|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-229 |
1.41e-104 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 304.68 E-value: 1.41e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIGY 83
Cdd:COG1131 1 IEVRGLTKRYGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDE 161
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELfgLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526563825 162 PTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGIIDKFTESL 229
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKARLLEDV 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-212 |
9.96e-82 |
|
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: 244.23 E-value: 9.96e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIGY 83
Cdd:cd03230 1 IEVRNLSKRYGK---KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPGKFSLYQDLSVEENLKffatlfgttieenyhlikdiyqqiepfknrragaLSGGMKQKLALSCALIHKPEILILDEPT 163
Cdd:cd03230 78 LPEEPSLYENLTVRENLK----------------------------------LSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2526563825 164 TGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKF 212
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-228 |
2.33e-81 |
|
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: 245.92 E-value: 2.33e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIG 82
Cdd:COG4555 1 MIEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILD 160
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIEllGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526563825 161 EPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGIIDKFTES 228
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-302 |
3.20e-79 |
|
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: 242.68 E-value: 3.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 11 KSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIGYMPGKFSL 90
Cdd:TIGR01188 1 KVYGDF---KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 91 YQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQIE--PFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDP 168
Cdd:TIGR01188 78 DEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFElgEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 169 VSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGIIDKFT-----------ESLwAVEGSR 236
Cdd:TIGR01188 158 RTRRAIWDYIRALKEEGVTILLTTHYMEEADKlCDRIAIIDHGRIIAEGTPEELKRRLGkdtlesrprdiQSL-KVEVSM 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526563825 237 MSAILHElrNHEGIKRSFAFGDKIHITV-DDDLQIDELKQYLLDKEFSDVKIASIEPTVEDCFMALT 302
Cdd:TIGR01188 237 LIAELGE--TGLGLLAVTVDSDRIKILVpDGDETVPEIVEAAIRNGIRIRSISTERPSLDDVFLKLT 301
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-219 |
7.33e-73 |
|
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: 223.54 E-value: 7.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYgKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIGY 83
Cdd:cd03263 1 LQIRNLTKTY-KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDE 161
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVlgLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2526563825 162 PTTGVDPVSRKEFWDMLARLKeQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPK 219
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQ 217
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-298 |
2.63e-69 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 217.28 E-value: 2.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMN--RYDivkdyRKIRQI 80
Cdd:COG4152 1 MLELKGLTKRFGD---KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDgePLD-----PEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 81 IGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIHKPEILI 158
Cdd:COG4152 73 IGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLErlGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 159 LDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGIIDKFTESLWAVEgsrM 237
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLE---A 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526563825 238 SAILHELRNHEGIKRSFAFGDKIHITVDDDLQIDELKQYLLDK----EFSDVkiasiEPTVEDCF 298
Cdd:COG4152 230 DGDAGWLRALPGVTVVEEDGDGAELKLEDGADAQELLRALLARgpvrEFEEV-----RPSLNEIF 289
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-218 |
1.54e-68 |
|
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: 212.62 E-value: 1.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIGY 83
Cdd:cd03265 1 IEVENLVKKYGDF---EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQIE--PFKNRRAGALSGGMKQKLALSCALIHKPEILILDE 161
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGllEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2526563825 162 PTTGVDPVSRKEFWDMLARLK-EQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTP 218
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKeEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTP 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-215 |
3.37e-67 |
|
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: 209.15 E-value: 3.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYG-KSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQII 81
Cdd:cd03266 1 MITADALTKRFRdVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIHKPEILIL 159
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2526563825 160 DEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIAS 215
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYE 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-219 |
5.69e-67 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 224.62 E-value: 5.69e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFrilaSLIlpdSGSAIMNRYDI------VKDYRKI 77
Cdd:NF033858 2 ARLEGVSHRYGK---TVALDDVSLDIPAGCMVGLIGPDGVGKSSLL----SLI---AGARKIQQGRVevlggdMADARHR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 78 RQI---IGYMP---GKfSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCA 149
Cdd:NF033858 72 RAVcprIAYMPqglGK-NLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRAtgLAPFADRPAGKLSGGMKQKLGLCCA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 150 LIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQ--GITILLSTAYMDEAGRCDRIALIREGKFIASDTPK 219
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPA 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-215 |
1.41e-59 |
|
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: 189.33 E-value: 1.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGeIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIGY 83
Cdd:cd03264 1 LQLENLTKRYGK---KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDE 161
Cdd:cd03264 77 LPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLElvNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2526563825 162 PTTGVDPVSRKEFWDMLARLKEqGITILLSTAYM-DEAGRCDRIALIREGKFIAS 215
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGE-DRIVILSTHIVeDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-214 |
3.37e-58 |
|
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: 185.56 E-value: 3.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGsaimnryDIVKDYRKI----RQ 79
Cdd:cd03269 1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSG-------EVLFDGKPLdiaaRN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 IIGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALIHKPEIL 157
Cdd:cd03269 71 RIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERleLSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2526563825 158 ILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIA 214
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVL 208
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-224 |
5.94e-58 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 199.58 E-value: 5.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSA-----IMNRYDIvkdyrKIR 78
Cdd:NF033858 267 IEARGLTMRFGDF---TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDI-----ATR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIIGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALIHKPEI 156
Cdd:NF033858 339 RRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERfdLADVADALPDSLPLGIRQRLSLAVAVIHKPEL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526563825 157 LILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGRCDRIALIREGKFIASDTPKGIIDK 224
Cdd:NF033858 419 LILDEPTSGVDPVARDMFWRLLIELsREDGVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVAA 487
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-222 |
3.81e-57 |
|
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: 183.69 E-value: 3.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYgkSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV-KDYRKIRQIIG 82
Cdd:COG1122 1 IELENLSFSY--PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YmpgkfsLYQD-------LSVEENLKFFATLFGTTIEEnyhlIKDIYQQ------IEPFKNRRAGALSGGMKQKLALSCA 149
Cdd:COG1122 79 L------VFQNpddqlfaPTVEEDVAFGPENLGLPREE----IRERVEEalelvgLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 150 LIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGII 222
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-211 |
6.71e-55 |
|
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: 177.27 E-value: 6.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 5 EVKDLHKSYGKsGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQIIGY 83
Cdd:cd03225 1 ELKNLSFSYPD-GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 mpgkfsLYQD-------LSVEENLKFFATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALIHKP 154
Cdd:cd03225 80 ------VFQNpddqffgPTVEEEVAFGLENLGLPEEEIEERVEEALELvgLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2526563825 155 EILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDE-AGRCDRIALIREGK 211
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLlLELADRVIVLEDGK 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-215 |
1.76e-52 |
|
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: 170.86 E-value: 1.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQI--- 80
Cdd:cd03268 1 LKTNDLTKTYGK---KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIgal 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 81 IGYmPGkfsLYQDLSVEENLKFFATLFGttIEEnyhliKDIYQQIE-----PFKNRRAGALSGGMKQKLALSCALIHKPE 155
Cdd:cd03268 78 IEA-PG---FYPNLTARENLRLLARLLG--IRK-----KRIDEVLDvvglkDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 156 ILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIAS 215
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEE 207
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-223 |
2.17e-52 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 173.84 E-value: 2.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIGY 83
Cdd:PRK13537 8 IDFRNVEKRYGD---KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDI--YQQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDE 161
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLleFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526563825 162 PTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGIID 223
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-224 |
4.46e-52 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 174.25 E-value: 4.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIGY 83
Cdd:PRK13536 42 IDLAGVSKSYGD---KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDI--YQQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDE 161
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLleFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 162 PTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGIIDK 224
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-243 |
1.07e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 170.27 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRydivKDYRKIRQI 80
Cdd:COG1121 4 MPAIELENLTVSYGG---RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----KPPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 81 IGYMPGKFSLYQD--LSVEEnlkFFAT-------LFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCA 149
Cdd:COG1121 77 IGYVPQRAEVDWDfpITVRD---VVLMgrygrrgLFRRPSRADREAVDEALERvgLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 150 LIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKfIASDTPKGIIDKftES 228
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREyFDRVLLLNRGL-VAHGPPEEVLTP--EN 230
|
250
....*....|....*
gi 2526563825 229 LWAVEGSRMSAILHE 243
Cdd:COG1121 231 LSRAYGGPVALLAHG 245
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-192 |
7.67e-49 |
|
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: 161.49 E-value: 7.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIG 82
Cdd:COG4133 2 MLEAENLSCRRGE---RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPGKFSLYQDLSVEENLKFFATLFGTTI--EENYHLIKDIyqQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILD 160
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALYGLRAdrEAIDEALEAV--GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|..
gi 2526563825 161 EPTTGVDPVSRKEFWDMLARLKEQGITILLST 192
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLARGGAVLLTT 188
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-222 |
7.92e-49 |
|
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: 162.33 E-value: 7.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKD--YRKIRQII 81
Cdd:cd03218 1 LRAENLSKRYGK---RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmHKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIHKPEILIL 159
Cdd:cd03218 78 GYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEefHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 160 DEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEA-GRCDRIALIREGKFIASDTPKGII 222
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETlSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-223 |
1.95e-48 |
|
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: 161.69 E-value: 1.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV----KDYRKIR 78
Cdd:COG1127 5 MIEVRNLTKSFGD---RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIIGYMpgkF---SLYQDLSVEENLKFFatlfgttIEENYHLIKDIYQQI----------EPFKNRRAGALSGGMKQKLA 145
Cdd:COG1127 82 RRIGML---FqggALFDSLTVFENVAFP-------LREHTDLSEAEIRELvleklelvglPGAADKMPSELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 146 LSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGIID 223
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-211 |
2.51e-48 |
|
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: 160.73 E-value: 2.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKKN-ALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-------DYR 75
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 76 kiRQIIGYMPGKFSLYQDLSVEENLK---FFATLFGTTIEEN-YHLIKDIyqQIEPFKNRRAGALSGGMKQKLALSCALI 151
Cdd:cd03255 81 --RRHIGFVFQSFNLLPDLTALENVElplLLAGVPKKERRERaEELLERV--GLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 152 HKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGRCDRIALIREGK 211
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-247 |
4.36e-48 |
|
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: 160.98 E-value: 4.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvKDY--RKIRQI 80
Cdd:COG1120 1 MLEAENLSVGYGG---RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL-ASLsrRELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 81 IGYMPGKFSLYQDLSVEENLKF----FATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALIHKP 154
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALgrypHLGLFGRPSAEDREAVEEALERtgLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 155 EILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGIIDKftESLWAV 232
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVLTP--ELLEEV 234
|
250
....*....|....*
gi 2526563825 233 EGSRMSAILHELRNH 247
Cdd:COG1120 235 YGVEARVIEDPVTGR 249
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-219 |
1.27e-47 |
|
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: 158.75 E-value: 1.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI--VKDYRKIRQII 81
Cdd:cd03224 1 LEVENLNAGYGKS---QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItgLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYMPGKFSLYQDLSVEENLKFFATLFG-----TTIEENYHLIKDIYQqiepFKNRRAGALSGGMKQKLALSCALIHKPEI 156
Cdd:cd03224 78 GYVPEGRRIFPELTVEENLLLGAYARRrakrkARLERVYELFPRLKE----RRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 157 LILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEA-GRCDRIALIREGKFIASDTPK 219
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAA 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-219 |
1.28e-47 |
|
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: 159.38 E-value: 1.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKD--YRKIR 78
Cdd:COG0410 1 MPMLEVENLHAGYGGI---HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLppHRIAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIIGYMPGKFSLYQDLSVEENLK--FFATLFGTTIEENYHLIKDIYQQIEPFKNRRAGALSGGMKQKLALSCALIHKPEI 156
Cdd:COG0410 78 LGIGYVPEGRRIFPSLTVEENLLlgAYARRDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 157 LILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPK 219
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAA 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-223 |
1.36e-47 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 159.42 E-value: 1.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKD--YRKIR 78
Cdd:COG1137 1 MMTLEAENLVKSYGK---RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmHKRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIIGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIHKPEI 156
Cdd:COG1137 78 LGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEefGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 157 LILDEPTTGVDPVSRKEFWDMLARLKEQGITILLStaymDEAGR-----CDRIALIREGKFIASDTPKGIID 223
Cdd:COG1137 158 ILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLIT----DHNVRetlgiCDRAYIISEGKVLAEGTPEEILN 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-216 |
2.44e-47 |
|
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: 158.08 E-value: 2.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 5 EVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRydivKDYRKIRQIIGYM 84
Cdd:cd03235 1 EVEDLTVSYGG---HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG----KPLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 85 PGKFSLYQD--LSVEE----NLKFFATLFGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIHKPEI 156
Cdd:cd03235 74 PQRRSIDRDfpISVRDvvlmGLYGHKGLFRRLSKADKAKVDEALErvGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 157 LILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIrEGKFIASD 216
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-218 |
7.29e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 157.13 E-value: 7.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MK-MIEVKDLHKSYGK-SGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK------ 72
Cdd:COG1136 1 MSpLLELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 73 -DYRkiRQIIGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCA 149
Cdd:COG1136 81 aRLR--RRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERvgLGDRLDHRPSQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 150 LIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGRCDRIALIREGKfIASDTP 218
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELAARADRVIRLRDGR-IVSDER 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-223 |
1.31e-46 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 156.89 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV----KDYRKIRQ 79
Cdd:cd03261 1 IELRGLTKSFGG---RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 IIGYMPGKFSLYQDLSVEENLKFFatlfgttIEENY----HLIKDIYQQ------IEPFKNRRAGALSGGMKQKLALSCA 149
Cdd:cd03261 78 RMGMLFQSGALFDSLTVFENVAFP-------LREHTrlseEEIREIVLEkleavgLRGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526563825 150 LIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGIID 223
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-211 |
2.23e-46 |
|
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: 154.27 E-value: 2.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI---VKDYRKIRQI 80
Cdd:cd03229 1 LELKNVSKRYGQ---KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdlEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 81 IGYMPGKFSLYQDLSVEENLKFfatlfgttieenyhlikdiyqqiepfknrragALSGGMKQKLALSCALIHKPEILILD 160
Cdd:cd03229 78 IGMVFQDFALFPHLTVLENIAL--------------------------------GLSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2526563825 161 EPTTGVDPVSRKEFWDMLARLKEQ-GITILLSTAYMDEAGR-CDRIALIREGK 211
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-221 |
2.40e-45 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 153.81 E-value: 2.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKSGKKN-ALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGS------AIMNRYDivKDYR 75
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEvtfdgrPVTRRRR--KAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 76 KIRQIIgympgkfslYQD--LSVeeNLKFfaTLfGTTIEE--NYHLIKDIYQQI----------EPFKNRRAGALSGGMK 141
Cdd:COG1124 79 RRVQMV---------FQDpyASL--HPRH--TV-DRILAEplRIHGLPDREERIaelleqvglpPSFLDRYPHQLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 142 QKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLST------AYMdeagrCDRIALIREGKFIA 214
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVShdlavvAHL-----CDRVAVMQNGRIVE 219
|
....*..
gi 2526563825 215 SDTPKGI 221
Cdd:COG1124 220 ELTVADL 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-296 |
3.56e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 152.93 E-value: 3.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSY-------GKSG-----------KKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAI 64
Cdd:COG4586 1 IIEVENLSKTYrvyekepGLKGalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 65 MNRYDIVKDYRKIRQIIGYMPG-KFSLYQDLSVEENLKFFATLFG---TTIEENYHLIKDIYqQIEPFKNRRAGALSGGM 140
Cdd:COG4586 81 VLGYVPFKRRKEFARRIGVVFGqRSQLWWDLPAIDSFRLLKAIYRipdAEYKKRLDELVELL-DLGELLDTPVRQLSLGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 141 KQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTP 218
Cdd:COG4586 160 RMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 219 KGIIDKFTeslwavEGSRMSAILHELRNHEGIKRSFAF----GDKIHITVDDDLQIDELKQYLLDK-EFSDVKIasIEPT 293
Cdd:COG4586 240 EELKERFG------PYKTIVLELAEPVPPLELPRGGEViereGNRVRLEVDPRESLAEVLARLLARyPVRDLTI--EEPP 311
|
...
gi 2526563825 294 VED 296
Cdd:COG4586 312 IEE 314
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-211 |
3.62e-44 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 147.78 E-value: 3.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 5 EVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQIIGY 83
Cdd:cd00267 1 EIENLSFRYGG---RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPGkfslyqdlsveenlkffatlfgttieenyhlikdiyqqiepfknrragaLSGGMKQKLALSCALIHKPEILILDEPT 163
Cdd:cd00267 78 VPQ-------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2526563825 164 TGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGK 211
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-211 |
4.64e-43 |
|
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: 146.90 E-value: 4.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKdyRKIRQI-IG 82
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG--VPPERRnIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPGKFSLYQDLSVEENLKF---FATLFGTTIEENYHLIKDIYqQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILIL 159
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFglkLRGVPKAEIRARVRELLELV-GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 160 DEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGK 211
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALAlADRIAVMNEGR 208
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-213 |
5.47e-43 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 147.16 E-value: 5.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV-KDYRKIRQIIG 82
Cdd:TIGR03740 1 LETKNLSKRFGK---QTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTrKDLHKIGSLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPgkfsLYQDLSVEENLKFFATLFG---TTIEENYHLIkdiyqQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILIL 159
Cdd:TIGR03740 78 SPP----LYENLTARENLKVHTTLLGlpdSRIDEVLNIV-----DLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLIL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2526563825 160 DEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFI 213
Cdd:TIGR03740 149 DEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQlADHIGIISEGVLG 203
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-227 |
8.46e-43 |
|
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: 146.94 E-value: 8.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGksGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI----VKDYRKIRQ 79
Cdd:cd03256 1 IEVENLSKTYP--NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 IIGYMPGKFSLYQDLSVEEN--------LKFFATLFG----TTIEENYHLIKDIyqQIEPFKNRRAGALSGGMKQKLALS 147
Cdd:cd03256 79 QIGMIFQQFNLIERLSVLENvlsgrlgrRSTWRSLFGlfpkEEKQRALAALERV--GLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 148 CALIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKfIASDtpkGIIDKF 225
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREyADRIVGLKDGR-IVFD---GPPAEL 232
|
..
gi 2526563825 226 TE 227
Cdd:cd03256 233 TD 234
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-218 |
1.15e-42 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 147.11 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGksGKKnALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI--VKDYRKIR 78
Cdd:COG0411 2 DPLLEVRGLTKRFG--GLV-AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItgLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 -------QIIgympgkfSLYQDLSVEENLK----------FFATLFGT---------TIEENYHLIKDIyqQIEPFKNRR 132
Cdd:COG0411 79 lgiartfQNP-------RLFPELTVLENVLvaaharlgrgLLAALLRLprarreereARERAEELLERV--GLADRADEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 133 AGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLK-EQGITILLstayMDEAGR-CDRIALIREG 210
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLiehdMDLVMGlADRIVVLDFG 229
|
....*...
gi 2526563825 211 KFIASDTP 218
Cdd:COG0411 230 RVIAEGTP 237
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-206 |
1.83e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 146.77 E-value: 1.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYG-KSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvkdyRKIRQ 79
Cdd:COG1116 5 APALELRGVSKRFPtGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV----TGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 IIGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQI--EPFKNRRAGALSGGMKQKLALSCALIHKPEIL 157
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVglAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 158 ILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIAL 206
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFlADRVVV 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-214 |
2.16e-42 |
|
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: 145.31 E-value: 2.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYG-KSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMnrydivkDYRKIRQI-- 80
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLV-------DGEPVTGPgp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 81 -IGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENY----HLIKDIyqQIEPFKNRRAGALSGGMKQKLALSCALIHKPE 155
Cdd:cd03293 74 dRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEAReraeELLELV--GLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526563825 156 ILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALI--REGKFIA 214
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFlADRVVVLsaRPGRIVA 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-221 |
3.93e-42 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 145.27 E-value: 3.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGksGKKnALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI--VKDYRKIRQII 81
Cdd:cd03219 1 LEVRGLTKRFG--GLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItgLPPHEIARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYmpgKF---SLYQDLSVEENL----------KFFATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLAL 146
Cdd:cd03219 78 GR---TFqipRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERvgLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526563825 147 SCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGI 221
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEV 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-216 |
1.23e-41 |
|
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: 144.01 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGK------------------KNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIM 65
Cdd:cd03267 1 IEVSNLSKSYRVYSKepgligslkslfkrkyreVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 66 NRYDIVKDYRKIRQIIGYMPG-KFSLYQDLSVEENLKFFATL-------FGTTIEENYHLIkdiyqQIEPFKNRRAGALS 137
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVVFGqKTQLWWDLPVIDSFYLLAAIydlpparFKKRLDELSELL-----DLEELLDTPVRQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 138 GGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYM-DEAGRCDRIALIREGKFIAS 215
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMkDIEALARRVLVIDKGRLLYD 235
|
.
gi 2526563825 216 D 216
Cdd:cd03267 236 G 236
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-222 |
1.53e-41 |
|
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: 143.95 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 6 VKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKD--YRKIRQIIGY 83
Cdd:TIGR04406 4 AENLIKSYKK---RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLpmHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPGKFSLYQDLSVEENLK----FFATLFGTTIEENYH-LIKDIyqQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILI 158
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMavleIRKDLDRAEREERLEaLLEEF--QISHLRDNKAMSLSGGERRRVEIARALATNPKFIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526563825 159 LDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEA-GRCDRIALIREGKFIASDTPKGII 222
Cdd:TIGR04406 159 LDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETlDICDRAYIISDGKVLAEGTPAEIV 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-220 |
1.60e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 143.27 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGksGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKI---R 78
Cdd:COG2884 1 MIRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIpylR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIIGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALIHKPEI 156
Cdd:COG2884 79 RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLvgLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526563825 157 LILDEPTTGVDPVSRKEFWDMLARLKEQGITILLST---AYMDEAGRcdRIALIREGKfIASDTPKG 220
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAThdlELVDRMPK--RVLELEDGR-LVRDEARG 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-231 |
1.96e-41 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 150.05 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKSGKKN--ALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI----VKDYRK 76
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtklsRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 77 IRQIIGYmpgkfsLYQD--------LSVEENLKFFATLFGT-TIEENYHLIKDIYQQI---EPFKNRRAGALSGGMKQKL 144
Cdd:COG1123 340 LRRRVQM------VFQDpysslnprMTVGDIIAEPLRLHGLlSRAERRERVAELLERVglpPDLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 145 ALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLST------AYMdeagrCDRIALIREGKFIASDT 217
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFIShdlavvRYI-----ADRVAVMYDGRIVEDGP 488
|
250
....*....|....*...
