|
Name |
Accession |
Description |
Interval |
E-value |
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-248 |
0e+00 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 507.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLALSPEDRAGEGI 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMA 160
Cdd:PRK09580 81 FMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 161 VLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQG 240
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQG 240
|
....*...
gi 16129638 241 YGWLTEQQ 248
Cdd:PRK09580 241 YGWLTEQQ 248
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-247 |
5.05e-163 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 450.67 E-value: 5.05e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLALSPEDRAGEGIF 81
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGEDILELSPDERARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQYPVEIPGVSNQFFLQTALNAVRsyrgQETLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAV 161
Cdd:COG0396 81 LAFQYPVEIPGVSVSNFLRTALNARR----GEELSAREFLKLLKEKMKELGLDEDFLDRYVNEGFSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 162 LEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQGY 241
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIKPDFVHVLVDGRIVKSGGKELALELEEEGY 236
|
....*.
gi 16129638 242 GWLTEQ 247
Cdd:COG0396 237 DWLKEE 242
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-244 |
3.77e-160 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 443.24 E-value: 3.77e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLALSPEDRAGEGIF 81
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVTSGTILFKGQDLLELEPDERARAGLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQYPVEIPGVSNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAV 161
Cdd:TIGR01978 81 LAFQYPEEIPGVSNLEFLRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEGFSGGEKKRNEILQMAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 162 LEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQGY 241
Cdd:TIGR01978 161 LEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKPDYVHVLLDGRIVKSGDVELAKELEAKGY 240
|
...
gi 16129638 242 GWL 244
Cdd:TIGR01978 241 DWV 243
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-246 |
8.46e-131 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 369.36 E-value: 8.46e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLALSPEDRAGEGI 80
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMA 160
Cdd:CHL00131 87 FLAFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEGFSGGEKKRNEILQMA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 161 VLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQG 240
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHVMQNGKIIKTGDAELAKELEKKG 246
|
....*.
gi 16129638 241 YGWLTE 246
Cdd:CHL00131 247 YDWLKQ 252
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-241 |
5.95e-119 |
|
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: 337.58 E-value: 5.95e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLALSPEDRAGEGIF 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQYPVEIPGVSNQFFLqtalnavrsyrgqetldrfdfqdlmeekiallkmpedlltRSVNVGFSGGEKKRNDILQMAV 161
Cdd:cd03217 81 LAFQYPPEIPGVKNADFL----------------------------------------RYVNEGFSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 162 LEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQGY 241
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYDGRIVKSGDKELALEIEKKGY 200
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-223 |
1.31e-33 |
|
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: 120.65 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 3 SIKDLHVSVED--KAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRAGEgI 80
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL--GPTSGEVLVDGKDLTKLSLKELRRK-V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAFQYPveipgvSNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMA 160
Cdd:cd03225 78 GLVFQNP------DDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGL-EGLRDRSPFT-LSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 161 VLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYqriLDYIKP--DYVHVLYQGR 223
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHD---LDLLLElaDRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-228 |
8.74e-32 |
|
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: 116.45 E-value: 8.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKA----ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRA 76
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL--KPTSGSIIFDGKDLLKLSRRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 77 --GEGIFMAFQYPveipgvsnqfflQTALNAVRSYRGQ--ETL---DRFDFQDLMEEKIALLKM----PEDLLTRSVNvG 145
Cdd:cd03257 79 irRKEIQMVFQDP------------MSSLNPRMTIGEQiaEPLrihGKLSKKEARKEAVLLLLVgvglPEEVLNRYPH-E 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 146 FSGGEKKRNDIlQMA-VLEPELCILDESDSGLDIDALKVVADGVNSLRDGK-RSFIIVTHYQRILDYIKpDYVHVLYQGR 223
Cdd:cd03257 146 LSGGQRQRVAI-ARAlALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELgLTLLFITHDLGVVAKIA-DRVAVMYAGK 223
|
....*
gi 16129638 224 IVKSG 228
Cdd:cd03257 224 IVEEG 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-238 |
3.71e-31 |
|
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: 114.74 E-value: 3.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVED-KAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPED---RAG 77
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL--LKPTSGEVLVDGKDITKKNLRElrrKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 78 egifMAFQYPveipgvSNQFFLQTAL--------------NAVRSyRGQETLDRFDFQDLMEEKIALLkmpedlltrsvn 143
Cdd:COG1122 79 ----LVFQNP------DDQLFAPTVEedvafgpenlglprEEIRE-RVEEALELVGLEHLADRPPHEL------------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 144 vgfSGGEKKRndiLQMA---VLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYqriLDYIKP--DYVHV 218
Cdd:COG1122 136 ---SGGQKQR---VAIAgvlAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHD---LDLVAElaDRVIV 206
|
250 260
....*....|....*....|....
gi 16129638 219 LYQGRIVKSGD----FTLVKQLEE 238
Cdd:COG1122 207 LDDGRIVADGTprevFSDYELLEE 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-228 |
9.98e-31 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 113.75 E-value: 9.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPED--RAGEG 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGL--LRPDSGEVLIDGEDISGLSEAElyRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 80 IFMAFQypveipgvSNQFFlqTALNA-------VRSYRgqeTLDRFDFQDLMEEKIALL-------KMPEDLltrsvnvg 145
Cdd:cd03261 79 MGMLFQ--------SGALF--DSLTVfenvafpLREHT---RLSEEEIREIVLEKLEAVglrgaedLYPAEL-------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 146 fSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKR-SFIIVTHYQRILDYIkPDYVHVLYQGRI 224
Cdd:cd03261 138 -SGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGlTSIMVTHDLDTAFAI-ADRIAVLYDGKI 215
|
....
gi 16129638 225 VKSG 228
Cdd:cd03261 216 VAEG 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
1.59e-30 |
|
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: 118.08 E-value: 1.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSV--EDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEVT-GGTVEFKGKDLLALSPEDRAG 77
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRiSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 78 EgIFMAFQYPveipgvSNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDIL 157
Cdd:COG1123 84 R-IGMVFQDP------MTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGL-ERRLDRYPHQ-LSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129638 158 QMAVLEPELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTHYQRILDYIkPDYVHVLYQGRIVKSGD 229
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEI-ADRVVVMDDGRIVEDGP 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-229 |
3.47e-30 |
|
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: 112.53 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRAGEGIF 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF--LRPTSGSVLFDGEDITGLPPHEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQYPVEIPG--------VSNQFFLQTALNAVRSYRGQ--------ETLDRFDFQDLMEEKIALLkmpedlltrsvnvg 145
Cdd:cd03219 79 RTFQIPRLFPEltvlenvmVAAQARTGSGLLLARARREEreareraeELLERVGLADLADRPAGEL-------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 146 fSGGEKKRndiLQMA---VLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHyqrILDYIKP--DYVHVLY 220
Cdd:cd03219 145 -SYGQQRR---LEIAralATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEH---DMDVVMSlaDRVTVLD 217
|
....*....
gi 16129638 221 QGRIVKSGD 229
Cdd:cd03219 218 QGRVIAEGT 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-223 |
2.43e-29 |
|
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: 107.72 E-value: 2.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 3 SIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEdRAGEGIFM 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGL--LKPTSGEILIDGKDIAKLPLE-ELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 83 AFQypveipgvsnqfflqtalnavrsyrgqetldrfdfqdlmeekiallkmpedlltrsvnvgFSGGEKKRNDILQMAVL 162
Cdd:cd00267 78 VPQ------------------------------------------------------------LSGGQRQRVALARALLL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129638 163 EPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYIkPDYVHVLYQGR 223
Cdd:cd00267 98 NPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELA-ADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
1.15e-28 |
|
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: 113.07 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVS-----VEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDR 75
Cdd:COG1123 260 LLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLL--RPTSGSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 76 A--GEGIFMAFQYPveipgvsnqfflQTALNAVRS--------YRGQETLDRFDFQDLMEEKIALLKMPEDLLTRSVNvG 145
Cdd:COG1123 338 RelRRRVQMVFQDP------------YSSLNPRMTvgdiiaepLRLHGLLSRAERRERVAELLERVGLPPDLADRYPH-E 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLDidaLKVVADGVNSLRDGKR----SFIIVTHYQRILDYIKpDYVHVLYQ 221
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALD---VSVQAQILNLLRDLQRelglTYLFISHDLAVVRYIA-DRVAVMYD 480
|
....*...
gi 16129638 222 GRIVKSGD 229
Cdd:COG1123 481 GRIVEDGP 488
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-230 |
1.54e-28 |
|
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: 108.14 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRAG--E 78
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGL--LRPDSGEILVDGQDITGLSEKELYElrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 79 GIFMAFQY-------PVEipgvSN-QFFLqtalnavrsyRGQETLDRFDFQDLMEEKIALL-------KMPEDLltrsvn 143
Cdd:COG1127 83 RIGMLFQGgalfdslTVF----ENvAFPL----------REHTDLSEAEIRELVLEKLELVglpgaadKMPSEL------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 144 vgfSGGEKKRndilqmA------VLEPELCILDESDSGLDIDALKVVADGVNSLRDG-KRSFIIVTHyqrILDYIK--PD 214
Cdd:COG1127 143 ---SGGMRKR------ValaralALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTH---DLDSAFaiAD 210
|
250
....*....|....*.
gi 16129638 215 YVHVLYQGRIVKSGDF 230
Cdd:COG1127 211 RVAVLADGKIIAEGTP 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-203 |
2.07e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.82 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDLLALSPED-RAgeGI 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPP--TSGEIYLDGKPLSAMPPPEwRR--QV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAFQYPVEIPGVsnqffLQTALNAVRSYRgQETLDRFDFQDLMEEkialLKMPEDLLTRSVNvGFSGGEKKRNDILQMA 160
Cdd:COG4619 77 AYVPQEPALWGGT-----VRDNLPFPFQLR-ERKFDRERALELLER----LGLPPDILDKPVE-RLSGGERQRLALIRAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16129638 161 VLEPELCILDESDSGLDIDALKVVADGVNSLRDGK-RSFIIVTH 203
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgRAVLWVSH 189
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-229 |
2.18e-28 |
|
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: 108.21 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLALSPEDRAGEgi 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG--LLKPSSGEVLLDGRDLASLSRRELARR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 fMAF--QYPVEIPGVsnqfflqTALNAVRSYR--GQETLDRFDFQD--LMEEKIALLKMpEDLLTRSVNvGFSGGEKkrn 154
Cdd:COG1120 77 -IAYvpQEPPAPFGL-------TVRELVALGRypHLGLFGRPSAEDreAVEEALERTGL-EHLADRPVD-ELSGGER--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 155 dilQMAVL------EPELCILDESDSGLDI----DALKVVADGVnslRDGKRSFIIVTHYqriLD----YIkpDYVHVLY 220
Cdd:COG1120 144 ---QRVLIaralaqEPPLLLLDEPTSHLDLahqlEVLELLRRLA---RERGRTVVMVLHD---LNlaarYA--DRLVLLK 212
|
....*....
gi 16129638 221 QGRIVKSGD 229
Cdd:COG1120 213 DGRIVAQGP 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-229 |
1.31e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 105.53 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRAgeGIF 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGL--LRPTSGEVRVLGEDVARDPAEVRR--RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQYPVEIPGVSnqffLQTALNAVRSYRGqetLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAV 161
Cdd:COG1131 77 YVPQEPALYPDLT----VRENLRFFARLYG---LPRKEARERIDELLELFGL-TDAADRKVG-TLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129638 162 LEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHY----QRILdyikpDYVHVLYQGRIVKSGD 229
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYleeaERLC-----DRVAIIDKGRIVADGT 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-228 |
3.75e-27 |
|
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: 104.55 E-value: 3.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDLLALSPEDRAGEGI 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKP--DSGSILIDGEDVRKEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FmafqyPVEIPGVSNqfflQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMA 160
Cdd:COG4555 79 L-----PDERGLYDR----LTVRENIRYFAELYGLFDEELKKRIEELIELLGL-EEFLDRRVG-ELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 161 VLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHyqrILDYIKP--DYVHVLYQGRIVKSG 228
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSH---IMQEVEAlcDRVVILHKGKVVAQG 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-225 |
2.53e-26 |
|
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: 102.57 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVS----VEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLALSPEDRA 76
Cdd:COG1124 1 MLEVRNLSVSygqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER--PWSGEVTFDGRPVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 77 GEgIFMAFQYPveipgvsnqfflQTALNAVRSYRGQ--ETLDRFDFQDLMEEKIALLK---MPEDLLTRSVNvGFSGGEK 151
Cdd:COG1124 79 RR-VQMVFQDP------------YASLHPRHTVDRIlaEPLRIHGLPDREERIAELLEqvgLPPSFLDRYPH-QLSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 152 KRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLR-DGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIV 225
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHLC-DRVAVMQNGRIV 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-229 |
8.54e-26 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 100.72 E-value: 8.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRED---YEVTGGTVEFKGKDLLALSP---EDR 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipGAPDEGEVLLDGKDIYDLDVdvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 76 AGEGifMAFQYPVEIPGvsnqfflqTALNAVRsY--RGQETLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKR 153
Cdd:cd03260 81 RRVG--MVFQKPNPFPG--------SIYDNVA-YglRLHGIKLKEELDERVEEALRKAALWDEVKDRLHALGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 154 NDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDgKRSFIIVTH----YQRIldyikPDYVHVLYQGRIVKSGD 229
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHnmqqAARV-----ADRTAFLLNGRLVEFGP 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-229 |
2.04e-25 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 101.67 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVS--VEDKAI--LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAG-REDYEVTGGTVEFKGKDLLALSPEDR 75
Cdd:COG0444 1 LLEVRNLKVYfpTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGlLPPPGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 76 A---GEGIFMAFQYPveipgvsnqfflQTALNAVRSYRGQ--ETL---DRFDFQDLMEEKIALLKM-----PEDLLTRsv 142
Cdd:COG0444 81 RkirGREIQMIFQDP------------MTSLNPVMTVGDQiaEPLrihGGLSKAEARERAIELLERvglpdPERRLDRyp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 143 nvgFSGGEKKRNDILqMA-VLEPELCILDESDSGLDIDalkVVADGVNSLRDGKR----SFIIVTHyqrilD-----YIK 212
Cdd:COG0444 149 -heLSGGMRQRVMIA-RAlALEPKLLIADEPTTALDVT---IQAQILNLLKDLQRelglAILFITH-----DlgvvaEIA 218
|
250
....*....|....*..
gi 16129638 213 pDYVHVLYQGRIVKSGD 229
Cdd:COG0444 219 -DRVAVMYAGRIVEEGP 234
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-229 |
9.48e-25 |
|
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: 98.57 E-value: 9.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVS---VedKAiLRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRAG 77
Cdd:COG0411 4 LLEVRGLTKRfggL--VA-VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF--YRPTSGRILFDGRDITGLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 78 EGIFMAFQYPVEIPGVS-------------NQFFLQTALNAVRSYRG--------QETLDRFDFQDLMEEKIALLkmped 136
Cdd:COG0411 79 LGIARTFQNPRLFPELTvlenvlvaaharlGRGLLAALLRLPRARREereareraEELLERVGLADRADEPAGNL----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 137 lltrsvnvgfSGGEKKRndiLQMA---VLEPELCILDESDSGLDIDALKVVADGVNSLRDG-KRSFIIVTHyqrILDYIK 212
Cdd:COG0411 154 ----------SYGQQRR---LEIAralATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEH---DMDLVM 217
|
250
....*....|....*....
gi 16129638 213 P--DYVHVLYQGRIVKSGD 229
Cdd:COG0411 218 GlaDRIVVLDFGRVIAEGT 236
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-171 |
3.03e-24 |
|
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: 94.25 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRAGEgIFMAFQYPVEIPGVsnq 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGL--LSPTEGTILLDGQDLTDDERKSLRKE-IGYVFQDPQLFPRL--- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129638 97 fflqTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:pfam00005 75 ----TVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPgtLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-203 |
8.24e-24 |
|
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: 94.85 E-value: 8.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLlaLSPEDRAGEGI 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLL--PPSAGEVLWNGEPI--RDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAFQYpveiPGVSNQFFLQTALNAVRSYRG--------QETLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKK 152
Cdd:COG4133 78 AYLGHA----DGLKPELTVRENLRFWAALYGlradreaiDEALEAVGLAGLADLPVRQL---------------SAGQKR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16129638 153 RNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTH 203
Cdd:COG4133 139 RVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-203 |
9.16e-24 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 94.63 E-value: 9.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 3 SIKDLHVSVEDKA-ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDllaLSPEDRAgEGIF 81
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGL--IKESSGSILLNGKP---IKAKERR-KSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQypveipGVSNQFFLQTALNAVR-----SYRGQET----LDRFDFQDLMEekiallKMPEDLltrsvnvgfSGGEKK 152
Cdd:cd03226 75 YVMQ------DVDYQLFTDSVREELLlglkeLDAGNEQaetvLKDLDLYALKE------RHPLSL---------SGGQKQ 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16129638 153 RNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTH 203
Cdd:cd03226 134 RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-178 |
1.17e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.57 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLALSPEDRAGE-G 79
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG--ELTPSSGEVRLNGRPLAAWSPWELARRrA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 80 IF-----MAFQYPVE-------IPGVSNQFFLQTALnavrsyrgQETLDRFDFQDLMEEKIALLkmpedlltrsvnvgfS 147
Cdd:COG4559 79 VLpqhssLAFPFTVEevvalgrAPHGSSAAQDRQIV--------REALALVGLAHLAGRSYQTL---------------S 135
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16129638 148 GGEKKRndiLQMA-VL---------EPELCILDESDSGLDI 178
Cdd:COG4559 136 GGEQQR---VQLArVLaqlwepvdgGPRWLFLDEPTSALDL 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-228 |
1.35e-23 |
|
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: 93.65 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 3 SIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRAGEgifM 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGL--LKPSSGEILLDGKDLASLSPKELARK---I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 83 AfqypveipgvsnqfFLQTALNAVrsyrgqetldrfdfqDLmeekiallkmpEDLLTRSVNVgFSGGEKKRNDILQMAVL 162
Cdd:cd03214 76 A--------------YVPQALELL---------------GL-----------AHLADRPFNE-LSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129638 163 EPELCILDESDSGLDI----DALKVVADGVnslRDGKRSFIIVTHYqriLD--YIKPDYVHVLYQGRIVKSG 228
Cdd:cd03214 115 EPPILLLDEPTSHLDIahqiELLELLRRLA---RERGKTVVMVLHD---LNlaARYADRVILLKDGRIVAQG 180
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-229 |
1.54e-23 |
|
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: 94.42 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLALSPEDRAGEGIF 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP--PRSGSIRFDGRDITGLPPHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQypveipgvSNQFF--------LQTALNAVRSYRGQETLDR-FD-FQDLMEEkiallkmpedlltRSVNVG-FSGGE 150
Cdd:cd03224 79 YVPE--------GRRIFpeltveenLLLGAYARRRAKRKARLERvYElFPRLKER-------------RKQLAGtLSGGE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 151 KKrndILQMA---VLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHY-QRILDYIkpDYVHVLYQGRIVK 226
Cdd:cd03224 138 QQ---MLAIAralMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNaRFALEIA--DRAYVLERGRVVL 212
|
...
gi 16129638 227 SGD 229
Cdd:cd03224 213 EGT 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-224 |
3.71e-23 |
|
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: 92.08 E-value: 3.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRagEGIF 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGL--LKPDSGEIKVLGKDIKKEPEEVK--RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQYPVEIPGVSnqfflqtalnavrsyrGQETLDrfdfqdlmeekiallkmpedlltrsvnvgFSGGEKKRNDILQMAV 161
Cdd:cd03230 77 YLPEEPSLYENLT----------------VRENLK-----------------------------LSGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129638 162 LEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRI 224
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLC-DRVAILNNGRI 173
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-229 |
5.00e-23 |
|
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: 93.51 E-value: 5.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLALSPEDRAGEGI 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISG--LLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMA------FqypveiPGVS---NqffLQTALNAVRSYRG-QETLDR-FD-FQDLMEekiaLLKMPEDLLtrsvnvgfSG 148
Cdd:COG0410 81 GYVpegrriF------PSLTveeN---LLLGAYARRDRAEvRADLERvYElFPRLKE----RRRQRAGTL--------SG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 149 GEKkrndilQM-A-----VLEPELCILDESDSGLdidALKVVA---DGVNSLRDGKRSFIIVTHY-QRILDYIkpDYVHV 218
Cdd:COG0410 140 GEQ------QMlAigralMSRPKLLLLDEPSLGL---APLIVEeifEIIRRLNREGVTILLVEQNaRFALEIA--DRAYV 208
|
250
....*....|.
gi 16129638 219 LYQGRIVKSGD 229
Cdd:COG0410 209 LERGRIVLEGT 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-228 |
1.55e-22 |
|
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: 92.45 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLsATLAGREDYEVTGGTVEFKGKDLLALSPED-RAGEG 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTL-LSLITGDLPPTYGNDVRLFGERRGGEDVWElRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 80 IF---MAFQYPVEIpgvsnqfflqTALNAVRS--------YRGQETLDRfdfqDLMEEKIALLKMpEDLLTRSVNvGFSG 148
Cdd:COG1119 82 LVspaLQLRFPRDE----------TVLDVVLSgffdsiglYREPTDEQR----ERARELLELLGL-AHLADRPFG-TLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 149 GEKKRndiLQMA---VLEPELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTHYqriLDYIKPDYVHVLY--QG 222
Cdd:COG1119 146 GEQRR---VLIAralVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHH---VEEIPPGITHVLLlkDG 219
|
....*.
gi 16129638 223 RIVKSG 228
Cdd:COG1119 220 RVVAAG 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-224 |
2.41e-22 |
|
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: 91.40 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSV----EDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLALSPEDRA- 76
Cdd:cd03255 1 IELKNLSKTYggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR--PTSGEVRVDGTDISKLSEKELAa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 77 --GEGIFMAFQYP-----------VEIPgvsnqFFLQTALNAVRSYRGQETLDRFDFQDLMEekiallKMPEDLltrsvn 143
Cdd:cd03255 79 frRRHIGFVFQSFnllpdltalenVELP-----LLLAGVPKKERRERAEELLERVGLGDRLN------HYPSEL------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 144 vgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTHYQRILDYIkpDYVHVLYQG 222
Cdd:cd03255 142 ---SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELAEYA--DRIIELRDG 216
|
..
