215 |
2.55e-10 |
|
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: 58.39 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLK-ALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKS----VAFL 77
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrsmIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 SDGDFLDPKlTPLKAIAFYKDFFSDFDESKAL----------NLLKRFSVPLKREFKALSKGMREKLQLILTLSRNASLY 147
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGRPNATDEEVIEAAkeagahdfimKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488135840 148 LFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHL--VVDVEKylnsAIFLKEAKVVAFGDVGEL--KKG 215
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLstIKNADK----ILVLDDGKIIEEGTHDELlaKKG 229
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-152 |
2.99e-10 |
|
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: 59.41 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 22 SLKLPKQ-QFIGLLGPNGAGKTTLLKILAGL---NL-NYQGEV---KILNQKIGIETKKSVAFLSDGD--------FLD- 84
Cdd:COG1245 92 GLPVPKKgKVTGILGPNGIGKSTALKILSGElkpNLgDYDEEPswdEVLKRFRGTELQDYFKKLANGEikvahkpqYVDl 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488135840 85 -PKLTPLKAiafyKDFFSDFDESKALN-LLKRFSVP--LKREFKALSKGMREKLQLILTLSRNASLYLFDEP 152
Cdd:COG1245 172 iPKVFKGTV----RELLEKVDERGKLDeLAEKLGLEniLDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-66 |
3.60e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 58.12 E-value: 3.60e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLN-----LNYQGEVKILNQKI 66
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgARVEGEILLDGEDI 80
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-61 |
5.67e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 58.64 E-value: 5.67e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488135840 3 VEIENLTKTY-GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLnlnY---QGEVKI 61
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF---YdptSGRILI 399
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-207 |
6.24e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.35 E-value: 6.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 29 QFIGLLGPNGAGKTTLLKILAGL--NLNYQGEVKILNQKIGIETKKSVAFLSDGDFLDPKLTPLKAIAF----------Y 96
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFcsllrlpkslT 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 97 KDFFSDFDES--KALNLLKRFSVPLKREF-KALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFS 173
Cdd:PLN03211 175 KQEKILVAESviSELGLTKCENTIIGNSFiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQ 254
|
170 180 190
....*....|....*....|....*....|....*
gi 488135840 174 QNASLLVSTHLVVD-VEKYLNSAIFLKEAKVVAFG 207
Cdd:PLN03211 255 KGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFG 289
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-189 |
6.60e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 57.43 E-value: 6.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGL-------------NLNYQGEVKILNQKIG 67
Cdd:COG4674 9 PILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKtrpdsgsvlfggtDLTGLDEHEIARLGIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 68 IETKKSVAFLSdgdfldpkLTPLK----AIAFYKDFFSDF-------DESKALNLLKRFSVPLKREFKA--LSKGMREKL 134
Cdd:COG4674 89 RKFQKPTVFEE--------LTVFEnlelALKGDRGVFASLfarltaeERDRIEEVLETIGLTDKADRLAglLSHGQKQWL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488135840 135 QLILTLSRNASLYLFDEPVAGIDPIAREEIFELIASefsqnaslLVSTHLVVDVE 189
Cdd:COG4674 161 EIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKS--------LAGKHSVVVVE 207
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-223 |
9.18e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.10 E-value: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 18 LDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVkILNQKIgIETKKSVAFLSDGDFLDPKLTP-------- 89
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQP-LESWSSKAFARKVAYLPQQLPAaegmtvre 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 90 LKAIAFY----------KDFFSDFDESKALNLLKRFSvplKREFKALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPI 159
Cdd:PRK10575 105 LVAIGRYpwhgalgrfgAADREKVEEAISLVGLKPLA---HRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 160 AREEIFELIaSEFSQNASLLVST--HLVVDVEKYLNSAIFLKEAKVVAFGDVGELKKGySSLEVAY 223
Cdd:PRK10575 182 HQVDVLALV-HRLSQERGLTVIAvlHDINMAARYCDYLVALRGGEMIAQGTPAELMRG-ETLEQIY 245
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-66 |
9.20e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.40 E-value: 9.20e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488135840 3 VEIENLTKTY----GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI 66
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL 69
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-161 |
9.81e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 57.35 E-value: 9.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIG-IE-TKKSVAFLSDG 80
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNdVPpAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 81 DFLDPKLTPLKAIAF----YKDFFSDFDE-----SKALNLLKRfsvpLKREFKALSKGMREKLQLILTLSRNASLYLFDE 151
Cdd:PRK11000 84 YALYPHLSVAENMSFglklAGAKKEEINQrvnqvAEVLQLAHL----LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170
....*....|
gi 488135840 152 PVAGIDPIAR 161
Cdd:PRK11000 160 PLSNLDAALR 169
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-208 |
1.17e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.17 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLT-----KTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKSVAF 76
Cdd:PRK13631 21 ILRVKNLYcvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 77 LSDG-----DFldPKLTPLKAIAF----YKdFFSDFDE---------------------SKALNLLKRFSVPLKREFKAL 126
Cdd:PRK13631 101 TNPYskkikNF--KELRRRVSMVFqfpeYQ-LFKDTIEkdimfgpvalgvkkseakklaKFYLNKMGLDDSYLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 127 SKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAF 206
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
..