gi 2526563825 218 PKGIIDK----FTESLWA 231
Cdd:COG1123 489 TEEVFANpqhpYTRALLA 506
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-215 |
7.79e-41 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 139.88 E-value: 7.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 5 EVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQIIGY 83
Cdd:cd03214 1 EVENLSVGYGG---RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPgkfslyQDLSveenlkffatLFGttieenyhlikdiyqqIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPT 163
Cdd:cd03214 78 VP------QALE----------LLG----------------LAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 164 TGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIAS 215
Cdd:cd03214 126 SHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQ 179
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-217 |
8.14e-41 |
|
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: 141.56 E-value: 8.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKSGKK-NALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV----KDYRKI 77
Cdd:cd03258 1 MIELKNVSKVFGDTGGKvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 78 RQIIGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQI--EPFKNRRAGALSGGMKQKLALSCALIHKPE 155
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVglEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 156 ILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDT 217
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-211 |
8.25e-40 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 138.79 E-value: 8.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYG-KSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQII 81
Cdd:cd03257 1 LLEVKNLSVSFPtGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GympGKFSL-YQD--------LSVEENLKFFATLFGTTI--EENYHLIKDIYQQIEP---FKNRRAGALSGGMKQKLALS 147
Cdd:cd03257 81 R---KEIQMvFQDpmsslnprMTIGEQIAEPLRIHGKLSkkEARKEAVLLLLVGVGLpeeVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 148 CALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLST------AYMdeagrCDRIALIREGK 211
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFIThdlgvvAKI-----ADRVAVMYAGK 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-223 |
1.27e-39 |
|
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: 145.05 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGkSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPD---SGSAIMNRYDIVKDYRKIR- 78
Cdd:COG1123 4 LLEVRDLSVRYP-GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIIGYMPgkfslyQD-------LSVEENLKFFATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCA 149
Cdd:COG1123 83 RRIGMVF------QDpmtqlnpVTVGDQIAEALENLGLSRAEARARVLELLEAvgLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526563825 150 LIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDE-AGRCDRIALIREGKFIASDTPKGIID 223
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-222 |
1.67e-39 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 139.32 E-value: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKKN---------------------ALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGS 62
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAfkllakgkskeeilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 63 AIMNRYDIV----KDYRKIR-QIIGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQI--EPFKNRRAGA 135
Cdd:cd03294 81 VLIDGQDIAamsrKELRELRrKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVglEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 136 LSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGRC-DRIALIREGKFI 213
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLgDRIAIMKDGRLV 240
|
....*....
gi 2526563825 214 ASDTPKGII 222
Cdd:cd03294 241 QVGTPEEIL 249
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-211 |
3.60e-39 |
|
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: 135.59 E-value: 3.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGkSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQIIG 82
Cdd:cd03228 1 IEFKNVSFSYP-GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPgkfslyQDlsveenlkffATLFGTTIEENyhlikdiyqqIepfknrragaLSGGMKQKLALSCALIHKPEILILDEP 162
Cdd:cd03228 80 YVP------QD----------PFLFSGTIREN----------I----------LSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2526563825 163 TTGVDPVSRKEFWDMLARLKeQGITILLSTAYMDEAGRCDRIALIREGK 211
Cdd:cd03228 124 TSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-250 |
6.25e-39 |
|
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: 145.93 E-value: 6.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 6 VKDLHKSYGKSGKKnALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIGYMP 85
Cdd:TIGR01257 931 VKNLVKIFEPSGRP-AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 86 GKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPT 163
Cdd:TIGR01257 1010 QHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 164 TGVDPVSRKEFWDMLARLKeQGITILLSTAYMDEAGRC-DRIALIREGKFIASDTPKGIIDKFTESLWAVEGSRMSAILH 242
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQS 1168
|
....*...
gi 2526563825 243 ELRNHEGI 250
Cdd:TIGR01257 1169 QRGGCEGT 1176
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-218 |
3.82e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 137.92 E-value: 3.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI--VKDYRkiR 78
Cdd:COG3842 3 MPALELENVSKRYGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtgLPPEK--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIiGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIHKPEI 156
Cdd:COG3842 78 NV-GMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLElvGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 157 LILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTP 218
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALAlADRIAVMNDGRIEQVGTP 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-223 |
5.68e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 137.20 E-value: 5.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMN--RYDIVKDYRKiRQIi 81
Cdd:COG1118 3 IEVRNISKRFGS---FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNgrDLFTNLPPRE-RRV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYMPGKFSLYQDLSVEENLKFFATLFGTTIEEnyhlIKDIYQ------QIEPFKNRRAGALSGGMKQKLALSCALIHKPE 155
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGLRVRPPSKAE----IRARVEellelvQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 156 ILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGIID 223
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALElADRVVVMNQGRIEQVGTPDEVYD 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-222 |
6.10e-38 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 134.35 E-value: 6.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGksGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQIIG 82
Cdd:cd03295 1 IEFENVTKRYG--GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPGKFSLYQDLSVEENLKFFATLFG----TTIEENYHLIKDIYQQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILI 158
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVPKLLKwpkeKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526563825 159 LDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGII 222
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEIL 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-217 |
1.63e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 135.98 E-value: 1.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSY-GKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV----KDYRKI 77
Cdd:COG1135 1 MIELENLSKTFpTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalseRELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 78 RQIIGYMPGKFSLYQDLSVEEN----LKffatLFGTTIEEnyhlikdIYQQIEP---------FKNRRAGALSGGMKQKL 144
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENvalpLE----IAGVPKAE-------IRKRVAEllelvglsdKADAYPSQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526563825 145 ALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDT 217
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-212 |
1.79e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.55 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAI-----MNRYDIvkdyRKIR 78
Cdd:COG4619 1 LELEGLSFRVGG---KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkpLSAMPP----PEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIIGYMPGKFSLYQDlSVEENLKFFATLFGTTIeeNYHLIKDIYQQI---EPFKNRRAGALSGGMKQKLALSCALIHKPE 155
Cdd:COG4619 74 RQVAYVPQEPALWGG-TVRDNLPFPFQLRERKF--DRERALELLERLglpPDILDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2526563825 156 ILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKF 212
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-229 |
2.16e-35 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 127.89 E-value: 2.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 2 KMIEVKDLHKSY-------------------GKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGS 62
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 63 AIMNrydivkdyRKIRQIIGYMPGkfsLYQDLSVEENLKFFATLFGTTIEEnyhlIKDIYQQIE-----------PFKNr 131
Cdd:COG1134 83 VEVN--------GRVSALLELGAG---FHPELTGRENIYLNGRLLGLSRKE----IDEKFDEIVefaelgdfidqPVKT- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 132 ragaLSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREG 210
Cdd:COG1134 147 ----YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKG 222
|
250
....*....|....*....
gi 2526563825 211 KFIASDTPKGIIDKFTESL 229
Cdd:COG1134 223 RLVMDGDPEEVIAAYEALL 241
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-224 |
4.28e-35 |
|
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: 134.19 E-value: 4.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQIIG 82
Cdd:COG2274 474 IELENVSFRYPGDSP-PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPGKFSLYQDlSVEENLKFFATlfGTTIEENYHLIKDIyqQIEPFKNR-----------RAGALSGGMKQKLALSCALI 151
Cdd:COG2274 553 VVLQDVFLFSG-TIRENITLGDP--DATDEEIIEAARLA--GLHDFIEAlpmgydtvvgeGGSNLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526563825 152 HKPEILILDEPTTGVDPVSRKEFWDMLARLKeQGITILLSTAYMDEAGRCDRIALIREGKFIASDTPKGIIDK 224
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-221 |
1.97e-34 |
|
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: 124.99 E-value: 1.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLI-----LPDSGSAIM---NRYDIVKDYR 75
Cdd:cd03260 1 IELRDLNVYYGD---KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLdgkDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 76 KIRQIIGyM----PGKFslyqDLSVEENLKFFATLFGttiEENYHLIKDIYQQI-------EPFKNR-RAGALSGGMKQK 143
Cdd:cd03260 78 ELRRRVG-MvfqkPNPF----PGSIYDNVAYGLRLHG---IKLKEELDERVEEAlrkaalwDEVKDRlHALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526563825 144 LALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQgITILLSTAYMDEAGRC-DRIALIREGKFIASDTPKGI 221
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-213 |
2.67e-34 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 123.91 E-value: 2.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 5 EVKDLHKSYGKSGKknALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvkDYRKIRQIIGYM 84
Cdd:cd03226 1 RIENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI--KAKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 85 PG--KFSLYQDlSVEENLKFFATLFGTTIEENYHLIKDIyqQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEP 162
Cdd:cd03226 77 MQdvDYQLFTD-SVREELLLGLKELDAGNEQAETVLKDL--DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 163 TTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFI 213
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-164 |
3.43e-34 |
|
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: 121.99 E-value: 3.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 22 LNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKI-RQIIGYMPGKFSLYQDLSVEENL 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 101 KFFATLFG-TTIEENYHLIKDIYQ-QIEPFKNRRAGA----LSGGMKQKLALSCALIHKPEILILDEPTT 164
Cdd:pfam00005 81 RLGLLLKGlSKREKDARAEEALEKlGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-215 |
3.92e-34 |
|
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: 122.15 E-value: 3.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSaimnrydIVKDYRKIRqiigy 83
Cdd:cd03216 1 LELRGITKRFGGV---KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE-------ILVDGKEVS----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 mpgkfslyqdlsveenlkffatlFGTTIEENYHLIKDIYQqiepfknrragaLSGGMKQKLALSCALIHKPEILILDEPT 163
Cdd:cd03216 66 -----------------------FASPRDARRAGIAMVYQ------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2526563825 164 TGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIAS 215
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-211 |
4.27e-34 |
|
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: 123.41 E-value: 4.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV---KDYRKIRQI 80
Cdd:cd03262 1 IEIKNLHKSFGD---FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 81 IGYMPGKFSLYQDLSVEENLKF-FATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALIHKPEIL 157
Cdd:cd03262 78 VGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKvgLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2526563825 158 ILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGK 211
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGR 212
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-221 |
5.20e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.19 E-value: 5.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKSGKknALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMN----RYDiVKDYRKIR 78
Cdd:PRK13639 1 ILETRDLKYSYPDGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepiKYD-KKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIIGYMpgkFSLYQDL----SVEENLKFFATLFGTTIEENYHLIKDIYQQI--EPFKNRRAGALSGGMKQKLALSCALIH 152
Cdd:PRK13639 78 KTVGIV---FQNPDDQlfapTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVgmEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 153 KPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGI 221
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-212 |
7.20e-34 |
|
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: 122.16 E-value: 7.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 5 EVKDLHKsygksgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV-KDYRK-IRQIIG 82
Cdd:cd03215 6 EVRGLSV-------KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrRSPRDaIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPG---KFSLYQDLSVEENLkffatlfgttieenyhLIKDIyqqiepfknrragaLSGGMKQKLALSCALIHKPEILIL 159
Cdd:cd03215 79 YVPEdrkREGLVLDLSVAENI----------------ALSSL--------------LSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 160 DEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEA-GRCDRIALIREGKF 212
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-218 |
2.25e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.19 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI----VKDyRK 76
Cdd:COG3839 1 MASLELENVSKSYGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlpPKD-RN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 77 irqiIGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIHKP 154
Cdd:COG3839 77 ----IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAEllGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 155 EILILDEPTTGVDPVSRkefWDM---LARL-KEQGITILLSTAYMDEA---GrcDRIALIREGKFIASDTP 218
Cdd:COG3839 153 KVFLLDEPLSNLDAKLR---VEMraeIKRLhRRLGTTTIYVTHDQVEAmtlA--DRIAVMNDGRIQQVGTP 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-216 |
5.70e-33 |
|
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: 121.10 E-value: 5.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 9 LHKSYGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNrydivkdyRKIRQIIGYMPGkf 88
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR--------GRVSSLLGLGGG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 89 sLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGV 166
Cdd:cd03220 95 -FNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEfsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 167 DPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASD 216
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-217 |
7.50e-33 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 123.76 E-value: 7.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSY-GKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV----KDYRKI 77
Cdd:PRK11153 1 MIELKNISKVFpQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalseKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 78 RQIIGYMPGKFSLYQDLSVEENLKFFATLFGTTIEEnyhlikdIYQQIEPF---------KNRRAGALSGGMKQKLALSC 148
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAE-------IKARVTELlelvglsdkADRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 149 ALIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDT 217
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-223 |
1.09e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 120.24 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKSgkknALNgISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKdyrkirqiig 82
Cdd:COG3840 1 MLRLDDLTYRYGDF----PLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPGK--FS-LYQD------LSVEENLkffatlfGTTIEENYHL-------IKDIYQQ--IEPFKNRRAGALSGGMKQKL 144
Cdd:COG3840 66 LPPAErpVSmLFQEnnlfphLTVAQNI-------GLGLRPGLKLtaeqraqVEQALERvgLAGLLDRLPGQLSGGQRQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 145 ALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGII 222
Cdd:COG3840 139 ALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
.
gi 2526563825 223 D 223
Cdd:COG3840 219 D 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-223 |
2.17e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 119.71 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV---KDYRKIRQ 79
Cdd:COG1126 1 MIEIENLHKSFGD---LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 IIGYMPGKFSLYQDLSVEENLkffaTL-----FGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALIH 152
Cdd:COG1126 78 KVGMVFQQFNLFPHLTVLENV----TLapikvKKMSKAEAEERAMELLERvgLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 153 KPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGIID 223
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-273 |
2.18e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 120.96 E-value: 2.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 2 KMIEVKDLHKSYGKSGKKN---ALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI--VKDYRK 76
Cdd:PRK13633 3 EMIKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsdEENLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 77 IRQIIGYmpgkfsLYQDLS-------VEENLKFFATLFGTTIEENYHLIKDIYQQIEPFKNRRAGA--LSGGMKQKLALS 147
Cdd:PRK13633 83 IRNKAGM------VFQNPDnqivatiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPhlLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 148 CALIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGRCDRIALIREGKFIASDTPKGIIDKFT 226
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKEVE 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2526563825 227 E-SLWAVEGSRMSAILHELRNhEGIKRSfafgdkihitvDDDLQIDEL 273
Cdd:PRK13633 237 MmKKIGLDVPQVTELAYELKK-EGVDIP-----------SDILTIDEM 272
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-221 |
3.44e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.51 E-value: 3.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 2 KMIEVKDLHKSYgKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRY----DIVKDyrkI 77
Cdd:PRK13635 4 EIIRVEHISFRY-PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseETVWD---V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 78 RQIIGyMpgkfsLYQD-------LSVEENLKFFATLFGTTIEENYHLIKDIYQQI--EPFKNRRAGALSGGMKQKLALSC 148
Cdd:PRK13635 80 RRQVG-M-----VFQNpdnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVgmEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 149 ALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLSTAYMDEAGRCDRIALIREGKFIASDTPKGI 221
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-222 |
9.69e-32 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 118.06 E-value: 9.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV--KDYRKIR 78
Cdd:PRK11614 3 KVMLSFDKVSAHYGKI---QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIIGYMPGKFSLYQDLSVEENLK---FFA--TLFGTTIEENYHLIKDIYQQiepfKNRRAGALSGGMKQKLALSCALIHK 153
Cdd:PRK11614 80 EAVAIVPEGRRVFSRMTVEENLAmggFFAerDQFQERIKWVYELFPRLHER----RIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 154 PEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGII 222
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALL 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-224 |
1.05e-31 |
|
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: 117.82 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYgksgKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVkDYRKIRQIIGY 83
Cdd:cd03299 1 LKVENLSKDW----KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-NLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDE 161
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEmlGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526563825 162 PTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGIIDK 224
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-224 |
2.88e-31 |
|
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: 116.57 E-value: 2.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQiIGY 83
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP-VNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPGKFSLYQDLSVEENLKFFATLFGTT-------IEENYHLIkdiyqQIEPFKNRRAGALSGGMKQKLALSCALIHKPEI 156
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLRLKKLPkaeikerVAEALDLV-----QLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 157 LILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEA-GRCDRIALIREGKFIASDTPKGIIDK 224
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEAlTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-212 |
8.15e-31 |
|
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: 115.04 E-value: 8.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQiIGY 83
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD-IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPGKFSLYQDLSVEENLKFFATLFGT---TIEENYHLIKDIYqQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILD 160
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLRKVpkdEIDERVREVAELL-QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 161 EPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEA-GRCDRIALIREGKF 212
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQI 209
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
1.81e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 115.67 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYgkSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQ 79
Cdd:PRK13652 1 MHLIETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKeNIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 IIGYMpgkFSLYQDL----SVEENLKFFATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALIHK 153
Cdd:PRK13652 79 FVGLV---FQNPDDQifspTVEQDIAFGPINLGLDEETVAHRVSSALHMlgLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 154 PEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMD-EAGRCDRIALIREGKFIASDTPKGI 221
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-219 |
2.14e-30 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 119.87 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvKDYRK--IRQII 81
Cdd:COG4987 334 LELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL-RDLDEddLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYMPgkfslyQDlsveenlkffATLFGTTIEENYHLIK------DIYQ-----QIEPF-KNRRAG----------ALSGG 139
Cdd:COG4987 412 AVVP------QR----------PHLFDTTLRENLRLARpdatdeELWAalervGLGDWlAALPDGldtwlgeggrRLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 140 MKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFW-DMLARLKEQgiTILLSTAYMDEAGRCDRIALIREGKFIASDTP 218
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLaDLLEALAGR--TVLLITHRLAGLERMDRILVLEDGRIVEQGTH 553
|
.
gi 2526563825 219 K 219
Cdd:COG4987 554 E 554
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-224 |
4.33e-30 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 113.97 E-value: 4.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQiIGY 83
Cdd:cd03296 3 IEVRNVSKRFGDF---VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN-VGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPGKFSLYQDLSVEENLKF-------FATLFGTTIEENYHLIKDIYqQIEPFKNRRAGALSGGMKQKLALSCALIHKPEI 156
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFglrvkprSERPPEAEIRAKVHELLKLV-QLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 157 LILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGIIDK 224
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-211 |
5.43e-30 |
|
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: 111.54 E-value: 5.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGkSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQIIG 82
Cdd:cd03246 1 LEVENVSFRYP-GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPgkfslyQDlsveenlkffATLFGTTIEENyhlikdiyqqiepfknrragALSGGMKQKLALSCALIHKPEILILDEP 162
Cdd:cd03246 80 YLP------QD----------DELFSGSIAEN--------------------ILSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2526563825 163 TTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGRCDRIALIREGK 211
Cdd:cd03246 124 NSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGR 172
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-205 |
7.90e-30 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 115.15 E-value: 7.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYG-KSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILP---DSGSAIMNRYDIV----KDY 74
Cdd:COG0444 1 LLEVRNLKVYFPtRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLklseKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 75 RKIR----QIIgympgkfslYQD--------LSVeenlkffatlfGTTIEE--NYHLI---KDIYQQIE--------PFK 129
Cdd:COG0444 81 RKIRgreiQMI---------FQDpmtslnpvMTV-----------GDQIAEplRIHGGlskAEARERAIellervglPDP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 130 NRRAGA----LSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLST------AYMdea 198
Cdd:COG0444 141 ERRLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFIThdlgvvAEI--- 217
|
....*..
gi 2526563825 199 grCDRIA 205
Cdd:COG0444 218 --ADRVA 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-215 |
1.47e-29 |
|
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: 112.49 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAI------MNRYDIvkdyRK 76
Cdd:COG1119 3 LLELRNVTVRRGG---KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDV----WE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 77 IRQIIGYmpgkFS--LYQDLSVEENLK------FFAT--LFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKL 144
Cdd:COG1119 76 LRKRIGL----VSpaLQLRFPRDETVLdvvlsgFFDSigLYREPTDEQRERARELLELlgLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526563825 145 ALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGRC-DRIALIREGKFIAS 215
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAA 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-216 |
1.58e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 111.62 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 25 ISFTVDdGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKI-----RQIIGYMPGKFSLYQDLSVEEN 99
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqQRKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 100 LkffatLFGTTIEENyHLIKD------IYQQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKE 173
Cdd:cd03297 96 L-----AFGLKRKRN-REDRIsvdellDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2526563825 174 FWDMLARLKEQ-GITILLSTAYMDEAGR-CDRIALIREGKFIASD 216
Cdd:cd03297 170 LLPELKQIKKNlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-227 |
2.52e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.49 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSY--GKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI--VKDYRKIR 78
Cdd:COG1101 1 MLELKNLSKTFnpGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtkLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIigympGKfsLYQD--------LSVEENL-------KFFATLFGTTIEEnyhliKDIYQ-QIEPFK----NR---RAGA 135
Cdd:COG1101 81 YI-----GR--VFQDpmmgtapsMTIEENLalayrrgKRRGLRRGLTKKR-----RELFReLLATLGlgleNRldtKVGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 136 LSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGRC-DRIALIREGKFI 213
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYgNRLIMMHEGRII 228
|
250 260
....*....|....*....|..
gi 2526563825 214 --------ASDTPKGIIDKFTE 227
Cdd:COG1101 229 ldvsgeekKKLTVEDLLELFEE 250
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-213 |
4.33e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 112.87 E-value: 4.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKmIEVKDLHKSYGK--SGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKD----- 73
Cdd:PRK13651 1 MQ-IKVKNIVKIFNKklPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 74 --------------YRKIRQI------IGYMpGKFSLYQ--DLSVEENLKFFATLFGTTIEENYHLIKDIYQQI---EPF 128
Cdd:PRK13651 80 kekvleklviqktrFKKIKKIkeirrrVGVV-FQFAEYQlfEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVgldESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 129 KNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEA-GRCDRIALI 207
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVlEWTKRTIFF 238
|
....*.