gi 16129638 223 RI 224
Cdd:cd03255 217 KI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-228 |
3.47e-22 |
|
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: 90.66 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRageGIF 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLE--RPDSGEILIDGRDVTGVPPERR---NIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEtldrfdfQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAV 161
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLRGVPKAEI-------RARVRELLELVGL-EGLLNRYPH-ELSGGQQQRVALARALA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129638 162 LEPELCILDESDSGLDID-ALKVVADGVNSLRDGKRSFIIVTHYQ----RILDYIKpdyvhVLYQGRIVKSG 228
Cdd:cd03259 147 REPSLLLLDEPLSALDAKlREELREELKELQRELGITTIYVTHDQeealALADRIA-----VMNEGRIVQVG 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-229 |
5.31e-21 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 88.22 E-value: 5.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLlalspeDRAGEGI 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILG--LLPPTSGTVRLFGKPP------RRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 -----FMAF--QYPVeipgvsnqfflqTALNAVRS--YRGQETLDRFDFQD--LMEEKIALLKMpEDLLTRSVNvGFSGG 149
Cdd:COG1121 78 gyvpqRAEVdwDFPI------------TVRDVVLMgrYGRRGLFRRPSRADreAVDEALERVGL-EDLADRPIG-ELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTH-YQRILDYIKpdyvHVLY-QGRIVKS 227
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHdLGAVREYFD----RVLLlNRGLVAH 219
|
..
gi 16129638 228 GD 229
Cdd:COG1121 220 GP 221
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-229 |
9.57e-21 |
|
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: 90.60 E-value: 9.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVS--VEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLALSPEDRAgeg 79
Cdd:COG4987 334 LELEDVSFRypGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR--FLDPQSGSITLGGVDLRDLDEDDLR--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 80 ifmafqypvEIPGVSNQ---FFLQTALNAVRSYRGQ-------ETLDRFDFQDLMEEkiallkMPEDLLTRsvnVG---- 145
Cdd:COG4987 409 ---------RRIAVVPQrphLFDTTLRENLRLARPDatdeelwAALERVGLGDWLAA------LPDGLDTW---LGeggr 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 146 -FSGGEKKRndiLQMA-VL--EPELCILDESDSGLDID-ALKVVADGVNSLRDgkRSFIIVTHYQRILDYIkpDYVHVLY 220
Cdd:COG4987 471 rLSGGERRR---LALArALlrDAPILLLDEPTEGLDAAtEQALLADLLEALAG--RTVLLITHRLAGLERM--DRILVLE 543
|
....*....
gi 16129638 221 QGRIVKSGD 229
Cdd:COG4987 544 DGRIVEQGT 552
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-226 |
1.94e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 86.25 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKA----ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLALSPEDRA 76
Cdd:COG1136 4 LLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDR--PTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 77 ---GEGIFMAFQYP-----------VEIPGVsnqffLQTALNAVRSYRGQETLDRFDFQDLMEekiallKMPEDLltrsv 142
Cdd:COG1136 82 rlrRRHIGFVFQFFnllpeltalenVALPLL-----LAGVSRKERRERARELLERVGLGDRLD------HRPSQL----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 143 nvgfSGGEKKRndilqMA-----VLEPELCILDE------SDSGLDI-DALKVVAdgvnslRDGKRSFIIVTHYQRILDY 210
Cdd:COG1136 146 ----SGGQQQR-----VAiaralVNRPKLILADEptgnldSKTGEEVlELLRELN------RELGTTIVMVTHDPELAAR 210
|
250
....*....|....*.
gi 16129638 211 IkpDYVHVLYQGRIVK 226
Cdd:COG1136 211 A--DRVIRLRDGRIVS 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-227 |
3.90e-20 |
|
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: 84.02 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLALSPEDRAGEGIF 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSG--LYKPDSGEILVDGKEVSFASPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQYPVeipgvsnqfflqtalnavrsyrgqetldrfdfqdlmeekiallkmpedlltrsvnvgfsgGEKKRNDILQMAV 161
Cdd:cd03216 79 MVYQLSV------------------------------------------------------------GERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129638 162 LEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYqriLDYIKP--DYVHVLYQGRIVKS 227
Cdd:cd03216 99 RNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHR---LDEVFEiaDRVTVLRDGRVVGT 163
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-229 |
6.28e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 87.08 E-value: 6.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRageGI 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFE--TPDSGRILLDGRDVTGLPPEKR---NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAFQ---------------YPVEIPGVSnqfflqtalNAVRSYRGQETLDRFDFQDLMEekiallKMPEDLltrsvnvg 145
Cdd:COG3842 80 GMVFQdyalfphltvaenvaFGLRMRGVP---------KAEIRARVAELLELVGLEGLAD------RYPHQL-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 146 fSGGEKKRndilqMA-----VLEPELCILDESDSGLDidalkvvadgvNSLRDG-----KR-------SFIIVTHYQ--- 205
Cdd:COG3842 137 -SGGQQQR-----VAlaralAPEPRVLLLDEPLSALD-----------AKLREEmreelRRlqrelgiTFIYVTHDQeea 199
|
250 260
....*....|....*....|....*....
gi 16129638 206 -----RILdyikpdyvhVLYQGRIVKSGD 229
Cdd:COG3842 200 laladRIA---------VMNDGRIEQVGT 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-203 |
6.97e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.46 E-value: 6.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEVTG-GTVEFKGKDLLALSPEDRageG 79
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSAsGEVLLNGRRLTALPAEQR---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 80 IFMAFQYPVEIPGVS---N-QFFLQTALN-AVRSYRGQETLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRN 154
Cdd:COG4136 78 IGILFQDDLLFPHLSvgeNlAFALPPTIGrAQRRARVEQALEEAGLAGFADRDPATL---------------SGGQRARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129638 155 DILQMAVLEPELCILDESDSGLDIDalkvvadgvnsLRDGKRSF------------IIVTH 203
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAA-----------LRAQFREFvfeqirqrgipaLLVTH 192
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-223 |
7.17e-20 |
|
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: 83.59 E-value: 7.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKA--ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLALSPEdrageg 79
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR--LYDPTSGEILIDGVDLRDLDLE------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 80 ifmafqypveipgvsnqfflqtalnavrSYRgqetldrfdfqdlmeEKIALLkmPED--LLTRSV--NVgFSGGEKKRND 155
Cdd:cd03228 73 ----------------------------SLR---------------KNIAYV--PQDpfLFSGTIreNI-LSGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129638 156 ILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGR 223
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALRALAKG-KTVIVIAH--RLSTIRDADRIIVLDDGR 171
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-178 |
2.13e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.05 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLALSPEDRAG--- 77
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG--ELSPDSGEVRLNGRPLADWSPAELARrra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 78 ---EGIFMAFQYPVE-------IPGVSNQFFLQTALnavrsyrgQETLDRFDFQDLMEEKIALLkmpedlltrsvnvgfS 147
Cdd:PRK13548 80 vlpQHSSLSFPFTVEevvamgrAPHGLSRAEDDALV--------AAALAQVDLAHLAGRDYPQL---------------S 136
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16129638 148 GGEKKRndiLQMA-VL--------EPELCILDESDSGLDI 178
Cdd:PRK13548 137 GGEQQR---VQLArVLaqlwepdgPPRWLLLDEPTSALDL 173
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-203 |
2.17e-19 |
|
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: 83.35 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPE-DRAGEGI 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLE--EPDSGTIIIDGLKLTDDKKNiNELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAFQypveipgvsnQFFL---QTALnavrsyrgqetldrfdfQDLMEEKIALLKMP--------EDLLTRsvnVG---- 145
Cdd:cd03262 79 GMVFQ----------QFNLfphLTVL-----------------ENITLAPIKVKGMSkaeaeeraLELLEK---VGladk 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 146 -------FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTH 203
Cdd:cd03262 129 adaypaqLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
3.78e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 83.89 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVS--VEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALS-PEDRAG 77
Cdd:PRK13632 7 MIKVENVSFSypNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGL--LKPQSGEIKIDGITISKENlKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 78 EGIFmaFQYPveipgvSNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDIL 157
Cdd:PRK13632 85 IGII--FQNP------DNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGM-EDYLDKEPQ-NLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129638 158 QMAVLEPELCILDESDSGLDIDALKVVADGVNSLRD-GKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGD 229
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtRKKTLISITH--DMDEAILADKVIVFSEGKLIAQGK 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-248 |
5.59e-19 |
|
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: 85.66 E-value: 5.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 12 EDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLALSPEDRAgEGIFMAFQypveip 91
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG--LYEPTSGRILIDGIDLRQIDPASLR-RQIGVVLQ------ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 92 gvSNQFFLQTALNAVRSYRGQETLDRfdfqdlMEE--KIA-----LLKMPEDLLTRsvnVG-----FSGGEKKRndiLQM 159
Cdd:COG2274 557 --DVFLFSGTIRENITLGDPDATDEE------IIEaaRLAglhdfIEALPMGYDTV---VGeggsnLSGGQRQR---LAI 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 160 A---VLEPELCILDESDSGLDIDALKVVADGVNSLRDGkRSFIIVTHYQRILDYIkpDYVHVLYQGRIVKSGDFtlvKQL 236
Cdd:COG2274 623 AralLRNPRILILDEATSALDAETEAIILENLRRLLKG-RTVIIIAHRLSTIRLA--DRIIVLDKGRIVEDGTH---EEL 696
|
250
....*....|....
gi 16129638 237 EEQG--YGWLTEQQ 248
Cdd:COG2274 697 LARKglYAELVQQQ 710
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
14-226 |
5.76e-19 |
|
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: 83.32 E-value: 5.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 14 KAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRAgegifmAFQYPVeipgv 93
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLE--KPAQGTVSFRGQDLYQLDRKQRR------AFRRDV----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 94 snQFFLQTALNAV--RSYRGQ------ETLDRFDFQDLMEEKIALLKM----PEDLltRSVNVGFSGGEKKRNDILQMAV 161
Cdd:TIGR02769 91 --QLVFQDSPSAVnpRMTVRQiigeplRHLTSLDESEQKARIAELLDMvglrSEDA--DKLPRQLSGGQLQRINIARALA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129638 162 LEPELCILDESDSGLDIDALKVVADGVNSLR-DGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVK 226
Cdd:TIGR02769 167 VKPKLIVLDEAVSNLDMVLQAVILELLRKLQqAFGTAYLFITHDLRLVQSFC-QRVAVMDKGQIVE 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-228 |
7.52e-19 |
|
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: 82.03 E-value: 7.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKA----ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRA 76
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL--LEPDAGFATVDGFDVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 77 GEGIFmafqypveiPGVSNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDI 156
Cdd:cd03266 79 RLGFV---------SDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGM-EELLDRRVG-GFSTGMRQKVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129638 157 LQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHyqrILDYIKP--DYVHVLYQGRIVKSG 228
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTH---IMQEVERlcDRVVVLHRGRVVYEG 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-228 |
8.63e-19 |
|
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: 81.49 E-value: 8.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLAL-SPEDRAGEGI 80
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI--KPDSGEITFDGKSYQKNiEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 fmafQYPVEIPGVSNQFFLQTALNA--VRSYRGQETLDRFDFQDLMEEKIAllkmpedlltrsvnvGFSGGEKKRNDILQ 158
Cdd:cd03268 79 ----EAPGFYPNLTARENLRLLARLlgIRKKRIDEVLDVVGLKDSAKKKVK---------------GFSLGMKQRLGIAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 159 MAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVhVLYQGRIVKSG 228
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIG-IINKGKLIEEG 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-231 |
1.00e-18 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 84.81 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVS-VEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRAgEGI 80
Cdd:COG4988 337 IELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF--LPPYSGSILINGVDLSDLDPASWR-RQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAFQYPVEIPG------------VSNQfFLQTALNAVRsyrgqetLDRFdfqdlmeekIALLkmPEDLLTR--SVNVGF 146
Cdd:COG4988 414 AWVPQNPYLFAGtirenlrlgrpdASDE-ELEAALEAAG-------LDEF---------VAAL--PDGLDTPlgEGGRGL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVK 226
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG-RTVILITH--RLALLAQADRILVLDDGRIVE 551
|
....*
gi 16129638 227 SGDFT 231
Cdd:COG4988 552 QGTHE 556
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-228 |
1.07e-18 |
|
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: 81.06 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVE------DKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLALSPEDR 75
Cdd:cd03213 4 LSFRNLTVTVKsspsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 76 AG----EGIFMAFqypveipgvsnqfflQTAlnavrsyrgQETLdrfDFQdlmeekiALLKmpedlltrsvnvGFSGGEK 151
Cdd:cd03213 84 IGyvpqDDILHPT---------------LTV---------RETL---MFA-------AKLR------------GLSGGER 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129638 152 KRNDI-LQMaVLEPELCILDESDSGLD-IDALKVVaDGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:cd03213 118 KRVSIaLEL-VSNPSLLFLDEPTSGLDsSSALQVM-SLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-203 |
1.88e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 81.75 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDY--EVT-GGTVEFKGKDLlaLSPEDRAG 77
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpEVTiTGSIVYNGHNI--YSPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 78 E---GIFMAFQYPveipgvsNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKI---ALLKMPEDLLTRSVnVGFSGGEK 151
Cdd:PRK14239 83 DlrkEIGMVFQQP-------NPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLkgaSIWDEVKDRLHDSA-LGLSGGQQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16129638 152 KRNDILQMAVLEPELCILDESDSGLD-IDALKvVADGVNSLRDgKRSFIIVTH 203
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDpISAGK-IEETLLGLKD-DYTMLLVTR 205
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-203 |
3.93e-18 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 79.39 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 12 EDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLlalsPEDRAG-----EGIFMAFQY 86
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGL--LRPQSGAVLIDGEPL----DYSRKGllerrQRVGLVFQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 87 PveipgvSNQFFLQTA--------LN------AVRSyRGQETLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKK 152
Cdd:TIGR01166 77 P------DDQLFAADVdqdvafgpLNlglseaEVER-RVREALTAVGASGLRERPTHCL---------------SGGEKK 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16129638 153 RNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTH 203
Cdd:TIGR01166 135 RVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-85 |
8.57e-18 |
|
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: 79.40 E-value: 8.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKA----ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLALSPEDRA 76
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDR--PTSGTVRLAGQDLFALDEDARA 85
|
90
....*....|....*
gi 16129638 77 ---GEGI---FMAFQ 85
Cdd:COG4181 86 rlrARHVgfvFQSFQ 100
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-248 |
3.54e-17 |
|
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: 77.97 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 16 ILRGLSLDVHPGEVHAIMGPNGSGKSTLsATLAGREdYEVTGGTVEFKGKDLLALSPEDRAGEgIFMAFQYPVeipgvsn 95
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTV-VSLLERF-YDPTSGEILLDGVDIRDLNLRWLRSQ-IGLVSQEPV------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 96 qFFLQTALNAVRsyrgqetLDRFDFQDLMEEKIALL--------KMPEDLLTRSVNVGF--SGGEKKRNDILQMAVLEPE 165
Cdd:cd03249 88 -LFDGTIAENIR-------YGKPDATDEEVEEAAKKanihdfimSLPDGYDTLVGERGSqlSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 166 LCILDESDSGLDIDALKVVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF-TLVKQleEQGYGWL 244
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKG-RTTIVIAH--RLSTIRNADLIAVLQNGQVVEQGTHdELMAQ--KGVYAKL 234
|
....
gi 16129638 245 TEQQ 248
Cdd:cd03249 235 VKAQ 238
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-229 |
3.82e-17 |
|
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: 80.11 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSV----EDKAILRGLSLDVHPGEVHAIMGPNGSGKS--TLSAT--LAgrEDYEVTGGTVEFKGKDLLALSP 72
Cdd:COG4172 6 LLSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSvtALSILrlLP--DPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 73 ED-RA--GEGIFMAFQYPveipgvsnqfflQTALNAVRSYRGQ--ETL---DRFDFQDLMEEKIALLKM-----PEDLLT 139
Cdd:COG4172 84 RElRRirGNRIAMIFQEP------------MTSLNPLHTIGKQiaEVLrlhRGLSGAAARARALELLERvgipdPERRLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 140 RsvnvgF----SGGEKKRNDIlQMAVL-EPELCILDESDSGLD------IDALkvvadgvnsLRDGKRS------FI--- 199
Cdd:COG4172 152 A-----YphqlSGGQRQRVMI-AMALAnEPDLLIADEPTTALDvtvqaqILDL---------LKDLQRElgmallLIthd 216
|
250 260 270
....*....|....*....|....*....|..
gi 16129638 200 --IVTHYQrildyikpDYVHVLYQGRIVKSGD 229
Cdd:COG4172 217 lgVVRRFA--------DRVAVMRQGEIVEQGP 240
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-203 |
5.10e-17 |
|
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: 76.94 E-value: 5.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALS-------PED 74
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGI--ILPDSGEVLFDGKPLDIAArnrigylPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 75 RA---GEGIFMAFQYPVEIPGVSnqffLQTALNAVRSYrgqetLDRFDFQDLMEEKIallkmpEDLltrsvnvgfSGGEK 151
Cdd:cd03269 79 RGlypKMKVIDQLVYLAQLKGLK----KEEARRRIDEW-----LERLELSEYANKRV------EEL---------SKGNQ 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16129638 152 KRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTH 203
Cdd:cd03269 135 QKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTH 186
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-225 |
5.34e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.80 E-value: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 14 KAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRAgegifmAFQYPVeipgv 93
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLE--SPSQGNVSWRGEPLAKLNRAQRK------AFRRDI----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 94 snQFFLQTALNAV-----------RSYRGQETLDRFDFQDLMEEKIALLKMPEDLLTRsVNVGFSGGEKKRNDILQMAVL 162
Cdd:PRK10419 92 --QMVFQDSISAVnprktvreiirEPLRHLLSLDKAERLARASEMLRAVDLDDSVLDK-RPPQLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129638 163 EPELCILDESDSGLDIdalkVVADGVNSL-----RDGKRSFIIVTHYQRILDYIkPDYVHVLYQGRIV 225
Cdd:PRK10419 169 EPKLLILDEAVSNLDL----VLQAGVIRLlkklqQQFGTACLFITHDLRLVERF-CQRVMVMDNGQIV 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-203 |
5.67e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.72 E-value: 5.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFkgkdllalspedraGEGI 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGEL--EPDSGTVKL--------------GETV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAF--QypveipgvsNQFFL---QTALNAVRSYR--GQET-----LDRFDFQdlmeekiallkmPEDLLTRsVNVgFSG 148
Cdd:COG0488 379 KIGYfdQ---------HQEELdpdKTVLDELRDGApgGTEQevrgyLGRFLFS------------GDDAFKP-VGV-LSG 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129638 149 GEKKRndiLQMAVL---EPELCILDESDSGLDIDALKVVADGvnsLRDGKRSFIIVTH 203
Cdd:COG0488 436 GEKAR---LALAKLllsPPNVLLLDEPTNHLDIETLEALEEA---LDDFPGTVLLVSH 487
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
17-228 |
5.68e-17 |
|
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: 77.02 E-value: 5.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRAGEGIfmAFQYPV---EIPGV 93
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTL--LKPTSGRATVAGHDVVREPREVRRRIGI--VFQDLSvddELTGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 94 SNqFFLQTAL----NAVRSYRGQETLdrfDFQDLMEEKIALLKMpedlltrsvnvgFSGGEKKRNDILQMAVLEPELCIL 169
Cdd:cd03265 92 EN-LYIHARLygvpGAERRERIDELL---DFVGLLEAADRLVKT------------YSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 170 DESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLC-DRVAIIDHGRIIAEG 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-223 |
6.31e-17 |
|
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: 75.69 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRAGEG-I 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE--EPDSGSILIDGEDLTDLEDELPPLRRrI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAFQYPVEIPGVSnqfflqtalnaVRsyrgqetldrfdfqdlmeEKIALlkmpedlltrsvnvGFSGGEKKRNDILQMA 160
Cdd:cd03229 79 GMVFQDFALFPHLT-----------VL------------------ENIAL--------------GLSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129638 161 VLEPELCILDESDSGLDIDALKVVADGVNSLRDG-KRSFIIVTHYQRILDYIKpDYVHVLYQGR 223
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLA-DRVVVLRDGK 178
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-203 |
7.87e-17 |
|
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: 76.42 E-value: 7.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 3 SIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLALSpeDRAGegiFM 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILG--LLKPTSGSIRVFGKPLEKER--KRIG---YV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 83 A------FQYPVEIPGVsnqfflqTALNAVRSYRGQETLDRFDFQDLME--EKIALLKMPEDLLTRsvnvgFSGGEKKRN 154
Cdd:cd03235 74 PqrrsidRDFPISVRDV-------VLMGLYGHKGLFRRLSKADKAKVDEalERVGLSELADRQIGE-----LSGGQQQRV 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16129638 155 DILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTH 203
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTH 190
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-228 |
1.08e-16 |
|
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: 76.51 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 13 DKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRageGIFMAFQYPVEIPG 92
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFE--TPTSGEILLDGKDITNLPPHKR---PVNTVFQNYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 93 VS---N-QFFLQTAlnavrsyrgqeTLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCI 168
Cdd:cd03300 87 LTvfeNiAFGLRLK-----------KLPKAEIKERVAEALDLVQL-EGYANRKPS-QLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129638 169 LDESDSGLDidaLKVVADGVNSLRDGKRS----FIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:cd03300 154 LDEPLGALD---LKLRKDMQLELKRLQKElgitFVFVTHDQEEALTMS-DRIAVMNKGKIQQIG 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-240 |
1.36e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.98 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGkdlLALSPED----RAGEGifMAFQYPveipg 92
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE--AGTITVGG---MVLSEETvwdvRRQVG--MVFQNP----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 93 vSNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDES 172
Cdd:PRK13635 91 -DNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGM-EDFLNREPH-RLSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129638 173 DSGLDIDALKVVADGVNSLRDGKRSFII-VTHyqRILDYIKPDYVHVLYQGRIVKSGD----FTLVKQLEEQG 240
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLsITH--DLDEAAQADRVIVMNKGEILEEGTpeeiFKSGHMLQEIG 238
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-228 |
1.77e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 76.24 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGR-EDYEV---TGGTVEFKGKDLLALSPEDRA 76
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSkikVDGKVLYFGKDIFQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 77 GEgIFMAFQYPVEIPGVSnqfflqTALNAVRSYRGQETLDRFDFQDLMEE---KIALLKMPEDLLTRSVNvGFSGGEKKR 153
Cdd:PRK14246 90 KE-VGMVFQQPNPFPHLS------IYDNIAYPLKSHGIKEKREIKKIVEEclrKVGLWKEVYDRLNSPAS-QLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 154 NDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDgKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKN-EIAIVIVSHNPQQVARVA-DYVAFLYNGELVEWG 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-177 |
1.90e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 76.28 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHV-----SVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLALSPEDR 75
Cdd:COG1101 1 MLELKNLSKtfnpgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAG--SLPPDSGSILIDGKDVTKLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 76 AGegiFMA--FQYPVeipgvsnqffLQTALN-------AVRSYRGQetldRFDFQ--------DLMEEKIALLKMP-EDL 137
Cdd:COG1101 79 AK---YIGrvFQDPM----------MGTAPSmtieenlALAYRRGK----RRGLRrgltkkrrELFRELLATLGLGlENR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16129638 138 LTrsVNVGF-SGGEkkRNDI-LQMAVL-EPELCILDESDSGLD 177
Cdd:COG1101 142 LD--TKVGLlSGGQ--RQALsLLMATLtKPKLLLLDEHTAALD 180
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-240 |
1.91e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 78.23 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 13 DKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLalspedragegifmafQYpveipg 92
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL--QNLYQPTGGQVLLDGVPLV----------------QY------ 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 93 vsNQFFLQTALNAV--------RSYRGQET--LDRFDFQDLMEEKIA------LLKMPEDLLTrsvNVG-----FSGGEK 151
Cdd:TIGR00958 549 --DHHYLHRQVALVgqepvlfsGSVRENIAygLTDTPDEEIMAAAKAanahdfIMEFPNGYDT---EVGekgsqLSGGQK 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 152 KRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSlrdGKRSFIIVTHYQRILDyiKPDYVHVLYQGRIVKSGDFt 231
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR---ASRTVLLIAHRLSTVE--RADQILVLKKGSVVEMGTH- 697
|
....*....