gi 488135840 207 GD 208
Cdd:PRK13631 258 GT 259
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-216 |
1.52e-09 |
|
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: 55.61 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 4 EIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGlNLNY---QGEVKILNQKIgieTKKSVA----- 75
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKYevtEGEILFKGEDI---TDLPPEerarl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 --FLSdgdFLDPKLTPLKAIAfykDFFSDFDESkalnllkrfsvplkrefkaLSKGMREKLQLILTLSRNASLYLFDEPV 153
Cdd:cd03217 78 giFLA---FQYPPEIPGVKNA---DFLRYVNEG-------------------FSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488135840 154 AGIDPIAREEIFELIASEFSQNASLLVSTHLvvdvEKYLNSAI-----FLKEAKVVAFGD---VGEL-KKGY 216
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREEGKSVLIITHY----QRLLDYIKpdrvhVLYDGRIVKSGDkelALEIeKKGY 200
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-183 |
1.82e-09 |
|
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: 55.67 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTY--GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIG----IETKKSVAF 76
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqldpADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 77 LSDgdflDPKL---TPLKAIAFYKDFFSDFDESKALNLL----------KRFSVPLKREFKALSKGMREKLQLILTLSRN 143
Cdd:cd03245 83 VPQ----DVTLfygTLRDNITLGAPLADDERILRAAELAgvtdfvnkhpNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488135840 144 ASLYLFDEPVAGIDPIAREEIFELIASEFSQNAsLLVSTH 183
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKT-LIIITH 197
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-188 |
2.12e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.77 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLnlnYQ---GEVKILNQKIG----------- 67
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGF---YKptgGTILLRGQHIEglpghqiarmg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 68 -IETKKSVAFLSDGDFLDPKLTP-------------LKAIAFYKdffsdfDESKALNL----LKRfsVPLK----REFKA 125
Cdd:PRK11300 82 vVRTFQHVRLFREMTVIENLLVAqhqqlktglfsglLKTPAFRR------AESEALDRaatwLER--VGLLehanRQAGN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488135840 126 LSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIAS---EFsqNASLLVSTH---LVVDV 188
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAElrnEH--NVTVLLIEHdmkLVMGI 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-183 |
2.45e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.56 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGS----LKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQ---KIGIETK--- 71
Cdd:PRK10584 6 IVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhQMDEEARakl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 72 --KSVAFLSDGDFLDPKLTPLKAI---AFYKDFFSDFDESKALNLLKRFSVP--LKREFKALSKGMREKLQLILTLSRNA 144
Cdd:PRK10584 86 raKHVGFVFQSFMLIPTLNALENVelpALLRGESSRQSRNGAKALLEQLGLGkrLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488135840 145 SLYLFDEPVAGIDPIAREEIFELIaseFSQN----ASLLVSTH 183
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLL---FSLNrehgTTLILVTH 205
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-207 |
2.56e-09 |
|
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: 55.19 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTY--GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI------------LNQKIGI 68
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdgvdiskiglhdLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 69 ETKKSVAFlsDGDF---LDPkltplkaiafykdfFSDFDESKALNLLKRfsVPLKREFKALSKGMREKL----------- 134
Cdd:cd03244 83 IPQDPVLF--SGTIrsnLDP--------------FGEYSDEELWQALER--VGLKEFVESLPGGLDTVVeeggenlsvgq 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 135 -QLI-LT--LSRNASLYLFDEPVAGIDPIAREEIFELIASEFSqNASLLVSTH---LVVDVEKYLnsaiFLKEAKVVAFG 207
Cdd:cd03244 145 rQLLcLAraLLRKSKILVLDEATASVDPETDALIQKTIREAFK-DCTVLTIAHrldTIIDSDRIL----VLDKGRVVEFD 219
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-183 |
2.57e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.84 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 23 LKLPKQ-QFIGLLGPNGAGKTTLLKILAGL---NL-NYQGE---VKILNQKIGIETKKSVAFLSDGD--------FLD-- 84
Cdd:cd03236 20 LPVPREgQVLGLVGPNGIGKSTALKILAGKlkpNLgKFDDPpdwDEILDEFRGSELQNYFTKLLEGDvkvivkpqYVDli 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 85 PKLTPLKAIafykDFFSDFDESKALN-LLKRFSVP--LKREFKALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAR 161
Cdd:cd03236 100 PKAVKGKVG----ELLKKKDERGKLDeLVDQLELRhvLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180
....*....|....*....|..
gi 488135840 162 EEIFELIASEFSQNASLLVSTH 183
Cdd:cd03236 176 LNAARLIRELAEDDNYVLVVEH 197
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-183 |
2.62e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.59 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTY--GSLKA--LDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEV----------------KI 61
Cdd:PRK11629 5 LLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmsklssaakaEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 62 LNQKIGietkksvaFLSDGDFLDPKLTPLKAIA---FYKDFFSDFDESKALNLLKrfSVPLKREFK----ALSKGMREKL 134
Cdd:PRK11629 85 RNQKLG--------FIYQFHHLLPDFTALENVAmplLIGKKKPAEINSRALEMLA--AVGLEHRANhrpsELSGGERQRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488135840 135 QLILTLSRNASLYLFDEPVAGIDPIAREEIFELIAS-EFSQNASLLVSTH 183
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGElNRLQGTAFLVVTH 204
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-207 |
2.65e-09 |
|
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: 54.94 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 13 GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLN--YQGEVKILNQKIGIETKKSVAFLSDGDFLDPKLTPL 90
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDKNFQRSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 91 KAIafykdffsdfdeskalnllkRFSVPLkrefKALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIAS 170
Cdd:cd03232 98 EAL--------------------RFSALL----RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKK 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 488135840 171 EFSQNASLLVSTHL-VVDVEKYLNSAIFLKE-AKVVAFG 207
Cdd:cd03232 154 LADSGQAILCTIHQpSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-207 |
2.74e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.80 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 16 KALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETK--------KSVAFLSDgdFLDPKL 87
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnkklkplrKKVGIVFQ--FPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 88 ---TPLKAIAFYKDFF--SDFD-ESKALNLLKRFSVP---LKREFKALSKGMREKLQLILTLSRNASLYLFDEPVAGIDP 158
Cdd:PRK13634 99 feeTVEKDICFGPMNFgvSEEDaKQKAREMIELVGLPeelLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488135840 159 IAREEIFELIAS-EFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFG 207
Cdd:PRK13634 179 KGRKEMMEMFYKlHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-60 |
4.08e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 4.08e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 488135840 3 VEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVK 60
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
5-207 |
5.65e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.89 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 5 IENLTKTY-GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKS-VAFLSDGDF 82
Cdd:PRK15056 9 VNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNlVAYVPQSEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 83 LD---PKLTP-LKAIAFYKDF-----FSDFDESKALNLLKRFSVP--LKREFKALSKGMREKLQLILTLSRNASLYLFDE 151
Cdd:PRK15056 89 VDwsfPVLVEdVVMMGRYGHMgwlrrAKKRDRQIVTAALARVDMVefRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 152 PVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKeAKVVAFG 207
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASG 223
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-181 |
6.43e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 4 EIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAglnlnyqGEVKILNQKIGIETKKSVAFlsdgdF- 82
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLML-------GQLQADSGRIHCGTKLEVAY-----Fd 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 83 -----LDPKLTPLKAIAFYK-DFFSDFDESKALNLLKRFSVPLKREF---KALSKGMREKLQLILTLSRNASLYLFDEPV 153
Cdd:PRK11147 389 qhraeLDPEKTVMDNLAEGKqEVMVNGRPRHVLGYLQDFLFHPKRAMtpvKALSGGERNRLLLARLFLKPSNLLILDEPT 468
|
170 180
....*....|....*....|....*...