gi 2526563825 208 REGKFI 213
Cdd:PRK13651 239 KDGKII 244
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-214 |
8.22e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.12 E-value: 8.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 5 EVKDLhksygksGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMN--RYDIvKDYRK-IRQII 81
Cdd:COG1129 258 EVEGL-------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgkPVRI-RSPRDaIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYMPG---KFSLYQDLSVEENLkffaTLfgTTIEE--NYHLI--KDIYQQIEPFKNR----------RAGALSGGMKQKL 144
Cdd:COG1129 330 AYVPEdrkGEGLVLDLSIRENI----TL--ASLDRlsRGGLLdrRRERALAEEYIKRlriktpspeqPVGNLSGGNQQKV 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 145 ALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDE-AGRCDRIALIREGKFIA 214
Cdd:COG1129 404 VLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPElLGLSDRILVMREGRIVG 474
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-219 |
1.05e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 115.24 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGksGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvKDYRK--IRQII 81
Cdd:COG4988 337 IELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL-SDLDPasWRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYMPgkfslyQDlsveenlkffATLFGTTIEENYHL------IKDIYQ-----QIEPFKNR-----------RAGALSGG 139
Cdd:COG4988 414 AWVP------QN----------PYLFAGTIRENLRLgrpdasDEELEAaleaaGLDEFVAAlpdgldtplgeGGRGLSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 140 MKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKeQGITILLSTAYMDEAGRCDRIALIREGKFIASDTPK 219
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQADRILVLDDGRIVEQGTHE 556
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-237 |
1.44e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 109.98 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYgkSGKKnALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI--VKDYRKIR 78
Cdd:PRK10895 1 MATLTAKNLAKAY--KGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIslLPLHARAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIIGYMPGKFSLYQDLSVEENLkfFATL---FGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALIHK 153
Cdd:PRK10895 78 RGIGYLPQEASIFRRLSVYDNL--MAVLqirDDLSAEQREDRANELMEEfhIEHLRDSMGQSLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 154 PEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEA-GRCDRIALIREGKFIASDTPKGII-DKFTESLWA 231
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETlAVCERAYIVSQGHLIAHGTPTEILqDEHVKRVYL 235
|
....*.
gi 2526563825 232 VEGSRM 237
Cdd:PRK10895 236 GEDFRL 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-221 |
1.67e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.96 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGksGKKnALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMN--RYDIvKDYRKIRQI 80
Cdd:COG1129 4 LLEMRGISKSFG--GVK-ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgePVRF-RSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 81 -IGYMPGKFSLYQDLSVEENLkFFATLFGT--------TIEENYHLIKDIYQQIEPfkNRRAGALSGGMKQKLALSCALI 151
Cdd:COG1129 80 gIAIIHQELNLVPNLSVAENI-FLGREPRRgglidwraMRRRARELLARLGLDIDP--DTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 152 HKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGI 221
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-219 |
3.24e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.94 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYgkSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI---VKDYRKIRQ 79
Cdd:PRK13636 5 ILKVEELNYNY--SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 IIGYmpgkfsLYQD-------LSVEENLKFFATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCAL 150
Cdd:PRK13636 83 SVGM------VFQDpdnqlfsASVYQDVSFGAVNLKLPEDEVRKRVDNALKRtgIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 151 IHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDE-AGRCDRIALIREGKFIASDTPK 219
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPK 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-219 |
3.32e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.20 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGksGKKnALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMN--RYDIvKDYRK-IRQ 79
Cdd:COG3845 5 ALELRGITKRFG--GVV-ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkPVRI-RSPRDaIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 IIGYMPGKFSLYQDLSVEENL-------KFFATLFGTTIEEnyhlIKDIYQQ----IEPfkNRRAGALSGGMKQKLALSC 148
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIvlgleptKGGRLDRKAARAR----IRELSERygldVDP--DAKVEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 149 ALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPK 219
Cdd:COG3845 155 ALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAiADRVTVLRRGKVVGTVDTA 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-221 |
3.36e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.11 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSY--GKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV-----KDYRK 76
Cdd:PRK13634 3 ITFQKVEHRYqyKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 77 IRQIIGyMPGKFSLYQ--DLSVEENLKFFATLFGTTIEENYHLIKDIYQQI---EPFKNRRAGALSGGMKQKLALSCALI 151
Cdd:PRK13634 83 LRKKVG-IVFQFPEHQlfEETVEKDICFGPMNFGVSEEDAKQKAREMIELVglpEELLARSPFELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 152 HKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGI 221
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-223 |
4.32e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 108.64 E-value: 4.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV---KDYRKIRQ 79
Cdd:PRK09493 1 MIEFKNVSKHFGPT---QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 IIGYMPGKFSLYQDLSVEENLKFFAT-LFGTTIEENYHLIKDIYQQI--EPFKNRRAGALSGGMKQKLALSCALIHKPEI 156
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENVMFGPLrVRGASKEEAEKQARELLAKVglAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526563825 157 LILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGRC-DRIALIREGKfIASD-TPKGIID 223
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVaSRLIFIDKGR-IAEDgDPQVLIK 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-213 |
5.59e-28 |
|
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: 106.87 E-value: 5.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDL---HKSYGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLI--LPDSGSAIMNRYDIVKdyRKIR 78
Cdd:cd03213 4 LSFRNLtvtVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGRPLDK--RSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIIGYMPGKFSLYQDLSVEENLKFFATLFGttieenyhlikdiyqqiepfknrragaLSGGMKQKLALSCALIHKPEILI 158
Cdd:cd03213 82 KIIGYVPQDDILHPTLTVRETLMFAAKLRG---------------------------LSGGERKRVSIALELVSNPSLLF 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2526563825 159 LDEPTTGVDPVSRKEFWDMLARLKEQGITILLST---AYMDEaGRCDRIALIREGKFI 213
Cdd:cd03213 135 LDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIhqpSSEIF-ELFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
7.31e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.54 E-value: 7.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 2 KMIEVKDLHKSYGKSgKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKD-YRKIRQI 80
Cdd:PRK13632 6 VMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 81 IGYmpgkfsLYQD-------LSVEENLKFFATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALI 151
Cdd:PRK13632 85 IGI------IFQNpdnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKvgMEDYLDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 152 HKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLS-TAYMDEAGRCDRIALIREGKFIASDTPKGI 221
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-192 |
1.36e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 106.11 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHksyGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvkDYRKIRQIIG 82
Cdd:PRK13539 2 MLEGEDLA---CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIyqQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEP 162
Cdd:PRK13539 77 YLGHRNAMKPALTVAENLEFWAAFLGGEELDIAAALEAV--GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|
gi 2526563825 163 TTGVDPVSRKEFWDMLARLKEQGITILLST 192
Cdd:PRK13539 155 TAALDAAAVALFAELIRAHLAQGGIVIAAT 184
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-221 |
1.58e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 107.38 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 2 KMIEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMN-------------RY 68
Cdd:PRK11300 4 PLLSVSGLMMRFGGL---LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRgqhieglpghqiaRM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 69 DIVKDYRKIRqiigympgkfsLYQDLSVEENL----------KFFATLFGT---------TIEENYHLIKDIyqQIEPFK 129
Cdd:PRK11300 81 GVVRTFQHVR-----------LFREMTVIENLlvaqhqqlktGLFSGLLKTpafrraeseALDRAATWLERV--GLLEHA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 130 NRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLSTAYMDEA-GRCDRIALI 207
Cdd:PRK11300 148 NRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVmGISDRIYVV 227
|
250
....*....|....
gi 2526563825 208 REGKFIASDTPKGI 221
Cdd:PRK11300 228 NQGTPLANGTPEEI 241
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-218 |
1.63e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 111.80 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGksGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvKDYRK--IRQII 81
Cdd:COG1132 340 IEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI-RDLTLesLRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYMPGKFSLYQDlSVEENLKFFATlfGTTIEEnyhlikdIYQ-----QIEPFKNR-----------RAGALSGGMKQKLA 145
Cdd:COG1132 417 GVVPQDTFLFSG-TIRENIRYGRP--DATDEE-------VEEaakaaQAHEFIEAlpdgydtvvgeRGVNLSGGQRQRIA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526563825 146 LSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITIL----LSTAyMDeagrCDRIALIREGKFIASDTP 218
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIViahrLSTI-RN----ADRILVLDDGRIVEQGTH 558
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-187 |
1.76e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 107.02 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIM--NRYDI-----VKDYRK 76
Cdd:COG4161 3 IQLKNINCFYGSH---QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIagHQFDFsqkpsEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 77 IRQIIGYMPGKFSLYQDLSVEENL-----KFFATLFGTTIEENYHLIKDIyqQIEPFKNRRAGALSGGMKQKLALSCALI 151
Cdd:COG4161 80 LRQKVGMVFQQYNLWPHLTVMENLieapcKVLGLSKEQAREKAMKLLARL--RLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 2526563825 152 HKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGIT 187
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGIT 193
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-225 |
2.16e-27 |
|
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: 112.41 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKSGKKnALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIG 82
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSP-AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQI--EPFKNRRAGALSGGMKQKLALSCALIHKPEILILD 160
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLglSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLD 2095
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526563825 161 EPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEA-GRCDRIALIREGKFIASDTPKGIIDKF 225
Cdd:TIGR01257 2096 EPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECeALCTRLAIMVKGAFQCLGTIQHLKSKF 2161
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-221 |
2.41e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.52 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 21 ALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV-----KDYRKIRQIIGYMpGKFSLYQ--D 93
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknKDIKQIRKKVGLV-FQFPESQlfE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 94 LSVEENLKFFATLFGTTIEENYHLIKDIYQQI---EPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVS 170
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVSQEEAEALAREKLALVgisESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 171 RKEFWDMLARLKEQGITILLSTAYMDE-AGRCDRIALIREGKFIASDTPKGI 221
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-218 |
3.23e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 107.40 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 21 ALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI------VKDYRKIRQIIG--YMPGKFSLYQ 92
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkkIKEVKRLRKEIGlvFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 93 DlSVEENLKFFATLFGTTIEENYHLIK---DIYQQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPV 169
Cdd:PRK13645 106 E-TIEKDIAFGPVNLGENKQEAYKKVPellKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 170 SRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTP 218
Cdd:PRK13645 185 GEEDFINLFERLnKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSP 235
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-229 |
5.88e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.87 E-value: 5.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvKDY--RKIRQI 80
Cdd:PRK11231 2 TLRTENLTVGYGT---KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI-SMLssRQLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 81 IGYMPGKFSLYQDLSVEENLKF----FATLFGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIHKP 154
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVAYgrspWLSLWGRLSAEDNARVNQAMEqtRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526563825 155 EILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGIIdkfTESL 229
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM---TPGL 230
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-214 |
7.51e-27 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 104.59 E-value: 7.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYgKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQIIG 82
Cdd:cd03245 3 IEFRNVSFSY-PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPgkfslyQDlsveenlkffATLFGTTIEEN----YHLIKD--IYQQIE-----PFKNR-----------RAGALSGGM 140
Cdd:cd03245 82 YVP------QD----------VTLFYGTLRDNitlgAPLADDerILRAAElagvtDFVNKhpngldlqigeRGRGLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 141 KQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEqGITILLSTAYMDEAGRCDRIALIREGKFIA 214
Cdd:cd03245 146 RQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLLDLVDRIIVMDSGRIVA 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-226 |
8.35e-27 |
|
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: 109.51 E-value: 8.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYG--KSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIR-- 78
Cdd:TIGR03269 279 IIKVRNVSKRYIsvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGpd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 ------QIIGYMPGKFSLYQDLSVEENLkffATLFGTTIEENYHLIKDIY---------QQIEPFKNRRAGALSGGMKQK 143
Cdd:TIGR03269 359 grgrakRYIGILHQEYDLYPHRTVLDNL---TEAIGLELPDELARMKAVItlkmvgfdeEKAEEILDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 144 LALSCALIHKPEILILDEPTTGVDPVSRKEFWD--MLARlKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKG 220
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsiLKAR-EEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEE 514
|
....*.
gi 2526563825 221 IIDKFT 226
Cdd:TIGR03269 515 IVEELT 520
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-192 |
9.94e-27 |
|
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: 104.41 E-value: 9.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKknALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRK----IRQ 79
Cdd:cd03292 1 IEFINVTKTYPNGTA--ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 IIGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQI--EPFKNRRAGALSGGMKQKLALSCALIHKPEIL 157
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVglSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 2526563825 158 ILDEPTTGVDPVSRKEFWDMLARLKEQGITILLST 192
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAT 193
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-214 |
1.14e-26 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 109.45 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLhkSYGKSGKKNA-LNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAimnRYD--IVKDYRK--IR 78
Cdd:COG4618 331 LSVENL--TVVPPGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV---RLDgaDLSQWDReeLG 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIIGYMPgkfslyQDlsVEenlkffatLFGTTIEENyhlikdiyqqIEPFKN----------RRAGA------------- 135
Cdd:COG4618 406 RHIGYLP------QD--VE--------LFDGTIAEN----------IARFGDadpekvvaaaKLAGVhemilrlpdgydt 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 136 --------LSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGRCDRIALI 207
Cdd:COG4618 460 rigeggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVL 539
|
....*..
gi 2526563825 208 REGKFIA 214
Cdd:COG4618 540 RDGRVQA 546
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-278 |
1.14e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 105.90 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSY--GKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI------VKDYR 75
Cdd:PRK13637 3 IKIENLTHIYmeGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkkvkLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 76 KIRQIIGYMPgKFSLYQDlSVEENLKFFATLFGTTIEENYHLIKDIYQQI----EPFKNRRAGALSGGMKQKLALSCALI 151
Cdd:PRK13637 83 KKVGLVFQYP-EYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVgldyEDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 152 HKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGI---IDKFT 226
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVfkeVETLE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 227 ESLWAVegSRMSAILHELRNHEgikrsfafgdkIHITvDDDLQIDELKQYLL 278
Cdd:PRK13637 241 SIGLAV--PQVTYLVRKLRKKG-----------FNIP-DDIFTIEEAKEEIL 278
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-210 |
1.27e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 105.09 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDS---------GSAIMNRYDIVKD 73
Cdd:PRK09984 4 IIRVEKLAKTFNQH---QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 74 YRKIRQIIGYMPGKFSLYQDLSVEENL--------KFFATLFG-TTIEENYHLIKDIYQ-QIEPFKNRRAGALSGGMKQK 143
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENVligalgstPFWRTCFSwFTREQKQRALQALTRvGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526563825 144 LALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLSTAYMDEAGR-CDRIALIREG 210
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRyCERIVALRQG 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-187 |
1.45e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 104.71 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIM--NRYDI-----VKDYRK 76
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFsktpsDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 77 IRQIIGYMPGKFSLYQDLSVEENL-----KFFATLFGTTIEENYHLIKDIyqQIEPFKNRRAGALSGGMKQKLALSCALI 151
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPHLTVQQNLieapcRVLGLSKDQALARAEKLLERL--RLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 2526563825 152 HKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGIT 187
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGIT 193
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-218 |
1.94e-26 |
|
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: 104.05 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYG-KSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK---DYR-KI 77
Cdd:COG4181 8 IIELRGLTKTVGtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldeDARaRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 78 R-QIIGYMPGKFSLYQDLSVEENLKFFATLFGTtieenyhliKDIYQQIEPFKNR-----RAGA----LSGGMKQKLALS 147
Cdd:COG4181 88 RaRHVGFVFQSFQLLPTLTALENVMLPLELAGR---------RDARARARALLERvglghRLDHypaqLSGGEQQRVALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 148 CALIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGRCDRIALIREGKfIASDTP 218
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAARCDRVLRLRAGR-LVEDTA 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-221 |
5.39e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 105.69 E-value: 5.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI--VKDYRKirqI 80
Cdd:PRK11607 19 LLEIRNLTKSFDG---QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLshVPPYQR---P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 81 IGYMPGKFSLYQDLSVEENLKF-------FATLFGTTIEENYHLIkdiyqQIEPFKNRRAGALSGGMKQKLALSCALIHK 153
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFglkqdklPKAEIASRVNEMLGLV-----HMQEFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526563825 154 PEILILDEPTTGVDPVSRK----EFWDMLARLkeqGITILLSTAYMDEA-GRCDRIALIREGKFIASDTPKGI 221
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-221 |
5.68e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 105.80 E-value: 5.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK---DYRKIRQI 80
Cdd:PRK09452 15 VELRGISKSFDG---KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpaENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 81 IGympgKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIHKPEILI 158
Cdd:PRK09452 92 FQ----SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRmvQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526563825 159 LDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLSTAYMDEA-GRCDRIALIREGKFIASDTPKGI 221
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEAlTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-219 |
6.47e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 103.66 E-value: 6.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKD-YRKIRQ 79
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 IIGYmpgkfsLYQD-------LSVEENLKFFATLFGTTIEENYHLIKDIYQQI--EPFKNRRAGALSGGMKQKLALSCAL 150
Cdd:PRK13650 82 KIGM------VFQNpdnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVgmQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 151 IHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLSTAYMDEAGRCDRIALIREGKFIASDTPK 219
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPR 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-222 |
1.16e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 105.31 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI-VKDYRKIRQ 79
Cdd:PRK09536 1 MPMIDVSDLSVEFGDT---TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 IIGYMPGKFSLYQDLSVEENLKFFAT----LFGTTIEENYHLIKDIYQQIE--PFKNRRAGALSGGMKQKLALSCALIHK 153
Cdd:PRK09536 78 RVASVPQDTSLSFEFDVRQVVEMGRTphrsRFDTWTETDRAAVERAMERTGvaQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 154 PEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGII 222
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-223 |
1.22e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 105.12 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYG---------------------KSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGS 62
Cdd:PRK10070 5 LEIKNLYKIFGehpqrafkyieqglskeqileKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 63 AIMNRYDIVK----DYRKIR-QIIGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQI--EPFKNRRAGA 135
Cdd:PRK10070 85 VLIDGVDIAKisdaELREVRrKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVglENYAHSYPDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 136 LSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLK-EQGITILLSTAYMDEAGRC-DRIALIREGKFI 213
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVV 244
|
250
....*....|
gi 2526563825 214 ASDTPKGIID 223
Cdd:PRK10070 245 QVGTPDEILN 254
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-214 |
2.37e-25 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 103.66 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTlFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIG- 82
Cdd:NF000106 14 VEVRGLVKHFGEV---KAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALIHKPEILILD 160
Cdd:NF000106 90 HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERfsLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2526563825 161 EPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIA 214
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIA 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-189 |
4.63e-25 |
|
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: 99.36 E-value: 4.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 17 GKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIGYMPGKFSLYQDLSV 96
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 97 EENLKFFATLFGTTIeenyhliKDIYQQIEP-----FKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSR 171
Cdd:TIGR01189 91 LENLHFWAAIHGGAQ-------RTIEDALAAvgltgFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170
....*....|....*....
gi 2526563825 172 KEFWDML-ARLKEQGITIL 189
Cdd:TIGR01189 164 ALLAGLLrAHLARGGIVLL 182
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-221 |
6.51e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.24 E-value: 6.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASL--ILPD---SGSAIMNRYDIVK---DY 74
Cdd:PRK14239 5 ILQVSDLSVYYNK---KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSprtDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 75 RKIRQIIGYM-----PGKFSLYQ-----------------DLSVEENLKffatlfGTTIEENyhlIKDIYQQiepfknrR 132
Cdd:PRK14239 82 VDLRKEIGMVfqqpnPFPMSIYEnvvyglrlkgikdkqvlDEAVEKSLK------GASIWDE---VKDRLHD-------S 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 133 AGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQgITILLSTAYMDEAGR-CDRIALIREGK 211
Cdd:PRK14239 146 ALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRiSDRTGFFLDGD 224
|
250
....*....|
gi 2526563825 212 FIASDTPKGI 221
Cdd:PRK14239 225 LIEYNDTKQM 234
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-218 |
7.75e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.23 E-value: 7.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvKDY--RKIRQI 80
Cdd:PRK13548 2 MLEARNLSVRLGG---RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPL-ADWspAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 81 IGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALI------H 152
Cdd:PRK13548 78 RAVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQvdLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 153 KPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITIL-------LSTAYmdeagrCDRIALIREGKFIASDTP 218
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIvvlhdlnLAARY------ADRIVLLHQGRLVADGTP 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-236 |
8.84e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 102.08 E-value: 8.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIiGY 83
Cdd:PRK10851 3 IEIANIKKSFGRT---QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKV-GF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIK-DIYQ-----QIEPFKNRRAGALSGGMKQKLALSCALIHKPEIL 157
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKaKVTQllemvQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 158 ILDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLSTAYMDEAGR-CDRIALIREGKFIASDTPkgiidkftESLWAVEGS 235
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTP--------DQVWREPAT 230
|
.
gi 2526563825 236 R 236
Cdd:PRK10851 231 R 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-192 |
1.22e-24 |
|
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: 98.33 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 22 LNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIGYMPGKFSLYQDLSVEENLK 101
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 102 FFATLFGT-TIEENYHLIkdiyqQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLAR 180
Cdd:cd03231 96 FWHADHSDeQVEEALARV-----GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG 170
|
170
....*....|..