gi 16129638 232 lvKQLEEQG 240
Cdd:TIGR00958 698 --KQLMEDQ 704
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
12-240 |
2.54e-16 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 75.93 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 12 EDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDllALSPE------DRAGegifMAFQ 85
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGL--LLPTSGKVTVDGLD--TLDEEnlweirKKVG----MVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 86 YPveipgvSNQFFLQTALNAVRSyrGQETL--DRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAVLE 163
Cdd:TIGR04520 85 NP------DNQFVGATVEDDVAF--GLENLgvPREEMRKRVDEALKLVGM-EDFRDREPHL-LSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 164 PELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTHYqrILDYIKPDYVHVLYQGRIVKSGD----FTLVKQLEE 238
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHD--MEEAVLADRVIVMNKGKIVAEGTpreiFSQVELLKE 232
|
..
gi 16129638 239 QG 240
Cdd:TIGR04520 233 IG 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-203 |
2.59e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.14 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEdRAGEGI 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASL--ISPTSGTLLFEGEDISTLKPE-IYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAFQYPVeipgvsnqFFLQTAL-NAVRSY--RGQeTLDRFDFQDlmeeKIALLKMPEDLLTRSVNvGFSGGEKKRNDIL 157
Cdd:PRK10247 84 SYCAQTPT--------LFGDTVYdNLIFPWqiRNQ-QPDPAIFLD----DLERFALPDTILTKNIA-ELSGGEKQRISLI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16129638 158 QMAVLEPELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTH 203
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTH 196
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-229 |
2.65e-16 |
|
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: 75.31 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKA----ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDLLALSPEDR- 75
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERP--TSGSVLVDGTDLTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 76 -AGEGIFMAFQ---------------YPVEIPGVSnqfflqtalnavRSYRGQETLDRFDFQDLMEEKIAllkMPEDLlt 139
Cdd:cd03258 79 kARRRIGMIFQhfnllssrtvfenvaLPLEIAGVP------------KAEIEERVLELLELVGLEDKADA---YPAQL-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 140 rsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVadgVNSLRDGKRSF----IIVTHYqriLDYIKP-- 213
Cdd:cd03258 142 -------SGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSI---LALLRDINRELgltiVLITHE---MEVVKRic 208
|
250
....*....|....*.
gi 16129638 214 DYVHVLYQGRIVKSGD 229
Cdd:cd03258 209 DRVAVMEKGEVVEEGT 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-203 |
3.39e-16 |
|
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: 77.33 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDK-AILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRaGEGI 80
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF--VDPTEGSIAVNGVPLADADADSW-RDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAFQYPveipgvsnQFFLQTALNAVRSYRG-------QETLDRFDFQDLMEEkiallkMPEDLLTR--SVNVGFSGGEK 151
Cdd:TIGR02857 399 AWVPQHP--------FLFAGTIAENIRLARPdasdaeiREALERAGLDEFVAA------LPQGLDTPigEGGAGLSGGQA 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16129638 152 KRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGkRSFIIVTH 203
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG-RTVLLVTH 515
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-228 |
5.87e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 76.74 E-value: 5.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 12 EDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPED-RagEGIFMAFQypvei 90
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF--YDPTSGRILIDGVDIRDLTLESlR--RQIGVVPQ----- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 91 pgvsnQFFL--QTALNAVRSYRGQETLDRfdfqdlMEE--KIA-----LLKMPEDLLT----RSVNvgFSGGEKKRNDIL 157
Cdd:COG1132 422 -----DTFLfsGTIRENIRYGRPDATDEE------VEEaaKAAqahefIEALPDGYDTvvgeRGVN--LSGGQRQRIAIA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129638 158 QMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFII------VTHYQRILdyikpdyvhVLYQGRIVKSG 228
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIahrlstIRNADRIL---------VLDDGRIVEQG 556
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-230 |
6.26e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.90 E-value: 6.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDL--HVSVED------------KAIlRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKD 66
Cdd:PRK15079 8 LLEVADLkvHFDIKDgkqwfwqppktlKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGL--VKATDGEVAWLGKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 67 LLALSPEDR--AGEGIFMAFQYPVeipgvsnqfflqTALN-----------AVRSYR----GQETLDRFdfqDLMEEKIA 129
Cdd:PRK15079 85 LLGMKDDEWraVRSDIQMIFQDPL------------ASLNprmtigeiiaePLRTYHpklsRQEVKDRV---KAMMLKVG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 130 LLkmpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIdalKVVADGVNSLRDGKR----SFIIVTHYQ 205
Cdd:PRK15079 150 LL---PNLINRYPH-EFSGGQCQRIGIARALILEPKLIICDEPVSALDV---SIQAQVVNLLQQLQRemglSLIFIAHDL 222
|
250 260
....*....|....*....|....*
gi 16129638 206 RILDYIKpDYVHVLYQGRIVKSGDF 230
Cdd:PRK15079 223 AVVKHIS-DRVLVMYLGHAVELGTY 246
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
17-228 |
7.01e-16 |
|
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: 75.12 E-value: 7.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRagEGIFMAFQYPV---EIPGV 93
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTL--LRPTSGTARVAGYDVVREPRKVR--RSIGIVPQYASvdeDLTGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 94 SNQFF---LQTALNAVRSYRGQETLDRFDFQDLMEEKIAllkmpedlltrsvnvGFSGGEKKRNDILQMAVLEPELCILD 170
Cdd:TIGR01188 85 ENLEMmgrLYGLPKDEAEERAEELLELFELGEAADRPVG---------------TYSGGMRRRLDIAASLIHQPDVLFLD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129638 171 ESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:TIGR01188 150 EPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLC-DRIAIIDHGRIIAEG 206
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-228 |
7.79e-16 |
|
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: 73.83 E-value: 7.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRageGIF 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLE--EPTSGRIYIGGRDVTDLPPKDR---DIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQ----YPvEIPGVSNQFFlqtALNaVRSYRGQETLDRfdfqdlMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDIL 157
Cdd:cd03301 76 MVFQnyalYP-HMTVYDNIAF---GLK-LRKVPKDEIDER------VREVAELLQI-EHLLDRKPK-QLSGGQRQRVALG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129638 158 QMAVLEPELCILDESDSGLDIdALKVV--ADGVNSLRDGKRSFIIVTHyqrilDYIKP----DYVHVLYQGRIVKSG 228
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDA-KLRVQmrAELKRLQQRLGTTTIYVTH-----DQVEAmtmaDRIAVMNDGQIQQIG 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-228 |
1.06e-15 |
|
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: 73.38 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGeVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRAGEGiF 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATL--TPPSSGTIRIDGQDVLKQPQKLRRRIG-Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQYPVeIPGVSNQFFL--QTALNAVRSYRGQETLDRfdfqdlMEEKIALlkmpEDLLTRSVNvGFSGGEKKRNDILQM 159
Cdd:cd03264 77 LPQEFGV-YPNFTVREFLdyIAWLKGIPSKEVKARVDE------VLELVNL----GDRAKKKIG-SLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129638 160 AVLEPELCILDESDSGLDIDALKVVADGVNSLRDGkRSFIIVTHyqrILDYIKP--DYVHVLYQGRIVKSG 228
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED-RIVILSTH---IVEDVESlcNQVAVLNKGKLVFEG 211
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
13-177 |
1.91e-15 |
|
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: 72.69 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 13 DKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGR-EDYEVTGGTVEFKGKdllALSPEdragegifmafQYPVEIP 91
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvEGGGTTSGQILFNGQ---PRKPD-----------QFQKCVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 92 GVSNQFFLQTALnAVRSY-------RGQETLDrfDFQDLMEEKIALLKMPEDLLTRSVNV-GFSGGEKKRNDILQMAVLE 163
Cdd:cd03234 85 YVRQDDILLPGL-TVRETltytailRLPRKSS--DAIRKKRVEDVLLRDLALTRIGGNLVkGISGGERRRVSIAVQLLWD 161
|
170
....*....|....
gi 16129638 164 PELCILDESDSGLD 177
Cdd:cd03234 162 PKVLILDEPTSGLD 175
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-228 |
2.08e-15 |
|
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: 72.54 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDL--HVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLlaLSPEDRAGEG 79
Cdd:cd03263 1 LQIRNLtkTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL--RPTSGTAYINGYSI--RTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 80 IFMAFQYPVEIPGVsnqfflqTALNAVRSY---RGqetLDRFDFQDLMEEKIALLKMPEDLLTRSVNvgFSGGEKKRndi 156
Cdd:cd03263 77 LGYCPQFDALFDEL-------TVREHLRFYarlKG---LPKSEIKEEVELLLRVLGLTDKANKRART--LSGGMKRK--- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 157 LQ--MAVL-EPELCILDESDSGLDIDALKVVADGVNSLRDGkRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:cd03263 142 LSlaIALIgGPSVLLLDEPTSGLDPASRRAIWDLILEVRKG-RSIILTTHSMDEAEALC-DRIAIMSDGKLRCIG 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
17-228 |
3.10e-15 |
|
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: 71.94 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVH---PGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDL------LALSPEDRageGIFMAFQYP 87
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLE--KPDGGTIVLNGTVLfdsrkkINLPPQQR---KIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 88 VEIPGVS---N-QFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLE 163
Cdd:cd03297 85 ALFPHLNvreNlAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQL---------------SGGEKQRVALARALAAQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129638 164 PELCILDESDSGLDiDALKVVAdgVNSLRDGKRSF----IIVTHYQRILDYIKPDYVhVLYQGRIVKSG 228
Cdd:cd03297 150 PELLLLDEPFSALD-RALRLQL--LPELKQIKKNLnipvIFVTHDLSEAEYLADRIV-VMEDGRLQYIG 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
3.17e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 73.19 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVED-KAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKG-------KDLLalsp 72
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGI--LKPTSGEVLIKGepikydkKSLL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 73 EDRAGEGIfmAFQYPveipgvSNQFFLQTalnavrsyrgqetldrfdfqdlMEEKIAL----LKMPEDLLTRSVN----- 143
Cdd:PRK13639 75 EVRKTVGI--VFQNP------DDQLFAPT----------------------VEEDVAFgplnLGLSKEEVEKRVKealka 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 144 VG-----------FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHyQRILDYIK 212
Cdd:PRK13639 125 VGmegfenkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTH-DVDLVPVY 203
|
250
....*....|....*.
gi 16129638 213 PDYVHVLYQGRIVKSG 228
Cdd:PRK13639 204 ADKVYVMSDGKIIKEG 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-241 |
3.64e-15 |
|
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: 74.37 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 8 HVSVE----DKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLALSPED-RAgegifm 82
Cdd:TIGR02203 335 NVTFRypgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIP--RFYEPDSGQILLDGHDLADYTLASlRR------ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 83 afqypvEIPGVSNQFFL--QTALNAVRsYRGQETLDRFDFQDLMEEKIALL---KMPEDLLTrsvNVG-----FSGGEKK 152
Cdd:TIGR02203 407 ------QVALVSQDVVLfnDTIANNIA-YGRTEQADRAEIERALAAAYAQDfvdKLPLGLDT---PIGengvlLSGGQRQ 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 153 RNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGdfTL 232
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQG-RTTLVIAH--RLSTIEKADRIVVMDDGRIVERG--TH 551
|
....*....
gi 16129638 233 VKQLEEQGY 241
Cdd:TIGR02203 552 NELLARNGL 560
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-228 |
3.82e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 72.64 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLagredyevtggtvefkgKDLLALSPEDRA----- 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-----------------NRLIELYPEARVsgevy 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 77 --GEGIF------------MAFQYPVEIPGVSnqFFLQTALNA-----VRSYRGQETLDRFDFQ--DLMEEKIALLKMPE 135
Cdd:PRK14247 67 ldGQDIFkmdvielrrrvqMVFQIPNPIPNLS--IFENVALGLklnrlVKSKKELQERVRWALEkaQLWDEVKDRLDAPA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 136 DLLtrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDgKRSFIIVTHYQRILDYIKpDY 215
Cdd:PRK14247 145 GKL--------SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFPQQAARIS-DY 214
|
250
....*....|...
gi 16129638 216 VHVLYQGRIVKSG 228
Cdd:PRK14247 215 VAFLYKGQIVEWG 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-228 |
3.98e-15 |
|
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: 72.13 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 16 ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPED-RAGEGIFMAfqypveipgvS 94
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF--YVPENGRVLVDGHDLALADPAWlRRQVGVVLQ----------E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 95 NQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIA-LLKMPE--DLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:cd03252 85 NVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDfISELPEgyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129638 172 SDSGLDIDALKVVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDICAG-RTVIIIAH--RLSTVKNADRIIVMEKGRIVEQG 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-228 |
4.23e-15 |
|
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: 71.87 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 12 EDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALsPEDRAGEGIFMAFQYPVEIP 91
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF--YDPQKGQILIDGIDIRDI-SRKSLRSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 92 GvsnqfflqTALNAVRsyrgqetLDRFDFQDLMEEKIA--------LLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAV 161
Cdd:cd03254 91 G--------TIMENIR-------LGRPNATDEEVIEAAkeagahdfIMKLPNGYDTVLGENGgnLSQGERQLLAIARAML 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129638 162 LEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDyikPDYVHVLYQGRIVKSG 228
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKN---ADKILVLDDGKIIEEG 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-203 |
4.34e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.11 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRAgegifmafqypveipgVSNQ 96
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL--RPTSGTVRRAGGARVAYVPQRSE----------------VPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 97 FFLqTALNAVRSYRGQE--TLDRFDFQDLMEEKIALLKMP-EDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESD 173
Cdd:NF040873 70 LPL-TVRDLVAMGRWARrgLWRRLTRDDRAAVDDALERVGlADLAGRQLG-ELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|
gi 16129638 174 SGLDIDALKVVADGVNSLRDGKRSFIIVTH 203
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTH 177
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-85 |
5.57e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.51 E-value: 5.57e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLALSPEDRAGEGIFMAFQ 85
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSG--VYQPDSGEILLDGEPVRFRSPRDAQAAGIAIIHQ 86
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-229 |
8.20e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.06 E-value: 8.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDllaLSPEDRAGEGi 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAP--DSGEVLWDGEP---LDPEDRRRIG- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMafqyPVEiPG------VSNQ--FFLQ----TALNAVRsyRGQETLDRFDFQDLMEEKIallkmpEDLltrsvnvgfSG 148
Cdd:COG4152 75 YL----PEE-RGlypkmkVGEQlvYLARlkglSKAEAKR--RADEWLERLGLGDRANKKV------EEL---------SK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 149 GEKKRndiLQM--AVL-EPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHyqrILDYIKP--DYVHVLYQGR 223
Cdd:COG4152 133 GNQQK---VQLiaALLhDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSH---QMELVEElcDRIVIINKGR 206
|
....*.
gi 16129638 224 IVKSGD 229
Cdd:COG4152 207 KVLSGS 212
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-229 |
8.30e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.45 E-value: 8.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVE----DKAILRGLSLDVHPGEVHAIMGPNGSGKS----TLSATLA--GRedyevTGGTVEFKGKDLLAL 70
Cdd:PRK09473 12 LLDVKDLRVTFStpdgDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGR-----IGGSATFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 71 sPED-----RAgEGIFMAFQYPVeipgvsnqfflqTALNAVRSYRGQ--ETL---DRFDFQDLMEEKIALL---KMPEdl 137
Cdd:PRK09473 87 -PEKelnklRA-EQISMIFQDPM------------TSLNPYMRVGEQlmEVLmlhKGMSKAEAFEESVRMLdavKMPE-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 138 LTRSVNV---GFSGGEKKRNDIlQMAVL-EPELCILDESDSGLDIdalKVVADGVNSLRDGKRSF----IIVTHYQRILD 209
Cdd:PRK09473 151 ARKRMKMyphEFSGGMRQRVMI-AMALLcRPKLLIADEPTTALDV---TVQAQIMTLLNELKREFntaiIMITHDLGVVA 226
|
250 260
....*....|....*....|
gi 16129638 210 YIkPDYVHVLYQGRIVKSGD 229
Cdd:PRK09473 227 GI-CDKVLVMYAGRTMEYGN 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-203 |
1.43e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 4 IKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEF-KGKDLLALSPEDRAGEG--- 79
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEP--DSGEVSIpKGLRIGYLPQEPPLDDDltv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 80 ---IFMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQETLDRFDFQDL--MEEKIA--L--LKMPEDLLTRSVNVgFSGGE 150
Cdd:COG0488 79 ldtVLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALGGweAEARAEeiLsgLGFPEEDLDRPVSE-LSGGW 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16129638 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKVVADgvnSLRDGKRSFIIVTH 203
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEE---FLKNYPGTVLVVSH 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-229 |
1.68e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRAGEGIFMAFQYPVEIP----- 91
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGL--YQPDSGEILIDGKPVRIRSPRDAIALGIGMVHQHFMLVPnltva 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 92 -----GVSNQFFLQTALNAVRSyRGQETLDRFDFqdlmeeKIALLKMPEDLltrSVnvgfsgGEKKRNDILQMAVLEPEL 166
Cdd:COG3845 99 enivlGLEPTKGGRLDRKAARA-RIRELSERYGL------DVDPDAKVEDL---SV------GEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129638 167 CILDESDSGL---DIDALKVVadgVNSLRDGKRSFIIVTHYqriLDYIKP--DYVHVLYQGRIVKSGD 229
Cdd:COG3845 163 LILDEPTAVLtpqEADELFEI---LRRLAAEGKSIIFITHK---LREVMAiaDRVTVLRRGKVVGTVD 224
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-223 |
2.27e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.22 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 3 SIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDlLALSPEDRAGegiFM 82
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRK-PTKQILKRTG---FV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 83 AfQYPVEIPGVSnqffLQTALNAVRSYRGQETLDRFDFQDLMEEKIA---LLKMPEDLLTRSVNVGFSGGEKKRNDILQM 159
Cdd:PLN03211 146 T-QDDILYPHLT----VRETLVFCSLLRLPKSLTKQEKILVAESVISelgLTKCENTIIGNSFIRGISGGERKRVSIAHE 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129638 160 AVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGR 223
Cdd:PLN03211 221 MLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
10-225 |
2.29e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.99 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 10 SVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEfkgkdllalspedragegiFMAFQYPVE 89
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-------------------VPDNQFGRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 90 IPGVSNQFFLQTALNAVrsyrgqETLDRFDFQDlmeeKIALLKMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCIL 169
Cdd:COG2401 100 ASLIDAIGRKGDFKDAV------ELLNAVGLSD----AVLWLRRFKEL---------STGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129638 170 DESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTHYQRILDYIKPD-YVHVLYQGRIV 225
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATHHYDVIDDLQPDlLIFVGYGGVPE 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-242 |
2.90e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.54 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPED-----RAGEGifMAFQYPveip 91
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGL--HVPTQGSVRVDDTLITSTSKNKdikqiRKKVG--LVFQFP---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 92 gvSNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMPEDLLTRSvNVGFSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:PRK13649 95 --ESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKN-PFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129638 172 SDSGLDIDALKVVADGVNSLRDGKRSFIIVTH-YQRILDYikPDYVHVLYQGRIVKSGD----FTLVKQLEEQGYG 242
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlMDDVANY--ADFVYVLEKGKLVLSGKpkdiFQDVDFLEEKQLG 245
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-231 |
3.46e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 69.68 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLaGR-----EDYEVTgGTVEFKGKDLLA--LSPED 74
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL-NRmndliPGARVE-GEILLDGEDIYDpdVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 75 ---RAGegifMAFQYPveipgvsNQFFLQTALNAVRSYRGQETLDRFDFQDLMEE---KIAL---LKmpeDLLTRSVnVG 145
Cdd:COG1117 90 lrrRVG----MVFQKP-------NPFPKSIYDNVAYGLRLHGIKSKSELDEIVEEslrKAALwdeVK---DRLKKSA-LG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 146 FSGGEKKRndiLQMA---VLEPELCILDESDSGLDIDALKVVADGVNSLRDgKRSFIIVTH--YQ--RIldyikPDYVHV 218
Cdd:COG1117 155 LSGGQQQR---LCIAralAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIVTHnmQQaaRV-----SDYTAF 225
|
250
....*....|....*..