gi 488135840 154 AGIDPIAREEIFELIASefSQNASLLVS 181
Cdd:PRK11147 469 NDLDVETLELLEELLDS--YQGTVLLVS 494
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-184 |
9.13e-09 |
|
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: 53.20 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTygslKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIET-----KKSVAF 76
Cdd:cd03215 4 VLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSprdaiRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 77 LSDgdflDPKLTPLkaiafykdfFSDFdeSKALNL-LKRFsvplkrefkaLSKGMREKLQLILTLSRNASLYLFDEPVAG 155
Cdd:cd03215 80 VPE----DRKREGL---------VLDL--SVAENIaLSSL----------LSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190
....*....|....*....|....*....|
gi 488135840 156 IDPIAREEIFELIASEFSQNAS-LLVSTHL 184
Cdd:cd03215 135 VDVGAKAEIYRLIRELADAGKAvLLISSEL 164
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-72 |
1.54e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 1.54e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488135840 5 IENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKK 72
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSK 68
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-157 |
1.82e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 53.90 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 18 LDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLN---YQGEVKILNQKIGIETKKSV-AFLSDGDFLDPKLTPLKAI 93
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIsAYVQQDDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 94 AFYKDFFSDFDESK------------ALNLLK----RFSVPlkREFKALSKGMREKLQLILTLSRNASLYLFDEPVAGID 157
Cdd:TIGR00955 121 MFQAHLRMPRRVTKkekrervdevlqALGLRKcantRIGVP--GRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2-183 |
2.92e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQ-KIGIETKKSVAFL-SD 79
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGiKLGYFAQHQLEFLrAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 80 GDFLD--PKLTPLKAIAFYKDFFSD--FDESKALNLLKRFsvplkrefkalSKGMREKLQLILTLSRNASLYLFDEPVAG 155
Cdd:PRK10636 392 ESPLQhlARLAPQELEQKLRDYLGGfgFQGDKVTEETRRF-----------SGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
170 180
....*....|....*....|....*....
gi 488135840 156 IDPIAREEIFE-LIASEfsqnASLLVSTH 183
Cdd:PRK10636 461 LDLDMRQALTEaLIDFE----GALVVVSH 485
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2-50 |
3.82e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.87 E-value: 3.82e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAG 50
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-218 |
4.07e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 51.89 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLvEIENLTKTYGSLKALDNISLKLPKQqfIGLLGPNGAGKTTLLKILAGLNLNYQGEVkILNQKIGIET---KKSVAFL 77
Cdd:PRK10771 1 ML-KLTDITWLYHHLPMRFDLTVERGER--VAILGPSGAGKSTLLNLIAGFLTPASGSL-TLNGQDHTTTppsRRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 SDGDFLDPKLT----------P-LKAIAFYKDFFSDFDESKAL-NLLKRFSvplkrefKALSKGMREKLQLILTLSRNAS 145
Cdd:PRK10771 77 FQENNLFSHLTvaqniglglnPgLKLNAAQREKLHAIARQMGIeDLLARLP-------GQLSGGQRQRVALARCLVREQP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 146 LYLFDEPVAGIDPIAREEIFEL---IASEfsQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGELKKGYSS 218
Cdd:PRK10771 150 ILLLDEPFSALDPALRQEMLTLvsqVCQE--RQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKAS 223
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-228 |
5.05e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 17 ALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKIlnqkigietKKSVAFLSDGDFLDPKLTPLKAIAFy 96
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI---------KGSAALIAISSGLNGQLTGIENIEL- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 97 KDFFSDFDESKALNLlkrfsVPLKREF-----------KALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIF 165
Cdd:PRK13545 109 KGLMMGLTKEKIKEI-----IPEIIEFadigkfiyqpvKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488135840 166 ELIaSEFSQNA-SLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDV-------GELKKGYSSLEVAYKERLK 228
Cdd:PRK13545 184 DKM-NEFKEQGkTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIkevvdhyDEFLKKYNQMSVEERKDFR 253
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-228 |
5.96e-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: 52.61 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 5 IENLTKTY--GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLnLNYQGEVKI------------LNQKIGIET 70
Cdd:TIGR01271 1220 VQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIdgvswnsvtlqtWRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 71 KKsvAFLSDGDF---LDPKltplkaiAFYKD--FFSDFDESKALNLLKRFsvPLKREFK------ALSKGMREKLQLILT 139
Cdd:TIGR01271 1299 QK--VFIFSGTFrknLDPY-------EQWSDeeIWKVAEEVGLKSVIEQF--PDKLDFVlvdggyVLSNGHKQLMCLARS 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 140 LSRNASLYLFDEPVAGIDPIAREEIFELIASEFSqNASLLVSTHlvvDVEKYLNSAIFL--KEAKVVAFGDVGELKKGYS 217
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFS-NCTVILSEH---RVEALLECQQFLviEGSSVKQYDSIQKLLNETS 1443
|
250
....*....|...