gi 2526563825 181 LKEQGITILLST 192
Cdd:cd03231 171 HCARGGMVVLTT 182
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-214 |
1.47e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.80 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 5 EVKDLhkSYGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV-KDYRKIRQI-IG 82
Cdd:COG3845 259 EVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITgLSPRERRRLgVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPG---KFSLYQDLSVEENL---KFFATLFGTTIEENYHLIKDIYQQ-IEPFK------NRRAGALSGGMKQKLALSCA 149
Cdd:COG3845 337 YIPEdrlGRGLVPDMSVAENLilgRYRRPPFSRGGFLDRKAIRAFAEElIEEFDvrtpgpDTPARSLSGGNQQKVILARE 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526563825 150 LIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEA-GRCDRIALIREGKFIA 214
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEIlALSDRIAVMYEGRIVG 482
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-230 |
1.90e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.90 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSY--GKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV-----KDYRK 76
Cdd:PRK13641 3 IKFENVDYIYspGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 77 IRQIIGyMPGKFSLYQ--DLSVEENLKFFATLFGTTIEENYHLIKDIYQQI---EPFKNRRAGALSGGMKQKLALSCALI 151
Cdd:PRK13641 83 LRKKVS-LVFQFPEAQlfENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVglsEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 152 HKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDE-AGRCDRIALIREGKFIASDTPKGIidkFTESLW 230
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDvAEYADDVLVLEHGKLIKHASPKEI---FSDKEW 238
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-218 |
1.99e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.78 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 2 KMIEVKDLHKSYGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV-KDYRKIRQI 80
Cdd:PRK13642 3 KILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 81 IGYM-PGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQIE--PFKNRRAGALSGGMKQKLALSCALIHKPEIL 157
Cdd:PRK13642 83 IGMVfQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNmlDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 158 ILDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLSTAYMDEAGRCDRIALIREGKFIASDTP 218
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAP 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-224 |
2.32e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.42 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYgKSGKKnALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSA-IMNRYDIVKDYRKIRQIIG 82
Cdd:PRK13647 5 IEVEDLHFRY-KDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YmpgkfsLYQD-------LSVEENLKFFATLFGTTIEENYHLIKDIYQQI--EPFKNRRAGALSGGMKQKLALSCALIHK 153
Cdd:PRK13647 83 L------VFQDpddqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVrmWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 154 PEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGIIDK 224
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
3-218 |
2.44e-24 |
|
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: 100.95 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVkDLHKSYGKSgkknALNgISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKI----- 77
Cdd:COG4148 2 MLEV-DFRLRRGGF----TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIflpph 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 78 -RQIiGYMpgkF---SLYQDLSVEENLkffatLFG---TTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSC 148
Cdd:COG4148 76 rRRI-GYV---FqeaRLFPHLSVRGNL-----LYGrkrAPRAERRISFDEVVEllGIGHLLDRRPATLSGGERQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 149 ALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLSTAYMDEAGR-CDRIALIREGKFIASDTP 218
Cdd:COG4148 147 ALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPL 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-211 |
3.61e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.60 E-value: 3.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 6 VKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNR---YDIVKDYRKIRQIIG 82
Cdd:PRK11247 15 LNAVSKRYGE---RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTaplAEAREDTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPGKfslyqdlSVEENLkffatlfGTTIEENYHliKDIYQQIEPFK-NRRAG----ALSGGMKQKLALSCALIHKPEIL 157
Cdd:PRK11247 92 LLPWK-------KVIDNV-------GLGLKGQWR--DAALQALAAVGlADRANewpaALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2526563825 158 ILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEA-GRCDRIALIREGK 211
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAvAMADRVLLIEEGK 211
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-215 |
3.79e-24 |
|
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: 96.23 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKKnALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIGY 83
Cdd:cd03247 1 LSINNVSFSYPEQEQQ-VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPGKfslyqdlsveenlkffATLFGTTIEENYhlikdiyqqiepfkNRRagaLSGGMKQKLALSCALIHKPEILILDEPT 163
Cdd:cd03247 80 LNQR----------------PYLFDTTLRNNL--------------GRR---FSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2526563825 164 TGVDPVSRKEFWDMLAR-LKEQgiTILLSTAYMDEAGRCDRIALIREGKFIAS 215
Cdd:cd03247 127 VGLDPITERQLLSLIFEvLKDK--TLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-213 |
6.52e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 97.68 E-value: 6.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLI--LPD---SGSAIMNRYDIVK--- 72
Cdd:PRK14247 1 MNKIEIRDLKVSFGQV---EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelYPEarvSGEVYLDGQDIFKmdv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 73 -DYRKIRQIIGYMPGKFSlyqDLSVEENLKFFATL-----FGTTIEENYHLIKDIYQQIEPFKNR---RAGALSGGMKQK 143
Cdd:PRK14247 78 iELRRRVQMVFQIPNPIP---NLSIFENVALGLKLnrlvkSKKELQERVRWALEKAQLWDEVKDRldaPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 144 LALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQgITILLSTAYMDEAGRC-DRIALIREGKFI 213
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARIsDYVAFLYKGQIV 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-214 |
7.06e-24 |
|
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: 96.41 E-value: 7.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 26 SFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvkdyrkirqiiGYMPGK----FSLYQD------LS 95
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-----------TAAPPAdrpvSMLFQEnnlfahLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 96 VEENLkffatlfGTTIEENYHL-------IKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGV 166
Cdd:cd03298 87 VEQNV-------GLGLSPGLKLtaedrqaIEVALARvgLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2526563825 167 DPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGRC-DRIALIREGKFIA 214
Cdd:cd03298 160 DPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIAA 209
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-248 |
7.74e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.14 E-value: 7.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLhkSYGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDiVKDYRK---IRQ 79
Cdd:PRK13644 1 MIRLENV--SYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-TGDFSKlqgIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 IIGYM-PGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQI--EPFKNRRAGALSGGMKQKLALSCALIHKPEI 156
Cdd:PRK13644 78 LVGIVfQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIglEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 157 LILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGRCDRIALIREGKFIASDTPKGIIDKFTESLWAVEGSR 236
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPS 237
|
250
....*....|..
gi 2526563825 237 MSAILHELRNHE 248
Cdd:PRK13644 238 LIELAENLKMHG 249
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-163 |
8.09e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 8.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 6 VKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNrydivKDYRkirqiIGYMP 85
Cdd:COG0488 1 LENLSKSFGG---RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-----KGLR-----IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 86 GKFSLYQDLSVEEN-LKFFATLF------------GTTIEENYHLIKDIYQQIE-----------------------PFk 129
Cdd:COG0488 68 QEPPLDDDLTVLDTvLDGDAELRaleaeleeleakLAEPDEDLERLAELQEEFEalggweaearaeeilsglgfpeeDL- 146
|
170 180 190
....*....|....*....|....*....|....
gi 2526563825 130 NRRAGALSGGMKQKLALSCALIHKPEILILDEPT 163
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-218 |
1.05e-23 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 99.03 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 25 ISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKI-----RQIIGYMPGKFSLYQDLSVEEN 99
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppeKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 100 LKFfaTLFGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDM 177
Cdd:TIGR02142 96 LRY--GMKRARPSERRISFERVIEllGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2526563825 178 LARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTP 218
Cdd:TIGR02142 174 LERLhAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPI 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-219 |
1.08e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.93 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 18 KKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV-----KDYRKIRQIIGyMPGKF---S 89
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdKYIRPVRKRIG-MVFQFpesQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 90 LYQDlSVEENLKFFATLFGTTIEE----NYHLI------KDIYQQiEPFKnrragaLSGGMKQKLALSCALIHKPEILIL 159
Cdd:PRK13646 98 LFED-TVEREIIFGPKNFKMNLDEvknyAHRLLmdlgfsRDVMSQ-SPFQ------MSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 160 DEPTTGVDPVSRKEFWDMLARLK-EQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPK 219
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPK 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-204 |
5.32e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.40 E-value: 5.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 15 KSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV----KDYrkiRQIIGYMPGKFSL 90
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlkpEIY---RQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 91 YQDlSVEENLKFFATLFGTTIEENyHLIKDI--YQQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDP 168
Cdd:PRK10247 93 FGD-TVYDNLIFPWQIRNQQPDPA-IFLDDLerFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 2526563825 169 VSRKEFWDMLARL-KEQGITILLSTAYMDEAGRCDRI 204
Cdd:PRK10247 171 SNKHNVNEIIHRYvREQNIAVLWVTHDKDEINHADKV 207
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-224 |
7.65e-23 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 94.22 E-value: 7.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGksGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvKDYR--KIRQII 81
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI-REVTldSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYMPGKFSLYQDlSVEENLKfFATLfGTTIEENYHLIK--DIYQQIEPFKN-------RRAGALSGGMKQKLALSCALIH 152
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIR-YGRP-DATDEEVIEAAKaaQIHDKIMRFPDgydtivgERGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526563825 153 KPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITIL----LSTAyMDeagrCDRIALIREGKFIASDTPKGIIDK 224
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIViahrLSTI-VN----ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-213 |
8.30e-23 |
|
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: 94.22 E-value: 8.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvKDY--RKIRQII 81
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV-RDYtlASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYMPGKFSLYQDlSVEENLKFfaTLFGTTIEE--------NYH-LIKDIYQQIEPFKNRRAGALSGGMKQKLALSCALIH 152
Cdd:cd03251 79 GLVSQDVFLFND-TVAENIAY--GRPGATREEveeaaraaNAHeFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526563825 153 KPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITIL----LSTAYmdeagRCDRIALIREGKFI 213
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKNRTTFViahrLSTIE-----NADRIVVLEDGKIV 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-218 |
8.47e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 94.26 E-value: 8.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 26 SFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRydivKDYRKIRqiigymPGK--FS-LYQdlsvEENLkf 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG----QDHTTTP------PSRrpVSmLFQ----ENNL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 103 FATLfgtTIEEN---------------YHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTG 165
Cdd:PRK10771 83 FSHL---TVAQNiglglnpglklnaaqREKLHAIARQmgIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2526563825 166 VDPVSRKEfwdMLARLK----EQGITILLSTAYMDEAGR-CDRIALIREGKfIASDTP 218
Cdd:PRK10771 160 LDPALRQE---MLTLVSqvcqERQLTLLMVSHSLEDAARiAPRSLVVADGR-IAWDGP 213
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-219 |
1.21e-22 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 93.76 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLfrilASLIL----PDSGSAIMNRYDIvKDY--RKI 77
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTV----VSLLErfydPTSGEILLDGVDI-RDLnlRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 78 RQIIGYMPGKFSLYqDLSVEENLKFfaTLFGTTIEENYHLIKD--IYQQIEPFKNR-------RAGALSGGMKQKLALSC 148
Cdd:cd03249 76 RSQIGLVSQEPVLF-DGTIAENIRY--GKPDATDEEVEEAAKKanIHDFIMSLPDGydtlvgeRGSQLSGGQKQRIAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526563825 149 ALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEqGITIL-----LSTAYmdeagRCDRIALIREGKFIASDTPK 219
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAESEKLVQEALDRAMK-GRTTIviahrLSTIR-----NADLIAVLQNGQVVEQGTHD 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-224 |
1.83e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.48 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYgKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGS-------AIMNRYDIVKDYRK 76
Cdd:PRK13640 6 VEFKHVSFTY-PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 77 IRQIIGYMPGkfSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQIE--PFKNRRAGALSGGMKQKLALSCALIHKP 154
Cdd:PRK13640 85 KVGIVFQNPD--NQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGmlDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 155 EILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGRCDRIALIREGKFIASDTPKGIIDK 224
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-204 |
2.93e-22 |
|
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: 96.59 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGksGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQIIG 82
Cdd:TIGR02857 322 LEFSGVSVAYP--GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPGKFSLYQDlSVEENLKFF---ATlfGTTIEENYH------LIKDIYQQIEPFKNRRAGALSGGMKQKLALSCALIHK 153
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLArpdAS--DAEIREALEragldeFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 154 PEILILDEPTTGVDPVSRKEFWDMLARLKeQGITILLSTAYMDEAGRCDRI 204
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALADRI 526
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-218 |
4.05e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 92.87 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvKDYR-----KI 77
Cdd:COG4559 1 MLEAENLSVRLGG---RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL-AAWSpwelaRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 78 RqiiGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCAL--IHK 153
Cdd:COG4559 77 R---AVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALvgLAHLAGRSYQTLSGGEQQRVQLARVLaqLWE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526563825 154 PE-----ILILDEPTTGVDPVSRKEFWDMLARLKEQGITIL-------LSTAYmdeagrCDRIALIREGKFIASDTP 218
Cdd:COG4559 154 PVdggprWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVavlhdlnLAAQY------ADRILLLHQGRLVAQGTP 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-224 |
5.85e-22 |
|
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: 91.90 E-value: 5.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRK-IRQIIG 82
Cdd:cd03254 3 IEFENVNFSYDE--KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKsLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPGKFSLYQDlSVEENLKFF-----------------ATLFgttIEenyHLIKDIYQQIEPfknrRAGALSGGMKQKLA 145
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLGrpnatdeevieaakeagAHDF---IM---KLPNGYDTVLGE----NGGNLSQGERQLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 146 LSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITIL----LSTAYmdeagRCDRIALIREGKFIASDTPKGI 221
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIiahrLSTIK-----NADKILVLDDGKIIEEGTHDEL 224
|
...
gi 2526563825 222 IDK 224
Cdd:cd03254 225 LAK 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-198 |
1.10e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 91.85 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSY-GKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSaimnrydIVKDYRKIRQ 79
Cdd:COG4525 1 MSMLTVRHVSVRYpGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGE-------ITLDGVPVTG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 iigymPG--------KFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQI--EPFKNRRAGALSGGMKQKLALSCA 149
Cdd:COG4525 74 -----PGadrgvvfqKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVglADFARRRIWQLSGGMRQRVGIARA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2526563825 150 LIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEA 198
Cdd:COG4525 149 LAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEA 198
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-263 |
1.79e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 91.72 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKSG--KKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNryDIV-------KD 73
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIVvsstskqKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 74 YRKIRQIIG--YMPGKFSLYQDlSVEENLKFFATLFGTTIEENYHLIKDIYQQI---EPFKNRRAGALSGGMKQKLALSC 148
Cdd:PRK13643 79 IKPVRKKVGvvFQFPESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVglaDEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 149 ALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDE-AGRCDRIALIREGKFIASDTPKgiiDKFTE 227
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDvADYADYVYLLEKGHIISCGTPS---DVFQE 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 2526563825 228 slwavegsrmsaiLHELRNHE-GIKRSFAFGDKIHIT 263
Cdd:PRK13643 235 -------------VDFLKAHElGVPKATHFADQLQKT 258
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-218 |
1.80e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.22 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 21 ALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSA----IMNRYDI-------------VKDYRKIRQIIGy 83
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKnnhelitnpyskkIKNFKELRRRVS- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPGKFSLYQDL--SVEENLKFFATLFGTTIEENYHLIKDIYQQI---EPFKNRRAGALSGGMKQKLALSCALIHKPEILI 158
Cdd:PRK13631 120 MVFQFPEYQLFkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMgldDSYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526563825 159 LDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMD---EAGrcDRIALIREGKFIASDTP 218
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEhvlEVA--DEVIVMDKGKILKTGTP 260
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-210 |
1.86e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 90.60 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 22 LNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMnrydivkdyrKIRQIIGYMPGKFSLYQD------LS 95
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL----------EGKQITEPGPDRMVVFQNysllpwLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 96 VEEN--LKFFATLFGTTIEENYHLIKDIYQQI--EPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSR 171
Cdd:TIGR01184 71 VRENiaLAVDRVLPDLSKSERRAIVEEHIALVglTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2526563825 172 KEFWDMLARL-KEQGITILLSTAYMDEA-GRCDRIALIREG 210
Cdd:TIGR01184 151 GNLQEELMQIwEEHRVTVLMVTHDVDEAlLLSDRVVMLTNG 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-207 |
2.40e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.22 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 21 ALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAImnrydivkdyRKIRQIIGYMPGKFSLYQDL--SVEE 98
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR----------RAGGARVAYVPQRSEVPDSLplTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 99 --NLKFFA--TLFGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRK 172
Cdd:NF040873 77 lvAMGRWArrGLWRRLTRDDRAAVDDALErvGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 2526563825 173 EFWDMLARLKEQGITILLSTAYMDEAGRCDRIALI 207
Cdd:NF040873 157 RIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
17-184 |
4.86e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 89.79 E-value: 4.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 17 GKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSaimnrydiVKDYRKIRqiIGYMPGKfsLYQDLSV 96
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV--------IKRNGKLR--IGYVPQK--LYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 97 EENLKFFATLFGTTIEENY----------HLIKDIYQQiepfknrragaLSGGMKQKLALSCALIHKPEILILDEPTTGV 166
Cdd:PRK09544 83 PLTVNRFLRLRPGTKKEDIlpalkrvqagHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170
....*....|....*...
gi 2526563825 167 DPVSRKEFWDMLARLKEQ 184
Cdd:PRK09544 152 DVNGQVALYDLIDQLRRE 169
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-213 |
4.95e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 89.81 E-value: 4.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKD------- 73
Cdd:PRK11264 1 MSAIEVKNLVKKFHG---QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 74 --YRKIRQIIGYMPGKFSLYQDLSVEENLKFFATLF-GTTIEENYHLIKDIYQQI-----EPFKNRRagaLSGGMKQKLA 145
Cdd:PRK11264 78 glIRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVkGEPKEEATARARELLAKVglagkETSYPRR---LSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526563825 146 LSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFI 213
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIV 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-192 |
6.89e-21 |
|
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: 92.42 E-value: 6.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGksGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQIIG 82
Cdd:TIGR02868 335 LELRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPgkfslyQDlsveenlkffATLFGTTIEENYHLIK------DIYQQIEpfknrRAG---------------------A 135
Cdd:TIGR02868 413 VCA------QD----------AHLFDTTVRENLRLARpdatdeELWAALE-----RVGladwlralpdgldtvlgeggaR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2526563825 136 LSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFW-DMLARLkeQGITILLST 192
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLeDLLAAL--SGRTVVLIT 527
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-211 |
1.16e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 91.60 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 22 LNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRK--IRQIIGYMP------GkfsLYQD 93
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdgLANGIVYISedrkrdG---LVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 94 LSVEEN-----LKFFATLFGTTIEENYHLIKDIYQQI----EPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTT 164
Cdd:PRK10762 345 MSVKENmsltaLRYFSRAGGSLKHADEQQAVSDFIRLfnikTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2526563825 165 GVDPVSRKEFWDMLARLKEQGITILLSTAYMDEA-GRCDRIALIREGK 211
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVlGMSDRILVMHEGR 472
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-211 |
1.44e-20 |
|
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: 85.58 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGsaimnrydIVKDYRKIRqiIGY 83
Cdd:cd03221 1 IELENLSKTYGG---KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG--------IVTWGSTVK--IGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPgkfslyQdlsveenlkffatlfgttieenyhlikdiyqqiepfknrragaLSGGMKQKLALSCALIHKPEILILDEPT 163
Cdd:cd03221 68 FE------Q-------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2526563825 164 TGVDPVSRKEFWDMLarLKEQGITILLS--TAYMDEAgrCDRIALIREGK 211
Cdd:cd03221 99 NHLDLESIEALEEAL--KEYPGTVILVShdRYFLDQV--ATKIIELEDGK 144
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-227 |
1.49e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 91.65 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 15 KSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPD---SGSAIMNryDIVKDYRKIRQIIGYmpgkfsLY 91
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLN--GMPIDAKEMRAISAY------VQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 92 QD------LSVEENLKFFATLF---GTTIEENYHLIKDIYQQ--IEPFKNRRAGA------LSGGMKQKLALSCALIHKP 154
Cdd:TIGR00955 106 QDdlfiptLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQAlgLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526563825 155 EILILDEPTTGVDPVSRKEFWDMLARLKEQGITILL------STAYmdeaGRCDRIALIREGKFIASDTPKGIIDKFTE 227
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICtihqpsSELF----ELFDKIILMAEGRVAYLGSPDQAVPFFSD 260
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-198 |
2.78e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.83 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSaimnrydIVKDYRKIRQiig 82
Cdd:PRK11248 1 MLQISHLYADYGG---KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGS-------ITLDGKPVEG--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 ymPG--KFSLYQD------LSVEENLKFFATLFGTTIEENYHLIKDIYQQI--EPFKNRRAGALSGGMKQKLALSCALIH 152
Cdd:PRK11248 68 --PGaeRGVVFQNegllpwRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVglEGAEKRYIWQLSGGQRQRVGIARALAA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2526563825 153 KPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEA 198
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEA 192
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-227 |
6.05e-20 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 87.01 E-value: 6.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILaslilpdsgsaimNR-YDIVKDYR------- 75
Cdd:COG1117 12 IEVRNLNVYYGD---KQALKDINLDIPENKVTALIGPSGCGKSTLLRCL-------------NRmNDLIPGARvegeill 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 76 -------------KIRQIIGYMPGKfslyqdlsveenlkffATLFGTTIEEN------YHLIKD--IYQQI--------- 125
Cdd:COG1117 76 dgediydpdvdvvELRRRVGMVFQK----------------PNPFPKSIYDNvayglrLHGIKSksELDEIveeslrkaa 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 126 --EPFKNR---RAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQgITILLSTAYMDEAGR 200
Cdd:COG1117 140 lwDEVKDRlkkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAAR 218
|
250 260 270
....*....|....*....|....*....|..
gi 2526563825 201 C-DRIALIREGKFIASDTPKGI----IDKFTE 227
Cdd:COG1117 219 VsDYTAFFYLGELVEFGPTEQIftnpKDKRTE 250
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-204 |
6.09e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 86.33 E-value: 6.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKS---YGKSGKK-NALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSaIMNRY-----DIVK- 72
Cdd:COG4778 4 LLEVENLSKTftlHLQGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGS-ILVRHdggwvDLAQa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 73 DYRKI----RQIIGY-------MPGKFSLyqDLsVEENLKffatLFGTTIEENYhlikdiyqqiepfknRRAGAL----- 136
Cdd:COG4778 83 SPREIlalrRRTIGYvsqflrvIPRVSAL--DV-VAEPLL----ERGVDREEAR---------------ARARELlarln 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 137 -------------SGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILlsTAYMDEAGR--- 200
Cdd:COG4778 141 lperlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII--GIFHDEEVReav 218
|
....
gi 2526563825 201 CDRI 204
Cdd:COG4778 219 ADRV 222
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-211 |
6.38e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.78 E-value: 6.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQ--- 79
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRqva 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 IIGYMPGKFSlyqdLSVEENLKFfaTLFGTTIEE--------NYH-LIKDIYQQIEPFKNRRAGALSGGMKQKLALSCAL 150
Cdd:TIGR00958 559 LVGQEPVLFS----GSVRENIAY--GLTDTPDEEimaaakaaNAHdFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARAL 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 151 IHKPEILILDEPTTGVDPVSRKEFWDMLARlkeQGITILLSTAYMDEAGRCDRIALIREGK 211
Cdd:TIGR00958 633 VRKPRVLILDEATSALDAECEQLLQESRSR---ASRTVLLIAHRLSTVERADQILVLKKGS 690
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-171 |
6.71e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 6.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 2 KMIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNrydivkdyRKIRqiI 81
Cdd:COG0488 314 KVLELEGLSKSYGD---KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG--------ETVK--I 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYmpgkFSLYQD-LSVEENLkffatlfgttIEEnyhlIKDIYQQIEP-----------FK----NRRAGALSGGMKQKLA 145
Cdd:COG0488 381 GY----FDQHQEeLDPDKTV----------LDE----LRDGAPGGTEqevrgylgrflFSgddaFKPVGVLSGGEKARLA 442
|
170 180
....*....|....*....|....*.
gi 2526563825 146 LSCALIHKPEILILDEPTTGVDPVSR 171
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLDIETL 468
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-192 |
2.93e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 83.70 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 24 GISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK---DYRKIRQIIGYMPGkfsLYQDLSVEENL 100
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRqrdEYHQDLLYLGHQPG---IKTELTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 101 KFFATLFGTTIEENyhlIKDIYQQI--EPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDML 178
Cdd:PRK13538 96 RFYQRLHGPGDDEA---LWEALAQVglAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
170
....*....|....