gi 16129638 219 LYQGRIVKSGD----FT 231
Cdd:COG1117 226 FYLGELVEFGPteqiFT 242
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-203 |
4.26e-14 |
|
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: 67.47 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFkgkdllalspedragegif 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGEL--EPDEGIVTW------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 mafqypveIPGVSNQFFLQtalnavrsyrgqetldrfdfqdlmeekiallkmpedlltrsvnvgFSGGEKKRNDILQMAV 161
Cdd:cd03221 60 --------GSTVKIGYFEQ---------------------------------------------LSGGEKMRLALAKLLL 86
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16129638 162 LEPELCILDESDSGLDIDALKVVADGvnsLRDGKRSFIIVTH 203
Cdd:cd03221 87 ENPNLLLLDEPTNHLDLESIEALEEA---LKEYPGTVILVSH 125
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-229 |
6.29e-14 |
|
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: 68.80 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 12 EDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLsATLAGREdYEVTGGTVEFKGKDLLALSpedragegifmafqypveip 91
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTL-VNLIPRF-YDVDSGRILIDGHDVRDYT-------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 92 gvsnqfflqtaLNAVRSYRGQETLDRFDFQDLMEEKIA-----------------------LLKMPEDLLT----RSVNV 144
Cdd:cd03251 71 -----------LASLRRQIGLVSQDVFLFNDTVAENIAygrpgatreeveeaaraanahefIMELPEGYDTvigeRGVKL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 145 gfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFII------VTHYQRILdyikpdyvhV 218
Cdd:cd03251 140 --SGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIahrlstIENADRIV---------V 208
|
250
....*....|.
gi 16129638 219 LYQGRIVKSGD 229
Cdd:cd03251 209 LEDGKIVERGT 219
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
8-229 |
6.67e-14 |
|
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: 70.55 E-value: 6.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 8 HVSVE---------DKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRaGE 78
Cdd:COG4618 330 RLSVEnltvvppgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGV--WPPTAGSVRLDGADLSQWDREEL-GR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 79 GIfmafQY-PVEIpgvsnQFFLQT-ALNAVRsyrgqetldrfdFQDLMEEKI-----------ALLKMPEDLLTRsvnVG 145
Cdd:COG4618 407 HI----GYlPQDV-----ELFDGTiAENIAR------------FGDADPEKVvaaaklagvheMILRLPDGYDTR---IG 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 146 -----FSGGEKKRndI-LQMAVL-EPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYIkpDYVHV 218
Cdd:COG4618 463 eggarLSGGQRQR--IgLARALYgDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAV--DKLLV 538
|
250
....*....|.
gi 16129638 219 LYQGRIVKSGD 229
Cdd:COG4618 539 LRDGRVQAFGP 549
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-228 |
7.28e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.18 E-value: 7.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGK-----DLLALSPEDR 75
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSAR--LAPDAGEVHYRMRdgqlrDLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 76 --------------AGEGIFMAfqypveipgVSNQFFLQTALNAV--RSY-----RGQETLDRFDfqdlmeekIALLKMp 134
Cdd:PRK11701 84 rrllrtewgfvhqhPRDGLRMQ---------VSAGGNIGERLMAVgaRHYgdiraTAGDWLERVE--------IDAARI- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 135 eDLLTRSvnvgFSGGEKKRndiLQMA---VLEPELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTH---YQRI 207
Cdd:PRK11701 146 -DDLPTT----FSGGMQQR---LQIArnlVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHdlaVARL 217
|
250 260
....*....|....*....|.
gi 16129638 208 LdyikPDYVHVLYQGRIVKSG 228
Cdd:PRK11701 218 L----AHRLLVMKQGRVVESG 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-229 |
7.76e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.20 E-value: 7.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRAGEGIFMAFQYPVEIPGVSNQ 96
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI--HEPTKGTITINNINYNKLDHKLAAQLGIGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 97 FFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSggEKKRNDILQMAVLEPELCILDESDSGL 176
Cdd:PRK09700 99 ENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSIS--HKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16129638 177 ---DIDALKVVadgVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGD 229
Cdd:PRK09700 177 tnkEVDYLFLI---MNQLRKEGTAIVYISHKLAEIRRIC-DRYTVMKDGSSVCSGM 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-228 |
1.02e-13 |
|
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: 67.34 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSV--EDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLALspedrageg 79
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQQGEITLDGVPVSDL--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 80 ifmafqypveipgvsnqfflqtalnavrsyrgqetldrfdfQDLMEEKIALLKMPEDLLTRSV--NVG--FSGGEKKRND 155
Cdd:cd03247 70 -----------------------------------------EKALSSLISVLNQRPYLFDTTLrnNLGrrFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129638 156 ILQMAVLEPELCILDESDSGLD-IDALKVVADGVNSLRDgkRSFIIVTHYQRILDYIkpDYVHVLYQGRIVKSG 228
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDpITERQLLSLIFEVLKD--KTLIWITHHLTGIEHM--DKILFLENGKIIMQG 178
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-229 |
1.56e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 68.95 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKA----ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRA 76
Cdd:COG1135 1 MIELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLE--RPTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 77 GE--GIFMAFQ---------------YPVEIPGVSnqfflqtalNAVRSYRGQETLDRFDfqdlMEEKIAllKMPEDLlt 139
Cdd:COG1135 79 AArrKIGMIFQhfnllssrtvaenvaLPLEIAGVP---------KAEIRKRVAELLELVG----LSDKAD--AYPSQL-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 140 rsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLD------IDALkvvadgvnsLRDGKRSF----IIVTH----YQ 205
Cdd:COG1135 142 -------SGGQKQRVGIARALANNPKVLLCDEATSALDpettrsILDL---------LKDINRELgltiVLITHemdvVR 205
|
250 260
....*....|....*....|....
gi 16129638 206 RILdyikpDYVHVLYQGRIVKSGD 229
Cdd:COG1135 206 RIC-----DRVAVLENGRIVEQGP 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-84 |
1.80e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 66.69 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVsvedKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDL------------L 68
Cdd:cd03215 4 VLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFG--LRPPASGEITLDGKPVtrrsprdairagI 77
|
90
....*....|....*.
gi 16129638 69 ALSPEDRAGEGIFMAF 84
Cdd:cd03215 78 AYVPEDRKREGLVLDL 93
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-228 |
1.82e-13 |
|
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: 67.64 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 13 DKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLALSPED-RAGEGIFmafqyPVEIP 91
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF--RFYDVSSGSILIDGQDIREVTLDSlRRAIGVV-----PQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 92 gvsnqFFLQTALNAVRSYRgqetLDRFDFQdlMEE--KIA-----LLKMPEDLLTRsvnVG-----FSGGEKKRNDILQM 159
Cdd:cd03253 86 -----LFNDTIGYNIRYGR----PDATDEE--VIEaaKAAqihdkIMRFPDGYDTI---VGerglkLSGGEKQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129638 160 AVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSfIIVTHyqRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTT-IVIAH--RLSTIVNADKIIVLKDGRIVERG 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-228 |
2.05e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.22 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 20 LSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDR---AGEGIFMAFQYPveipgvSNQ 96
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGL--LQPTEGKVTVGDIVVSSTSKQKEikpVRKKVGVVFQFP------ESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 97 FFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMPEDLLTRSvNVGFSGGEKKRNDILQMAVLEPELCILDESDSGL 176
Cdd:PRK13643 97 LFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKS-PFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16129638 177 DIDALKVVADGVNSLRDGKRSFIIVTH-YQRILDYikPDYVHVLYQGRIVKSG 228
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTHlMDDVADY--ADYVYLLEKGHIISCG 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-229 |
3.17e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.08 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVefkgkdllalspedRAGEgi 80
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLE--QPEAGTI--------------RVGD-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 fmafqypVEIpgvsnqfflqtalNAVRSYRGQETLDR-------FDFQ------------DLMEEKIALLKMPED----- 136
Cdd:PRK11264 65 -------ITI-------------DTARSLSQQKGLIRqlrqhvgFVFQnfnlfphrtvleNIIEGPVIVKGEPKEeatar 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 137 ---LLTRsvnVG-----------FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVT 202
Cdd:PRK11264 125 areLLAK---VGlagketsyprrLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT 201
|
250 260
....*....|....*....|....*..
gi 16129638 203 HYQRILDYIKpDYVHVLYQGRIVKSGD 229
Cdd:PRK11264 202 HEMSFARDVA-DRAIFMDQGRIVEQGP 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
12-228 |
3.33e-13 |
|
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: 66.46 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 12 EDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPED-RAGEGIFMafQYPVEI 90
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL--YKPTSGSVLLDGTDIRQLDPADlRRNIGYVP--QDVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 91 PGvsnqfflqtalnavrSYRGQETLDR--FDFQDLME--------EKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMA 160
Cdd:cd03245 91 YG---------------TLRDNITLGAplADDERILRaaelagvtDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129638 161 VLEPELCILDESDSGLDIDALKVVADGVNSLRDGKrSFIIVTHYQRILDYIkpDYVHVLYQGRIVKSG 228
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK-TLIIITHRPSLLDLV--DRIIVMDSGRIVADG 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-224 |
5.83e-13 |
|
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: 65.96 E-value: 5.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 13 DKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLALSPEdRAGEGIFMAFQYPVEIPG 92
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL--ENFYQPQGGQVLLDGKPISQYEHK-YLHSKVSLVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 93 vSNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEkiallkMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILD 170
Cdd:cd03248 103 -SLQDNIAYGLQSCSFECVKEAAQKAHAHSFISE------LASGYDTEVGEKGsqLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16129638 171 ESDSGLDIDALKVVAdgvNSLRDG--KRSFIIVTHyqRILDYIKPDYVHVLYQGRI 224
Cdd:cd03248 176 EATSALDAESEQQVQ---QALYDWpeRRTVLVIAH--RLSTVERADQILVLDGGRI 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-203 |
6.86e-13 |
|
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: 65.57 E-value: 6.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKA----ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDLLALSPeDRAg 77
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERP--TSGEVLVDGEPVTGPGP-DRG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 78 egifMAFQ---------------YPVEIPGVSnqfflqtalNAVRSYRGQETLDRFDFQDlmeekiALLKMPEDLltrsv 142
Cdd:cd03293 77 ----YVFQqdallpwltvldnvaLGLELQGVP---------KAEARERAEELLELVGLSG------FENAYPHQL----- 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129638 143 nvgfSGGEKKRNDILQMAVLEPELCILDESDSGLD-IDALKVVADGVNSLRDGKRSFIIVTH 203
Cdd:cd03293 133 ----SGGMRQRVALARALAVDPDVLLLDEPFSALDaLTREQLQEELLDIWRETGKTVLLVTH 190
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-177 |
8.47e-13 |
|
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: 65.67 E-value: 8.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVS-VEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPED----RA 76
Cdd:cd03256 1 IEVENLSKTyPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLV--EPTSGSVLIDGTDINKLKGKAlrqlRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 77 GEG-IFMAFQYPVEIPGVSNqfFLQTALNAVRSYRGqeTLDRFDFQDLmEEKIALLK---MPEDLLTRSVNVgfSGGEKK 152
Cdd:cd03256 79 QIGmIFQQFNLIERLSVLEN--VLSGRLGRRSTWRS--LFGLFPKEEK-QRALAALErvgLLDKAYQRADQL--SGGQQQ 151
|
170 180
....*....|....*....|....*
gi 16129638 153 RNDILQMAVLEPELCILDESDSGLD 177
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLD 176
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-229 |
8.49e-13 |
|
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: 65.64 E-value: 8.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRAGEGIf 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV--KPDSGKILLDGQDITKLPMHKRARLGI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 mafQY-PVEiPGVSNQFFLQTALNAVRSYRGqetLDRFDFQDLMEEKIALLKMPEdlLTRSVNVGFSGGEKKRNDILQMA 160
Cdd:cd03218 78 ---GYlPQE-ASIFRKLTVEENILAVLEIRG---LSKKEREEKLEELLEEFHITH--LRKSKASSLSGGERRRVEIARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 161 VLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQR-ILDYIkpDYVHVLYQGRIVKSGD 229
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVReTLSIT--DRAYIIYEGKVLAEGT 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-203 |
1.28e-12 |
|
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: 66.62 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAI-LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLALSPEDRAgegi 80
Cdd:TIGR02868 335 LELRDLSAGYPGAPPvLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD--PLQGEVTLDGVPVSSLDQDEVR---- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 fmafqypvEIPGVSNQ---FFLQTALNAVRSYRGQET-------LDRFDFQDLMEEkiallkMPEDLLTRSVNVG--FSG 148
Cdd:TIGR02868 409 --------RRVSVCAQdahLFDTTVRENLRLARPDATdeelwaaLERVGLADWLRA------LPDGLDTVLGEGGarLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSfIIVTH 203
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTV-VLITH 528
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-246 |
2.01e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.03 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAG---REDYEV--TGGTVEFKGKDLLALSPEdr 75
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGllrPQKGAVlwQGKPLDYSKRGLLALRQQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 76 agegIFMAFQYPveipgvSNQFFlqtalnavrsYRGQETLDRFDFQDL--MEEKIAllKMPEDLLTRSVNVGF------- 146
Cdd:PRK13638 79 ----VATVFQDP------EQQIF----------YTDIDSDIAFSLRNLgvPEAEIT--RRVDEALTLVDAQHFrhqpiqc 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 147 -SGGEKKRNDILQMAVLEPELCILDESDSGLD-------IDALKVVAdgvnslrdGKRSFIIVTHYQRILDYIKPDYVHV 218
Cdd:PRK13638 137 lSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagrtqmIAIIRRIV--------AQGNHVIISSHDIDLIYEISDAVYV 208
|
250 260 270
....*....|....*....|....*....|....
gi 16129638 219 LYQGRIVKSGD----FTLVKQLEEQGYG--WLTE 246
Cdd:PRK13638 209 LRQGQILTHGApgevFACTEAMEQAGLTqpWLVK 242
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-228 |
2.48e-12 |
|
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: 64.97 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPED-RA--GEGIFMAFQ-------- 85
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRL--IEPTSGKVLIDGQDIAAMSRKElRElrRKKISMVFQsfallphr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 86 -------YPVEIPGVSNQfflqtalnaVRSYRGQETLDRFDFQDLMEekiallKMPEDLltrsvnvgfSGGEKKRNDILQ 158
Cdd:cd03294 118 tvlenvaFGLEVQGVPRA---------EREERAAEALELVGLEGWEH------KYPDEL---------SGGMQQRVGLAR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 159 MAVLEPELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTH----YQRILDYIKpdyvhVLYQGRIVKSG 228
Cdd:cd03294 174 ALAVDPDILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHdldeALRLGDRIA-----IMKDGRLVQVG 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-225 |
2.65e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 63.92 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 8 HVSVE---DKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLALSPEDRA------Ge 78
Cdd:COG2884 6 NVSKRypgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG--EERPTSGQVLVNGQDLSRLKRREIPylrrriG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 79 gifMAFQ---------------YPVEIPGVSnqfflqtalNAVRSYRGQETLDRFDFQDLMEekiallKMPEDLltrsvn 143
Cdd:COG2884 83 ---VVFQdfrllpdrtvyenvaLPLRVTGKS---------RKEIRRRVREVLDLVGLSDKAK------ALPHEL------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 144 vgfSGGEKKRNDIlqmA---VLEPELCILDESDSGLDID-ALKVVA--DGVNslRDGKrSFIIVTHYQRILDYIkPDYVH 217
Cdd:COG2884 139 ---SGGEQQRVAI---AralVNRPELLLADEPTGNLDPEtSWEIMEllEEIN--RRGT-TVLIATHDLELVDRM-PKRVL 208
|
....*...
gi 16129638 218 VLYQGRIV 225
Cdd:COG2884 209 ELEDGRLV 216
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
8-178 |
3.54e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.18 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 8 HVSVEDKaiLRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEvtgGTVEFKGKDLLALSPEDRAGEGIFMA---- 83
Cdd:PRK03695 5 DVAVSTR--LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS---GSIQFAGQPLEAWSAAELARHRAYLSqqqt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 84 --FQYPVeipgvsnqF-FLQTALNA-VRSYrgqetldrfDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKR----ND 155
Cdd:PRK03695 80 ppFAMPV--------FqYLTLHQPDkTRTE---------AVASALNEVAEALGL-DDKLGRSVN-QLSGGEWQRvrlaAV 140
|
170 180
....*....|....*....|....*.
gi 16129638 156 ILQMA-VLEPE--LCILDESDSGLDI 178
Cdd:PRK03695 141 VLQVWpDINPAgqLLLLDEPMNSLDV 166
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-228 |
3.86e-12 |
|
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: 63.44 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 16 ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGR-EDYEVTGGTVEFKGKDLLAlspedragegifMAFQYPVEIPGVS 94
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtEGNVSVEGDIHYNGIPYKE------------FAEKYPGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 95 NQFFLQTALnAVRsyrgqETLDrfdfqdlmeekiALLKMPEDLLTRsvnvGFSGGEKKRNDILQMAVLEPELCILDESDS 174
Cdd:cd03233 90 EEDVHFPTL-TVR-----ETLD------------FALRCKGNEFVR----GISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129638 175 GLD-IDALKVvadgVNSLR---DGKRSFIIVTHYQ---RILDYIkpDYVHVLYQGRIVKSG 228
Cdd:cd03233 148 GLDsSTALEI----LKCIRtmaDVLKTTTFVSLYQasdEIYDLF--DKVLVLYEGRQIYYG 202
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
2-229 |
4.92e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 63.71 E-value: 4.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEdkaiLRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEvtgGTVEFKGKDLLALSPedragegif 81
Cdd:COG4138 1 LQLNDVAVAGR----LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ---GEILLNGRPLSDWSA--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 mafqypveipgvsnqfflqTALNAVRSYRGQETLDRFD---FQ----------------DLMEEKIALLKMpEDLLTRSV 142
Cdd:COG4138 65 -------------------AELARHRAYLSQQQSPPFAmpvFQylalhqpagasseaveQLLAQLAEALGL-EDKLSRPL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 143 NvGFSGGEKKRndILQMAVL---------EPELCILDESDSGLDIdALKVVADG-VNSLRDGKRSFIIVTHyqrilD--- 209
Cdd:COG4138 125 T-QLSGGEWQR--VRLAAVLlqvwptinpEGQLLLLDEPMNSLDV-AQQAALDRlLRELCQQGITVVMSSH-----Dlnh 195
|
250 260
....*....|....*....|.
gi 16129638 210 -YIKPDYVHVLYQGRIVKSGD 229
Cdd:COG4138 196 tLRHADRVWLLKQGKLVASGE 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
17-229 |
6.46e-12 |
|
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: 63.12 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRageGIFMAFQYPVEIPGVSNQ 96
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGF--IKPDSGKILLNGKDITNLPPEKR---DISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 97 FFLQTALNAVRSYRGQetldrfdfqdlMEEKI----ALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDES 172
Cdd:cd03299 90 KNIAYGLKKRKVDKKE-----------IERKVleiaEMLGI-DHLLNRKPET-LSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129638 173 DSGLDIDALKVVadgVNSLRDGKRSF----IIVTHYQ---RILDyikpDYVHVLYQGRIVKSGD 229
Cdd:cd03299 157 FSALDVRTKEKL---REELKKIRKEFgvtvLHVTHDFeeaWALA----DKVAIMLNGKLIQVGK 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-229 |
8.07e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 62.85 E-value: 8.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAiLRgLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRageGI 80
Cdd:COG3840 1 MLRLDDLTYRYGDFP-LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFL--PPDSGRILWNGQDLTALPPAER---PV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAFQypveipgvSNQFF--LQTA------------LNAVRSYRGQETLDRFDFQDLMEekiallKMPEDLltrsvnvgf 146
Cdd:COG3840 74 SMLFQ--------ENNLFphLTVAqniglglrpglkLTAEQRAQVEQALERVGLAGLLD------RLPGQL--------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIdALKV-VADGVNSL-RDGKRSFIIVTHY----QRIldyikPDYVHVLY 220
Cdd:COG3840 131 SGGQRQRVALARCLVRKRPILLLDEPFSALDP-ALRQeMLDLVDELcRERGLTVLMVTHDpedaARI-----ADRVLLVA 204
|
....*....
gi 16129638 221 QGRIVKSGD 229
Cdd:COG3840 205 DGRIAADGP 213
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-228 |
8.91e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 63.50 E-value: 8.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDkailrglsldvhpGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEF---------KGKDLLALsp 72
Cdd:PRK13634 21 RALYDVNVSIPS-------------GSYVAIIGHTGSGKSTLLQHLNGL--LQPTSGTVTIgervitagkKNKKLKPL-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 73 edRAGEGIfmAFQYPveipgvSNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMPEDLLTRSvNVGFSGGEKK 152
Cdd:PRK13634 84 --RKKVGI--VFQFP------EHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARS-PFELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129638 153 RNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTH-YQRILDYikPDYVHVLYQGRIVKSG 228
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHsMEDAARY--ADQIVVMHKGTVFLQG 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-228 |
9.68e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.11 E-value: 9.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAgREDYEVTgGTVEFKGKDLLALSPEDRAGEGI 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RLLTPQS-GTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAFQYPVeiP-GVSNQFFLQTALNAVRSYRGQ-ETLDRFDFQDLMeEKIALLKMPEDLLTRsvnvgFSGGEKKRNDILQ 158
Cdd:PRK11231 80 LLPQHHLT--PeGITVRELVAYGRSPWLSLWGRlSAEDNARVNQAM-EQTRINHLADRRLTD-----LSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129638 159 MAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTH-YQRILDYIkpDYVHVLYQGRIVKSG 228
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdLNQASRYC--DHLVVLANGHVMAQG 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-203 |
1.55e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 62.42 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDR----- 75
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLE--EITSGDLIVDGLKVNDPKVDERlirqe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 76 AGegifMAFQypveipgvsnQFFL---QTALNAV----RSYRGQetldrfdfqdlmeEKIALLKMPEDLLTRsvnVG--- 145
Cdd:PRK09493 79 AG----MVFQ----------QFYLfphLTALENVmfgpLRVRGA-------------SKEEAEKQARELLAK---VGlae 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 146 --------FSGGEKKRNDILQMAVLEPELCILDESDSGLDI----DALKVVADgvnsLRDGKRSFIIVTH 203
Cdd:PRK09493 129 rahhypseLSGGQQQRVAIARALAVKPKLMLFDEPTSALDPelrhEVLKVMQD----LAEEGMTMVIVTH 194
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-176 |
1.73e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.53 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLALSPEDRAGEGI 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD--SGTLEIGGNPCARLTPAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAFQYPVEIPgvsNQFFLQTALnaVRSYRGQETLDRfdfqdlMEEKIALLKMPEDL--LTRSVNVgfsgGEKKRNDILQ 158
Cdd:PRK15439 89 YLVPQEPLLFP---NLSVKENIL--FGLPKRQASMQK------MKQLLAALGCQLDLdsSAGSLEV----ADRQIVEILR 153
|
170
....*....|....*...