gi 488135840 218 SLEVAYK--ERLK 228
Cdd:TIGR01271 1444 LFKQAMSaaDRLK 1456
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-59 |
6.26e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 52.11 E-value: 6.26e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488135840 3 VEIENLTKTY----GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEV 59
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV 62
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-68 |
6.66e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 6.66e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGL------NLNYQGEVKILN-----QKIGI 68
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIytrdagSILYLGKEVTFNgpkssQEAGI 81
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-183 |
7.00e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 52.13 E-value: 7.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTY--GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKIlagLNLNY---QGEVKILNQKIgietkksvaf 76
Cdd:PRK11160 338 SLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQL---LTRAWdpqQGEILLNGQPI---------- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 77 lsdGDFLDPKLTplKAIAFYK---DFFSDF-------------DE-----------SKALNLLKRFSVPLKREFKALSKG 129
Cdd:PRK11160 405 ---ADYSEAALR--QAISVVSqrvHLFSATlrdnlllaapnasDEalievlqqvglEKLLEDDKGLNAWLGEGGRQLSGG 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488135840 130 MREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIAsEFSQNASLLVSTH 183
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLA-EHAQNKTVLMITH 532
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-65 |
7.40e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 51.38 E-value: 7.40e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 488135840 18 LDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLnLNYQGEVkILNQK 65
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEI-LLNGR 57
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-168 |
9.38e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.29 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 17 ALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKSVAFLSDGDFLDPKLTPLKAIAFY 96
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 97 KDFFSdfdeskalnlLKRFSVPLKR--------------------EFKALSKGMREKLQLILTLSRNASLYLFDEPVAGI 156
Cdd:PRK13648 104 DVAFG----------LENHAVPYDEmhrrvsealkqvdmleradyEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170
....*....|..
gi 488135840 157 DPIAREEIFELI 168
Cdd:PRK13648 174 DPDARQNLLDLV 185
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-61 |
9.40e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.77 E-value: 9.40e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTY-GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI 61
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWI 63
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2-50 |
9.58e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.08 E-value: 9.58e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAG 50
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA 54
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-214 |
1.03e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 51.77 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 18 LDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGlNLNYQGEVKIlNqkiGIETK--------KSVAF------------- 76
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKI-N---GIELReldpeswrKHLSWvgqnpqlphgtlr 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 77 ----LSDGDFLDPKLTPLKAIAFYKDFFSDfdeskalnLLKRFSVPLKREFKALSKGMREKLQLILTLSRNASLYLFDEP 152
Cdd:PRK11174 441 dnvlLGNPDASDEQLQQALENAWVSEFLPL--------LPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488135840 153 VAGIDPIAREEIFELIASEFSQNASLLVsTHLVVDVEKYlNSAIFLKEAKVVAFGDVGELKK 214
Cdd:PRK11174 513 TASLDAHSEQLVMQALNAASRRQTTLMV-THQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQ 572
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-168 |
1.86e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.48 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTY---GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIET----KKSV 74
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 75 AFL---SDGDFLDPKLTPLKAIAF------YKDFFSDFDES-KALNLLKRFSvplkREFKALSKGMREKLQLILTLSRNA 144
Cdd:PRK13642 84 GMVfqnPDNQFVGATVEDDVAFGMenqgipREEMIKRVDEAlLAVNMLDFKT----REPARLSGGQKQRVAVAGIIALRP 159
|
170 180
....*....|....*....|....
gi 488135840 145 SLYLFDEPVAGIDPIAREEIFELI 168
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVI 183
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-48 |
1.90e-07 |
|
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: 49.92 E-value: 1.90e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 488135840 3 VEIENLTKTYGS--LKALDNISLKLPKQQFIGLLGPNGAGKTTLLKIL 48
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI 48
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-183 |
2.03e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.03 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGlNLNYQ---GEVKILNQKIGIETKKSVA--- 75
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAYKileGDILFKGESILDLEPEERAhlg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 -FL-----------SDGDFL------------DPKLTPLKaiafykdFFSDFDESkaLNLLKRFSVPLKRE----FKALS 127
Cdd:CHL00131 86 iFLafqypieipgvSNADFLrlaynskrkfqgLPELDPLE-------FLEIINEK--LKLVGMDPSFLSRNvnegFSGGE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 128 KGMREKLQLILTlsrNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTH 183
Cdd:CHL00131 157 KKRNEILQMALL---DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-61 |
2.89e-07 |
|
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: 50.10 E-value: 2.89e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488135840 1 MLVEIeNLTKTYGSLkALDnISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI 61
Cdd:COG4148 1 MMLEV-DFRLRRGGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRL 58
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-228 |
2.91e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 49.85 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTY--GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLnLNYQGEVKI------------LNQKIGI 68
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIdgvswnsvplqkWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 69 ETKKsvAFLSDGDF---LDPKltplkaiAFYKD--FFSDFDESKALNLLKRFsvPLKREFK------ALSKGMREKLQLI 137
Cdd:cd03289 82 IPQK--VFIFSGTFrknLDPY-------GKWSDeeIWKVAEEVGLKSVIEQF--PGQLDFVlvdggcVLSHGHKQLMCLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 138 LTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSqNASLLVSTHlvvDVEKYLNSAIFL--KEAKVVAFGDVGELKKG 215