gi 2526563825 179 ARLKEQGITILLST 192
Cdd:PRK13538 173 AQHAEQGGMVILTT 186
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-218 |
3.25e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.86 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYgKSGKKN--ALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGS--------AIMNRyDIVK 72
Cdd:PRK10535 4 LLELKDIRRSY-PSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdvATLDA-DALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 73 DYRkiRQIIGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQI--EPFKNRRAGALSGGMKQKLALSCAL 150
Cdd:PRK10535 82 QLR--REHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLglEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526563825 151 IHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGRCDRIALIREGKfIASDTP 218
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGE-IVRNPP 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-191 |
7.17e-19 |
|
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: 83.47 E-value: 7.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 14 GKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPD---SGSAIMNRYDIVKDyrKIRQIIGYMPGKFSL 90
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPD--QFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 91 YQDLSVEENLKFFATLFGT--------TIEENYHLIKDIyqQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEP 162
Cdd:cd03234 93 LPGLTVRETLTYTAILRLPrkssdairKKRVEDVLLRDL--ALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180
....*....|....*....|....*....
gi 2526563825 163 TTGVDPVSRKEFWDMLARLKEQGITILLS 191
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILT 199
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-218 |
8.07e-19 |
|
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: 82.85 E-value: 8.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKKnALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQIIG 82
Cdd:cd03369 7 IEVENLSVRYAPDLPP-VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPgkfslyQDlsveenlkffATLFGTTIEENYHlIKDIYQQIEPFKNRRAGA----LSGGMKQKLALSCALIHKPEILI 158
Cdd:cd03369 86 IIP------QD----------PTLFSGTIRSNLD-PFDEYSDEEIYGALRVSEgglnLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526563825 159 LDEPTTGVDPVS--------RKEFwdmlarlkeQGITILLSTAYMDEAGRCDRIALIREGKFIASDTP 218
Cdd:cd03369 149 LDEATASIDYATdaliqktiREEF---------TNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-232 |
8.97e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 83.59 E-value: 8.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV----KDYRKIR 78
Cdd:COG4604 1 MIEIKNVSKRYGG---KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAttpsRELAKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIigympgkfsLYQD------LSVEENLKF--FATLFGTTIEENYHLIKD-I-YQQIEPFKNRRAGALSGGMKQKLALSC 148
Cdd:COG4604 78 AI---------LRQEnhinsrLTVRELVAFgrFPYSKGRLTAEDREIIDEaIaYLDLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 149 ALIHKPEILILDEPTTGVDPV-SRkefwDMLARLK----EQGITILL-------STAYmdeagrCDRIALIREGKFIASD 216
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKhSV----QMMKLLRrladELGKTVVIvlhdinfASCY------ADHIVAMKDGRVVAQG 218
|
250
....*....|....*.
gi 2526563825 217 TPKGIIDkfTESLWAV 232
Cdd:COG4604 219 TPEEIIT--PEVLSDI 232
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-229 |
1.07e-18 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 86.33 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQIIG 82
Cdd:TIGR01193 474 IVINDVSYSYGYG--SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPGKFSLYqDLSVEENLKFFATLfGTTIEENYHL--IKDIYQQIEPFK-------NRRAGALSGGMKQKLALSCALIHK 153
Cdd:TIGR01193 552 YLPQEPYIF-SGSILENLLLGAKE-NVSQDEIWAAceIAEIKDDIENMPlgyqtelSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526563825 154 PEILILDEPTTGVDPVSRKEFWDMLARLKEQgiTILLSTAYMDEAGRCDRIALIREGKFIASDTPKGIIDK--FTESL 229
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRngFYASL 705
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-224 |
1.09e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 83.65 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYgKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV-KDYRKIRQII 81
Cdd:PRK13648 7 IIVFKNVSFQY-QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITdDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYMpgkFSLYQDLSVEENLKFfATLFGTtieENYHLIKDIYQQIEP----------FKNRRAGALSGGMKQKLALSCALI 151
Cdd:PRK13648 86 GIV---FQNPDNQFVGSIVKY-DVAFGL---ENHAVPYDEMHRRVSealkqvdmleRADYEPNALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 152 HKPEILILDEPTTGVDPVSRKEFWDMLARLK-EQGITILLSTAYMDEAGRCDRIALIREGKFIASDTPKGIIDK 224
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-211 |
1.40e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.52 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 2 KMIEVKDLHKSYGKSGKK-NALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLilpDSGSA--------IMNRYDivK 72
Cdd:PRK10584 5 NIVEVHHLKKSVGQGEHElSILTGVELVVKRGETIALIGESGSGKSTLLAILAGL---DDGSSgevslvgqPLHQMD--E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 73 DYR-KIR-QIIGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQIEPFK--NRRAGALSGGMKQKLALSC 148
Cdd:PRK10584 80 EARaKLRaKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKrlDHLPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 149 ALIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGRCDRIALIREGK 211
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLAARCDRRLRLVNGQ 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-224 |
2.41e-18 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 82.15 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 21 ALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI-VKDYRKIRQIIGYMpgkfslyqdlsVEEN 99
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGVV-----------LQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 100 lkffaTLFGTTIEENYHL----------------------IKDIYQQIEPFKNRRAGALSGGMKQKLALSCALIHKPEIL 157
Cdd:cd03252 86 -----VLFNRSIRDNIALadpgmsmervieaaklagahdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526563825 158 ILDEPTTGVDPVSRKEFWDMLARLKEqGITILLSTAYMDEAGRCDRIALIREGKFIASDTPKGIIDK 224
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-213 |
2.62e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.58 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAI--------MNRYDIVKDYR 75
Cdd:PRK14267 5 IETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVegevrlfgRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 76 KIRQIIGYM---PGKF---SLYQDLSVEENLKFFATLFGTTIEENYHLIKD--IYQQIEPFKNRRAGALSGGMKQKLALS 147
Cdd:PRK14267 82 EVRREVGMVfqyPNPFphlTIYDNVAIGVKLNGLVKSKKELDERVEWALKKaaLWDEVKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526563825 148 CALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQgITILLSTAYMDEAGR-CDRIALIREGKFI 213
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARvSDYVAFLYLGKLI 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-219 |
2.72e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.00 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKdyRKIRQI-IG 82
Cdd:PRK11432 7 VVLKNITKRFGSN---TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH--RSIQQRdIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILD 160
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALElvDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 161 EPTTGVDPVSRKEFWDMLARLKEQ-GITILLSTAYMDEA-GRCDRIALIREGKFIASDTPK 219
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAfAVSDTVIVMNKGKIMQIGSPQ 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-198 |
3.60e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.94 E-value: 3.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI--VKD-------- 73
Cdd:PRK10619 6 LNVIDLHKRYGE---HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlVRDkdgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 74 ----YRKIRQIIGYMPGKFSLYQDLSVEEN-LKFFATLFGTTIEENYHLIKDIYQQI---EPFKNRRAGALSGGMKQKLA 145
Cdd:PRK10619 83 dknqLRLLRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVgidERAQGKYPVHLSGGQQQRVS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2526563825 146 LSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEA 198
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFA 215
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-219 |
4.14e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.81 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 22 LNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLiLPDSGSAIMNRYDIvKDY--RKIRQIIGY----------MPGkF- 88
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPL-SDWsaAELARHRAYlsqqqsppfaMPV-Fq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 89 --SLYQDLSVEEnlkffatlfgttiEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQ--KLALSCALIHkPEI------ 156
Cdd:COG4138 89 ylALHQPAGASS-------------EAVEQLLAQLAEalGLEDKLSRPLTQLSGGEWQrvRLAAVLLQVW-PTInpegql 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 157 LILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPK 219
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRhADRVWLLKQGKLVASGETA 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-222 |
4.58e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.96 E-value: 4.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 17 GKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRK-IRQIIGYMPGKFSLYQDLS 95
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 96 VEENLKF----FATLFGTTIEENYHLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPV 169
Cdd:PRK10253 98 VQELVARgrypHQPLFTRWRKEDEEAVTKAMQAtgITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2526563825 170 SRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGII 222
Cdd:PRK10253 178 HQIDLLELLSELnREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-238 |
7.19e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 7.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYgkSGKkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQII 81
Cdd:PRK15439 11 LLCARSISKQY--SGV-EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYM-PGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQIEPfkNRRAGALSGGMKQKLALSCALIHKPEILILD 160
Cdd:PRK15439 88 IYLvPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDL--DSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 161 EPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGK--------------FIASDTPKGIIDKF 225
Cdd:PRK15439 166 EPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTialsgktadlstddIIQAITPAAREKSL 245
|
250
....*....|....*.
gi 2526563825 226 TES--LW-AVEGSRMS 238
Cdd:PRK15439 246 SASqkLWlELPGNRRQ 261
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-213 |
9.16e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.86 E-value: 9.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 5 EVKDLHKSYGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLI-LPDS-----GSAIMNRYDIVK-DYRKI 77
Cdd:PRK14246 9 DVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeIYDSkikvdGKVLYFGKDIFQiDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 78 RQIIGYMPGKFSLYQDLSVEENLKFFATLFGTT--------IEENYH---LIKDIYQQIepfkNRRAGALSGGMKQKLAL 146
Cdd:PRK14246 89 RKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKekreikkiVEECLRkvgLWKEVYDRL----NSPASQLSGGQQQRLTI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526563825 147 SCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGRCDRIALIREGKFI 213
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-217 |
2.55e-17 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 82.07 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKKnALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvKDY--RKIRQII 81
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRP-ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL-ADYtlASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYMPGKFSLYQDlSVEENLKFfATLFGTTIEENYHLIKDIYQQiePFKNR-----------RAGALSGGMKQKLALSCAL 150
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAY-GRTEQADRAEIERALAAAYAQ--DFVDKlplgldtpigeNGVLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 151 IHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITIL----LSTayMDEAgrcDRIALIREGKFIASDT 217
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQGRTTLViahrLST--IEKA---DRIVVMDDGRIVERGT 550
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-231 |
4.31e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.30 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 34 IFGVigpDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKI-----RQIIGYmpgkfsLYQD------LSVEENLKf 102
Cdd:PRK11144 29 IFGR---SGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppeKRRIGY------VFQDarlfphYKVRGNLR- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 103 fatlFGTTIEENYHLiKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLAR 180
Cdd:PRK11144 99 ----YGMAKSMVAQF-DKIVAllGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2526563825 181 L-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTpkgiidkfTESLWA 231
Cdd:PRK11144 174 LaREINIPILYVSHSLDEILRlADRVVVLEQGKVKAFGP--------LEEVWA 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-211 |
4.55e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.13 E-value: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 23 NGISFTVDDGEIFGVIGPDGAGKSTLFR-ILASLILPDSGSAIMN--RYDIVKDYRKIRQIIGYMP---GKFSLYQDLSV 96
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDgkPVKIRNPQQAIAQGIAMVPedrKRDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 97 EEN-----LKFFAtlFGTTIEENYHLiKDIYQQIEPFKNRRA------GALSGGMKQKLALSCALIHKPEILILDEPTTG 165
Cdd:PRK13549 359 GKNitlaaLDRFT--GGSRIDDAAEL-KTILESIQRLKVKTAspelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2526563825 166 VDPVSRKEFWDMLARLKEQGITILLSTAYMDEA-GRCDRIALIREGK 211
Cdd:PRK13549 436 IDVGAKYEIYKLINQLVQQGVAIIVISSELPEVlGLSDRVLVMHEGK 482
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-211 |
4.73e-17 |
|
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: 78.28 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIM-----NRYDiVKDYRKIR 78
Cdd:cd03248 12 VKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdgkpiSQYE-HKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIIGYMPGKFSLyqdlSVEENLKF------FATLFGTTIEENYH-LIKDIYQQIEPFKNRRAGALSGGMKQKLALSCALI 151
Cdd:cd03248 91 SLVGQEPVLFAR----SLQDNIAYglqscsFECVKEAAQKAHAHsFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526563825 152 HKPEILILDEPTTGVDPVSRKEfwdmlarlKEQGI-------TILLSTAYMDEAGRCDRIALIREGK 211
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQ--------VQQALydwperrTVLVIAHRLSTVERADQILVLDGGR 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-233 |
6.03e-17 |
|
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: 81.00 E-value: 6.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASL--ILPDSGSAIMNR-------------- 67
Cdd:TIGR03269 1 IEVKNLTKKFDG---KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHValcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 68 -------------------YDIVKDYRK-IRQIIGYMPGK-FSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQIE 126
Cdd:TIGR03269 78 vgepcpvcggtlepeevdfWNLSDKLRRrIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 127 pFKNRR---AGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDML-ARLKEQGITILLsTAYMDE--AGR 200
Cdd:TIGR03269 158 -LSHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeEAVKASGISMVL-TSHWPEviEDL 235
|
250 260 270
....*....|....*....|....*....|...
gi 2526563825 201 CDRIALIREGKFIASDTPKGIIDKFTESLWAVE 233
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAVFMEGVSEVE 268
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-218 |
8.39e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.51 E-value: 8.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 22 LNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvkDYRK-----IRQIIGYM---PGKFSLYQD 93
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL--DYSKrgllaLRQQVATVfqdPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 94 lsVEENLKFFATLFGTTIEENYHLIKDIYQQIEP--FKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSR 171
Cdd:PRK13638 95 --IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAqhFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2526563825 172 KEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTP 218
Cdd:PRK13638 173 TQMIAIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAP 220
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
5-188 |
9.50e-17 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 80.32 E-value: 9.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 5 EVKDLHKSYGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAimnrydivkDYRKIRQIIGYM 84
Cdd:PRK13545 23 KLKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV---------DIKGSAALIAIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 85 PGkfsLYQDLSVEENLKFFATLFGTTIEENYHLIKDI--YQQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEP 162
Cdd:PRK13545 94 SG---LNGQLTGIENIELKGLMMGLTKEKIKEIIPEIieFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEA 170
|
170 180
....*....|....*....|....*.
gi 2526563825 163 TTGVDPVSRKEFWDMLARLKEQGITI 188
Cdd:PRK13545 171 LSVGDQTFTKKCLDKMNEFKEQGKTI 196
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-215 |
1.14e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.83 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 2 KMIEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRydivKDYRKIRQII 81
Cdd:PRK09700 4 PYISMAGIGKSFGPV---HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN----INYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYMPGKFSLYQDLSVEENLKFFATLF----------GTTI-------EENYHLIKDIYQQIEPfkNRRAGALSGGMKQKL 144
Cdd:PRK09700 77 AAQLGIGIIYQELSVIDELTVLENLYigrhltkkvcGVNIidwremrVRAAMMLLRVGLKVDL--DEKVANLSISHKQML 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 145 ALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIAS 215
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCS 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-211 |
1.53e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 5 EVKDLhksYGKSGKKnaLNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV--KDYRKIRQIIG 82
Cdd:PRK09700 267 EVRNV---TSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprSPLDAVKKGMA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMP---------GKFSLYQDLSVEENLKF--FATLFGTTIEENYHLIKDIYQQIEPFK----NRRAGALSGGMKQKLALS 147
Cdd:PRK09700 342 YITesrrdngffPNFSIAQNMAISRSLKDggYKGAMGLFHEVDEQRTAENQRELLALKchsvNQNITELSGGNQQKVLIS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526563825 148 CALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDE-AGRCDRIALIREGK 211
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEiITVCDRIAVFCEGR 486
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-215 |
1.72e-16 |
|
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: 79.48 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 18 KKNALNGISFTVDDGEIFGVIGPDGAGKSTLFR-ILASLILPDSGSAIMN--RYDIVKDYRKIRQIIGYMP---GKFSLY 91
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINgkPVDIRNPAQAIRAGIAMVPedrKRHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 92 QDLSVEEN-----LKFFATLfgTTIEENYHLiKDIYQQIEPFKNRRA------GALSGGMKQKLALSCALIHKPEILILD 160
Cdd:TIGR02633 352 PILGVGKNitlsvLKSFCFK--MRIDAAAEL-QIIGSAIQRLKVKTAspflpiGRLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2526563825 161 EPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEA-GRCDRIALIREGKFIAS 215
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVlGLSDRVLVIGEGKLKGD 484
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-211 |
2.35e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 79.25 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 2 KMIEVKDLHKSYGKSGkkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI-VKDYRKIRQI 80
Cdd:PRK10522 321 QTLELRNVTFAYQDNG--FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 81 IGYMPGKFSLYQDL-----------SVEENLKFFATLFGTTIEENYhlIKDIyqqiepfknrragALSGGMKQKLALSCA 149
Cdd:PRK10522 399 FSAVFTDFHLFDQLlgpegkpanpaLVEKWLERLKMAHKLELEDGR--ISNL-------------KLSKGQKKRLALLLA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526563825 150 LIHKPEILILDEPTTGVDPVSRKEFW-DMLARLKEQGITILLST---AYMDEAgrcDRIALIREGK 211
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRREFYqVLLPLLQEMGKTIFAIShddHYFIHA---DRLLEMRNGQ 526
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-215 |
3.31e-16 |
|
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: 78.71 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGksGKKnALNGISFTVDDGEIFGVIGPDGAGKSTLFRILaSLILPD---SGSAIMNRYDIVKdyRKIRQ 79
Cdd:TIGR02633 1 LLEMKGIVKTFG--GVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKIL-SGVYPHgtwDGEIYWSGSPLKA--SNIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 I----IGYMPGKFSLYQDLSVEENLkFFA---TLFGTTIEEN--YHLIKDIYQQIE-PFKN--RRAGALSGGMKQKLALS 147
Cdd:TIGR02633 75 TeragIVIIHQELTLVPELSVAENI-FLGneiTLPGGRMAYNamYLRAKNLLRELQlDADNvtRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526563825 148 CALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDE-AGRCDRIALIREGKFIAS 215
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEvKAVCDTICVIRDGQHVAT 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-167 |
4.47e-16 |
|
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: 78.44 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 2 KMIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNryDIVKdyrkirqiI 81
Cdd:TIGR03719 321 KVIEAENLTKAFGD---KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETVK--------L 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYM--------PGKfSLYQDLS----------VEENLKFFATLFGttieenyhlIKDIYQQiepfknRRAGALSGGMKQK 143
Cdd:TIGR03719 388 AYVdqsrdaldPNK-TVWEEISggldiiklgkREIPSRAYVGRFN---------FKGSDQQ------KKVGQLSGGERNR 451
|
170 180
....*....|....*....|....
gi 2526563825 144 LALSCALIHKPEILILDEPTTGVD 167
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-213 |
4.66e-16 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 76.38 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSY------GKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGS--------AIMNRY 68
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTvsfrgqdlYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 69 DIVKDYRKIRQIIGYMPGKFSLYQDL--SVEENLKFFATLFGTTIEEN-YHLIKDIYQQIEpFKNRRAGALSGGMKQKLA 145
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPSAVNPRMTVrqIIGEPLRHLTSLDESEQKARiAELLDMVGLRSE-DADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 146 LSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLSTAYMDEAGR-CDRIALIREGKFI 213
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSfCQRVAVMDKGQIV 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-212 |
4.87e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.17 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 25 ISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIG--YMP---GKFSLYQDLSVEEN 99
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvYLPedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 100 --------LKFFA-TLFGTTIEENYHLIKDI-YQQIEpfknRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPV 169
Cdd:PRK15439 362 vcalthnrRGFWIkPARENAVLERYRRALNIkFNHAE----QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2526563825 170 SRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKF 212
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-242 |
6.20e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.48 E-value: 6.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYgKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK----DYRKIR 78
Cdd:PLN03232 1234 SIKFEDVHLRY-RPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgltDLRRVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIIGYMPGKFSlyqdLSVEENLKFFATLFGTTIEENYHL--IKDIYQQiEPFK-----NRRAGALSGGMKQKLALSCALI 151
Cdd:PLN03232 1313 SIIPQSPVLFS----GTVRFNIDPFSEHNDADLWEALERahIKDVIDR-NPFGldaevSEGGENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 152 HKPEILILDEPTTGVDpVSRKEFWDMLARLKEQGITILLSTAYMDEAGRCDRIALIREGKFIASDTPkgiidkftESLWA 231
Cdd:PLN03232 1388 RRSKILVLDEATASVD-VRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSP--------QELLS 1458
|
250
....*....|.
gi 2526563825 232 VEGSRMSAILH 242
Cdd:PLN03232 1459 RDTSAFFRMVH 1469
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-226 |
6.93e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.88 E-value: 6.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSY------GKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGS--------AIMN 66
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNvswrgeplAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 67 RYDIVKDYRKIRQIIGYMPGKFSLYQDL--SVEENLKFFATLfgtTIEENYHLIKDIYQQIE---PFKNRRAGALSGGMK 141
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDSISAVNPRKTVreIIREPLRHLLSL---DKAERLARASEMLRAVDlddSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 142 QKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLSTAYMDEAGR-CDRIALIREGKfIASDTPK 219
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERfCQRVMVMDNGQ-IVETQPV 236
|
....*..
gi 2526563825 220 GIIDKFT 226
Cdd:PRK10419 237 GDKLTFS 243
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-189 |
7.80e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 76.69 E-value: 7.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSY--------GKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV---- 71
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITglsg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 72 ---KDYRKIRQIIgympgkfslYQD----L--------SVEENLKFFATLFGTTIEENyhlIKDIYQQI---EPFKNRRA 133
Cdd:COG4608 88 relRPLRRRMQMV---------FQDpyasLnprmtvgdIIAEPLRIHGLASKAERRER---VAELLELVglrPEHADRYP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2526563825 134 GALSGGMKQKLALSCALIHKPEILILDEPTTGVDpVS-RKEFWDMLARLKEQ-GITIL 189
Cdd:COG4608 156 HEFSGGQRQRIGIARALALNPKLIVCDEPVSALD-VSiQAQVLNLLEDLQDElGLTYL 212
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-218 |
8.28e-16 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 74.84 E-value: 8.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYgKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQIIG 82
Cdd:cd03244 3 IEFKNVSLRY-RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPgkfslyQDlsveenlkffATLFGTTIEEN-----YHLIKDIYQQIEPFKNRRA---------------GA-LSGGMK 141
Cdd:cd03244 82 IIP------QD----------PVLFSGTIRSNldpfgEYSDEELWQALERVGLKEFveslpggldtvveegGEnLSVGQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 142 QKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLaRLKEQGITIL-----LSTAyMDeagrCDRIALIREGKFIASD 216
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTI-REAFKDCTVLtiahrLDTI-ID----SDRILVLDKGRVVEFD 219
|
..
gi 2526563825 217 TP 218
Cdd:cd03244 220 SP 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
10-167 |
8.42e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 77.69 E-value: 8.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 10 HKSYGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRK-IRQIIGympgkf 88
Cdd:PRK13657 339 DVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAsLRRNIA------ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 89 SLYQDlsveenlkffATLFGTTIEENYHLIKD-------------------IYQQIEPFKNR---RAGALSGGMKQKLAL 146
Cdd:PRK13657 413 VVFQD----------AGLFNRSIEDNIRVGRPdatdeemraaaeraqahdfIERKPDGYDTVvgeRGRQLSGGERQRLAI 482
|
170 180
....*....|....*....|.