gi 16129638 159 MAVLEPELCILDESDSGL 176
Cdd:PRK15439 154 GLMRDSRILILDEPTASL 171
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
12-224 |
1.74e-11 |
|
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: 61.08 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 12 EDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDragegifmafqypveip 91
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLL--RPTSGRVRLDGADISQWDPNE----------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 92 gvsnqfflqtalnavrsYRGQetldrfdfqdlmeekIALLkmPED--LLTRSV--NVgFSGGEKKRndILQMAVL--EPE 165
Cdd:cd03246 74 -----------------LGDH---------------VGYL--PQDdeLFSGSIaeNI-LSGGQRQR--LGLARALygNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129638 166 LCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYIkpDYVHVLYQGRI 224
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA--DRILVLEDGRV 173
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-203 |
1.84e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.43 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDllalSPEDRAGEgi 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGL--LPPAAGTIKLDGGD----IDDPDVAE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 fmAFQYpveipgVSNQFFLQTALNAV------RSYRGQ------ETLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSG 148
Cdd:PRK13539 74 --ACHY------LGHRNAMKPALTVAenlefwAAFLGGeeldiaAALEAVGLAPLAHLPFGYL---------------SA 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTH 203
Cdd:PRK13539 131 GQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-84 |
1.91e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.12 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAI-LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAG-RedyEVTGGTVEFKGKDLLALS-------- 71
Cdd:COG3845 258 LEVENLSVRDDRGVPaLKDVSLEVRAGEILGIAGVAGNGQSELAEALAGlR---PPASGSIRLDGEDITGLSprerrrlg 334
|
90
....*....|....*..
gi 16129638 72 ----PEDRAGEGIFMAF 84
Cdd:COG3845 335 vayiPEDRLGRGLVPDM 351
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
15-203 |
2.19e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 61.72 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 15 AILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLALSPEDRA---GEGIFMAFQypveip 91
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDD--GSSGEVSLVGQPLHQMDEEARAklrAKHVGFVFQ------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 92 gvsnQFFLQTALNAVRS------YRGQ-ETLDRFDFQDLMEE---KIALLKMPEDLltrsvnvgfSGGEKKRNDILQMAV 161
Cdd:PRK10584 96 ----SFMLIPTLNALENvelpalLRGEsSRQSRNGAKALLEQlglGKRLDHLPAQL---------SGGEQQRVALARAFN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16129638 162 LEPELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTH 203
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTH 205
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-177 |
2.43e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.55 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRAgegI 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE--QPTAGQIMLDGVDLSHVPPYQRP---I 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAFQYPVEIPGVSNQFFLQTALNavrsyrgQETLDRFDFQDLMEEKIALLKMPEdlLTRSVNVGFSGGEKKRNDILQMA 160
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLK-------QDKLPKAEIASRVNEMLGLVHMQE--FAKRKPHQLSGGQRQRVALARSL 164
|
170
....*....|....*..
gi 16129638 161 VLEPELCILDESDSGLD 177
Cdd:PRK11607 165 AKRPKLLLLDEPMGALD 181
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-239 |
2.81e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.06 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 4 IKDLHVSVED--KAiLRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLAlSPEDRAGEGIF 81
Cdd:PRK13647 7 VEDLHFRYKDgtKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI--YLPQRGRVKVMGREVNA-ENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQYPveipgvSNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAV 161
Cdd:PRK13647 83 LVFQDP------DDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRM-WDFRDKPPY-HLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 162 LEPELCILDESDSGLD---IDALKVVADGVNslRDGKrSFIIVTHYqriLDYIK--PDYVHVLYQGRIVKSGDFTLV--K 234
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDprgQETLMEILDRLH--NQGK-TVIVATHD---VDLAAewADQVIVLKEGRVLAEGDKSLLtdE 228
|
....*
gi 16129638 235 QLEEQ 239
Cdd:PRK13647 229 DIVEQ 233
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-193 |
4.12e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.16 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 19 GLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRAGEGIFMAFQY--------PVEI 90
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGF--YKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHvrlfremtVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 91 PGVSNQFFLQT----ALNAVRSYR--GQETLDRFDFqdlMEEKIALLkmpeDLLTRSV-NVGFsgGEKKRNDILQMAVLE 163
Cdd:PRK11300 101 LLVAQHQQLKTglfsGLLKTPAFRraESEALDRAAT---WLERVGLL----EHANRQAgNLAY--GQQRRLEIARCMVTQ 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 16129638 164 PELCILDESDSGL------DIDALkvvadgVNSLRD 193
Cdd:PRK11300 172 PEILMLDEPAAGLnpketkELDEL------IAELRN 201
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-228 |
4.61e-11 |
|
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: 60.62 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKD--LLALSpedrage 78
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI--YPPDSGTVTVRGRVssLLGLG------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 79 gifMAFQYpvEIPGVSNQFFLQTALNAVRSYRGQETLDRFDFQDLmeekiallkmpEDLLTRSVNVgFSGGEKKRndiLQ 158
Cdd:cd03220 93 ---GGFNP--ELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSEL-----------GDFIDLPVKT-YSSGMKAR---LA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 159 MAV---LEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYqriLDYIKP--DYVHVLYQGRIVKSG 228
Cdd:cd03220 153 FAIataLEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHD---PSSIKRlcDRALVLEKGKIRFDG 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-230 |
5.38e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.90 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLALSpedRAG--EGIFMAFQYPveipGVS 94
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLL--QRVFDPQSGRILIDGTDIRTVT---RASlrRNIAVVFQDA----GLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 95 NqfflqtalnavRSYRGQETLDRFDFQDlmEEKIALLKMPE--DLLTRS-----VNVG-----FSGGEKKRNDILQmAVL 162
Cdd:PRK13657 422 N-----------RSIEDNIRVGRPDATD--EEMRAAAERAQahDFIERKpdgydTVVGergrqLSGGERQRLAIAR-ALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 163 -EPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFII------VTHYQRILdyikpdyvhVLYQGRIVKSGDF 230
Cdd:PRK13657 488 kDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIahrlstVRNADRIL---------VFDNGRVVESGSF 553
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-229 |
5.45e-11 |
|
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: 62.01 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVS-----------VEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDyevTGGTVEFKGKDLLAL 70
Cdd:COG4172 276 LEARDLKVWfpikrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP---SEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 71 SPED----RAgeGIFMAFQYPV----------EI---------PGVSnqfflqtalnavrsyrGQETLDRfdFQDLMEEk 127
Cdd:COG4172 353 SRRAlrplRR--RMQVVFQDPFgslsprmtvgQIiaeglrvhgPGLS----------------AAERRAR--VAEALEE- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 128 ialLKMPEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESDSGLDidaLKVVADGVNSLRDGKR----SFIIVTH 203
Cdd:COG4172 412 ---VGLDPAARHRYPH-EFSGGQRQRIAIARALILEPKLLVLDEPTSALD---VSVQAQILDLLRDLQRehglAYLFISH 484
|
250 260
....*....|....*....|....*.
gi 16129638 204 YQRILDYIKpDYVHVLYQGRIVKSGD 229
Cdd:COG4172 485 DLAVVRALA-HRVMVMKDGKVVEQGP 509
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-228 |
5.99e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.88 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 6 DLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLaGREDYEVTG----GTVEFKGKDLLALSPEDRAGEGIF 81
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL-NRMNDKVSGyrysGDVLLGGRSIFNYRDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQYPveipgvsNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGF--SGGEKKRNDILQM 159
Cdd:PRK14271 105 MLFQRP-------NPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFrlSGGQQQLLCLART 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129638 160 AVLEPELCILDESDSGLDIDALKVVADGVNSLRDgKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAD-RLTVIIVTHNLAQAARIS-DRAALFFDGRLVEEG 244
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-228 |
9.35e-11 |
|
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: 59.43 E-value: 9.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 20 LSLDVHPGEVHAIMGPNGSGKSTLSATLAGredYEV-TGGTVEFKGKDLLALSPEDRAgegIFMAFQypveipgvSNQFF 98
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAG---FETpQSGRVLINGVDVTAAPPADRP---VSMLFQ--------ENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 99 LQTA--------------LNAVRSYRGQETLDRFDFQDLMeekialLKMPEDLltrsvnvgfSGGEKKRNDILQMAVLEP 164
Cdd:cd03298 83 AHLTveqnvglglspglkLTAEDRQAIEVALARVGLAGLE------KRLPGEL---------SGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 165 ELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTHYQRILDYIKPDYVHvLYQGRIVKSG 228
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVF-LDNGRIAAQG 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-73 |
9.57e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.43 E-value: 9.57e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLALSPE 73
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLAR--PDAGEVLWQGEPIRRQRDE 71
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-228 |
9.58e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 60.24 E-value: 9.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSAT----LAGREDYEVTgGTVEFKGKDLlaLSPEDRAG 77
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrlLELNEEARVE-GEVRLFGRNI--YSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 78 E---GIFMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQETLDRFDFQDLmeEKIALLKMPEDLLtRSVNVGFSGGEKKRN 154
Cdd:PRK14267 82 EvrrEVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWAL--KKAALWDEVKDRL-NDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129638 155 DILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDgKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPAQAARVS-DYVAFLYLGKLIEVG 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
9.77e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.20 E-value: 9.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDL-HVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALS-PEDRAGE 78
Cdd:PRK13652 3 LIETRDLcYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGI--LKPTSGSVLIRGEPITKENiREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 79 GIfmAFQYPveipgvSNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMpEDLLTRsVNVGFSGGEKKRNDILQ 158
Cdd:PRK13652 81 GL--VFQNP------DDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGL-EELRDR-VPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 159 MAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYG 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
17-228 |
1.03e-10 |
|
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: 60.05 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLALSPEDRageGIFMAFQYPVEIPgvsnq 96
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLER--PDSGTILFGGEDATDVPVQER---NVGFVFQHYALFR----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 97 fFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMPE-DLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDSG 175
Cdd:cd03296 88 -HMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQlDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 176 LDIDALKVVADGVNSLRDGKR-SFIIVTHYQ-RILDYikPDYVHVLYQGRIVKSG 228
Cdd:cd03296 167 LDAKVRKELRRWLRRLHDELHvTTVFVTHDQeEALEV--ADRVVVMNKGRIEQVG 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-229 |
1.27e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.10 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 4 IKDLHVSVEDKAiLRGLSLDVHPGEVHAIMGPNGSGKST----LSATLAGredyevTGGTVEFKGKD---------LLAL 70
Cdd:PRK13651 11 IFNKKLPTELKA-LDNVSVEINQGEFIAIIGQTGSGKTTfiehLNALLLP------DTGTIEWIFKDeknkkktkeKEKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 71 SPEDRAGEGIFMAFQYPVEIP---GVSNQF-----FLQTALNAV----RSY--RGQETLDRfdfqdlMEEKIALLKMPED 136
Cdd:PRK13651 84 LEKLVIQKTRFKKIKKIKEIRrrvGVVFQFaeyqlFEQTIEKDIifgpVSMgvSKEEAKKR------AAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 137 LLTRSvNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTH-YQRILDYIKpdY 215
Cdd:PRK13651 158 YLQRS-PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHdLDNVLEWTK--R 234
|
250
....*....|....
gi 16129638 216 VHVLYQGRIVKSGD 229
Cdd:PRK13651 235 TIFFKDGKIIKDGD 248
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-75 |
1.29e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 60.55 E-value: 1.29e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLA-LSPEDR 75
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLE--TPDSGRIVLNGRDLFTnLPPRER 75
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
12-243 |
1.42e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.89 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 12 EDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSpEDRAGEGIFMAFQYPVEIP 91
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGY--YPLTEGEIRLDGRPLSSLS-HSVLRQGVAMVQQDPVVLA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 92 GvsnqfflqtalnavrSYRGQETLDRfdfqDLMEEKI---------ALL--KMPEDLLTRSVNVG--FSGGEKKrndILQ 158
Cdd:PRK10790 429 D---------------TFLANVTLGR----DISEEQVwqaletvqlAELarSLPDGLYTPLGEQGnnLSVGQKQ---LLA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 159 MA---VLEPELCILDESDSGLDIDALKVVADGVNSLRDgKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGdfTLVKQ 235
Cdd:PRK10790 487 LArvlVQTPQILILDEATANIDSGTEQAIQQALAAVRE-HTTLVVIAH--RLSTIVEADTILVLHRGQAVEQG--THQQL 561
|
....*...
gi 16129638 236 LEEQGYGW 243
Cdd:PRK10790 562 LAAQGRYW 569
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-229 |
1.59e-10 |
|
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: 60.59 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYE--------------------------- 54
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptsgriiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 55 ---VTGGTVEFKGKDLLALSPEDRAG--EGIFMAFQYPVEIPGvsNQFFLQTALNAVRS--YRGQETLDRfdfqdlmeeK 127
Cdd:TIGR03269 81 pcpVCGGTLEPEEVDFWNLSDKLRRRirKRIAIMLQRTFALYG--DDTVLDNVLEALEEigYEGKEAVGR---------A 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 128 IALLKMPEdLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTHY 204
Cdd:TIGR03269 150 VDLIEMVQ-LSHRITHIArdLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHW 228
|
250 260
....*....|....*....|....*
gi 16129638 205 QRILDYIKpDYVHVLYQGRIVKSGD 229
Cdd:TIGR03269 229 PEVIEDLS-DKAIWLENGEIKEEGT 252
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-205 |
1.89e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.04 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 3 SIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLALSPEDRageGIFM 82
Cdd:PRK11000 5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGDLFIGEKRMNDVPPAER---GVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 83 AFQ----YPvEIPGVSNQFF---LQTALNAVRSYRGQETLDRFDFQDLMEEKiallkmPEDLltrsvnvgfSGGEKKRND 155
Cdd:PRK11000 80 VFQsyalYP-HLSVAENMSFglkLAGAKKEEINQRVNQVAEVLQLAHLLDRK------PKAL---------SGGQRQRVA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16129638 156 ILQMAVLEPELCILDESDSGLDIdALKV-VADGVNSL-RDGKRSFIIVTHYQ 205
Cdd:PRK11000 144 IGRTLVAEPSVFLLDEPLSNLDA-ALRVqMRIEISRLhKRLGRTMIYVTHDQ 194
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-228 |
1.90e-10 |
|
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: 59.27 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 3 SIKDL-HVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRAGEGIF 81
Cdd:cd03267 22 SLKSLfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGL--LQPTSGEVRVAGLVPWKRRKKFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MA--FQYPVEIPGVSNQFFLQtalnavRSYRgqetLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQM 159
Cdd:cd03267 100 FGqkTQLWWDLPVIDSFYLLA------AIYD----LPPARFKKRLDELSELLDL-EELLDTPVR-QLSLGQRMRAEIAAA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 160 AVLEPELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTHYQRILDYIkPDYVHVLYQGRIVKSG 228
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEAL-ARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
1.93e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.48 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKA-ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKdllalsPEDRAGEG 79
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGI--LKPSSGRILFDGK------PIDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 80 IF-------MAFQYPveipgvSNQFFLQTAlnavrsyrgqetldrfdFQDLMEEKIAlLKMPEDLLTRSVNVG------- 145
Cdd:PRK13636 77 LMklresvgMVFQDP------DNQLFSASV-----------------YQDVSFGAVN-LKLPEDEVRKRVDNAlkrtgie 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 146 ---------FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDG-KRSFIIVTHYQRILDyIKPDY 215
Cdd:PRK13636 133 hlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVP-LYCDN 211
|
250
....*....|...
gi 16129638 216 VHVLYQGRIVKSG 228
Cdd:PRK13636 212 VFVMKEGRVILQG 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-235 |
2.06e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 59.84 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 10 SVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEVtgGTVEFKGKDLLALSPEDRAGEGIFMAFQypve 89
Cdd:PRK13536 50 SYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA--GKITVLGVPVPARARLARARIGVVPQFD---- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 90 ipGVSNQFFLQTALNAVRSYRGQETLDrfdfqdlMEEKI-ALLKMPEdlLTRSVNV---GFSGGEKKRNDILQMAVLEPE 165
Cdd:PRK13536 124 --NLDLEFTVRENLLVFGRYFGMSTRE-------IEAVIpSLLEFAR--LESKADArvsDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129638 166 LCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYIkPDYVHVLYQGR-IVKSGDFTLVKQ 235
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERL-CDRLCVLEAGRkIAEGRPHALIDE 262
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-228 |
2.08e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 59.38 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPED-RAGEGIfmAFQYPveipgvSN 95
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIE--KVKSGEIFYNNQAITDDNFEKlRKHIGI--VFQNP------DN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 96 QFflqtaLNAVRSYRGQETLDRFDF-QDLMEEKIALLKMPEDLLTR--SVNVGFSGGEKKRNDILQMAVLEPELCILDES 172
Cdd:PRK13648 95 QF-----VGSIVKYDVAFGLENHAVpYDEMHRRVSEALKQVDMLERadYEPNALSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129638 173 DSGLDIDALKVVADGVNSLRDGKRSFII-VTHyqRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKSEHNITIIsITH--DLSEAMEADHVIVMNKGTVYKEG 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-225 |
2.25e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.10 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSV----EDKAILRGLSLDVHPGEVHAIMGPNGSGKS--TLSAT-LAGREDYEVTGGTVEFKGKDLL-ALSP 72
Cdd:PRK15134 5 LLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvtALSILrLLPSPPVVYPSGDIRFHGESLLhASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 73 EDRA--GEGIFMAFQYP-VEIPGVSNqffLQTALNAVRS-YRGQ-------ETLDRFDFQDLMEEKIALLKMPEDLltrs 141
Cdd:PRK15134 85 TLRGvrGNKIAMIFQEPmVSLNPLHT---LEKQLYEVLSlHRGMrreaargEILNCLDRVGIRQAAKRLTDYPHQL---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 142 vnvgfSGGEKKRNDIlQMAVL-EPELCILDESDSGLDIdalKVVADGVNSLRDGKR----SFIIVTHYQRILDYIKpDYV 216
Cdd:PRK15134 158 -----SGGERQRVMI-AMALLtRPELLIADEPTTALDV---SVQAQILQLLRELQQelnmGLLFITHNLSIVRKLA-DRV 227
|
....*....
gi 16129638 217 HVLYQGRIV 225
Cdd:PRK15134 228 AVMQNGRCV 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-228 |
2.30e-10 |
|
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: 60.22 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 13 DKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPED-RAGEGIfmafqypveIP 91
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF--YDVTSGRILIDGQDIRDVTQASlRAAIGI---------VP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 92 gvsnqfflqtalnavrsyrgQET-LdrfdFQDLMEEKIA-----------------------LLKMPEDLLTRsvnVG-- 145
Cdd:COG5265 439 --------------------QDTvL----FNDTIAYNIAygrpdaseeeveaaaraaqihdfIESLPDGYDTR---VGer 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 146 ---FSGGEKKRNDILQMAVLEPELCILDESDSGLD------I-DALKVVADGVNSLrdgkrsfII------VTHYQRILd 209
Cdd:COG5265 492 glkLSGGEKQRVAIARTLLKNPPILIFDEATSALDsrteraIqAALREVARGRTTL-------VIahrlstIVDADEIL- 563
|
250
....*....|....*....
gi 16129638 210 yikpdyvhVLYQGRIVKSG 228
Cdd:COG5265 564 --------VLEAGRIVERG 574
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-76 |
2.31e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 58.94 E-value: 2.31e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLsATLAGREDyEVTGGTVEFKGKDLLALSPEDRA 76
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTL-LSMISRLL-PPDSGEVLVDGLDVATTPSRELA 74
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-82 |
2.38e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.03 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVsvedKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDL------------L 68
Cdd:COG1129 256 VLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGAD--PADSGEIRLDGKPVrirsprdairagI 329
|
90
....*....|....
gi 16129638 69 ALSPEDRAGEGIFM 82
Cdd:COG1129 330 AYVPEDRKGEGLVL 343
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-241 |
2.77e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 60.06 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 14 KAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEVTG-GTVEFKGKDLLAlsPEDRAGEGIFMafQYPVEIPG 92
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGsGSVLLNGMPIDA--KEMRAISAYVQ--QDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 93 --VSNQFFLQTALNAVRSYRGQETLDRFDfqDLMEEkIALLKMpEDLLTRSVNV--GFSGGEKKRNDILQMAVLEPELCI 168
Cdd:TIGR00955 114 ltVREHLMFQAHLRMPRRVTKKEKRERVD--EVLQA-LGLRKC-ANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 169 LDESDSGLD-------IDALKVVADgvnslrdgKRSFIIVTHYQ---RILDYIkpDYVHVLYQGRIVKSGDFT-LVKQLE 237
Cdd:TIGR00955 190 CDEPTSGLDsfmaysvVQVLKGLAQ--------KGKTIICTIHQpssELFELF--DKIILMAEGRVAYLGSPDqAVPFFS 259
|
....
gi 16129638 238 EQGY 241
Cdd:TIGR00955 260 DLGH 263
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-241 |
2.98e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.12 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 14 KAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRED-YEVT-GGTVEFKGkdllaLSPED----RAGEGIFMAfQYP 87
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgFHIGvEGVITYDG-----ITPEEikkhYRGDVVYNA-ETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 88 VEIPGVSNQFFLQTALNAVRSYRGQETLDRFDFQdlmeEKIALLKMPEDLL--TRSVNVG------FSGGEKKRNDILQM 159
Cdd:TIGR00956 148 VHFPHLTVGETLDFAARCKTPQNRPDGVSREEYA----KHIADVYMATYGLshTRNTKVGndfvrgVSGGERKRVSIAEA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 160 AVLEPELCILDESDSGLD-------IDALKVVADGVNSLrdgkrsfIIVTHYQRILD-YIKPDYVHVLYQGRIVKSGDFT 231
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDsatalefIRALKTSANILDTT-------PLVAIYQCSQDaYELFDKVIVLYEGYQIYFGPAD 296
|
250
....*....|.