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA-DCTVILSEH---RIEAMLECQRFLviEENKVRQYDSIQKLLNE 226
|
250
....*....|....*
gi 488135840 216 YSSLE--VAYKERLK 228
Cdd:cd03289 227 KSHFKqaISPSDRLK 241
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-183 |
3.31e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 49.33 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGI----ETKKSVAF 76
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlkpeIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 77 LsdgdFLDPKL---TPLKAIAF-YKDFFSDFDESKALNLLKRFSVP---LKREFKALSKGMREKLQLILTLSRNASLYLF 149
Cdd:PRK10247 86 C----AQTPTLfgdTVYDNLIFpWQIRNQQPDPAIFLDDLERFALPdtiLTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 488135840 150 DEPVAGIDPIAREEIFELI---ASEfsQNASLLVSTH 183
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIhryVRE--QNIAVLWVTH 196
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-184 |
4.37e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.66 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 20 NISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKI-----GIETKKSVAFLSD-----GDFLDPKLTP 89
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInalstAQRLARGLVYLPEdrqssGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 90 LKAIAFYKD--FFSDFDESKALnlLKRFSVPLKREF-------KALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIA 160
Cdd:PRK15439 361 NVCALTHNRrgFWIKPARENAV--LERYRRALNIKFnhaeqaaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180
....*....|....*....|....*
gi 488135840 161 REEIFELIASEFSQN-ASLLVSTHL 184
Cdd:PRK15439 439 RNDIYQLIRSIAAQNvAVLFISSDL 463
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-213 |
5.12e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.91 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 18 LDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQkigIETKKSVAFLSDGDFLDPKLTPLKAIAF-Y 96
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR---ISFSPQTSWIMPGTIKDNIIFGLSYDEYrY 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 97 KDFFSDFDESKALNLL-KRFSVPLKREFKALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQN 175
Cdd:TIGR01271 519 TSVIKACQLEEDIALFpEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSN 598
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488135840 176 ASLLVST----HLvvdveKYLNSAIFLKEAKVVAFGDVGELK 213
Cdd:TIGR01271 599 KTRILVTskleHL-----KKADKILLLHEGVCYFYGTFSELQ 635
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
33-207 |
5.24e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.78 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 33 LLGPNGAGKTTLLKILAGLnLNYQGEV----KILNQKIGIETKKSVAFLSDGD----------FLDPKLTPLKAIAFYKD 98
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGL-LPGSGSIqfagQPLEAWSAAELARHRAYLSQQQtppfampvfqYLTLHQPDKTRTEAVAS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 99 FFSDFDEskALNLLKRfsvpLKREFKALSKGMREK-------LQLILTLSRNASLYLFDEPVAGIDpIAREEIFELIASE 171
Cdd:PRK03695 106 ALNEVAE--ALGLDDK----LGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSLD-VAQQAALDRLLSE 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 488135840 172 F-SQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFG 207
Cdd:PRK03695 179 LcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASG 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-168 |
7.53e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 48.47 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTY--GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIET----KKSVA 75
Cdd:PRK13635 5 IIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwdvRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 FL---SDGDFLDPklTPLKAIAF--------YKDFFSDFDEskALNLLkRFSVPLKREFKALSKGMREKLQLILTLSRNA 144
Cdd:PRK13635 85 MVfqnPDNQFVGA--TVQDDVAFglenigvpREEMVERVDQ--ALRQV-GMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180
....*....|....*....|....
gi 488135840 145 SLYLFDEPVAGIDPIAREEIFELI 168
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETV 183
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
6-157 |
8.37e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.57 E-value: 8.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 6 ENLTKTYGSLKALDNISlKLPKQQFIGLLGPNGAGKTTLLKILAGLnlnyqgevkilnqkigietkksvaflsdgdfLDP 85
Cdd:cd03222 4 PDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQ-------------------------------LIP 51
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488135840 86 KltplkaiafykdffSDFDEskalnlLKRFSVPLKREFKALSKGMREKLQLILTLSRNASLYLFDEPVAGID 157
Cdd:cd03222 52 N--------------GDNDE------WDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-212 |
9.50e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.43 E-value: 9.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 5 IENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKK----SVAFLSDG 80
Cdd:PRK10619 8 VIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlKVADKNQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 81 DFLDPKLT---------------------PLKAIAFYKdffSDFDEsKALNLLKRFSVPLKREFK---ALSKGMREKLQL 136
Cdd:PRK10619 88 RLLRTRLTmvfqhfnlwshmtvlenvmeaPIQVLGLSK---QEARE-RAVKYLAKVGIDERAQGKypvHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 137 ILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-183 |
1.13e-06 |
|
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: 47.46 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGS-----LKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAglnlnyqGEVKILNQKigIETKKSVAFL 77
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL-------GELEKLSGS--VSVPGSIAYV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 SD---------------GDFLDPKL--TPLKAIAFYKDF--FSDFDES----KALNllkrfsvplkrefkaLSKGMREKL 134
Cdd:cd03250 72 SQepwiqngtirenilfGKPFDEERyeKVIKACALEPDLeiLPDGDLTeigeKGIN---------------LSGGQKQRI 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488135840 135 QLILTLSRNASLYLFDEPVAGIDPIAREEIFE-LIASEFSQNASLLVSTH 183
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTH 186
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
3-228 |
1.63e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.50 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTY--------------------GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEvkil 62
Cdd:PRK13546 5 VNIKNVTKEYriyrtnkermkdalipkhknKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 63 nqkigIETKKSVAFLSDGDFLDPKLTPLKAIAFyKDFFSDFDESKALNLLKR---FSVP---LKREFKALSKGMREKLQL 136
Cdd:PRK13546 81 -----VDRNGEVSVIAISAGLSGQLTGIENIEF-KMLCMGFKRKEIKAMTPKiieFSELgefIYQPVKKYSSGMRAKLGF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 137 ILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGELKKGY 216
Cdd:PRK13546 155 SINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY 234
|
250
....*....|..