gi 2526563825 147 SCALIHKPEILILDEPTTGVD 167
Cdd:PRK13657 483 ARALLKDPPILILDEATSALD 503
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-163 |
1.16e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.16 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGksgkknalnGISFTVDDGEIF-----GVIGPDGAGKSTLFRILASLILPDSGSaimnrydIVKDYRki 77
Cdd:PRK13409 340 LVEYPDLTKKLG---------DFSLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGE-------VDPELK-- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 78 rqiIGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENyHLIKDIyqQIEPFKNRRAGALSGGMKQKLALSCALIHKPEIL 157
Cdd:PRK13409 402 ---ISYKPQYIKPDYDGTVEDLLRSITDDLGSSYYKS-EIIKPL--QLERLLDKNVKDLSGGELQRVAIAACLSRDADLY 475
|
....*.
gi 2526563825 158 ILDEPT 163
Cdd:PRK13409 476 LLDEPS 481
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-162 |
2.79e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 75.26 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGksGKKNALNGISFTVDDGEiFGVI-GPDGAGKSTLFRILASLILPDSGsaimnryDIVKDYRKIRQ 79
Cdd:PRK11650 1 MAGLKLQAVRKSYD--GKTQVIKGIDLDVADGE-FIVLvGPSGCGKSTLLRMVAGLERITSG-------EIWIGGRVVNE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 I------IGYMPGKFSLYQDLSVEENLKFFATLFGT---TIEENyhlIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSC 148
Cdd:PRK11650 71 LepadrdIAMVFQNYALYPHMSVRENMAYGLKIRGMpkaEIEER---VAEAARilELEPLLDRKPRELSGGQRQRVAMGR 147
|
170
....*....|....
gi 2526563825 149 ALIHKPEILILDEP 162
Cdd:PRK11650 148 AIVREPAVFLFDEP 161
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-167 |
3.06e-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: 73.60 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 13 YGKSGKKNALNGISFTVD-----DGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDivkdyrkirqiIGYMPGK 87
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEggsisESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-----------VSYKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 88 FSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIyqQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVD 167
Cdd:cd03237 70 IKADYEGTVRDLLSSITKDFYTHPYFKTEIAKPL--QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-219 |
3.08e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.81 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 25 ISFTVDDGEIFGVIGPDGAGKSTLFRILASLiLPDSGSAIMNRYDiVKDYR--KIRQIIGYM----PGKFSL----YQDL 94
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQP-LEAWSaaELARHRAYLsqqqTPPFAMpvfqYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 95 SVEEnlkffatlfGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQK--LALSCALIHkPEI------LILDEPTT 164
Cdd:PRK03695 93 HQPD---------KTRTEAVASALNEVAEalGLDDKLGRSVNQLSGGEWQRvrLAAVVLQVW-PDInpagqlLLLDEPMN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2526563825 165 GVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPK 219
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRhADRVWLLKQGKLLASGRRD 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
24-192 |
3.42e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 72.90 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 24 GISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPD---SGSAIMNRYDIvkDYRKIRQ-IIGYmpgkfsLYQD------ 93
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRL--TALPAEQrRIGI------LFQDdllfph 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 94 LSVEENLKfFATLFGTTIEENYHLIKDIYQQIE--PFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSR 171
Cdd:COG4136 91 LSVGENLA-FALPPTIGRAQRRARVEQALEEAGlaGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALR 169
|
170 180
....*....|....*....|..
gi 2526563825 172 KEFWDM-LARLKEQGITILLST 192
Cdd:COG4136 170 AQFREFvFEQIRQRGIPALLVT 191
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-216 |
3.47e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.74 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGksGKKnALNGISFTVDDGEIFGVIGPDGAGKSTLFRILaSLILPD---SGSAIMN----RYDIVKDYR 75
Cdd:PRK13549 5 LLEMKNITKTFG--GVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-SGVYPHgtyEGEIIFEgeelQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 76 KIRQIIGYMpgKFSLYQDLSVEENL-------KFFATLFGTTIEENYHLIKDIYQQIEPfkNRRAGALSGGMKQKLALSC 148
Cdd:PRK13549 81 RAGIAIIHQ--ELALVKELSVLENIflgneitPGGIMDYDAMYLRAQKLLAQLKLDINP--ATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 149 ALIHKPEILILDEPTTgvdPVSRKE---FWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASD 216
Cdd:PRK13549 157 ALNKQARLLILDEPTA---SLTESEtavLLDIIRDLKAHGIACIYISHKLNEVKAiSDTICVIRDGRHIGTR 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-242 |
4.59e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.67 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 22 LNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQIIGYMPGKFSLYQDLSVEE-- 98
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRElv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 99 ---------NLKFFATLFGTTIEENYHLIKdiyqqIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPV 169
Cdd:PRK10575 107 aigrypwhgALGRFGAADREKVEEAISLVG-----LKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526563825 170 SRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGIIDkfTESLWAVEGSRMSAILH 242
Cdd:PRK10575 182 HQVDVLALVHRLsQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR--GETLEQIYGIPMGILPH 254
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-211 |
5.13e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 75.24 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 22 LNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvKDYRK--IRQIIGYMPgkfslyQDlSVeen 99
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-RDVTQasLRAAIGIVP------QD-TV--- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 100 lkffatLFGTTIEENyhlI---------KDIYQ-----QIEPFKNR-----------RAGALSGGMKQKLALSCALIHKP 154
Cdd:COG5265 443 ------LFNDTIAYN---IaygrpdaseEEVEAaaraaQIHDFIESlpdgydtrvgeRGLKLSGGEKQRVAIARTLLKNP 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 155 EILILDEPTTGVDPVSRKEFWDMLARLkEQGITIL-----LSTAyMDeagrCDRIALIREGK 211
Cdd:COG5265 514 PILIFDEATSALDSRTERAIQAALREV-ARGRTTLviahrLSTI-VD----ADEILVLEAGR 569
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-224 |
6.08e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.16 E-value: 6.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 22 LNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK----DYRKIRQIIGYMPGKFSlyqdLSVE 97
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfglmDLRKVLGIIPQAPVLFS----GTVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 98 ENLKFFatlfgttieeNYHLIKDIYQQIEP--FKN--RR-----------AGA-LSGGMKQKLALSCALIHKPEILILDE 161
Cdd:PLN03130 1331 FNLDPF----------NEHNDADLWESLERahLKDviRRnslgldaevseAGEnFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 162 PTTGVD--------PVSRKEFwdmlarlkeQGITILLSTAYMDEAGRCDRIALIREGKFIASDTPKGIIDK 224
Cdd:PLN03130 1401 ATAAVDvrtdaliqKTIREEF---------KSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-223 |
8.83e-15 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 72.56 E-value: 8.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGkSGKknALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAimnRYDI------------ 70
Cdd:TIGR02323 3 LLQVSGLSKSYG-GGK--GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTA---TYIMrsgaelelyqls 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 71 -VKDYRKIRQIIGYMP--GKFSLYQDLSVEENLKFFATLFGttiEENYHLIK----DIYQQIEPFKNR---RAGALSGGM 140
Cdd:TIGR02323 77 eAERRRLMRTEWGFVHqnPRDGLRMRVSAGANIGERLMAIG---ARHYGNIRataqDWLEEVEIDPTRiddLPRAFSGGM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 141 KQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAgR--CDRIALIREGKFIASDT 217
Cdd:TIGR02323 154 QQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLvRDLGLAVIIVTHDLGVA-RllAQRLLVMQQGRVVESGL 232
|
....*.
gi 2526563825 218 PKGIID 223
Cdd:TIGR02323 233 TDQVLD 238
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-215 |
1.07e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.18 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 21 ALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMN----RYDIVKDYRK-----IRQIIGYMPgkfsly 91
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqemRFASTTAALAagvaiIYQELHLVP------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 92 qDLSVEENLKF--FATLFG-----TTIEENYHLIKDIYQQIEPfkNRRAGALSGGMKQKLALSCALIHKPEILILDEPTT 164
Cdd:PRK11288 93 -EMTVAENLYLgqLPHKGGivnrrLLNYEAREQLEHLGVDIDP--DTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 165 GVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIAS 215
Cdd:PRK11288 170 SLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFAlCDAITVFKDGRYVAT 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-215 |
1.14e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.09 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvKDYRK--IRQII 81
Cdd:PRK11160 339 LTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-ADYSEaaLRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYMPGKFSLYQDlSVEENLKFFAtlfGTTIEEnyHLIkDIYQQIEPFK--NRRAG----------ALSGGMKQKLALSCA 149
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLAA---PNASDE--ALI-EVLQQVGLEKllEDDKGlnawlgeggrQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526563825 150 LIHKPEILILDEPTTGVDPVSRKEfwdMLARLKE--QGITILLSTAYMDEAGRCDRIALIREGKFIAS 215
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQ---ILELLAEhaQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQ 554
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-211 |
1.27e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 73.95 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSY--------GKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLIlPDSGSAIMNRYDIV---- 71
Cdd:COG4172 276 LEARDLKVWFpikrglfrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDglsr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 72 KDYRKIR---QIIgympgkfslYQD----LS--------VEENLKFFATlfGTTIEENYHLIKDIYQQI---EPFKNRRA 133
Cdd:COG4172 355 RALRPLRrrmQVV---------FQDpfgsLSprmtvgqiIAEGLRVHGP--GLSAAERRARVAEALEEVgldPAARHRYP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 134 GALSGGMKQKLALSCALIHKPEILILDEPTTGVDpVS-RKEFWDMLARL-KEQGITILLST------AYMdeagrCDRIA 205
Cdd:COG4172 424 HEFSGGQRQRIAIARALILEPKLLVLDEPTSALD-VSvQAQILDLLRDLqREHGLAYLFIShdlavvRAL-----AHRVM 497
|
....*.
gi 2526563825 206 LIREGK 211
Cdd:COG4172 498 VMKDGK 503
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-200 |
1.62e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.12 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSgkkNALNGISFTVDDGEIFGVIGPDGAGKSTL-------------FRILASLILPDSgsaimNRYDI 70
Cdd:PRK14243 11 LRTENLNVYYGSF---LAVKNVWLDIPKNQITAFIGPSGCGKSTIlrcfnrlndlipgFRVEGKVTFHGK-----NLYAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 71 VKDYRKIRQIIGYM---PGKFSLyqdlSVEENLKFFATLFGTTIEENyHLIKDIYQQIEPF-----KNRRAG-ALSGGMK 141
Cdd:PRK14243 83 DVDPVEVRRRIGMVfqkPNPFPK----SIYDNIAYGARINGYKGDMD-ELVERSLRQAALWdevkdKLKQSGlSLSGGQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2526563825 142 QKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQgITILLSTAYMDEAGR 200
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAAR 215
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-220 |
2.01e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.00 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 22 LNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIR-----QIIGYMPGKFSLYQDLSV 96
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 97 EENLKFFATLFGTTIEENYHLIKDIYQQI--EPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEF 174
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVglEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2526563825 175 WDMLARL-KEQGITILLSTAYMDEAGRCDRIALIREGKFIASDTPKG 220
Cdd:PRK11629 185 FQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLMG 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-184 |
2.35e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.75 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGKSG-KKNalngISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAI-----MNryDIVKDY 74
Cdd:PRK11000 1 MASVTLRNVTKAYGDVViSKD----INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFigekrMN--DVPPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 75 RKIrqiiGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGMKQKLALSCALIH 152
Cdd:PRK11000 75 RGV----GMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEvlQLAHLLDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190
....*....|....*....|....*....|..
gi 2526563825 153 KPEILILDEPTTGVDPVSRKEFWDMLARLKEQ 184
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKR 182
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-228 |
2.48e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 25 ISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMN--RYDIVKDYRKIRQII----------GYMPGKfslyq 92
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDgkPIDIRSPRDAIRAGImlcpedrkaeGIIPVH----- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 93 dlSVEENL-----KFFATlFGTTIEENY------HLIK-------DIYQQIepfknrraGALSGGMKQKLALSCALIHKP 154
Cdd:PRK11288 347 --SVADNInisarRHHLR-AGCLINNRWeaenadRFIRslniktpSREQLI--------MNLSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526563825 155 EILILDEPTTGVDPVSRKEFWDMLARLKEQGITILL-STAYMDEAGRCDRIALIREGKfIASDTPKgiiDKFTES 228
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFvSSDLPEVLGVADRIVVMREGR-IAGELAR---EQATER 486
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-192 |
3.10e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 70.29 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYgkSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRK----IR 78
Cdd:PRK10908 1 MIRFEHVSKAY--LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpfLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIIGYMPGKFSLYQDLSVEENLKFFATLFGTTIEENYHLIKDIYQQIEPFKNRRAG--ALSGGMKQKLALSCALIHKPEI 156
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFpiQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 2526563825 157 LILDEPTTGVDPVSRKEFWDMLARLKEQGITILLST 192
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMAT 194
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4-163 |
3.78e-14 |
|
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: 72.51 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGksgkknalnGISFTVDDGEIF-----GVIGPDGAGKSTLFRILASLILPDSGSAIMNrydiVKdyrkir 78
Cdd:COG1245 342 VEYPDLTKSYG---------GFSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDED----LK------ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 qiIGYMPGKFSLYQDLSVEENLKFFAT-LFGTTIEENyHLIKDIyqQIEPFKNRRAGALSGGMKQKLALSCALIHKPEIL 157
Cdd:COG1245 403 --ISYKPQYISPDYDGTVEEFLRSANTdDFGSSYYKT-EIIKPL--GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLY 477
|
....*.
gi 2526563825 158 ILDEPT 163
Cdd:COG1245 478 LLDEPS 483
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-163 |
4.35e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.46 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 2 KMIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNryDIVKdyrkirqiI 81
Cdd:PRK11819 323 KVIEAENLSKSFGD---RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG--ETVK--------L 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GY-------MPGKFSLYQDLS----------VEENLKFFATLFGttieenyhlikdiyqqiepFK----NRRAGALSGGM 140
Cdd:PRK11819 390 AYvdqsrdaLDPNKTVWEEISggldiikvgnREIPSRAYVGRFN-------------------FKggdqQKKVGVLSGGE 450
|
170 180
....*....|....*....|...
gi 2526563825 141 KQKLALSCALIHKPEILILDEPT 163
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPT 473
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-211 |
4.77e-14 |
|
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: 69.42 E-value: 4.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKKNA--LNGISFTVDDGEIFGVIGPDGAGKSTLFrilaslilpdsgSAIMNRYDIVKDYRKIRQII 81
Cdd:cd03250 1 ISVEDASFTWDSGEQETSftLKDINLEVPKGELVAIVGPVGSGKSSLL------------SALLGELEKLSGSVSVPGSI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYMPgKFSLYQDLSVEENLkffatLFGTTI-EENYH-------LIKDIyqQIEPFKNR-----RAGALSGGMKQKLALSC 148
Cdd:cd03250 69 AYVS-QEPWIQNGTIRENI-----LFGKPFdEERYEkvikacaLEPDL--EILPDGDLteigeKGINLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 149 ALIHKPEILILDEPTTGVDP-VSRKEFWDMLARLKEQGITILLSTAYMDEAGRCDRIALIREGK 211
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAhVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
21-215 |
4.91e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.68 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 21 ALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKirQIIGYMPGKFS-------LYQD 93
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK--NLVAYVPQSEEvdwsfpvLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 94 LSVEENLKFFATLFGTTiEENYHLIKDIYQQIE--PFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSR 171
Cdd:PRK15056 100 VVMMGRYGHMGWLRRAK-KRDRQIVTAALARVDmvEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2526563825 172 KEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIReGKFIAS 215
Cdd:PRK15056 179 ARIISLLRELRDEGKTMLVSTHNLGSVTEfCDYTVMVK-GTVLAS 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-170 |
5.05e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 70.56 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLhksYGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYR----KIR 78
Cdd:PRK11831 7 LVDMRGV---SFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRsrlyTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIIGYMPGKFSLYQDLSVEENLKFfatlfgtTIEENYHLIKDIYQQIEPFKNRRAG----------ALSGGMKQKLALSC 148
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNVAY-------PLREHTQLPAPLLHSTVMMKLEAVGlrgaaklmpsELSGGMARRAALAR 156
|
170 180
....*....|....*....|..
gi 2526563825 149 ALIHKPEILILDEPTTGVDPVS 170
Cdd:PRK11831 157 AIALEPDLIMFDEPFVGQDPIT 178
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-191 |
5.64e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.22 E-value: 5.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 18 KKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDS--GSAIMNRYDIVKdyrKIRQIIGYMPGKFSLYQDLS 95
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK---QILKRTGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 96 VEENLKFFATLF---GTTIEENYHLIKDIYQQIEPFK-------NRRAGALSGGMKQKLALSCALIHKPEILILDEPTTG 165
Cdd:PLN03211 157 VRETLVFCSLLRlpkSLTKQEKILVAESVISELGLTKcentiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180
....*....|....*....|....*.
gi 2526563825 166 VDPVSRKEFWDMLARLKEQGITILLS 191
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQKGKTIVTS 262
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-210 |
6.82e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.58 E-value: 6.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFrilaSLILPDSGSAIMNryDIVKDYRK------- 76
Cdd:PRK10938 261 IVLNNGVVSYND---RPILHNLSWQVNPGEHWQIVGPNGAGKSTLL----SLITGDHPQGYSN--DLTLFGRRrgsgeti 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 77 --IRQIIGYMPGkfSLYQDLSVEENLKffatlfgTTIEENYHLIKDIYQQIEP--------------FKNRRAGA----L 136
Cdd:PRK10938 332 wdIKKHIGYVSS--SLHLDYRVSTSVR-------NVILSGFFDSIGIYQAVSDrqqklaqqwldilgIDKRTADApfhsL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 137 SGGmKQKLAL-SCALIHKPEILILDEPTTGVDPVSR---KEFWDMLARlkeQGITILLSTAYMDE-AGRC--DRIALIRE 209
Cdd:PRK10938 403 SWG-QQRLALiVRALVKHPTLLILDEPLQGLDPLNRqlvRRFVDVLIS---EGETQLLFVSHHAEdAPACitHRLEFVPD 478
|
.
gi 2526563825 210 G 210
Cdd:PRK10938 479 G 479
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-211 |
1.52e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 69.75 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYG-KSGKKNALNGISFTVDDGEIFGVIGPDGAGKS-TLFRI---LAS--LIlpdSGSAIMNRYDIV-- 71
Cdd:PRK09473 10 DALLDVKDLRVTFStPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALmglLAAngRI---GGSATFNGREILnl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 72 --KDYRKIR--QIigYMpgkfsLYQD--------LSVEENLKFFATLF-----GTTIEENYHLIkDIYQQIEPFKNRR-- 132
Cdd:PRK09473 87 peKELNKLRaeQI--SM-----IFQDpmtslnpyMRVGEQLMEVLMLHkgmskAEAFEESVRML-DAVKMPEARKRMKmy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 133 AGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLK-EQGITILLSTAYMD-EAGRCDRIALIREG 210
Cdd:PRK09473 159 PHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGvVAGICDKVLVMYAG 238
|
.
gi 2526563825 211 K 211
Cdd:PRK09473 239 R 239
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-191 |
1.99e-13 |
|
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: 67.65 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 14 GKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILA-----SLIlpdSGSAIMNRYDIVKDYRKIrqiIGYMPGKF 88
Cdd:cd03232 15 VKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktaGVI---TGEILINGRPLDKNFQRS---TGYVEQQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 89 SLYQDLSVEENLKFFATLFGTTIEEnyhlikdiyqqiepfknrragalsggmKQKLALSCALIHKPEILILDEPTTGVDP 168
Cdd:cd03232 89 VHSPNLTVREALRFSALLRGLSVEQ---------------------------RKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180
....*....|....*....|...
gi 2526563825 169 VSRKEFWDMLARLKEQGITILLS 191
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQAILCT 164
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-200 |
2.06e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.91 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNR--------YDIVKDYR 75
Cdd:PRK14258 8 IKVNNLSFYYDT---QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRveffnqniYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 76 KIRQIIGYMPGKFSLYQdLSVEENLKFFATLFG-------TTIEENYHLIKDIYQQIEPFKNRRAGALSGGMKQKLALSC 148
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwrpkleiDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 149 ALIHKPEILILDEPTTGVDPVSRKEFWDML--ARLKEQgITILLSTAYMDEAGR 200
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSE-LTMVIVSHNLHQVSR 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-184 |
3.42e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.73 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYG--------KSGKKNALNGISFTVDDGEIFGVIGPDGAGKST----LFRILAS---LILPDSGSAIMNR 67
Cdd:PRK15134 275 LLDVEQLQVAFPirkgilkrTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSqgeIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 68 YDIVKDYRKIrQIIGYMPGKfSLYQDLSV----EENLKF-FATLFGTTIEENyhlIKDIYQQI--EP-FKNRRAGALSGG 139
Cdd:PRK15134 355 RQLLPVRHRI-QVVFQDPNS-SLNPRLNVlqiiEEGLRVhQPTLSAAQREQQ---VIAVMEEVglDPeTRHRYPAEFSGG 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2526563825 140 MKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQ 184
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQK 474
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-215 |
4.40e-13 |
|
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: 66.78 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSygkSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRilaslilpdsgsAIMNRYdivkDYRKIRQIIgy 83
Cdd:cd03217 1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAK------------TIMGHP----KYEVTEGEI-- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 mpgkfsLYQ-----DLSVEENLKffATLF----------GTTIEEnyhLIKDIyqqiepfknrRAGaLSGGMKQKLALSC 148
Cdd:cd03217 60 ------LFKgeditDLPPEERAR--LGIFlafqyppeipGVKNAD---FLRYV----------NEG-FSGGEKKRNEILQ 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526563825 149 ALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAY--MDEAGRCDRIALIREGKFIAS 215
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYqrLLDYIKPDRVHVLYDGRIVKS 186
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-211 |
1.04e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 68.17 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGKSGK-KNALNGISFTVDDGEIFGVIGPDGAGKS----TLFRILASLILPDSGSAIMNRYDIVK-DY 74
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGlSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 75 RKIRQIIGympGKFSL-YQD--------LSVE----ENLKFFATLFGTTIEEnyhLIKDIYQQI---EPfkNRRAGA--- 135
Cdd:COG4172 84 RELRRIRG---NRIAMiFQEpmtslnplHTIGkqiaEVLRLHRGLSGAAARA---RALELLERVgipDP--ERRLDAyph 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 136 -LSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLK-EQGITILLST------AYMdeagrCDRIALI 207
Cdd:COG4172 156 qLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQrELGMALLLIThdlgvvRRF-----ADRVAVM 230
|
....