gi 16129638 232 LVKQ-LEEQGY 241
Cdd:TIGR00956 297 KAKQyFEKMGF 307
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-210 |
3.35e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.89 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEV---TGGTVEFKGKDLLALSPE-DRAG 77
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrVEGRVEFFNQNIYERRVNlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 78 EGIFMAFQYPveipgvsNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMPEDL---LTRSVnVGFSGGEKKRN 154
Cdd:PRK14258 88 RQVSMVHPKP-------NLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIkhkIHKSA-LDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129638 155 DILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLR-DGKRSFIIVTH----YQRILDY 210
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHnlhqVSRLSDF 220
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-220 |
3.66e-10 |
|
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: 58.53 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 26 PGEVHAIMGPNGSGKSTLSATLA-------GREDYEVTGGTV--EFKGKDLLALSPEDRAGE-GIFMAFQYPVEIPgvsn 95
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAgklkpnlGKFDDPPDWDEIldEFRGSELQNYFTKLLEGDvKVIVKPQYVDLIP---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 96 qfflqtalNAVRSYRGqETLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESDSG 175
Cdd:cd03236 101 --------KAVKGKVG-ELLKKKDERGKLDELVDQLEL-RHVLDRNID-QLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16129638 176 LDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLY 220
Cdd:cd03236 170 LDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLS-DYIHCLY 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-205 |
4.05e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 59.19 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRagegif 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFE--TPDSGRIMLDGQDITHVPAENR------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 mafqyPVeipgvsNQFFLQTAL--------NAVRSYRGQETldrfDFQDLMEEKIALLKMP--EDLLTRSVNvGFSGGEK 151
Cdd:PRK09452 87 -----HV------NTVFQSYALfphmtvfeNVAFGLRMQKT----PAAEITPRVMEALRMVqlEEFAQRKPH-QLSGGQQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129638 152 KRNDILQMAVLEPELCILDESDSGLDIDALKVVAdgvNSLRDGKR----SFIIVTHYQ 205
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQ---NELKALQRklgiTFVFVTHDQ 205
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-58 |
4.17e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 4.17e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGredyEVTGG 58
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG----DLTGG 54
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-226 |
5.15e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 58.18 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGR-EDYEvtgGTVEFKGKDLLALSPEDRAGEgIFMAFQYPveipgvSN 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLfEEFE---GKVKIDGELLTAENVWNLRRK-IGMVFQNP------DN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 96 QFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMpEDLLTRSvNVGFSGGEKKRNDILQMAVLEPELCILDESDSG 175
Cdd:PRK13642 93 QFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNM-LDFKTRE-PARLSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16129638 176 LDIDALKVVADGVNSLRDgKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVK 226
Cdd:PRK13642 171 LDPTGRQEIMRVIHEIKE-KYQLTVLSITHDLDEAASSDRILVMKAGEIIK 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-65 |
5.43e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 57.78 E-value: 5.43e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 16129638 10 SVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGK 65
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG--ILEPTSGRVEVNGR 88
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-229 |
5.47e-10 |
|
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: 59.05 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAI--LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFK-GK---DLLALSPED 74
Cdd:TIGR03269 282 VRNVSKRYISVDRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGV--LEPTSGEVNVRvGDewvDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 75 --RAGEGIFMAFQ----YP-------------VEIPgvsNQFFLQTALNavrsyrgqeTLDRFDFQDLMEEKIaLLKMPE 135
Cdd:TIGR03269 360 rgRAKRYIGILHQeydlYPhrtvldnlteaigLELP---DELARMKAVI---------TLKMVGFDEEKAEEI-LDKYPD 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 136 DLltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLD-IDALKVVADGVNSLRDGKRSFIIVTHYqriLDYIKP- 213
Cdd:TIGR03269 427 EL---------SEGERHRVALAQVLIKEPRIVILDEPTGTMDpITKVDVTHSILKAREEMEQTFIIVSHD---MDFVLDv 494
|
250
....*....|....*..
gi 16129638 214 -DYVHVLYQGRIVKSGD 229
Cdd:TIGR03269 495 cDRAALMRDGKIVKIGD 511
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-178 |
7.09e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.88 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 3 SIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLaGREdYEVTGGTVEFKGKDLLALSPEDRAGEGIFM 82
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRH-QPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 83 AFQYPvEIPGVSNQfflqtALNAVRSYRGQETLDRFDFQDL--MEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMA 160
Cdd:PRK10575 91 PQQLP-AAEGMTVR-----ELVAIGRYPWHGALGRFGAADRekVEEAISLVGL-KPLAHRLVD-SLSGGERQRAWIAMLV 162
|
170
....*....|....*...
gi 16129638 161 VLEPELCILDESDSGLDI 178
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDI 180
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-87 |
7.28e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 58.32 E-value: 7.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKA-ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRageG 79
Cdd:PRK11650 3 GLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLE--RITSGEIWIGGRVVNELEPADR---D 77
|
90
....*....|..
gi 16129638 80 IFMAFQ----YP 87
Cdd:PRK11650 78 IAMVFQnyalYP 89
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-220 |
7.61e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.64 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 26 PGEVHAIMGPNGSGKST----LSATLA---GREDYEVTGGTV--EFKGKDLLALSPEDRAGEgIFMAF--QYPVEIPgvs 94
Cdd:COG1245 98 KGKVTGILGPNGIGKSTalkiLSGELKpnlGDYDEEPSWDEVlkRFRGTELQDYFKKLANGE-IKVAHkpQYVDLIP--- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 95 nqfflqtalnavRSYRG--QETLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDES 172
Cdd:COG1245 174 ------------KVFKGtvRELLEKVDERGKLDELAEKLGL-ENILDRDISE-LSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16129638 173 DSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLY 220
Cdd:COG1245 240 SSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLA-DYVHILY 286
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-65 |
7.63e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 7.63e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGK 65
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSG--NYQPDAGSILIDGQ 66
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-185 |
7.81e-10 |
|
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: 56.60 E-value: 7.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEdrAGEGIF 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLL--RPDSGEVRWNGTPLAEQRDE--PHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 mafqYPVEIPGVSNQFflqTALNAVRSYR---GQETLDRFDFQDLMEekialLKMPEDLLTRSVnvgfSGGEKKRNDILQ 158
Cdd:TIGR01189 77 ----YLGHLPGLKPEL---SALENLHFWAaihGGAQRTIEDALAAVG-----LTGFEDLPAAQL----SAGQQRRLALAR 140
|
170 180
....*....|....*....|....*..
gi 16129638 159 MAVLEPELCILDESDSGLDIDALKVVA 185
Cdd:TIGR01189 141 LWLSRRPLWILDEPTTALDKAGVALLA 167
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
14-229 |
9.86e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 57.67 E-value: 9.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 14 KAiLRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRAG--EGIFMAFQYP---- 87
Cdd:PRK11308 29 KA-LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIE--TPTGGELYYQGQDLLKADPEAQKLlrQKIQIVFQNPygsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 88 ---------VEIPGVSNqfflqTALNAvrSYRGQETLDrfdfqdlMEEKIALlkMPEDLlTRSVNVgFSGGEKKRNDILQ 158
Cdd:PRK11308 106 nprkkvgqiLEEPLLIN-----TSLSA--AERREKALA-------MMAKVGL--RPEHY-DRYPHM-FSGGQRQRIAIAR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 159 MAVLEPELCILDESDSGLDIdalKVVADGVNSLRDGKR----SFIIVTHYQRILDYIKPDyVHVLYQGRIVKSGD 229
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDV---SVQAQVLNLMMDLQQelglSYVFISHDLSVVEHIADE-VMVMYLGRCVEKGT 238
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-224 |
1.10e-09 |
|
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: 56.65 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALspEDRA----GEGIFMAFQ------- 85
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEE--LPTSGTIRVNGQDVSDL--RGRAipylRRKIGVVFQdfrllpd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 86 --------YPVEIPGVSNQfflqtalnaVRSYRGQETLDRFDFQDLMEEkiallkMPEDLltrsvnvgfSGGEKKRNDIL 157
Cdd:cd03292 93 rnvyenvaFALEVTGVPPR---------EIRKRVPAALELVGLSHKHRA------LPAEL---------SGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129638 158 QMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYIKPDyVHVLYQGRI 224
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHR-VIALERGKL 214
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-243 |
1.19e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 57.80 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 3 SIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLALSPEDRAGEgifM 82
Cdd:PRK10789 317 NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI--QRHFDVSEGDIRFHDIPLTKLQLDSWRSR---L 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 83 AfqypveipgVSNQ---FFLQTALNAVRSYRGQETldrfdfQDLMEE--KIA-----LLKMPEDLLTR--SVNVGFSGGE 150
Cdd:PRK10789 392 A---------VVSQtpfLFSDTVANNIALGRPDAT------QQEIEHvaRLAsvhddILRLPQGYDTEvgERGVMLSGGQ 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 151 KKRNDILQMAVLEPELCILDesdsgldiDALKVVaDG------VNSLRD--GKRSFIIVTHyqRILDYIKPDYVHVLYQG 222
Cdd:PRK10789 457 KQRISIARALLLNAEILILD--------DALSAV-DGrtehqiLHNLRQwgEGRTVIISAH--RLSALTEASEILVMQHG 525
|
250 260
....*....|....*....|.
gi 16129638 223 RIVKSGDftlVKQLEEQGyGW 243
Cdd:PRK10789 526 HIAQRGN---HDQLAQQS-GW 542
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-220 |
1.66e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 26 PGEVHAIMGPNGSGKST----LSATLA---GREDYEVTGGTV--EFKGKDLLALSPEDRAGEgIFMAF--QYPVEIPgvs 94
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTavkiLSGELIpnlGDYEEEPSWDEVlkRFRGTELQNYFKKLYNGE-IKVVHkpQYVDLIP--- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 95 nqfflqtalnavRSYRGQ--ETLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDES 172
Cdd:PRK13409 174 ------------KVFKGKvrELLKKVDERGKLDEVVERLGL-ENILDRDISE-LSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16129638 173 DSGLDIDALKVVADGVNSLRDGKrSFIIVTHYQRILDYIKpDYVHVLY 220
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAEGK-YVLVVEHDLAVLDYLA-DNVHIAY 285
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-229 |
1.75e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.52 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALspEDRAGE--- 78
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLE--KPSEGSIVVNGQTINLV--RDKDGQlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 79 -----------GIFMAFQY----------------PVEIPGVSNQfflqtalnaVRSYRGQETLDRFDFQDLmeekiALL 131
Cdd:PRK10619 82 adknqlrllrtRLTMVFQHfnlwshmtvlenvmeaPIQVLGLSKQ---------EARERAVKYLAKVGIDER-----AQG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 132 KMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYI 211
Cdd:PRK10619 148 KYPVHL---------SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHV 218
|
250
....*....|....*...
gi 16129638 212 KpDYVHVLYQGRIVKSGD 229
Cdd:PRK10619 219 S-SHVIFLHQGKIEEEGA 235
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-241 |
2.45e-09 |
|
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: 57.06 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 16 ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALspeDRAGEGIFMAF--QYPVEIPGV 93
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGF--FQARSGEILLNGFSLKDI---DRHTLRQFINYlpQEPYIFSGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 94 snqfFLQTALNAVRSYRGQETLDRFdfQDLMEEKIALLKMPEDLLTR--SVNVGFSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:TIGR01193 564 ----ILENLLLGAKENVSQDEIWAA--CEIAEIKDDIENMPLGYQTElsEEGSSISGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 172 SDSGLDIDALKVVADGVNSLRDgkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGdfTLVKQLEEQGY 241
Cdd:TIGR01193 638 STSNLDTITEKKIVNNLLNLQD--KTIIFVAH--RLSVAKQSDKIIVLDHGKIIEQG--SHDELLDRNGF 701
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-228 |
2.78e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 56.29 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVED-----KAILRgLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDY--EVTGGTVEFKGKDLLALSPE 73
Cdd:PRK11022 3 LLNVDKLSVHFGDesapfRAVDR-ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYpgRVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 74 DR---AGEGIFMAFQYPVEI--PGVSNQFFLQTALNA----VRSYRGQETLDRFDFQDLMEEKIALLKMPEDLltrsvnv 144
Cdd:PRK11022 82 ERrnlVGAEVAMIFQDPMTSlnPCYTVGFQIMEAIKVhqggNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQL------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 145 gfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTH--------YQRILdyikpdy 215
Cdd:PRK11022 155 --SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHdlalvaeaAHKII------- 225
|
250
....*....|...
gi 16129638 216 vhVLYQGRIVKSG 228
Cdd:PRK11022 226 --VMYAGQVVETG 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
16-177 |
3.24e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.25 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 16 ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDLLALSPEDRAgegIFMAFQYpveipgvsn 95
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ--TSGHIRFHGTDVSRLHARDRK---VGFVFQH--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 96 qfflqTALnavrsYRGQETLDRFDF------------QDLMEEKIA-LLKMPEdlLTRSVN---VGFSGGEKKRNDILQM 159
Cdd:PRK10851 83 -----YAL-----FRHMTVFDNIAFgltvlprrerpnAAAIKAKVTqLLEMVQ--LAHLADrypAQLSGGQKQRVALARA 150
|
170
....*....|....*...
gi 16129638 160 AVLEPELCILDESDSGLD 177
Cdd:PRK10851 151 LAVEPQILLLDEPFGALD 168
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-80 |
3.80e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 55.42 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRAGEGI 80
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLV--KPDSGRIFLDGEDITHLPMHKRARLGI 80
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-87 |
3.97e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 56.07 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVED-----KAILRgLSLDVHPGEVHAIMGPNGSGKSTLSATLAG--REDYEVTGGTVEFKGKDLLALSPE 73
Cdd:COG4170 3 LLDIRNLTIEIDTpqgrvKAVDR-VSLTLNEGEIRGLVGESGSGKSLIAKAICGitKDNWHVTADRFRWNGIDLLKLSPR 81
|
90
....*....|....*..
gi 16129638 74 DR---AGEGIFMAFQYP 87
Cdd:COG4170 82 ERrkiIGREIAMIFQEP 98
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
8-230 |
4.90e-09 |
|
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: 54.08 E-value: 4.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 8 HVSV---EDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGredyevtggtvefkgkdllaLSPedrAGEGIfmaf 84
Cdd:cd03223 5 NLSLatpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG--------------------LWP---WGSGR---- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 85 qypVEIPGVSNQFFL-QtalnavRSYRGQETLdrfdfqdlmeeKIALLKMPEDLLtrsvnvgfSGGEKKRNDILQMAVLE 163
Cdd:cd03223 58 ---IGMPEGEDLLFLpQ------RPYLPLGTL-----------REQLIYPWDDVL--------SGGEQQRLAFARLLLHK 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129638 164 PELCILDESDSGLDIDALKVVADgvnSLRDGKRSFIIVTHYQRILDYikpdYVHVLyqgRIVKSGDF 230
Cdd:cd03223 110 PKFVFLDEATSALDEESEDRLYQ---LLKELGITVISVGHRPSLWKF----HDRVL---DLDGEGGW 166
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-229 |
4.97e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 55.38 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLALS--PEDRAGEGIfmAFQYPveipgvS 94
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ--KGKVLVSGIDTGDFSklQGIRKLVGI--VFQNP------E 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 95 NQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDS 174
Cdd:PRK13644 88 TQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGL-EKYRHRSPKT-LSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 175 GLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDyiKPDYVHVLYQGRIVKSGD 229
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELH--DADRIIVMDRGKIVLEGE 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-195 |
5.39e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 55.62 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALS--------- 71
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGT--LTPTAGTVLVAGDDVEALSaraasrrva 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 72 --PEDRAgegifMAFQYPVEipgvsnqfflQTALNAVRSYRGqetldRFDFQDLMEEKIALLKMPEDLLTRSVNVGF--- 146
Cdd:PRK09536 81 svPQDTS-----LSFEFDVR----------QVVEMGRTPHRS-----RFDTWTETDRAAVERAMERTGVAQFADRPVtsl 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16129638 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDID----ALKVVADGVNslrDGK 195
Cdd:PRK09536 141 SGGERQRVLLARALAQATPVLLLDEPTASLDINhqvrTLELVRRLVD---DGK 190
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-241 |
1.27e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.73 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDL------------L 68
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG--DPRATSGRIVFDGKDItdwqtakimreaV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 69 ALSPEdraGEGIFMafQYPVEIPGVSNQFFlqtalnavrsyrgqetLDRFDFQDLMEEKIALLkmPEDLLTRSVNVG-FS 147
Cdd:PRK11614 83 AIVPE---GRRVFS--RMTVEENLAMGGFF----------------AERDQFQERIKWVYELF--PRLHERRIQRAGtMS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLR-DGKRSFIIVTHYQRILDYikPDYVHVLYQGRIV- 225
Cdd:PRK11614 140 GGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLReQGMTIFLVEQNANQALKL--ADRGYVLENGHVVl 217
|
250
....*....|....*..
gi 16129638 226 -KSGDFTLVKQLEEQGY 241
Cdd:PRK11614 218 eDTGDALLANEAVRSAY 234
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-228 |
1.27e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.74 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLALSPEDRAGEGIF 81
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD--AGNIIIDDEDISLLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQYPVEIPGVSNQFFLQTALNAVRSYRGQETLDRFDfqDLMEE-KIALLKmpeDLLTRSVnvgfSGGEKKRNDILQMA 160
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRAN--ELMEEfHIEHLR---DSMGQSL----SGGERRRVEIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129638 161 VLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQR-ILDYIKPDYvhVLYQGRIVKSG 228
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVReTLAVCERAY--IVSQGHLIAHG 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-203 |
1.62e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 54.73 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 12 EDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLaGREDyEVTGGTVEFKGKDLLALSPEDRAG---EGIFMAFQ--- 85
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLD-KPTSGTYRVAGQDVATLDADALAQlrrEHFGFIFQryh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 86 --------YPVEIPGVsnqfFLQTALNAvRSYRGQETLDRFDFQDLMEEKiallkmPEDLltrsvnvgfSGGEKKRNDIL 157
Cdd:PRK10535 97 llshltaaQNVEVPAV----YAGLERKQ-RLLRAQELLQRLGLEDRVEYQ------PSQL---------SGGQQQRVSIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16129638 158 QMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTH 203
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-229 |
1.66e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.09 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 16 ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGR----------EDYeVTGGTVEFKGKDLLALSPE----DRAGEGIF 81
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDI-YIGDKKNNHELITNPYSKKiknfKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQYPveipgvSNQFFlqtalnavrsyrgQETLDRfdfqDLMEEKIAL-----------------LKMPEDLLTRSvNV 144
Cdd:PRK13631 120 MVFQFP------EYQLF-------------KDTIEK----DIMFGPVALgvkkseakklakfylnkMGLDDSYLERS-PF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 145 GFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTH-YQRILDYikPDYVHVLYQGR 223
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHtMEHVLEV--ADEVIVMDKGK 253
|
....*.
gi 16129638 224 IVKSGD 229
Cdd:PRK13631 254 ILKTGT 259
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-228 |
1.77e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.48 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 20 LSLDVHPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGK--DLLALSPEDRAGEGIFMAFQYPVEI--PGVSN 95
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALL--RLVESQGGEIIFNGQriDTLSPGKLQALRRDIQFIFQDPYASldPRQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 96 QFFLQTALNAVRSYRGQETLDRFDFqdlMEEKIALLkmPEDLLTRSVNvgFSGGEKKRNDILQMAVLEPELCILDESDSG 175
Cdd:PRK10261 421 GDSIMEPLRVHGLLPGKAAAARVAW---LLERVGLL--PEHAWRYPHE--FSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129638 176 LDIdalKVVADGVNSLRDGKR----SFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:PRK10261 494 LDV---SIRGQIINLLLDLQRdfgiAYLFISHDMAVVERIS-HRVAVMYLGQIVEIG 546
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-184 |
1.80e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.31 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKdllalsPEDRAGEGI 80
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGL--LHVESGQIQIDGK------TATRGDRSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAfqYPVEIPG-------VSNQFFlqtaLNAVRSYRGQETLDRfdfqdlmEEKIALLKMPEDLLTRSVnvgfSGGEKKR 153
Cdd:PRK13543 83 FMA--YLGHLPGlkadlstLENLHF----LCGLHGRRAKQMPGS-------ALAIVGLAGYEDTLVRQL----SAGQKKR 145
|
170 180 190
....*....|....*....|....*....|.
gi 16129638 154 NDILQMAVLEPELCILDESDSGLDIDALKVV 184
Cdd:PRK13543 146 LALARLWLSPAPLWLLDEPYANLDLEGITLV 176
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-203 |
2.64e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.90 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 16 ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPEDRA---GEGIFMAFQYPVEIPG 92
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLD--TPTSGDVIFNGQPMSKLSSAAKAelrNQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 93 VsnqfflqTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDILQMAVLEPELCILDES 172
Cdd:PRK11629 102 F-------TALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSEL--SGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 16129638 173 DSGLDidalKVVADGVNSL------RDGKrSFIIVTH 203
Cdd:PRK11629 173 TGNLD----ARNADSIFQLlgelnrLQGT-AFLVVTH 204
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-177 |
4.11e-08 |
|
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: 52.47 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPeDRagegiFMAFQYPVEIPGVSNQ 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLA--QPTSGGVILEGKQITEPGP-DR-----MVVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 97 FFLQTALNAVRSyrgqeTLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDILQMAVLEPELCILDESDSGL 176
Cdd:TIGR01184 73 ENIALAVDRVLP-----DLSKSERRAIVEEHIALVGLTEAADKRPGQL--SGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
.
gi 16129638 177 D 177
Cdd:TIGR01184 146 D 146
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-211 |
4.12e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 52.89 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLALSPEDRAGEGIF 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPD--AGSISLCGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQypveipGVSNQFFLQTALNAVRSYRGQETLD-RFDFQDLMEekIALLKMPEDLLTRSVnvgfSGGEKKRNDILQMA 160
Cdd:PRK13537 86 PQFD------NLDPDFTVRENLLVFGRYFGLSAAAaRALVPPLLE--FAKLENKADAKVGEL----SGGMKRRLTLARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 161 VLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHY----QRILDYI 211
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFmeeaERLCDRL 208
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
16-229 |
4.38e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 52.32 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 16 ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRE-----DYEVTGGTVEFKG----KDLLALspedRAGEGifMAFQ- 85
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEmprsgTLNIAGNHFDFSKtpsdKAIREL----RRNVG--MVFQq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 86 Y---------------PVEIPGVSNQFFLQTALNAVRSYRGQETLDRFDFQdlmeekiallkmpedlltrsvnvgFSGGE 150
Cdd:PRK11124 91 YnlwphltvqqnlieaPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLH------------------------LSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYqriLDYIKPDYVHVLY--QGRIVKSG 228
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHE---VEVARKTASRVVYmeNGHIVEQG 223
|
.