gi 488135840 217 SSLEVAYKERLK 228
Cdd:PRK13546 235 EAFLNDFKKKSK 246
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-168 |
1.85e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.48 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 1 MLVEIENLTKTY---------GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKigietk 71
Cdd:PRK15112 3 TLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 72 ksvafLSDGD-----------FLDP--KLTPLKAIAFYKDF-------FSDFDESKALNLLKRfSVPLKREF-----KAL 126
Cdd:PRK15112 77 -----LHFGDysyrsqrirmiFQDPstSLNPRQRISQILDFplrlntdLEPEQREKQIIETLR-QVGLLPDHasyypHML 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488135840 127 SKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELI 168
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLM 192
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-183 |
2.14e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.80 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTY----GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKSVAFL 77
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 78 SDGDF--------LDPKLTPLKAI---AFYKDFFSDFDESKALNLLKRFSVPLKREFK--ALSKGMREKLQLILTLSRNA 144
Cdd:PRK10535 84 RREHFgfifqryhLLSHLTAAQNVevpAVYAGLERKQRLLRAQELLQRLGLEDRVEYQpsQLSGGQQQRVSIARALMNGG 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 488135840 145 SLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTH 183
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-66 |
3.62e-06 |
|
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: 46.99 E-value: 3.62e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 2 LVEIENLT-----------KTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLnLNYQGEVKILNQKI 66
Cdd:COG4172 275 LLEARDLKvwfpikrglfrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDL 349
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-168 |
3.75e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 46.62 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 17 ALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKIL-------------------------NQKIGIETK 71
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDgldtsdeenlwdirnkagmvfqnpdNQIVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 72 KSVAFLSDGDFLDPkltplkaiafyKDFFSDFDES-KALNL--LKRFSVPLkrefkaLSKGMREKLQLILTLSRNASLYL 148
Cdd:PRK13633 105 EDVAFGPENLGIPP-----------EEIRERVDESlKKVGMyeYRRHAPHL------LSGGQKQRVAIAGILAMRPECII 167
|
170 180
....*....|....*....|
gi 488135840 149 FDEPVAGIDPIAREEIFELI 168
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTI 187
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
2-183 |
4.17e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 46.52 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTY-GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILnqkiGIETkksvaflsdG 80
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVS----GIDT---------G 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 81 DFLD-PKLTPLKAIAFYK---DFFSDFDESK-----------ALNLLKRFSVPLK---------REFKALSKGMREKLQL 136
Cdd:PRK13644 68 DFSKlQGIRKLVGIVFQNpetQFVGRTVEEDlafgpenlclpPIEIRKRVDRALAeiglekyrhRSPKTLSGGQGQCVAL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488135840 137 ILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTH 183
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITH 194
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
8-212 |
5.76e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 46.57 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 8 LTKTYGSLKALDnISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEV--------KILNQKIGIETKKSVAFLSD 79
Cdd:PRK10070 35 LEKTGLSLGVKD-ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiaKISDAELREVRRKKIAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 80 GDFLDPKLTPLKAIAFYKDFF---SDFDESKALNLLKRFSVPLKREF--KALSKGMREKLQLILTLSRNASLYLFDEPVA 154
Cdd:PRK10070 114 SFALMPHMTVLDNTAFGMELAginAEERREKALDALRQVGLENYAHSypDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488135840 155 GIDPIAREEIF-ELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:PRK10070 194 ALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-212 |
6.17e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 45.83 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 7 NLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIG-IETKKSVAFLSDGD--FL 83
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAkLNRAQRKAFRRDIQmvFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 84 D------PKLTPLKAIAFYKDFFSDFDES----KALNLLKRFSVP---LKREFKALSKGMREKLQLILTLSRNASLYLFD 150
Cdd:PRK10419 97 DsisavnPRKTVREIIREPLRHLLSLDKAerlaRASEMLRAVDLDdsvLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488135840 151 EPVAGIDPIAREEIFELIAS--EFSQNASLLVsTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKlqQQFGTACLFI-THDLRLVERFCQRVMVMDNGQIVETQPVGDK 239
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
18-184 |
9.47e-06 |
|
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: 44.27 E-value: 9.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 18 LDNISLKLPKQQFIGLLGPNGAGKTTLLK-ILAGLNLNYQGEVKILNQKIGIETKKSVAFLsdgdfldpkltplkaiafy 96
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDaIGLALGGAQSATRRRSGVKAGCIVAAVSAEL------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 97 kdffsdfdeskalnllkRFSVPlkrefkALSKGMREKLQLILTLS----RNASLYLFDEPVAGIDPIAREEIFELIASEF 172
Cdd:cd03227 72 -----------------IFTRL------QLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHL 128
|
170
....*....|..
gi 488135840 173 SQNASLLVSTHL 184
Cdd:cd03227 129 VKGAQVIVITHL 140
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-157 |
9.51e-06 |
|
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: 44.95 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 10 KTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGL---NLNYQGEVK---ILNQKIGIETKKSVAFLSDGDFL 83
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHyngIPYKEFAEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 84 DPKLTPLKAIafykdffsdfdeskalnllkRFSVPLK--REFKALSKGMREKLQLILTLSRNASLYLFDEPVAGID 157
Cdd:cd03233 95 FPTLTVRETL--------------------DFALRCKgnEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-165 |
1.44e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 45.35 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLK-ALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKSV-----AF 76
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYrklfsAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 77 LSDGDFLDPKLTPLKAIAfykdffsdfDESKALNLLKRFSVPLKREFK-------ALSKGMREKLQLILTLSRNASLYLF 149
Cdd:PRK10522 403 FTDFHLFDQLLGPEGKPA---------NPALVEKWLERLKMAHKLELEdgrisnlKLSKGQKKRLALLLALAEERDILLL 473
|
170
....*....|....*.