gi 2526563825 208 REGK 211
Cdd:COG4172 231 RQGE 234
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-189 |
1.04e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.03 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 25 ISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDiVKDYRKIRQI--IGYMPGkfsLYQDLSVEENLKF 102
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-ATRGDRSRFMayLGHLPG---LKADLSTLENLHF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 103 FATLFGTTIEENYHLIKDIYqQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDML-ARL 181
Cdd:PRK13543 106 LCGLHGRRAKQMPGSALAIV-GLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMIsAHL 184
|
....*...
gi 2526563825 182 KEQGITIL 189
Cdd:PRK13543 185 RGGGAALV 192
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-211 |
1.15e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLhksygKSGKKNALNGISFTVDDGEIFGVIGPDGAGKS----TLF----RILASLIL-------PDSGSAIMNR 67
Cdd:PRK10982 250 ILEVRNL-----TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTdiveTLFgireKSAGTITLhgkkinnHNANEAINHG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 68 YDIVKDYRKIRQIIGYMPGKFSlyqdlSVEENLKFFATLFG----TTIEENYHLIKDIYQQIEPFKNRRAGALSGGMKQK 143
Cdd:PRK10982 325 FALVTEERRSTGIYAYLDIGFN-----SLISNIRNYKNKVGlldnSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQK 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 144 LALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARL--KEQGItILLSTAYMDEAGRCDRIALIREGK 211
Cdd:PRK10982 400 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELakKDKGI-IIISSEMPELLGITDRILVMSNGL 468
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-176 |
1.81e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.05 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 22 LNGISFTVDDGEIFGVIGPDGAGKSTLFrilaslilpdsgSAIMNRYDIVKDYRKIRQIIGYMPGKfSLYQDLSVEENLk 101
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLL------------SALLAEMDKVEGHVHMKGSVAYVPQQ-AWIQNDSLRENI- 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 102 ffatLFGTTIEENYH--------LIKDIyqQIEPFKNR-----RAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDP 168
Cdd:TIGR00957 720 ----LFGKALNEKYYqqvleacaLLPDL--EILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
....*...
gi 2526563825 169 VSRKEFWD 176
Cdd:TIGR00957 794 HVGKHIFE 801
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-192 |
4.94e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.82 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 22 LNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIGYMPGKFSLYQDLSVEENLk 101
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENC- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 102 FFATLFGTTIEENYHLIKdIYqQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARL 181
Cdd:PRK13540 96 LYDIHFSPGAVGITELCR-LF-SLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEH 173
|
170
....*....|.
gi 2526563825 182 KEQGITILLST 192
Cdd:PRK13540 174 RAKGGAVLLTS 184
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-195 |
6.80e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.43 E-value: 6.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 2 KMIEVKDLHKSYG-KSG-----KKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDI-VKDY 74
Cdd:PRK15112 3 TLLEVRNLSKTFRyRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhFGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 75 R----KIRQIigympgkfslYQDLSVEEN------------LKFFATLFGTTIEenyhliKDIYQQIepfknRRAG---- 134
Cdd:PRK15112 83 SyrsqRIRMI----------FQDPSTSLNprqrisqildfpLRLNTDLEPEQRE------KQIIETL-----RQVGllpd 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526563825 135 -------ALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKE-QGITILLSTAYM 195
Cdd:PRK15112 142 hasyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHL 210
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
4-194 |
8.18e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.60 E-value: 8.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSY-------GKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV----- 71
Cdd:PRK11308 6 LQAIDLKKHYpvkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 72 --KDYRKIRQIIGYMPgkfslyqdlsveenlkfFATL-----FGTTIEE----NYHLIKdiyqqiepfKNRRAGAL---- 136
Cdd:PRK11308 86 aqKLLRQKIQIVFQNP-----------------YGSLnprkkVGQILEEplliNTSLSA---------AERREKALamma 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526563825 137 ----------------SGGMKQKLALSCALIHKPEILILDEPTTGVDpVS-RKEFWDMLARLKEQgitilLSTAY 194
Cdd:PRK11308 140 kvglrpehydryphmfSGGQRQRIAIARALMLDPDVVVADEPVSALD-VSvQAQVLNLMMDLQQE-----LGLSY 208
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
6-211 |
1.65e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 63.30 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 6 VKDLHKSYGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSaiMNRYDIVkdyrkirQIIGYMP 85
Cdd:PRK13546 24 MKDALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK--VDRNGEV-------SVIAISA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 86 GkfsLYQDLSVEENLKFFATLFGTTIEENYHLIKDI--YQQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPT 163
Cdd:PRK13546 95 G---LSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIieFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2526563825 164 TGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGK 211
Cdd:PRK13546 172 SVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGK 220
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
25-189 |
2.24e-11 |
|
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: 61.02 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 25 ISFTVDDGEIFGVIGPDGAGKSTLFRILASL---------ILPDSGSAIMNRYdivkdyrkirqiiGYMPgkfslyqdls 95
Cdd:cd03223 20 LSFEIKPGDRLLITGPSGTGKSSLFRALAGLwpwgsgrigMPEGEDLLFLPQR-------------PYLP---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 96 veenlkffatlFGTTIEenyhlikdiyQQIEPFKNRragaLSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFW 175
Cdd:cd03223 77 -----------LGTLRE----------QLIYPWDDV----LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170
....*....|....
gi 2526563825 176 DMlarLKEQGITIL 189
Cdd:cd03223 132 QL---LKELGITVI 142
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
9-192 |
2.32e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 61.81 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 9 LHKSYGKSGKKNALNgISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAI---MNRYDIVKDYrkirqiIGYMP 85
Cdd:PRK13541 4 LHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYyknCNINNIAKPY------CTYIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 86 GKFSLYQDLSVEENLKFFATLFG--TTIEENYHlikdiYQQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPT 163
Cdd:PRK13541 77 HNLGLKLEMTVFENLKFWSEIYNsaETLYAAIH-----YFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVE 151
|
170 180
....*....|....*....|....*....
gi 2526563825 164 TGVDPVSRKEFWDMLARLKEQGITILLST 192
Cdd:PRK13541 152 TNLSKENRDLLNNLIVMKANSGGIVLLSS 180
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
24-223 |
2.56e-11 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 62.39 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 24 GISFTVDDGEIFGVIGPDGAGKSTLfrILASLILPDSGsAIMNRYDIVKDYR-----KIRQIigympgKFSLyqdlsVEE 98
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLT--CLAILGLLPPG-LTQTSGEILLDGRpllplSIRGR------HIAT-----IMQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 99 N-LKFFATLFgtTIEEnyHLIKDIYQQIEPFKNRRAGA----------------------LSGGMKQKLALSCALIHKPE 155
Cdd:TIGR02770 70 NpRTAFNPLF--TMGN--HAIETLRSLGKLSKQARALIlealeavglpdpeevlkkypfqLSGGMLQRVMIALALLLEPP 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 156 ILILDEPTTGVDPVSRKEFWDMLARLKEQ-GITILLSTAYMDEAGRC-DRIALIREGKFIASDTPKGIID 223
Cdd:TIGR02770 146 FLIADEPTTDLDVVNQARVLKLLRELRQLfGTGILLITHDLGVVARIaDEVAVMDDGRIVERGTVKEIFY 215
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-220 |
2.78e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.28 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKD--YRKIR 78
Cdd:PTZ00265 380 IKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDinLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 QIIGYMPG-------------KFSLY--QDLSVEEN-----------------------LKFFATLFGTT-------IEE 113
Cdd:PTZ00265 460 SKIGVVSQdpllfsnsiknniKYSLYslKDLEALSNyynedgndsqenknkrnscrakcAGDLNDMSNTTdsnelieMRK 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 114 NYHLIKD------------------IYQQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFW 175
Cdd:PTZ00265 540 NYQTIKDsevvdvskkvlihdfvsaLPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2526563825 176 DMLARLK--EQGITILLStaymdeagrcDRIALIREGK--FIASDTPKG 220
Cdd:PTZ00265 620 KTINNLKgnENRITIIIA----------HRLSTIRYANtiFVLSNRERG 658
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-211 |
2.95e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 26 SFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVK-DYRKIRQIIGympgkfSLYQD-----LSVEEN 99
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRlSFEQLQKLVS------DEWQRnntdmLSPGED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 100 LkffatlFGTT----IEENYH---LIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVS 170
Cdd:PRK10938 97 D------TGRTtaeiIQDEVKdpaRCEQLAQQfgITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2526563825 171 RKEFWDMLARLKEQGITILLST-------AYMDEAGRCDRIALIREGK 211
Cdd:PRK10938 171 RQQLAELLASLHQSGITLVLVLnrfdeipDFVQFAGVLADCTLAETGE 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-167 |
3.17e-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: 63.80 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 7 KDLHKSYGksGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAImnrydIVKDYRkirqiIGYMPG 86
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR-----PQPGIK-----VGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 87 KFSLYQDLSVEEN-----------LKFF---ATLFGTTIEENYHLIK---------------DIYQQIE--------PFK 129
Cdd:TIGR03719 76 EPQLDPTKTVRENveegvaeikdaLDRFneiSAKYAEPDADFDKLAAeqaelqeiidaadawDLDSQLEiamdalrcPPW 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 2526563825 130 NRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVD 167
Cdd:TIGR03719 156 DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-213 |
9.65e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 62.17 E-value: 9.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 25 ISFTVDDGEIFGVIGPDGAGKSTLFRILASLiLPDSGSAIMNRYDI----VKDYRKirQI--IGYMPgkfSLYQDlSVEE 98
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELreldPESWRK--HLswVGQNP---QLPHG-TLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 99 NLkffatLFGT---TIEENYHLIKDIYqqIEPFKNR-----------RAGALSGGMKQKLALSCALIHKPEILILDEPTT 164
Cdd:PRK11174 442 NV-----LLGNpdaSDEQLQQALENAW--VSEFLPLlpqgldtpigdQAAGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2526563825 165 GVDPVSRKEFWDMLARLKeQGITILLSTAYMDEAGRCDRIALIREGKFI 213
Cdd:PRK11174 515 SLDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDLAQWDQIWVMQDGQIV 562
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-167 |
1.05e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 27 FTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRyDI----------------VKDYrkIRQIIGYMPGKFSL 90
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLivarlqqdpprnvegtVYDF--VAEGIEEQAEYLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 91 YQDLSV-------EENLKFFATLFGTTIEEN-YHL---IKDIYQQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILIL 159
Cdd:PRK11147 101 YHDISHlvetdpsEKNLNELAKLQEQLDHHNlWQLenrINEVLAQLGLDPDAALSSLSGGWLRKAALGRALVSNPDVLLL 180
|
....*...
gi 2526563825 160 DEPTTGVD 167
Cdd:PRK11147 181 DEPTNHLD 188
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
133-214 |
1.18e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.73 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 133 AGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEA-GRCDRIALIREGK 211
Cdd:NF040905 402 VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELlGMCDRIYVMNEGR 481
|
...
gi 2526563825 212 FIA 214
Cdd:NF040905 482 ITG 484
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-214 |
2.46e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYgkSGKKnALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQI-- 80
Cdd:PRK10762 4 LLQLKGIDKAF--PGVK-ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 81 IGYMPGKFSLYQDLSVEENL---KFFATLFGTTieenyhLIKDIYQQIE--------PFKNRR-AGALSGGMKQKLALSC 148
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIflgREFVNRFGRI------DWKKMYAEADkllarlnlRFSSDKlVGELSIGEQQMVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526563825 149 ALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIA 214
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQFIA 221
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-167 |
2.95e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.68 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSaimnrydiVKDYRKIRqiIGY 83
Cdd:PRK15064 320 LEVENLTKGFDN---GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT--------VKWSENAN--IGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPgkfslyQDLSVEenlkfFA---TLFG-----TTIEENYHLIK-----------DIyqqiepfkNRRAGALSGGMKQKL 144
Cdd:PRK15064 387 YA------QDHAYD-----FEndlTLFDwmsqwRQEGDDEQAVRgtlgrllfsqdDI--------KKSVKVLSGGEKGRM 447
|
170 180
....*....|....*....|...
gi 2526563825 145 ALSCALIHKPEILILDEPTTGVD 167
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-213 |
3.03e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.72 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 19 KNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSG-----------SAIMNRYDIVKDYRKIRQIIgYMPGK 87
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggRSIFNYRDVLEFRRRVGMLF-QRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 88 FSLyqdlSVEENL------------KFFATLFGTTIEEN--YHLIKDIYQQiEPFKnrragaLSGGMKQKLALSCALIHK 153
Cdd:PRK14271 113 FPM----SIMDNVlagvrahklvprKEFRGVAQARLTEVglWDAVKDRLSD-SPFR------LSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 154 PEILILDEPTTGVDPVSRKEFWDMLARLKEQgITILLSTAYMDEAGR-CDRIALIREGKFI 213
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARiSDRAALFFDGRLV 241
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-192 |
4.03e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.17 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAimnRYDiVKDyrkirqiig 82
Cdd:PRK11701 6 LLSVRGLTKLYGP---RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV---HYR-MRD--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 ympGKFSLYQDLSVEENLKFFATLFG-------------------------TTIEENYHLIKDI----YQQIEPFKNR-- 131
Cdd:PRK11701 70 ---GQLRDLYALSEAERRRLLRTEWGfvhqhprdglrmqvsaggnigerlmAVGARHYGDIRATagdwLERVEIDAARid 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 132 -RAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDpVS-RKEFWDMLARL-KEQGITILLST 192
Cdd:PRK11701 147 dLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD-VSvQARLLDLLRGLvRELGLAVVIVT 209
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-213 |
5.64e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.03 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYgkSGKKN-ALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIvKDYR--KIRQI 80
Cdd:PRK11176 342 IEFRNVTFTY--PGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL-RDYTlaSLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 81 IGYMPGKFSLYQDlSVEENLKFFATLFgTTIEENYHLIKDIYQQ--IEPFKN-------RRAGALSGGMKQKLALSCALI 151
Cdd:PRK11176 419 VALVSQNVHLFND-TIANNIAYARTEQ-YSREQIEEAARMAYAMdfINKMDNgldtvigENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526563825 152 HKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGiTIL-----LSTayMDEAgrcDRIALIREGKFI 213
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKNR-TSLviahrLST--IEKA---DEILVVEDGEIV 557
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-216 |
6.46e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.04 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRIL------------------------------- 52
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 53 -----------------------ASLILPDSGSAIMNRYDI----VKDYRKIRQIIGYMPGKFslyqDLSVEENLKFFAT 105
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgeDSTVFKNSGKILLDGVDIcdynLKDLRNLFSIVSQEPMLF----NMSIYENIKFGKE 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 106 lfGTTIEENYHLIK--DIYQQIEPFKNRR-------AGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWD 176
Cdd:PTZ00265 1322 --DATREDVKRACKfaAIDEFIESLPNKYdtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2526563825 177 MLARLKEQGITILLSTAY-MDEAGRCDRIALI----REGKFIASD 216
Cdd:PTZ00265 1400 TIVDIKDKADKTIITIAHrIASIKRSDKIVVFnnpdRTGSFVQAH 1444
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
136-213 |
1.34e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.40 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 136 LSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGRC-DRIALIREGKFI 213
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLaDDVAVMSHGRIV 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-189 |
2.05e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 58.28 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 22 LNGISFTVDDGEIFGVIGPDGAGKSTLFRILASL--------ILPDSGSAIM--NR-YDIVKDyrkIRQIIGYmPGKFSL 90
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwpygsgriARPAGARVLFlpQRpYLPLGT---LREALLY-PATAEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 91 YQDLSVEE-----NLKffatlfgttieenyHLIKDIYQQiepfkNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTG 165
Cdd:COG4178 455 FSDAELREaleavGLG--------------HLAERLDEE-----ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180
....*....|....*....|....*.
gi 2526563825 166 VDPVSRKEfwdMLARLKEQ--GITIL 189
Cdd:COG4178 516 LDEENEAA---LYQLLREElpGTTVI 538
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-170 |
2.43e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.41 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKSGKK----------NALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV- 71
Cdd:PRK15079 8 LLEVADLKVHFDIKDGKqwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 72 ---KDYRKIRQIIgYMpgkfsLYQD-LS-----------VEENLK-FFATLFGTTIEENYHLIKDIYQQIEPFKNRRAGA 135
Cdd:PRK15079 88 mkdDEWRAVRSDI-QM-----IFQDpLAslnprmtigeiIAEPLRtYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHE 161
|
170 180 190
....*....|....*....|....*....|....*
gi 2526563825 136 LSGGMKQKLALSCALIHKPEILILDEPTTGVDpVS 170
Cdd:PRK15079 162 FSGGQCQRIGIARALILEPKLIICDEPVSALD-VS 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-211 |
2.70e-09 |
|
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: 58.00 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKKnALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMN-RYDIVKdYRKIRQIIG 82
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGvSWNSVT-LQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 YMPGKFSLYQDlSVEENLKFFATLfgtTIEENYHLIKDI--YQQIEPFKNRR-------AGALSGGMKQKLALSCALIHK 153
Cdd:TIGR01271 1296 VIPQKVFIFSG-TFRKNLDPYEQW---SDEEIWKVAEEVglKSVIEQFPDKLdfvlvdgGYVLSNGHKQLMCLARSILSK 1371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 154 PEILILDEPTTGVDPVSrkefWDMLARLKEQGI---TILLSTAYMDEAGRCDRIALIREGK 211
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVT----LQIIRKTLKQSFsncTVILSEHRVEALLECQQFLVIEGSS 1428
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-211 |
3.26e-09 |
|
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: 56.79 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKKnALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRKIRQIIGY 83
Cdd:cd03289 3 MTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPGKFSLYQDlSVEENLKFFAT-----LFGTTIEENYHLIKDIYQQIEPFKNRRAG-ALSGGMKQKLALSCALIHKPEIL 157
Cdd:cd03289 82 IPQKVFIFSG-TFRKNLDPYGKwsdeeIWKVAEEVGLKSVIEQFPGQLDFVLVDGGcVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 158 ILDEPTTGVDPVSRKEFWDMLaRLKEQGITILLSTAYMDEAGRCDRIALIREGK 211
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTL-KQAFADCTVILSEHRIEAMLECQRFLVIEENK 213
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-191 |
6.43e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.64 E-value: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 19 KNALNGISFTVDDGEIFGVIGPDGAGKSTLFrilaSLILP--DSGSAIMNRYDI------VKDYRKIRQIIGYMPGKFSl 90
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLL----SLIQRhfDVSEGDIRFHDIpltklqLDSWRSRLAVVSQTPFLFS- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 91 yqDlSVEENLKF---FATlfGTTIEE-----NYHliKDIYQQIEPFKNR---RAGALSGGMKQKLALSCALIHKPEILIL 159
Cdd:PRK10789 403 --D-TVANNIALgrpDAT--QQEIEHvarlaSVH--DDILRLPQGYDTEvgeRGVMLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190
....*....|....*....|....*....|....
gi 2526563825 160 DEPTTGVDpvSRKEFwDMLARLKE--QGITILLS 191
Cdd:PRK10789 476 DDALSAVD--GRTEH-QILHNLRQwgEGRTVIIS 506
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-163 |
6.72e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 7 KDLHKSYGksGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAImnrydIVKDYRkirqiIGYMPG 86
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR-----PAPGIK-----VGYLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 87 KFSLYQDLSVEEN-----------LKFF---ATLFGTTIEENYHLIK---------------DIYQQIE--------PFK 129
Cdd:PRK11819 78 EPQLDPEKTVRENveegvaevkaaLDRFneiYAAYAEPDADFDALAAeqgelqeiidaadawDLDSQLEiamdalrcPPW 157
|
170 180 190
....*....|....*....|....*....|....
gi 2526563825 130 NRRAGALSGGMKQKLALSCALIHKPEILILDEPT 163
Cdd:PRK11819 158 DAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
5-196 |
6.84e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.96 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 5 EVKDLHKSYGKSG---KKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLIL--PDSGSAimnryDIVKDyrkirq 79
Cdd:COG2401 26 RVAIVLEAFGVELrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCV-----DVPDN------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 80 iigympgkfSLYQDLSVEENLkffatlfgttieenyHLIKDIYQQIE----------PFKNRRAGALSGGMKQKLALSCA 149
Cdd:COG2401 95 ---------QFGREASLIDAI---------------GRKGDFKDAVEllnavglsdaVLWLRRFKELSTGQKFRFRLALL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2526563825 150 LIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMD 196
Cdd:COG2401 151 LAERPKLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATHHYD 198
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-229 |
8.54e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 55.68 E-value: 8.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 16 SGKKNALNGISFTVDDGEIFGVIGPDGAGKStlfrILASLILpdsgSAIMNRYDIVKD-------------YRKIRQIIG 82
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKS----LIAKAIC----GITKDNWHVTADrfrwngidllklsPRERRKIIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 83 Y---MpgkfsLYQD--------LSVEENLK----------FFATLFGTTIEENYHL-----IKDiYQQIE---PFKnrra 133
Cdd:COG4170 89 ReiaM-----IFQEpsscldpsAKIGDQLIeaipswtfkgKWWQRFKWRKKRAIELlhrvgIKD-HKDIMnsyPHE---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 134 gaLSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILL------STAYMdeagrCDRIAL 206
Cdd:COG4170 159 --LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLishdleSISQW-----ADTITV 231
|
250 260
....*....|....*....|....*..
gi 2526563825 207 IREGKFIASDTPKGIIDK----FTESL 229
Cdd:COG4170 232 LYCGQTVESGPTEQILKSphhpYTKAL 258
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-210 |
1.20e-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: 56.07 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 22 LNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGsaimnrydivkdyrKIRQI--IGYMPgKFSLYQDLSVEEN 99
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG--------------KIKHSgrISFSP-QTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 100 LkffatLFGTTIEENYH--LIK--DIYQQIEPFKNR------RAG-ALSGGMKQKLALSCALIHKPEILILDEPTTGVDP 168
Cdd:TIGR01271 507 I-----IFGLSYDEYRYtsVIKacQLEEDIALFPEKdktvlgEGGiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2526563825 169 VSRKE-FWDMLARLKEQGITILLsTAYMDEAGRCDRIALIREG 210
Cdd:TIGR01271 582 VTEKEiFESCLCKLMSNKTRILV-TSKLEHLKKADKILLLHEG 623
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-221 |
1.51e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 21 ALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRK--IRQIIGYMPGKFSLYQDLSVEE 98
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeaLENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 99 NL---KFFATLFGTTIEENYHLIKDIYQQ----IEPfkNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSR 171
Cdd:PRK10982 93 NMwlgRYPTKGMFVDQDKMYRDTKAIFDEldidIDP--RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 172 KEFWDMLARLKEQGITILLSTAYMDEAGR-CDRIALIREGKFIASDTPKGI 221
Cdd:PRK10982 171 NHLFTIIRKLKERGCGIVYISHKMEEIFQlCDEITILRDGQWIATQPLAGL 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-167 |
2.18e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 5 EVKDLhkSYGKSGKkNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSaimnrydiVKDYRKIRqiIGYm 84
Cdd:PRK11147 321 EMENV--NYQIDGK-QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGR--------IHCGTKLE--VAY- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 85 pgkFSLYQ-----DLSVEENL---KffatlfgTTIEEN---YHLIKdiYQQIEPFKNRRA----GALSGGMKQKLALSCA 149
Cdd:PRK11147 387 ---FDQHRaeldpEKTVMDNLaegK-------QEVMVNgrpRHVLG--YLQDFLFHPKRAmtpvKALSGGERNRLLLARL 454
|
170
....*....|....*...