gi 16129638 229 D 229
Cdd:PRK11124 224 D 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
12-242 |
4.49e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 52.74 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 12 EDKAiLRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDL----LALSpEDRAGEGIfmAFQYP 87
Cdd:PRK13637 19 EKKA-LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGL--LKPTSGKIIIDGVDItdkkVKLS-DIRKKVGL--VFQYP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 88 veipgvSNQFFLQTALNAV----------------RSYRGQET--LDRFDFQDlmeekiallKMPEDLltrsvnvgfSGG 149
Cdd:PRK13637 93 ------EYQLFEETIEKDIafgpinlglseeeienRVKRAMNIvgLDYEDYKD---------KSPFEL---------SGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDG-KRSFIIVTHYQRilDYIK-PDYVHVLYQGRIVKS 227
Cdd:PRK13637 149 QKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSME--DVAKlADRIIVMNKGKCELQ 226
|
250
....*....|....*....
gi 16129638 228 GD----FTLVKQLEEQGYG 242
Cdd:PRK13637 227 GTprevFKEVETLESIGLA 245
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-229 |
6.45e-08 |
|
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: 52.52 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLALSPEDRAGEGI 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 FMAFQYPVEIP--GVSNQFFL--QTALNAVRSYRGQETLDRfdfQDLMEEkialLKMPEDLLTRSVNvGFSGGEKKRNDI 156
Cdd:TIGR02633 81 VIIHQELTLVPelSVAENIFLgnEITLPGGRMAYNAMYLRA---KNLLRE----LQLDADNVTRPVG-DYGGGQQQLVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 157 LQMAVLEPELCILDESDSGLDIDALKVVADGVnslRDGKRSFIIVTHYQRILDYIKP--DYVHVLYQGRIVKSGD 229
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDII---RDLKAHGVACVYISHKLNEVKAvcDTICVIRDGQHVATKD 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-180 |
6.93e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.50 E-value: 6.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVED-KAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGredyevtggtvefkgkdllaLSPedrAGEG 79
Cdd:COG4178 362 ALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG--------------------LWP---YGSG 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 80 IfmafqypVEIPGVSNQFFL-QtalnavRSYRGQETL----------DRFDFQDLME--EKIALlkmpEDLLTRsVNVG- 145
Cdd:COG4178 419 R-------IARPAGARVLFLpQ------RPYLPLGTLreallypataEAFSDAELREalEAVGL----GHLAER-LDEEa 480
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16129638 146 -----FSGGEKKRndiLQMA---VLEPELCILDESDSGLDIDA 180
Cdd:COG4178 481 dwdqvLSLGEQQR---LAFArllLHKPDWLFLDEATSALDEEN 520
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-248 |
7.34e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.54 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHV-SVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEvtgGTVEFKGKDLLALSPED-RA--- 76
Cdd:PRK11174 350 IEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ---GSLKINGIELRELDPESwRKhls 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 77 --GegifmafQYPveipgvsnQFFLQTALNAVRsyRGQETLDRFDFQDLME-----EKIALLKMPEDLLTRSVNVGFSGG 149
Cdd:PRK11174 427 wvG-------QNP--------QLPHGTLRDNVL--LGNPDASDEQLQQALEnawvsEFLPLLPQGLDTPIGDQAAGLSVG 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 150 EKKRndI-LQMAVLEP-ELCILDESDSGLDIDALKVVADGVNSLRDGKrSFIIVTHyqRILDYIKPDYVHVLYQGRIVKS 227
Cdd:PRK11174 490 QAQR--LaLARALLQPcQLLLLDEPTASLDAHSEQLVMQALNAASRRQ-TTLMVTH--QLEDLAQWDQIWVMQDGQIVQQ 564
|
250 260
....*....|....*....|....
gi 16129638 228 GDF-TLVKQleeQG--YGWLTEQQ 248
Cdd:PRK11174 565 GDYaELSQA---GGlfATLLAHRQ 585
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-226 |
7.56e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.14 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTL-------------SATLAGredYEVTGGTvefKGKDLLALSPEdragegIFMA 83
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLmqhfnallkpssgTITIAG---YHITPET---GNKNLKKLRKK------VSLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 84 FQYPveipgvSNQFFLQTALNAVRSyrGQETldrFDFQDlMEEKIALLK------MPEDLLTRSvNVGFSGGEKKRNDIL 157
Cdd:PRK13641 91 FQFP------EAQLFENTVLKDVEF--GPKN---FGFSE-DEAKEKALKwlkkvgLSEDLISKS-PFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 158 QMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTH-YQRILDYikPDYVHVLYQGRIVK 226
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHnMDDVAEY--ADDVLVLEHGKLIK 225
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-210 |
8.31e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.55 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAG--------REDYEVTGGTVEFKGKdLLALSP 72
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksaGSHIELLGRTVQREGR-LARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 73 EDRAGEG-IFMAFQY--------PVEIPGVSNQFFLQTAL---NAVRSYRGQETLDRFDFQDLMEEKIALLkmpedlltr 140
Cdd:PRK09984 83 KSRANTGyIFQQFNLvnrlsvleNVLIGALGSTPFWRTCFswfTREQKQRALQALTRVGMVHFAHQRVSTL--------- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 141 svnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQriLDY 210
Cdd:PRK09984 154 ------SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQ--VDY 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-228 |
8.93e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.72 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVED--KAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAG------REDYEVTGGTVEFKGKDLLALspE 73
Cdd:PRK13640 6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddNPNSKITVDGITLTAKTVWDI--R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 74 DRAGegifMAFQYPveipgvSNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKR 153
Cdd:PRK13640 84 EKVG----IVFQNP------DNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANL--SGGQKQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129638 154 NDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFII-VTHyqRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVIsITH--DIDEANMADQVLVLDDGKLLAQG 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-177 |
9.59e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 6 DLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedyeVTGGTVEfkGKDLLAlspedrAGEGIFMAFQ 85
Cdd:TIGR00956 768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAER----VTTGVIT--GGDRLV------NGRPLDSSFQ 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 86 ypvEIPGVSNQFFLQTALNAVRS-------YRGQETLDRFDFQDLMEEKIALLKMPE--DLLTRSVNVGFSGGEKKRNDI 156
Cdd:TIGR00956 836 ---RSIGYVQQQDLHLPTSTVREslrfsayLRQPKSVSKSEKMEYVEEVIKLLEMESyaDAVVGVPGEGLNVEQRKRLTI 912
|
170 180
....*....|....*....|..
gi 16129638 157 LQMAVLEPELCI-LDESDSGLD 177
Cdd:TIGR00956 913 GVELVAKPKLLLfLDEPTSGLD 934
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
12-240 |
1.58e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.86 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 12 EDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSP----EDRAGegifMAFQYP 87
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAL--LIPSEGKVYVDGLDTSDEENlwdiRNKAG----MVFQNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 88 veipgvSNQFF--------------LQTALNAVRSyRGQETLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKR 153
Cdd:PRK13633 95 ------DNQIVativeedvafgpenLGIPPEEIRE-RVDESLKKVGMYEYRRHAPHLL---------------SGGQKQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 154 NDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTHYQRilDYIKPDYVHVLYQGRIVKSGD--- 229
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYME--EAVEADRIIVMDSGKVVMEGTpke 230
|
250
....*....|..
gi 16129638 230 -FTLVKQLEEQG 240
Cdd:PRK13633 231 iFKEVEMMKKIG 242
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
14-80 |
2.26e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.16 E-value: 2.26e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129638 14 KAiLRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPED--RAGEGI 80
Cdd:PRK10762 18 KA-LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGI--YTRDAGSILYLGKEVTFNGPKSsqEAGIGI 83
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-229 |
2.91e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.01 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDK----AILRGLSLDVHPGEVHAIMGPNGSGKSTlsATLAGREDYEVTGGTVEF-------KGKDLLA 69
Cdd:PRK10261 12 VLAVENLNIAFMQEqqkiAAVRNLSFSLQRGETLAIVGESGSGKSV--TALALMRLLEQAGGLVQCdkmllrrRSRQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 70 LSPEDRA------GEGIFMAFQYPVeipgvsnqfflqTALNAV--------RSYRGQETLDRFDFQDLMEEKIALLKMPE 135
Cdd:PRK10261 90 LSEQSAAqmrhvrGADMAMIFQEPM------------TSLNPVftvgeqiaESIRLHQGASREEAMVEAKRMLDQVRIPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 136 --DLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTHYQRILDYIK 212
Cdd:PRK10261 158 aqTILSRYPH-QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIA 236
|
250
....*....|....*..
gi 16129638 213 pDYVHVLYQGRIVKSGD 229
Cdd:PRK10261 237 -DRVLVMYQGEAVETGS 252
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-203 |
3.29e-07 |
|
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: 49.41 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEvtggtvefKGKDLLALSPEDRAGEGIF 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPL--------AGRVLLNGGPLDFQRDSIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQYPVEIPGVsnqfflQTALNAVRSYRgqeTLDRFDFQDLMEEKIAL--LKMPEDLLTRSVnvgfSGGEKKRNDILQM 159
Cdd:cd03231 73 RGLLYLGHAPGI------KTTLSVLENLR---FWHADHSDEQVEEALARvgLNGFEDRPVAQL----SAGQQRRVALARL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16129638 160 AVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTH 203
Cdd:cd03231 140 LLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-229 |
3.44e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.47 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVS-----------VEDKAILRGLSLDVHPGEVHAIMGPNGSGKST----LSATLAGRedyevtgGTVEFKGK 65
Cdd:PRK15134 275 LLDVEQLQVAfpirkgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-------GEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 66 DLLALS-----PEDRAgegIFMAFQYPveipgvsnqfflQTALNAvrsyrgqetldRFDFQDLMEEKIA----------- 129
Cdd:PRK15134 348 PLHNLNrrqllPVRHR---IQVVFQDP------------NSSLNP-----------RLNVLQIIEEGLRvhqptlsaaqr 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 130 ----LLKMPE---DLLTRSVNVG-FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKR-SFII 200
Cdd:PRK15134 402 eqqvIAVMEEvglDPETRHRYPAeFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLF 481
|
250 260
....*....|....*....|....*....
gi 16129638 201 VTHYQRILDYIkPDYVHVLYQGRIVKSGD 229
Cdd:PRK15134 482 ISHDLHVVRAL-CHQVIVLRQGEVVEQGD 509
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-203 |
3.63e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.78 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYeVTG----GTVEFKGKDLLA--LSP-ED 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDL-IPGfrveGKVTFHGKNLYApdVDPvEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 75 RAGEGifMAFQYPVEIPgvsNQFFLQTALNA-VRSYRGqetldrfDFQDLMEEKI---ALLKMPEDLLTRSvNVGFSGGE 150
Cdd:PRK14243 90 RRRIG--MVFQKPNPFP---KSIYDNIAYGArINGYKG-------DMDELVERSLrqaALWDEVKDKLKQS-GLSLSGGQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16129638 151 KKRNDILQMAVLEPELCILDESDSGLD-IDALKvVADGVNSLRDgKRSFIIVTH 203
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDpISTLR-IEELMHELKE-QYTIIIVTH 208
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
19-211 |
3.96e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 19 GLSLDVHPGEVHA-----IMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKdlLALSPedragegifmafQYPVEIPGV 93
Cdd:PRK13409 352 DFSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVL--KPDEGEVDPELK--ISYKP------------QYIKPDYDG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 94 SNQFFLQTALNAVR-SYRGQETLDRFDFQDLMEEKIallkmpEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILDES 172
Cdd:PRK13409 416 TVEDLLRSITDDLGsSYYKSEIIKPLQLERLLDKNV------KDL---------SGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16129638 173 DSGLDIDALKVVADGVNSLRDGKR-SFIIVTHYQRILDYI 211
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIAEEREaTALVVDHDIYMIDYI 520
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-243 |
4.54e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 50.21 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKA--ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAgREdYEVTGGTVEFKGKDLLALSPED-RAGe 78
Cdd:PRK11160 339 LTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-RA-WDPQQGEILLNGQPIADYSEAAlRQA- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 79 gifMAFqypveipgVSNQ--FF-------LQTALNAVRSYRGQETLDRFDFQDLMEEKIALlkmpeDLLTRSVNVGFSGG 149
Cdd:PRK11160 416 ---ISV--------VSQRvhLFsatlrdnLLLAAPNASDEALIEVLQQVGLEKLLEDDKGL-----NAWLGEGGRQLSGG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 150 EKKRNDILQmAVLEP-ELCILDESDSGLDIDALKVVADGVNSLRDGKrSFIIVTHYQRILDYIkpDYVHVLYQGRIVKSG 228
Cdd:PRK11160 480 EQRRLGIAR-ALLHDaPLLLLDEPTEGLDAETERQILELLAEHAQNK-TVLMITHRLTGLEQF--DRICVMDNGQIIEQG 555
|
250
....*....|....*
gi 16129638 229 DFTLVkqLEEQGYGW 243
Cdd:PRK11160 556 THQEL--LAQQGRYY 568
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-81 |
4.59e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.17 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 14 KAiLRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKG-----KDL--------------LALSPED 74
Cdd:NF040905 15 KA-LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEILFDGevcrfKDIrdsealgiviihqeLALIPYL 93
|
....*..
gi 16129638 75 RAGEGIF 81
Cdd:NF040905 94 SIAENIF 100
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-205 |
5.08e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 4 IKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATlagredyeVTGGTVEFKGKDLLALSPEDRAGEGIFMA 83
Cdd:PRK10938 263 LNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSL--------ITGDHPQGYSNDLTLFGRRRGSGETIWDI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 84 FQYpveIPGVSNQFFLQ-----TALNAVRS--------YrgQETLDRfdFQDLMEEKIALLKMPEDLLTRSVNvGFSGGE 150
Cdd:PRK10938 335 KKH---IGYVSSSLHLDyrvstSVRNVILSgffdsigiY--QAVSDR--QQKLAQQWLDILGIDKRTADAPFH-SLSWGQ 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16129638 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTHYQ 205
Cdd:PRK10938 407 QRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLiSEGETQLLFVSHHA 462
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-65 |
6.54e-07 |
|
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: 48.62 E-value: 6.54e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129638 2 LSIKDLHVSVEDKA-----ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGK 65
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG--ELEKLSGSVSVPGS 67
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-85 |
6.63e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 49.41 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLH--VSVEDKAI--LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALSPED-- 74
Cdd:PRK11153 1 MIELKNISkvFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLE--RPTSGRVLVDGQDLTALSEKElr 78
|
90
....*....|.
gi 16129638 75 RAGEGIFMAFQ 85
Cdd:PRK11153 79 KARRQIGMIFQ 89
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
14-87 |
6.67e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.42 E-value: 6.67e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129638 14 KAILRgLSLDVHPGEVHAIMGPNGSGKSTLSATLAG--REDYEVTGGTVEFKGKDLLALSPEDR---AGEGIFMAFQYP 87
Cdd:PRK15093 21 KAVDR-VSMTLTEGEIRGLVGESGSGKSLIAKAICGvtKDNWRVTADRMRFDDIDLLRLSPRERrklVGHNVSMIFQEP 98
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-222 |
8.45e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLALSPEDRAGE--- 78
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG--ELEPDSGTVKWSENANIGYYAQDHAYDfen 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 79 --GIF--MAfQYpvEIPGVSNQfflqtalnAVRSyrgqeTLDRFDFQdlmeekiallkmpEDLLTRSVNVgFSGGEKKRN 154
Cdd:PRK15064 398 dlTLFdwMS-QW--RQEGDDEQ--------AVRG-----TLGRLLFS-------------QDDIKKSVKV-LSGGEKGRM 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129638 155 DILQMAVLEPELCILDESDSGLD---IDALKvvadgvNSLRDGKRSFIIVTHYQ--------RILDyIKPDYVhVLYQG 222
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDmesIESLN------MALEKYEGTLIFVSHDRefvsslatRIIE-ITPDGV-VDFSG 518
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
12-248 |
8.97e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 48.57 E-value: 8.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 12 EDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLlalsPEDRAGE---GIFMAFQYPv 88
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGL--LEAESGQIIIDGDLL----TEENVWDirhKIGMVFQNP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 89 eipgvSNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMpEDLLTRSvNVGFSGGEKKRNDILQMAVLEPELCI 168
Cdd:PRK13650 91 -----DNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGM-QDFKERE-PARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 169 LDESDSGLDIDALKVVADGVNSLRDGKRSFII-VTHYqriLDYIK-PDYVHVLYQGRIVKSGD----------------- 229
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDYQMTVIsITHD---LDEVAlSDRVLVMKNGQVESTSTprelfsrgndllqlgld 240
|
250 260
....*....|....*....|....*..
gi 16129638 230 --FT--LVKQLEEQGY----GWLTEQQ 248
Cdd:PRK13650 241 ipFTtsLVQSLRQNGYdlpeGYLTEKE 267
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-228 |
1.02e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.47 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTL------------SATLAGreDYEVTGGTVefKGKDLLALSPEdragegIFMAF 84
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMiqltngliisetGQTIVG--DYAIPANLK--KIKEVKRLRKE------IGLVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 85 QYPveipgvSNQFFLQTALNAVRSYRGQETLDRFDFQDLMEEKIALLKMPEDLLTRSvNVGFSGGEKKRNDILQMAVLEP 164
Cdd:PRK13645 97 QFP------EYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRS-PFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129638 165 ELCILDESDSGLDIdalKVVADGVNSL----RDGKRSFIIVTH-YQRILDYikPDYVHVLYQGRIVKSG 228
Cdd:PRK13645 170 NTLVLDEPTGGLDP---KGEEDFINLFerlnKEYKKRIIMVTHnMDQVLRI--ADEVIVMHEGKVISIG 233
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
12-207 |
1.11e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.46 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 12 EDK-AILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyevTGGTVE-------F-KGKDLLAL-----------S 71
Cdd:PLN03140 890 EDRlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRK----TGGYIEgdirisgFpKKQETFARisgyceqndihS 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 72 PEDRAGEG-IFMAF-QYPVEipgVSNQfflqtalnavrsyrgqetlDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGG 149
Cdd:PLN03140 966 PQVTVRESlIYSAFlRLPKE---VSKE-------------------EKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTE 1023
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129638 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRI 207
Cdd:PLN03140 1024 QRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-177 |
1.19e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.16 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLALSPEdRAgegi 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ--HGSITLDGKPVEGPGAE-RG---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 fMAFQYPVEIPGVSNQ----FFLQTA--LNAVRSYRGQETLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRN 154
Cdd:PRK11248 74 -VVFQNEGLLPWRNVQdnvaFGLQLAgvEKMQRLEIAHQMLKKVGLEGAEKRYIWQL---------------SGGQRQRV 137
|
170 180
....*....|....*....|...
gi 16129638 155 DILQMAVLEPELCILDESDSGLD 177
Cdd:PRK11248 138 GIARALAANPQLLLLDEPFGALD 160
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-203 |
1.22e-06 |
|
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: 49.24 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 20 LSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLALSPEDRAGEGIFMAFQYPVEIPGVSNQFFL 99
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTG--DTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYL 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 100 QTALNAVRSyRGQETLDRFDFQDLMeekialLKMPEDLLTRSvnvgFSGGEKKRNDILQMAVLEPELCILDESDSGLDID 179
Cdd:TIGR01257 2036 YARLRGVPA-EEIEKVANWSIQSLG------LSLYADRLAGT----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 2104
|
170 180
....*....|....*....|....