gi 488135840 150 DEPVAGIDPIAREEIF 165
Cdd:PRK10522 474 DEWAADQDPHFRREFY 489
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-212 |
1.47e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 44.77 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLN-LNYQ----GEVKILNQKI------GIET 70
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdLNPEvtitGSIVYNGHNIysprtdTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 71 KKSVAFLsdgdFLDPKLTPLKA---------IAFYKDfFSDFDES-----KALNLLKRFSVPLKREFKALSKGMREKLQL 136
Cdd:PRK14239 85 RKEIGMV----FQQPNPFPMSIyenvvyglrLKGIKD-KQVLDEAvekslKGASIWDEVKDRLHDSALGLSGGQQQRVCI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 137 ILTLSRNASLYLFDEPVAGIDPIAREEIFELIAsEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFGDVGEL 212
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLL-GLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
35-184 |
1.50e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.09 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 35 GPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIETKKSVAFLSDGDFLDPKLTPLKAIAFYKDFFSDFDESKALNLLKR 114
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIHYFK 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 115 FSVPLKREFKALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHL 184
Cdd:PRK13541 113 LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHL 182
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-61 |
1.58e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 45.09 E-value: 1.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLK-ALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI 61
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL 400
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-184 |
1.64e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 4 EIENLTKTygSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIET-----KKSVAFLS 78
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 79 D-----GDFLDPKLTPLKAIA-FYKD--------FFSDFDESK----ALNLLKRFSVPLKREFKALSKGMREKLQLILTL 140
Cdd:PRK09700 345 EsrrdnGFFPNFSIAQNMAISrSLKDggykgamgLFHEVDEQRtaenQRELLALKCHSVNQNITELSGGNQQKVLISKWL 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488135840 141 SRNASLYLFDEPVAGIDPIAREEIFELIASEFSQN-ASLLVSTHL 184
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGkVILMVSSEL 469
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-183 |
2.33e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLN-LNYQGEVKILNQKIGI-ET----KKSVA 75
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpQGYSNDLTLFGRRRGSgETiwdiKKHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 76 FLSDGDFLDPKLTP----------LKAIAFYKDfFSDFDESKA---LNLLKRFSVPLKREFKALSKGmREKLQLIL-TLS 141
Cdd:PRK10938 340 YVSSSLHLDYRVSTsvrnvilsgfFDSIGIYQA-VSDRQQKLAqqwLDILGIDKRTADAPFHSLSWG-QQRLALIVrALV 417
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488135840 142 RNASLYLFDEPVAGIDPIAREEIFELIASEFSQNAS--LLVSTH 183
Cdd:PRK10938 418 KHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqlLFVSHH 461
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-166 |
2.84e-05 |
|
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: 44.08 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 18 LDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKilnqkigieTKKSVAFLSDGDFLDPKLTPLKAIafyk 97
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK---------HSGRISFSSQFSWIMPGTIKENII---- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 98 dFFSDFDESKALNLLK-------------RFSVPLKREFKALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEI 164
Cdd:cd03291 120 -FGVSYDEYRYKSVVKacqleeditkfpeKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
..
gi 488135840 165 FE 166
Cdd:cd03291 199 FE 200
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
126-183 |
4.58e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 43.53 E-value: 4.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488135840 126 LSKGMREKLQLILTLSRNA---SLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTH 183
Cdd:pfam13304 237 LSDGTKRLLALLAALLSALpkgGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
2-184 |
4.98e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.25 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTY----GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAG--------------------LNLNYQG 57
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdnwrvtadrmrfddidlLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 58 EVKILNQKIgietkkSVAFLSDGDFLDPK----LTPLKAIA-------FYKDFfsDFDESKALNLLKRFSVP----LKRE 122
Cdd:PRK15093 83 RRKLVGHNV------SMIFQEPQSCLDPServgRQLMQNIPgwtykgrWWQRF--GWRKRRAIELLHRVGIKdhkdAMRS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 123 FK-ALSKGMREKLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIASeFSQNAS---LLVSTHL 184
Cdd:PRK15093 155 FPyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTR-LNQNNNttiLLISHDL 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-203 |
6.84e-05 |
|
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: 42.46 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLKA---LDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEV------------KILNQKI 66
Cdd:cd03248 11 IVKFQNVTFAYPTRPDtlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldgkpisqyehKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 67 GIETKKSVAF---LSD------GDFLDPKLTPLKAIAFYKDFFSDFDeskalnllKRFSVPLKREFKALSKGMREKLQLI 137
Cdd:cd03248 91 SLVGQEPVLFarsLQDniayglQSCSFECVKEAAQKAHAHSFISELA--------SGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 138 LTLSRNASLYLFDEPVAGIDPIAREEIFELIaSEFSQNASLLVSTHLVVDVEKyLNSAIFLKEAKV 203
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQAL-YDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-50 |
7.42e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.89 E-value: 7.42e-05
10 20 30
....*....|....*....|....*....|...
gi 488135840 18 LDNISLKLPKQQFIGLLGPNGAGKTTLLKILAG 50
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG 49
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-157 |
7.85e-05 |
|
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: 42.47 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYG--SLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI------------LNQKIGI 68
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdghdlaladpawLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 69 ETKKSVAF---LSDGDFL-DPKLTPLKAIAFYK-----DFFSDFDESkalnllkrFSVPLKREFKALSKGMREKLQLILT 139
Cdd:cd03252 81 VLQENVLFnrsIRDNIALaDPGMSMERVIEAAKlagahDFISELPEG--------YDTIVGEQGAGLSGGQRQRIAIARA 152
|
170
....*....|....*...
gi 488135840 140 LSRNASLYLFDEPVAGID 157
Cdd:cd03252 153 LIHNPRILIFDEATSALD 170
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-207 |
8.38e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 42.48 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLTKTYGSLK--ALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNL----------------------NYQGE 58
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLpddnpnskitvdgitltaktvwDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 59 VKIL-----NQKIGIETKKSVAF-LSDGDFLDPKLTPLKAIAFYKDFFSDFDESKALNllkrfsvplkrefkaLSKGMRE 132
Cdd:PRK13640 86 VGIVfqnpdNQFVGATVGDDVAFgLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPAN---------------LSGGQKQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488135840 133 KLQLILTLSRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTHLVVDVEKYLNSAIFLKEAKVVAFG 207
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-78 |
1.02e-04 |
|
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: 41.37 E-value: 1.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488135840 18 LDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGevkilnqKIGIETKKSVAFLS 78
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG-------RIGMPEGEDLLFLP 70
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-50 |
2.40e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 2.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 488135840 7 NLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAG 50
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGG 49
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-63 |
2.76e-04 |
|
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: 40.05 E-value: 2.76e-04
10 20 30
....*....|....*....|....*....|....*..