gi 2526563825 150 LIHKPEILILDEPTTGVD 167
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLD 472
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-214 |
2.54e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 54.80 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKKN--ALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVKDYRkirqii 81
Cdd:COG4615 328 LELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNR------ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 gympgkfSLYQDLsveenlkfFATLFGttieeNYHLIKDIYQQIEPFKNRRAG----------------------ALSGG 139
Cdd:COG4615 402 -------EAYRQL--------FSAVFS-----DFHLFDRLLGLDGEADPARARellerleldhkvsvedgrfsttDLSQG 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 140 MKQKLALSCALI-HKPeILILDEPTTGVDPVSRKEFW-DMLARLKEQGITILLST---AYMDEAgrcDRIALIREGKFIA 214
Cdd:COG4615 462 QRKRLALLVALLeDRP-ILVFDEWAADQDPEFRRVFYtELLPELKARGKTVIAIShddRYFDLA---DRVLKMDYGKLVE 537
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-213 |
5.46e-08 |
|
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: 52.26 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 11 KSYGKSGKKnALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPD---SGSAIMNRYDIVKDYRKIRQIIGYMPGK 87
Cdd:cd03233 13 TGKGRSKIP-ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 88 FSLYQDLSVEENLKFFATLFGttieenyhlikdiyqqiepfkNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVD 167
Cdd:cd03233 92 DVHFPTLTVRETLDFALRCKG---------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2526563825 168 PVSRKEFWDMLARL-KEQGITILLS-TAYMDEAGRC-DRIALIREGKFI 213
Cdd:cd03233 151 SSTALEILKCIRTMaDVLKTTTFVSlYQASDEIYDLfDKVLVLYEGRQI 199
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-210 |
9.00e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 9.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMnrydivkdyrkIRQIIGY 83
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAY 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 84 MPgKFSLYQDLSVEENLkffatLFGTTIE-ENYHLIKDI---YQQIEPFKNR-------RAGALSGGMKQKLALSCALIH 152
Cdd:PLN03232 684 VP-QVSWIFNATVRENI-----LFGSDFEsERYWRAIDVtalQHDLDLLPGRdlteigeRGVNISGGQKQRVSMARAVYS 757
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2526563825 153 KPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGRCDRIALIREG 210
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEG 815
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-184 |
1.18e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.44 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGKSGKK-NALNGISFTVDDGEIFGVIGPDGAGKSTlfRILASLILPDSGSAIM------NRYDIVK- 72
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPfRAVDRISYSVKQGEVVGIVGESGSGKSV--SSLAIMGLIDYPGRVMaeklefNGQDLQRi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 73 DYRKIRQIIGY---MpgkfsLYQD------------LSVEENLKFF-----ATLFGTTIEENYHL-IKDIYQQIEPFKNR 131
Cdd:PRK11022 79 SEKERRNLVGAevaM-----IFQDpmtslnpcytvgFQIMEAIKVHqggnkKTRRQRAIDLLNQVgIPDPASRLDVYPHQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2526563825 132 ragaLSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQ 184
Cdd:PRK11022 154 ----LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQK 202
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-167 |
1.23e-07 |
|
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: 51.60 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 28 TVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGsaimnRY-------DIVKDYR---------KIR----------QII 81
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLG-----KFddppdwdEILDEFRgselqnyftKLLegdvkvivkpQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYMPGKFslyqDLSVEENLKffatlfgtTIEENYHLIKDIYQ-QIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILD 160
Cdd:cd03236 97 DLIPKAV----KGKVGELLK--------KKDERGKLDELVDQlELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFD 164
|
....*..
gi 2526563825 161 EPTTGVD 167
Cdd:cd03236 165 EPSSYLD 171
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-215 |
1.24e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 21 ALNGISFTVDDGEIFGVIGPDGAGKSTLFRILaSLILPdSGSaimnrY--DIVKD-----YRKIRQ-------IIgympg 86
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVL-SGVYP-HGS-----YegEILFDgevcrFKDIRDsealgivII----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 87 kfslYQDL------SVEENL-------KFFATLFGTTIEENYHLIKDIYQQIEPfkNRRAGALSGGMKQKLALSCALIHK 153
Cdd:NF040905 84 ----HQELalipylSIAENIflgneraKRGVIDWNETNRRARELLAKVGLDESP--DTLVTDIGVGKQQLVEIAKALSKD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526563825 154 PEILILDEPTTGVDPVSRKEFWDMLARLKEQGIT-ILLSTAYMDEAGRCDRIALIREGKFIAS 215
Cdd:NF040905 158 VKLLILDEPTAALNEEDSAALLDLLLELKAQGITsIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
65-192 |
1.75e-07 |
|
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: 51.62 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 65 MNRYDIVKDYRKIRQIIGYMPGKFSLYQDLsveENLKFFATLFGTTIEENYHLIKDIYQQIEPFKNRR---AGALSGGMK 141
Cdd:pfam13304 166 WAVLDLAADLALFPDLKELLQRLVRGLKLA---DLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGelpAFELSDGTK 242
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2526563825 142 QKLALSCALI---HKPEILILDEPTTGVDPVSRKEFWDMLARLKEQGITILLST 192
Cdd:pfam13304 243 RLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTT 296
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
12-167 |
3.03e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 12 SYGKSGKKnaLNGISfTVDDGEIFGVIGPDGAGKSTLFRILASLILPD-----------------SGSAIMNRYDIVKDy 74
Cdd:PRK13409 82 RYGVNGFK--LYGLP-IPKEGKVTGILGPNGIGKTTAVKILSGELIPNlgdyeeepswdevlkrfRGTELQNYFKKLYN- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 75 RKIR-----QIIGYMPGKFslyqDLSVEENLKffatlfgTTIEENyhLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALS 147
Cdd:PRK13409 158 GEIKvvhkpQYVDLIPKVF----KGKVRELLK-------KVDERG--KLDEVVERlgLENILDRDISELSGGELQRVAIA 224
|
170 180
....*....|....*....|
gi 2526563825 148 CALIHKPEILILDEPTTGVD 167
Cdd:PRK13409 225 AALLRDADFYFFDEPTSYLD 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-211 |
5.06e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.86 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGKSGK-KNALNGISFTVDDGEIFGVIGPDGAGKS----TLFRILAS--LILPdSGSAIMNRYDIVK- 72
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppVVYP-SGDIRFHGESLLHa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 73 DYRKIRQIIG-YMPGKFS---------------LYQDLSVEENLK-------FFATLFGTTIEENYHLIKDIYQQiepfk 129
Cdd:PRK15134 82 SEQTLRGVRGnKIAMIFQepmvslnplhtlekqLYEVLSLHRGMRreaargeILNCLDRVGIRQAAKRLTDYPHQ----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 130 nrragaLSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLK-EQGITILLSTAYMDEAGR-CDRIALI 207
Cdd:PRK15134 157 ------LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQqELNMGLLFITHNLSIVRKlADRVAVM 230
|
....
gi 2526563825 208 REGK 211
Cdd:PRK15134 231 QNGR 234
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
93-218 |
5.32e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.92 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 93 DLSVEENLKFFATLfgTTIEENYHLIKDI---YQQIepfkNRRAGALSGGMKQKLALSCALIHK---PEILILDEPTTGV 166
Cdd:cd03271 130 DMTVEEALEFFENI--PKIARKLQTLCDVglgYIKL----GQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGL 203
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2526563825 167 DPVSRKEFWDMLARLKEQGITILLSTAYMDEAGRCDRIALI------REGKFIASDTP 218
Cdd:cd03271 204 HFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLgpeggdGGGQVVASGTP 261
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-210 |
6.00e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 15 KSGKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLIlpDSGsaIMNRYDIVKDYRKI----RQIIGYMPgkfsl 90
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTG--VITGGDRLVNGRPLdssfQRSIGYVQ----- 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 91 YQDL-----SVEENLKFFATL---FGTTIEENYHLIKDIYQ--QIEPFKNRRAGALSGGM----KQKLALSCALIHKPEI 156
Cdd:TIGR00956 843 QQDLhlptsTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKllEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKL 922
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 157 LI-LDEPTTGVDPVSRKEFWDMLARLKEQGITILL-----STAYMDEAgrcDRIALIREG 210
Cdd:TIGR00956 923 LLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCtihqpSAILFEEF---DRLLLLQKG 979
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-53 |
8.12e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.26 E-value: 8.12e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2526563825 2 KMIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILA 53
Cdd:CHL00131 6 PILEIKNLHASVNE---NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA 54
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-189 |
9.55e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.13 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 22 LNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLiLPDSGSAImnrydivkdYRKIRQIIGYMPGK--FSL--------Y 91
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGRL---------TKPAKGKLFYVPQRpyMTLgtlrdqiiY 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 92 QDLSVEENLKFFATLFGTTIEENYHLiKDIYQQIEPFKNRR--AGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPv 169
Cdd:TIGR00954 538 PDSSEDMKRRGLSDKDLEQILDNVQL-THILEREGGWSAVQdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV- 615
|
170 180
....*....|....*....|....
gi 2526563825 170 srkefwDMLARL----KEQGITIL 189
Cdd:TIGR00954 616 ------DVEGYMyrlcREFGITLF 633
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-222 |
9.92e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.42 E-value: 9.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 1 MKMIEVKDLHKSYGKS-GKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASlILPDSGSAIMNRY-----DIVK-D 73
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRMrfddiDLLRlS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 74 YRKIRQIIGY-MPGKFSLYQ---DLSVEENLKFFATLFGTTIEENYhlikdiYQQIEPFKNR------RAG--------- 134
Cdd:PRK15093 80 PRERRKLVGHnVSMIFQEPQsclDPSERVGRQLMQNIPGWTYKGRW------WQRFGWRKRRaiellhRVGikdhkdamr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 135 ----ALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMDEAGR-CDRIALIR 208
Cdd:PRK15093 154 sfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQwADKINVLY 233
|
250
....*....|....
gi 2526563825 209 EGKFIASDTPKGII 222
Cdd:PRK15093 234 CGQTVETAPSKELV 247
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-210 |
1.60e-06 |
|
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: 48.70 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 22 LNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGsaimnrydIVKDYRKIR---QIIGYMPGkfslyqdlSVEE 98
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG--------KIKHSGRISfssQFSWIMPG--------TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 99 NLkffatLFGTTIEENYHL--IK--DIYQQIEPFKNR------RAG-ALSGGMKQKLALSCALIHKPEILILDEPTTGVD 167
Cdd:cd03291 117 NI-----IFGVSYDEYRYKsvVKacQLEEDITKFPEKdntvlgEGGiTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2526563825 168 PVSRKEFWD-MLARLKEQGITILLsTAYMDEAGRCDRIALIREG 210
Cdd:cd03291 192 VFTEKEIFEsCVCKLMANKTRILV-TSKMEHLKKADKILILHEG 234
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
93-226 |
2.03e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.44 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 93 DLSVEENLKFFATlfGTTIEENYHLIKDIYQQIEPFkNRRAGALSGGMKQKLALSCALIH---KPEILILDEPTTGVDPV 169
Cdd:PRK00635 770 EMTAYEAEKFFLD--EPSIHEKIHALCSLGLDYLPL-GRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTH 846
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526563825 170 SRKEFWDMLARLKEQGITILLSTAYMDEAGRCDR-IALIREGK-----FIASDTPKGIIDKFT 226
Cdd:PRK00635 847 DIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYvLELGPEGGnlggyLLASCSPEELIHLHT 909
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
13-163 |
2.04e-06 |
|
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: 49.01 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 13 YGKSGKKnaLNGISfTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGS--------AIMNRY--DIVKDY-RKIR--- 78
Cdd:COG1245 83 YGENGFR--LYGLP-VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDydeepswdEVLKRFrgTELQDYfKKLAnge 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 79 -------QIIGYMPGKFslyqDLSVEENLKffatlfgTTIEENyhLIKDIYQQ--IEPFKNRRAGALSGGMKQKLALSCA 149
Cdd:COG1245 160 ikvahkpQYVDLIPKVF----KGTVRELLE-------KVDERG--KLDELAEKlgLENILDRDISELSGGELQRVAIAAA 226
|
170
....*....|....
gi 2526563825 150 LIHKPEILILDEPT 163
Cdd:COG1245 227 LLRDADFYFFDEPS 240
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-231 |
2.59e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.70 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 3 MIEVKDLHKSYGKSGKK-NALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLIlPDSGSAIMNRYDIVKdyRKIRQII 81
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLL-EQAGGLVQCDKMLLR--RRSRQVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 82 GYMPGKFSLYQDLS-------VEENLKFFATLF--GTTIEENYHL------------IKDIYQQI-----EPFKNRRAGA 135
Cdd:PRK10261 89 ELSEQSAAQMRHVRgadmamiFQEPMTSLNPVFtvGEQIAESIRLhqgasreeamveAKRMLDQVripeaQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 136 LSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARL-KEQGITILLSTAYMD-EAGRCDRIALIREGKFI 213
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGvVAEIADRVLVMYQGEAV 248
|
250 260
....*....|....*....|..
gi 2526563825 214 ASDTPKGIIDK----FTESLWA 231
Cdd:PRK10261 249 ETGSVEQIFHApqhpYTRALLA 270
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-167 |
3.78e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.18 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 4 IEVKDLHKSYGKSgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGsaimnryDIVKDYRKI------ 77
Cdd:PRK10790 341 IDIDNVSFAYRDD--NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEG-------EIRLDGRPLsslshs 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 78 --RQiigympGKFSLYQDLSVEENlKFFA--TLfGTTIEENY-----------HLIKDIYQQIEPFKNRRAGALSGGMKQ 142
Cdd:PRK10790 412 vlRQ------GVAMVQQDPVVLAD-TFLAnvTL-GRDISEEQvwqaletvqlaELARSLPDGLYTPLGEQGNNLSVGQKQ 483
|
170 180
....*....|....*....|....*
gi 2526563825 143 KLALSCALIHKPEILILDEPTTGVD 167
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANID 508
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
93-218 |
6.44e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.70 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 93 DLSVEENLKFFATLfgTTIEENYHLIKDI---YQQIepfkNRRAGALSGGMKQKLALSCALIHK---PEILILDEPTTGV 166
Cdd:TIGR00630 790 DMTVEEAYEFFEAV--PSISRKLQTLCDVglgYIRL----GQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGL 863
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2526563825 167 DPVSRKEFWDMLARLKEQGITILLSTAYMDEAGRCDRIALI------REGKFIASDTP 218
Cdd:TIGR00630 864 HFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTP 921
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
22-189 |
1.01e-05 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 45.82 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 22 LNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVkdyrKIRQIIGYMPGkfslyqdLSVEENLK 101
Cdd:PRK15177 3 LDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFIGLRGDAL----PLGANSFILPG-------LTGEENAR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 102 FFATLFGTTIEENYHLIKDIyQQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLA-R 180
Cdd:PRK15177 72 MMASLYGLDGDEFSHFCYQL-TQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAALAcQ 150
|
....*....
gi 2526563825 181 LKEQGITIL 189
Cdd:PRK15177 151 LQQKGLIVL 159
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-190 |
2.70e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.85 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 20 NALNGISFTVDDGEIFGVIGPDGAGKSTLfrilaslilpdsgsaimnrydiVKDyrkirqiIGYMPGKFSLYQDLSV-EE 98
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTL----------------------VNE-------GLYASGKARLISFLPKfSR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 99 NLKFFATLFGTTIEENYHLIKdiyqqiepfKNRRAGALSGGMKQKLALSCALIHKPE--ILILDEPTTGVDPVSRKEFWD 176
Cdd:cd03238 60 NKLIFIDQLQFLIDVGLGYLT---------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE 130
|
170
....*....|....
gi 2526563825 177 MLARLKEQGITILL 190
Cdd:cd03238 131 VIKGLIDLGNTVIL 144
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-192 |
3.80e-05 |
|
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: 43.13 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 32 GEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMnrydivkdyrkirqiigympgkfslyqdlsveenlkffatlfgttI 111
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------I 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 112 EENYHLIKDIYQQIEPFKNRRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLA------RLKEQG 185
Cdd:smart00382 37 DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllllLKSEKN 116
|
....*..
gi 2526563825 186 ITILLST 192
Cdd:smart00382 117 LTVILTT 123
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-167 |
5.06e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 17 GKKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRyDIVKDYRKIRQiIGYMPGKFSLYQDLS- 95
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAK-GIKLGYFAQHQ-LEFLRADESPLQHLAr 400
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526563825 96 -----VEENLKFFATLFGTTIEEnyhlikdIYQQIEPFknrragalSGGMKQKLALSCALIHKPEILILDEPTTGVD 167
Cdd:PRK10636 401 lapqeLEQKLRDYLGGFGFQGDK-------VTEETRRF--------SGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-185 |
1.12e-04 |
|
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: 42.17 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 29 VDDGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIVkdyrkirqiigYMPGKFSlyqdlsveenlkffatlfg 108
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-----------YKPQYID------------------- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526563825 109 ttieenyhlikdiyqqiepfknrragaLSGGMKQKLALSCALIHKPEILILDEPTTGVDPVSRKEFWDMLARLKEQG 185
Cdd:cd03222 72 ---------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-53 |
2.66e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.70 E-value: 2.66e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2526563825 3 MIEVKDLHKSYGKsgkKNALNGISFTVDDGEIFGVIGPDGAGKSTLFRILA 53
Cdd:PRK09580 1 MLSIKDLHVSVED---KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLA 48
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
31-182 |
6.95e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.99 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 31 DGEIFGVIGPDGAGKSTLFRILASLILPDSGSAIMNRYDIV-----------------KDYRKIRQIigympGKFSLYQD 93
Cdd:COG0419 22 DDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLInvgseeasvelefehggKRYRIERRQ-----GEFAEFLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 94 LSVEENLKFFATLFGT-TIEENYHLIKDIYQQIEPFKNRRAGA-------------------LSGGMKQKLALSCALihk 153
Cdd:COG0419 97 AKPSERKEALKRLLGLeIYEELKERLKELEEALESALEELAELqklkqeilaqlsgldpietLSGGERLRLALADLL--- 173
|
170 180
....*....|....*....|....*....
gi 2526563825 154 peILILDEPTTgvDPVSRKEFWDMLARLK 182
Cdd:COG0419 174 --SLILDFGSL--DEERLERLLDALEELA 198
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
23-188 |
7.09e-04 |
|
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: 39.65 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 23 NGISFTvdDGEIFGVIGPDGAGKSTLFRILAsLILPDSGSAIMNRYDIvkdyrkirqiigyMPGKFSLYQDLsveenlkF 102
Cdd:cd03227 14 NDVTFG--EGSLTIITGPNGSGKSTILDAIG-LALGGAQSATRRRSGV-------------KAGCIVAAVSA-------E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 103 FATLFGTtieenyhlikdiyqqiepfknrragaLSGGMKQKLALSCALIH---KPEIL-ILDEPTTGVDPVSRKEFWDML 178
Cdd:cd03227 71 LIFTRLQ--------------------------LSGGEKELSALALILALaslKPRPLyILDEIDRGLDPRDGQALAEAI 124
|
170
....*....|...
gi 2526563825 179 ARL---KEQGITI 188
Cdd:cd03227 125 LEHlvkGAQVIVI 137
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
25-173 |
8.45e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.90 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 25 ISFtvdDGEIFGVIGPDGAGKSTLFR-ILASLilpdSGSAIMNRYDIVKDYRKIRQiigympGKFSLYQDLSVEENLKff 103
Cdd:cd03240 18 IEF---FSPLTLIVGQNGAGKTTIIEaLKYAL----TGELPPNSKGGAHDPKLIRE------GEVRAQVKLAFENANG-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 104 atlfgttieENYHlikdIYQQIEPFKN--------------RRAGALSGGMKQK------LALSCALIHKPEILILDEPT 163
Cdd:cd03240 83 ---------KKYT----ITRSLAILENvifchqgesnwpllDMRGRCSGGEKVLasliirLALAETFGSNCGILALDEPT 149
|
170
....*....|
gi 2526563825 164 TGVDPVSRKE 173
Cdd:cd03240 150 TNLDEENIEE 159
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
86-231 |
8.69e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 86 GK-FSLYQDLSVEENLKFFATLFGTTieenyhliKDIYQQIEPFKNR---------------RAGA-LSGGMKQKLALSC 148
Cdd:PRK00635 418 GKtFAEFQQMSLQELFIFLSQLPSKS--------LSIEEVLQGLKSRlsilidlglpyltpeRALAtLSGGEQERTALAK 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 149 ALihKPEIL----ILDEPTTGVDPVSRKEFWDMLARLKEQGITILLSTAYMDEAGRCDRI------ALIREGKFIASDTP 218
Cdd:PRK00635 490 HL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIidigpgAGIFGGEVLFNGSP 567
|
170
....*....|...
gi 2526563825 219 KGIIDKfTESLWA 231
Cdd:PRK00635 568 REFLAK-SDSLTA 579
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
34-113 |
5.46e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.75 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526563825 34 IFGVIGPDGAGKSTLFRILASL-----ILPDSGSAIMNRYDIVKDYRKIRQIIGYMPGKFSLYQDLSVEENLKFFATLFG 108
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLadfdaLVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLER 80
|
....*
gi 2526563825 109 TTIEE 113
Cdd:pfam13304 81 EDVEE 85
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
131-167 |
7.97e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.92 E-value: 7.97e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2526563825 131 RRAGALSGGMKQKLALSCALIHKPEILILDEPTTGVD 167
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
23-60 |
8.12e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.11 E-value: 8.12e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2526563825 23 NGISFTVDDGEIFGVIGPDGAGKSTLFRILASLILPDS 60
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| |