gi 16129638 180 ALKVVADGVNSLRDGKRSFIIVTH 203
Cdd:TIGR01257 2105 ARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
2-203 |
1.65e-06 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 47.26 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAI-LRGLsldvHPGEVHAIMGPNGSGKSTL--SATLAgredyevtggtvefkgkdLLALSPEDRAGE 78
Cdd:cd03279 6 LELKNFGPFREEQVIdFTGL----DNNGLFLICGPTGAGKSTIldAITYA------------------LYGKTPRYGRQE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 79 GIFMAFQYPVEIPGVSNQFFLQTALNAVRSYRGqetLDRFDFQdlmeeKIALLKMPE--DLLTRSVNvGFSGGEKKRNDI 156
Cdd:cd03279 64 NLRSVFAPGEDTAEVSFTFQLGGKKYRVERSRG---LDYDQFT-----RIVLLPQGEfdRFLARPVS-TLSGGETFLASL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129638 157 -LQMAVLEP---------ELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTH 203
Cdd:cd03279 135 sLALALSEVlqnrggarlEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISH 191
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-205 |
2.11e-06 |
|
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: 46.85 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVH----PGEVHAIMGPNGSGKSTLSATLAGREdyevTGGTVEfkGKDLLalspedrAG 77
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRQLLNNISgyvkPGTLTALMGESGAGKTTLLDVLAGRK----TAGVIT--GEILI-------NG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 78 EGIFMAFQypvEIPGVSNQFFLQTALNAVRsyrgqETLdRFDfqdlmeekiALLKmpedlltrsvnvGFSGGEKKRNDIL 157
Cdd:cd03232 71 RPLDKNFQ---RSTGYVEQQDVHSPNLTVR-----EAL-RFS---------ALLR------------GLSVEQRKRLTIG 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16129638 158 QMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSfIIVTHYQ 205
Cdd:cd03232 121 VELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQA-ILCTIHQ 167
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-229 |
2.43e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.39 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 13 DKAILRGLSLDVHPGEVHAIMGPNGSGKS-TLSATL----AGredYEVTGGTVEFKGKdllALSPEDRAGEGIFMAFQYP 87
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAG---VRQTAGRVLLDGK---PVAPCALRGRKIATIMQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 88 veipgvsnqfflQTALNAVRSYR--GQETL---DRFDFQDLMEEKIALLKMPEDL-LTRSVNVGFSGGEKKRNDIlQMAV 161
Cdd:PRK10418 89 ------------RSAFNPLHTMHthARETClalGKPADDATLTAALEAVGLENAArVLKLYPFEMSGGMLQRMMI-ALAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 162 L-EPELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGD 229
Cdd:PRK10418 156 LcEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLA-DDVAVMSHGRIVEQGD 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-85 |
3.43e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 3.43e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLALSPEDRAGEGIFMAFQ 85
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEELQASNIRDTERAGIAIIHQ 89
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-239 |
5.77e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 46.74 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 20 LSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYE-VTGGTVEFKGKDL------------LALSPEDRAGEGIfmafqy 86
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGA--YPgKFEGNVFINGKPVdirnpaqairagIAMVPEDRKRHGI------ 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 87 pVEIPGVSNQFflqtALNAVRSYRGQETLDRFDFQDLMEEKIALLKM----PEDLLTRsvnvgFSGGEKKRNDILQMAVL 162
Cdd:TIGR02633 351 -VPILGVGKNI----TLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVktasPFLPIGR-----LSGGNQQKAVLAKMLLT 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129638 163 EPELCILDESDSGLDIDALKVVADGVNSL-RDGKRSFIIVTHYQRILDYikPDYVHVLYQGRIvkSGDFTLVKQLEEQ 239
Cdd:TIGR02633 421 NPRVLILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGL--SDRVLVIGEGKL--KGDFVNHALTQEQ 494
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-209 |
6.84e-06 |
|
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: 46.47 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 13 DKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGReDYEVTGgtvefkgkdllalspEDRAGEGIFMAF--QYPVEI 90
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKDFNG---------------EARPQPGIKVGYlpQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 91 P----------GVSNQFFLQTALNAVRSYRGQETLdrfDFQDLMEEKIAL---------------LKMPEDLL-----TR 140
Cdd:TIGR03719 81 PtktvrenveeGVAEIKDALDRFNEISAKYAEPDA---DFDKLAAEQAELqeiidaadawdldsqLEIAMDALrcppwDA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129638 141 SVNVgFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDAlkvVADGVNSLRDGKRSFIIVTHYQRILD 209
Cdd:TIGR03719 158 DVTK-LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQEYPGTVVAVTHDRYFLD 222
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
19-211 |
7.15e-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: 46.70 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 19 GLSLDVHPGEVH-----AIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKdlLALSPedragegifmafQYPVEIPGV 93
Cdd:COG1245 353 GFSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVL--KPDEGEVDEDLK--ISYKP------------QYISPDYDG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 94 SNQFFLQTALNAV--RSYRGQETLDRFDFQDLMEEKIallkmpEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:COG1245 417 TVEEFLRSANTDDfgSSYYKTEIIKPLGLEKLLDKNV------KDL---------SGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16129638 172 SDSGLDIDALKVVADGVNSL-RDGKRSFIIVTHYQRILDYI 211
Cdd:COG1245 482 PSAHLDVEQRLAVAKAIRRFaENRGKTAMVVDHDIYLIDYI 522
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-192 |
7.36e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 45.88 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGK-------DLLALSPE 73
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGL--VAPDEGVIKRNGKlrigyvpQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 74 DRAGEGIFMAFQypveiPGVSNQFFLqtalnavrsyrgqETLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKR 153
Cdd:PRK09544 82 LPLTVNRFLRLR-----PGTKKEDIL-------------PALKRVQAGHLIDAPMQKL---------------SGGETQR 128
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16129638 154 NdILQMAVL-EPELCILDESDSGLDIDALKVVADGVNSLR 192
Cdd:PRK09544 129 V-LLARALLnRPQLLVLDEPTQGVDVNGQVALYDLIDQLR 167
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-231 |
9.00e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLALSP------------EDRAGEGIFMAF 84
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYG--ALPRTSGYVTLDGHEVVTRSPqdglangivyisEDRKRDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 85 QypveipgVSNQFFLqTALNAVRSYRGQetLDRFDFQDLMEEKIAL--LKMPedllTRSVNVGF-SGGEKKRNDILQMAV 161
Cdd:PRK10762 346 S-------VKENMSL-TALRYFSRAGGS--LKHADEQQAVSDFIRLfnIKTP----SMEQAIGLlSGGNQQKVAIARGLM 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129638 162 LEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTH--------YQRILdyikpdyvhVLYQGRIvkSGDFT 231
Cdd:PRK10762 412 TRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSempevlgmSDRIL---------VMHEGRI--SGEFT 478
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-74 |
1.35e-05 |
|
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: 44.79 E-value: 1.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129638 14 KAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPED 74
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRL--VELSSGSILIDGVDISKIGLHD 75
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-85 |
1.36e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 1.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRAGEGIFMAFQ 85
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGI--YQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-228 |
1.87e-05 |
|
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: 44.33 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 16 ILRGLSLDVHPGEVHAIMGPNGSGKSTLsaTLAGREDYEVTGGTVEFKGKDlLALSPEDRAGEGIFMAFQYPVEIPGvsn 95
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLEAEEGKIEIDGID-ISTIPLEDLRSSLTIIPQDPTLFSG--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 96 qfflqtalnAVRSyrgqeTLDRFDFQDlmEEKI-ALLKMPEDLLTrsvnvgFSGGEKKRNDILQMAVLEPELCILDESDS 174
Cdd:cd03369 97 ---------TIRS-----NLDPFDEYS--DEEIyGALRVSEGGLN------LSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16129638 175 GLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILDYikpDYVHVLYQGRIVKSG 228
Cdd:cd03369 155 SIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDY---DKILVMDAGEVKEYD 205
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-228 |
2.04e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 44.78 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 20 LSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRAgEGIFMAFQYPveipgvsnqffl 99
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGM--IEPTSGELLIDDHPLHFGDYSYRS-QRIRMIFQDP------------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 100 QTALNAvRSYRGQeTLD-------RFDFQDLMEEKIALLKMPeDLLTRSVNV---GFSGGEKKRNDILQMAVLEPELCIL 169
Cdd:PRK15112 97 STSLNP-RQRISQ-ILDfplrlntDLEPEQREKQIIETLRQV-GLLPDHASYyphMLAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 170 DESDSGLDIDALKVVADGVNSLRDGKR-SFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELQEKQGiSYIYVTQHLGMMKHIS-DQVLVMHQGEVVERG 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-177 |
2.58e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 44.19 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 21 SLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDRAgegIFMAFQypveipgvSNQFF-- 98
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGF--LTPASGSLTLNGQDHTTTPPSRRP---VSMLFQ--------ENNLFsh 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 99 LQTA------------LNAVRSYRGQETLDRFDFQDLMEekiallKMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPEL 166
Cdd:PRK10771 86 LTVAqniglglnpglkLNAAQREKLHAIARQMGIEDLLA------RLPGQL---------SGGQRQRVALARCLVREQPI 150
|
170
....*....|.
gi 16129638 167 CILDESDSGLD 177
Cdd:PRK10771 151 LLLDEPFSALD 161
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-222 |
3.09e-05 |
|
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: 44.54 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFkgKDLLALSPEDRAGEGIF 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQE--QPDSGTIEI--GETVKLAYVDQSRDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 82 MAFQYPVEIPGVSNQFFLQTALNAVRSYRGqetldRFDFQDLMEEKiallkmpedlltrsvNVG-FSGGEKKRndiLQMA 160
Cdd:TIGR03719 399 PNKTVWEEISGGLDIIKLGKREIPSRAYVG-----RFNFKGSDQQK---------------KVGqLSGGERNR---VHLA 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 161 VLEPE---LCILDESDSGLDIDALKvvadgvnSLRDGKRSF----IIVTHYQRILDYIKpdyVHVL-YQG 222
Cdd:TIGR03719 456 KTLKSggnVLLLDEPTNDLDVETLR-------ALEEALLNFagcaVVISHDRWFLDRIA---THILaFEG 515
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-177 |
4.53e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 43.60 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLALSPED--RAGE 78
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD--HGEILFDGENIPAMSRSRlyTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 79 GIFMAFQypveipgvSNQFFlqTALNavrsyrgqeTLDRFDFQdLMEEKiallKMPEDLLTRSV-----NVG-------- 145
Cdd:PRK11831 85 RMSMLFQ--------SGALF--TDMN---------VFDNVAYP-LREHT----QLPAPLLHSTVmmkleAVGlrgaaklm 140
|
170 180 190
....*....|....*....|....*....|....*
gi 16129638 146 ---FSGGEKKRNDILQMAVLEPELCILDESDSGLD 177
Cdd:PRK11831 141 pseLSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-216 |
4.59e-05 |
|
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: 43.55 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 19 GLSLDVHPG-----EVHAIMGPNGSGKSTLSATLAGR-----EDYEVTGGTVEFKGKDLLALSPedrageGIFMAFQYPV 88
Cdd:cd03237 12 EFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVlkpdeGDIEIELDTVSYKPQYIKADYE------GTVRDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 89 eIPGVSNQFFLQTalnavrsyrgqetldrfdfqdlmeEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCI 168
Cdd:cd03237 86 -TKDFYTHPYFKT------------------------EIAKPLQI-EQILDREVP-ELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16129638 169 LDESDSGLDIDALKVVADGVNSLRD-GKRSFIIVTHyqrilDYIKPDYV 216
Cdd:cd03237 139 LDEPSAYLDVEQRLMASKVIRRFAEnNEKTAFVVEH-----DIIMIDYL 182
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-43 |
1.04e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 42.77 E-value: 1.04e-04
10 20
....*....|....*....|....*..
gi 16129638 17 LRGLSLDVHPGEVHAIMGPNGSGKSTL 43
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTT 64
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-228 |
1.11e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.08 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 13 DKAILRGLSLDVHPGEVHAIMGPNGSGKSTLsATLAGREdYEVTGGTVEFKGKDLlalspEDragegifmafqYpvEIPG 92
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTI-ANLLTRF-YDIDEGEILLDGHDL-----RD-----------Y--TLAS 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 93 VSNQF---------FLQTALNAVrSYRGQETLDRFDFQDLMEEKIAL---LKMPEDLLTR--SVNVGFSGGEKKRNDILQ 158
Cdd:PRK11176 415 LRNQValvsqnvhlFNDTIANNI-AYARTEQYSREQIEEAARMAYAMdfiNKMDNGLDTVigENGVLLSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129638 159 mAVLE--PELcILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:PRK11176 494 -ALLRdsPIL-ILDEATSALDTESERAIQAALDELQKNRTSLVIA---HRLSTIEKADEILVVEDGEIVERG 560
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
144-209 |
1.17e-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: 41.58 E-value: 1.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 144 VGFSGGEKKRND---ILQMAVLEPE-LCILDESDSGLDIDALKVVADGVNSLRDGKRSFIIVTHYQRILD 209
Cdd:cd03227 76 LQLSGGEKELSAlalILALASLKPRpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAE 145
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-85 |
1.33e-04 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 41.97 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGtvefkgkDLLALS-PEDRAGEGI 80
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLE--TPSAG-------ELLAGTaPLAEAREDT 83
|
....*
gi 16129638 81 FMAFQ 85
Cdd:PRK11247 84 RLMFQ 88
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-180 |
1.50e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.35 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 18 RGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLALS------------PEDRAGEGIFM--- 82
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLR--PARGGRIMLNGKEINALStaqrlarglvylPEDRQSSGLYLdap 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 83 ----AFQYPVEIPGvsnqFFLQTAlnavrsyRGQETLDRFdfqdlmeekiallkmpedllTRSVNVGF----------SG 148
Cdd:PRK15439 358 lawnVCALTHNRRG----FWIKPA-------RENAVLERY--------------------RRALNIKFnhaeqaartlSG 406
|
170 180 190
....*....|....*....|....*....|....
gi 16129638 149 GEKKRndILQMAVLE--PELCILDESDSGLDIDA 180
Cdd:PRK15439 407 GNQQK--VLIAKCLEasPQLLIVDEPTRGVDVSA 438
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-239 |
1.50e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 1 MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGredyevtggtvefkgkDLLALSPEDRAGegi 80
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAG----------------ELPLLSGERQSQ--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 fmaFQYPVEIPG------VSNQFflQTALNAVRSYRGQET--------LDRFDFQDLMEEKIALLKMpEDLLTRSVNVgF 146
Cdd:PRK10938 64 ---FSHITRLSFeqlqklVSDEW--QRNNTDMLSPGEDDTgrttaeiiQDEVKDPARCEQLAQQFGI-TALLDRRFKY-L 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGKRSFI-IVTHYQRILDYIkpDYVHVLyqgriv 225
Cdd:PRK10938 137 STGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDFV--QFAGVL------ 208
|
250
....*....|....
gi 16129638 226 ksGDFTLVKQLEEQ 239
Cdd:PRK10938 209 --ADCTLAETGERE 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-228 |
1.60e-04 |
|
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: 41.90 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 14 KAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLALSP-EDRAGEGifmafqYPVEIPG 92
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI--NRLIEPTSGEIFIDGEDIREQDPvELRRKIG------YVIQQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 93 VSNQFFLQTALNAVRSYRGQEtldRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDES 172
Cdd:cd03295 86 LFPHMTVEENIALVPKLLKWP---KEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129638 173 DSGLD-IDALKVVADGVNSLRDGKRSFIIVTHyqRILDYIK-PDYVHVLYQGRIVKSG 228
Cdd:cd03295 163 FGALDpITRDQLQEEFKRLQQELGKTIVFVTH--DIDEAFRlADRIAIMKNGEIVQVG 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-61 |
1.71e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 1.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129638 5 KDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVE 61
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQE--QPDSGTIK 382
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
4-71 |
3.09e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.41 E-value: 3.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 4 IKDLHVSVEDKAI---LRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGredyeVT---GGTVEFKGK-DLLALS 71
Cdd:PRK13545 24 LKDLFFRSKDGEYhyaLNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAG-----VTmpnKGTVDIKGSaALIAIS 93
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-76 |
3.14e-04 |
|
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: 41.32 E-value: 3.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129638 20 LSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKdllALSPEDRA 76
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGL--YRPESGEILLDGQ---PVTADNRE 402
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
19-43 |
3.79e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.58 E-value: 3.79e-04
10 20
....*....|....*....|....*
gi 16129638 19 GLSLDVHPGEVHAIMGPNGSGKSTL 43
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTL 38
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-60 |
4.23e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 4.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 16129638 11 VEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTV 60
Cdd:PTZ00243 670 LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS--QFEISEGRV 717
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-181 |
4.29e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.09 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 4 IKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLA--------LSPE-- 73
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLG--QLQADSGRIHCGTKLEVAyfdqhraeLDPEkt 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 74 --DRAGEGifmafQYPVEIPGVSNQfflqtalnaVRSYrgqetldrfdFQD-LMEEKIALlkMPEDLLtrsvnvgfSGGE 150
Cdd:PRK11147 400 vmDNLAEG-----KQEVMVNGRPRH---------VLGY----------LQDfLFHPKRAM--TPVKAL--------SGGE 445
|
170 180 190
....*....|....*....|....*....|....
gi 16129638 151 KKRndiLQMA--VLEP-ELCILDESDSGLDIDAL 181
Cdd:PRK11147 446 RNR---LLLArlFLKPsNLLILDEPTNDLDVETL 476
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-248 |
4.70e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 13 DKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEF-KGKDLLALSPED----RAGEGifmAFQYP 87
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--ELAPVSGEIGLaKGIKLGYFAQHQleflRADES---PLQHL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 88 VEI-PGVSNQfflqtalnAVRSYRGQetldrFDFQ-DLMEEKIALlkmpedlltrsvnvgFSGGEKKRndiLQMAVL--- 162
Cdd:PRK10636 399 ARLaPQELEQ--------KLRDYLGG-----FGFQgDKVTEETRR---------------FSGGEKAR---LVLALIvwq 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 163 EPELCILDESDSGLDIDALKVVADgvnSLRDGKRSFIIVTHyQRILDYIKPDYVHVLYQGRI-VKSGDFTLVKQleeqgy 241
Cdd:PRK10636 448 RPNLLLLDEPTNHLDLDMRQALTE---ALIDFEGALVVVSH-DRHLLRSTTDDLYLVHDGKVePFDGDLEDYQQ------ 517
|
....*..
gi 16129638 242 gWLTEQQ 248
Cdd:PRK10636 518 -WLSDVQ 523
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
143-219 |
5.06e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 143 NVG-----FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRD-GKRSFIIVTHyqRILDYIKPDYV 216
Cdd:PTZ00265 1351 NVGpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkADKTIITIAH--RIASIKRSDKI 1428
|
...
gi 16129638 217 HVL 219
Cdd:PTZ00265 1429 VVF 1431
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
123-216 |
5.84e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.78 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 123 LMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVADGVNSLRDGK-RSFIIV 201
Cdd:PTZ00265 557 LIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEnRITIII 636
|
90
....*....|....*
gi 16129638 202 THYQRILDYIKPDYV 216
Cdd:PTZ00265 637 AHRLSTIRYANTIFV 651
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
12-228 |
6.72e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.49 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 12 EDKAIlRGLSLDVHPGEVHAIMGPNGSG--KSTLSATLAGREdyevtGGTVEFKGKDLLAlspeDRAGEGIFMAFQYPVE 89
Cdd:NF000106 25 EVKAV-DGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPD-----AGRRPWRF*TWCA----NRRALRRTIG*HRPVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 90 ------IPGVSNQFFLQTALNAVRS---YRGQETLDRFDFQDLMEEKIAllkmpedlltrsvnvGFSGGEKKRNDILQMA 160
Cdd:NF000106 95 *grresFSGRENLYMIGR*LDLSRKdarARADELLERFSLTEAAGRAAA---------------KYSGGMRRRLDLAASM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129638 161 VLEPELCILDESDSGLDIDALKVVADGVNSL-RDGKrSFIIVTHYQRILDYIKPDyVHVLYQGRIVKSG 228
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGA-TVLLTTQYMEEAEQLAHE-LTVIDRGRVIADG 226
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-171 |
6.79e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 40.34 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 2 LSIKDLHVSVEDKAILRG-LSLDVHPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLALSPEDragegi 80
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEILLDGKPVTAEQPED------ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 81 fmafqYPVEIPGVSNQFFLQTAL-----NAVRSYRGQETLDRFDfqdlMEEKIALlkmpEDLltRSVNVGFSGGEKKRND 155
Cdd:PRK10522 395 -----YRKLFSAVFTDFHLFDQLlgpegKPANPALVEKWLERLK----MAHKLEL----EDG--RISNLKLSKGQKKRLA 459
|
170
....*....|....*..
gi 16129638 156 ILqMAVLEP-ELCILDE 171
Cdd:PRK10522 460 LL-LALAEErDILLLDE 475
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-67 |
8.90e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.53 E-value: 8.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 16129638 16 ILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDL 67
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFM--RMVEVCGGEIRVNGREI 1374
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-239 |
1.23e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.84 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 4 IKDLH-----VSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGR------EDYEVTGGTVEFKGKDLLAL-- 70
Cdd:PLN03073 175 IKDIHmenfsISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHaidgipKNCQILHVEQEVVGDDTTALqc 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 71 ---SPEDRAG----EGIFMAFQYPVEIPGVSNQFflQTALNA-----VRSYRGQETLDRFDFQDLMEEK------IALLK 132
Cdd:PLN03073 255 vlnTDIERTQlleeEAQLVAQQRELEFETETGKG--KGANKDgvdkdAVSQRLEEIYKRLELIDAYTAEaraasiLAGLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 133 MPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKVVAdgvNSLRDGKRSFIIVTHYQRILDYIK 212
Cdd:PLN03073 333 FTPEMQVKATKT-FSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLE---TYLLKWPKTFIVVSHAREFLNTVV 408
|
250 260
....*....|....*....|....*...
gi 16129638 213 PDYVHVLYQGRIVKSGDF-TLVKQLEEQ 239
Cdd:PLN03073 409 TDILHLHGQKLVTYKGDYdTFERTREEQ 436
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-209 |
1.55e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.33 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 13 DKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDyevtggtvEFKGkdllalspEDRAGEGIFMAF--QYP--- 87
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK--------EFEG--------EARPAPGIKVGYlpQEPqld 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 88 --------VEiPGVSNQFFLQTALNAVRSYRGQETLdrfDFQDLMEEKIAL---------------LKMPEDLLtR---- 140
Cdd:PRK11819 83 pektvrenVE-EGVAEVKAALDRFNEIYAAYAEPDA---DFDALAAEQGELqeiidaadawdldsqLEIAMDAL-Rcppw 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129638 141 --SVNVgFSGGEKKRNDILQMAVLEPELCILDESDSGLDidalkvvADGV----NSLRDGKRSFIIVTHYQRILD 209
Cdd:PRK11819 158 daKVTK-LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD-------AESVawleQFLHDYPGTVVAVTHDRYFLD 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-81 |
2.66e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 38.74 E-value: 2.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129638 21 SLDVHPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDL------------LALSPEDRAGEGIF 81
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGAT--RRTAGQVYLDGKPIdirsprdairagIMLCPEDRKAEGII 343
|
|
| PRK06547 |
PRK06547 |
hypothetical protein; Provisional |
32-55 |
6.75e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235825 Cd Length: 172 Bit Score: 36.26 E-value: 6.75e-03
10 20
....*....|....*....|....
gi 16129638 32 IMGPNGSGKSTLSATLAGREDYEV 55
Cdd:PRK06547 20 IDGRSGSGKTTLAGALAARTGFQL 43
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-180 |
6.88e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 37.22 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 21 SLDVHPGEVHAIMGPNGSGKSTLSATLAG--REDYEvtgGTVEFKGKDL------------LALSPEDRAGEGIfmafqy 86
Cdd:PRK13549 282 SFSLRRGEILGIAGLVGAGRTELVQCLFGayPGRWE---GEIFIDGKPVkirnpqqaiaqgIAMVPEDRKRDGI------ 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129638 87 pVEIPGVSNQFflqtALNAVRSYRGQETLDRFDFQDLMEEKIALLKM----PEDLLTRsvnvgFSGGEKKRNDILQMAVL 162
Cdd:PRK13549 353 -VPVMGVGKNI----TLAALDRFTGGSRIDDAAELKTILESIQRLKVktasPELAIAR-----LSGGNQQKAVLAKCLLL 422
|
170
....*....|....*...
gi 16129638 163 EPELCILDESDSGLDIDA 180
Cdd:PRK13549 423 NPKILILDEPTRGIDVGA 440
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
110-177 |
8.93e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 37.03 E-value: 8.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129638 110 RGQETLDRFDFQDLMEEkiallkMPEDL-LtrsvnvgfsgGEKKRndiLQMAVL---EPELCILDESDSGLD 177
Cdd:NF033858 377 RVAEMLERFDLADVADA------LPDSLpL----------GIRQR---LSLAVAvihKPELLILDEPTSGVD 429
|
|
| |