gi 488135840 27 KQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILN 63
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID 37
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
3-72 |
3.44e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.75 E-value: 3.44e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488135840 3 VEIENLtktygslKALDNISLKLPKQ-QFIGLLGPNGAGKTTLLKILA-GLNLNYQGEVKILNQKIGIETKK 72
Cdd:COG3950 6 LTIENF-------RGFEDLEIDFDNPpRLTVLVGENGSGKTTLLEAIAlALSGLLSRLDDVKFRKLLIRNGE 70
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-182 |
3.50e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.14 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 4 EIENLTktyGSlkALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIET-----KKSVAFLS 78
Cdd:PRK10762 259 KVDNLS---GP--GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqdglANGIVYIS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 79 D---GDFL--------DPKLTPLkaiafykDFFSDF-------DESKAL-NLLKRFSV---PLKREFKALSKGMREKLQL 136
Cdd:PRK10762 334 EdrkRDGLvlgmsvkeNMSLTAL-------RYFSRAggslkhaDEQQAVsDFIRLFNIktpSMEQAIGLLSGGNQQKVAI 406
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488135840 137 ILTLSRNASLYLFDEPVAGIDPIAREEIFELIaSEFSQN--ASLLVST 182
Cdd:PRK10762 407 ARGLMTRPKVLILDEPTRGVDVGAKKEIYQLI-NQFKAEglSIILVSS 453
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
2-183 |
3.55e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 40.24 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTY-GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQG---------------EVKILNQK 65
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGkiwfsghditrlknrEVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 66 IGIETKKSvAFLSDGDFLDPKLTPLK-AIAFYKDF----FSDFDESKALNLLKRFSVplkrefkALSKGMREKLQLILTL 140
Cdd:PRK10908 81 IGMIFQDH-HLLMDRTVYDNVAIPLIiAGASGDDIrrrvSAALDKVGLLDKAKNFPI-------QLSGGEQQRVGIARAV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488135840 141 SRNASLYLFDEPVAGIDPIAREEIFELIaSEFSQ-NASLLVSTH 183
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLF-EEFNRvGVTVLMATH 195
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-48 |
4.02e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 41.10 E-value: 4.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 488135840 2 LVEIENLTKTY-GSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKIL 48
Cdd:PRK13657 334 AVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL 381
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-61 |
4.32e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.70 E-value: 4.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 2 LVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAG---LN---LNYQGEVKI 61
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDdgrIIYEQDLIV 68
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-48 |
4.73e-04 |
|
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: 40.22 E-value: 4.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 488135840 3 VEIENLTKTYGS---LKALDNISLKLPKQQFIGLLGPNGAGKTTLLKIL 48
Cdd:cd03249 1 IEFKNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL 49
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-212 |
6.00e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 40.70 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 18 LDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKI--LN-QKIGIETKKSvaflsdgdfldpKLT--PLKA 92
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdgLNiAKIGLHDLRF------------KITiiPQDP 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 93 IAFYK------DFFSDFDESK---ALNL--LKRF--SVPLKREFKA------LSKGMREKLQLILTLSRNASLYLFDEPV 153
Cdd:TIGR00957 1370 VLFSGslrmnlDPFSQYSDEEvwwALELahLKTFvsALPDKLDHECaeggenLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488135840 154 AGIDPIAREEIFELIASEFsQNASLLVSTHLVVDVEKYlNSAIFLKEAKVVAFGDVGEL 212
Cdd:TIGR00957 1450 AAVDLETDNLIQSTIRTQF-EDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNL 1506
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
3-183 |
1.19e-03 |
|
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: 39.22 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 3 VEIENLtktygslKALDNISLKLPKQQFIgLLGPNGAGKTTLLKILAGLN------------LNYQGEVKILNQKIGIE- 69
Cdd:COG3593 6 IKIKNF-------RSIKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLgpsssrkfdeedFYLGDDPDLPEIEIELTf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 70 -------------TKKSVAFLSDGDFLDPKLTP------------LKAIAFYKDFFSDFDESKALNLLKRFSVPL----K 120
Cdd:COG3593 78 gsllsrllrlllkEEDKEELEEALEELNEELKEalkalnellseyLKELLDGLDLELELSLDELEDLLKSLSLRIedgkE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 121 REFKALSKGMREKLQLILTL-------SRNASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVSTH 183
Cdd:COG3593 158 LPLDRLGSGFQRLILLALLSalaelkrAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1-48 |
1.25e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 39.31 E-value: 1.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 488135840 1 MLVEIENLTKTYGSLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKIL 48
Cdd:PRK10789 314 LDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI 361
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
14-64 |
3.04e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 38.15 E-value: 3.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 488135840 14 SLKALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQ 64
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGK 83
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-157 |
4.09e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.84 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 18 LDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGL------NLNYQGEVKI--LNQKIGIETKKSVAFLSDGDF----LDP 85
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEisadggSYTFPGNWQLawVNQETPALPQPALEYVIDGDReyrqLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 86 KLTPLK------AIAFYKDFFSDFD----ESKALNLLK--RFSVP-LKREFKALSKGMREKLQLILTLSRNASLYLFDEP 152
Cdd:PRK10636 97 QLHDANerndghAIATIHGKLDAIDawtiRSRAASLLHglGFSNEqLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
....*
gi 488135840 153 VAGID 157
Cdd:PRK10636 177 TNHLD 181
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-51 |
5.92e-03 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 37.48 E-value: 5.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 488135840 17 ALDNISLKLPKQQFI------------GLL--GPNGAGKTTLLKILAGL 51
Cdd:COG4178 364 ALEDLTLRTPDGRPLledlslslkpgeRLLitGPSGSGKSTLLRAIAGL 412
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-183 |
6.06e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 37.02 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 2 LVEIENLTKTYGSLK---ALDNISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVKILNQKIGIET------KK 72
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwdirhKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488135840 73 SVAFLS-DGDFLDPklTPLKAIAF--------YKDFFSDFDESKALNLLKRFSvplKREFKALSKGMREKLQLILTLSRN 143
Cdd:PRK13650 84 GMVFQNpDNQFVGA--TVEDDVAFglenkgipHEEMKERVNEALELVGMQDFK---EREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488135840 144 ASLYLFDEPVAGIDPIAREEIFELIASEFSQNASLLVS-TH 183
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISiTH 199
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-66 |
8.40e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 36.78 E-value: 8.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488135840 1 MLvEIeNLTKTYGSLkALDnISLKLPKQQFIGLLGPNGAGKTTLLKILAGLNLNYQGEVkILNQKI 66
Cdd:PRK11144 1 ML-EL-NFKQQLGDL-CLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRI-VLNGRV 61
|
|
| |
