|
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: 509.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVVGGSVEFKGKDLLELSPEDRAGEGI 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMA 160
Cdd:PRK09580 81 FMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 161 VLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQG 240
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQG 240
|
....*...
gi 157083167 241 YGWLTEQQ 248
Cdd:PRK09580 241 YGWLTEQQ 248
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-247 |
1.42e-161 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 446.82 E-value: 1.42e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVVGGSVEFKGKDLLELSPEDRAGEGIF 81
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGEDILELSPDERARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 82 MAFQYPVEIPGVSNQFFLQTALNAVRsyrgQESLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAV 161
Cdd:COG0396 81 LAFQYPVEIPGVSVSNFLRTALNARR----GEELSAREFLKLLKEKMKELGLDEDFLDRYVNEGFSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 162 LEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQGY 241
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIKPDFVHVLVDGRIVKSGGKELALELEEEGY 236
|
....*.
gi 157083167 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 |
1.23e-156 |
|
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: 434.38 E-value: 1.23e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVVGGSVEFKGKDLLELSPEDRAGEGIF 81
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVTSGTILFKGQDLLELEPDERARAGLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 82 MAFQYPVEIPGVSNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAV 161
Cdd:TIGR01978 81 LAFQYPEEIPGVSNLEFLRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEGFSGGEKKRNEILQMAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 162 LEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQGY 241
Cdd:TIGR01978 161 LEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKPDYVHVLLDGRIVKSGDVELAKELEAKGY 240
|
...
gi 157083167 242 GWL 244
Cdd:TIGR01978 241 DWV 243
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-246 |
1.33e-131 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 371.67 E-value: 1.33e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVVGGSVEFKGKDLLELSPEDRAGEGI 80
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMA 160
Cdd:CHL00131 87 FLAFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEGFSGGEKKRNEILQMA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 161 VLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQG 240
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHVMQNGKIIKTGDAELAKELEKKG 246
|
....*.
gi 157083167 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 |
7.63e-118 |
|
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: 334.50 E-value: 7.63e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVVGGSVEFKGKDLLELSPEDRAGEGIF 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 82 MAFQYPVEIPGVSNQFFLqtalnavrsyrgqesldrfdfqdlmeekiallkmpedlltRSVNVGFSGGEKKRNDILQMAV 161
Cdd:cd03217 81 LAFQYPPEIPGVKNADFL----------------------------------------RYVNEGFSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 162 LEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQGY 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 |
3.02e-32 |
|
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: 117.18 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 3 SIKDLQVSVED--KAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRAGEgI 80
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL--GPTSGEVLVDGKDLTKLSLKELRRK-V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQYPveipgvSNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMA 160
Cdd:cd03225 78 GLVFQNP------DDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGL-EGLRDRSPFT-LSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157083167 161 VLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYqriLDYIKP--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 |
2.51e-30 |
|
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: 112.60 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKA----ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRA 76
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL--KPTSGSIIFDGKDLLKLSRRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 77 --GEGIFMAFQYPveipgvsnqfflQTALNAVRSYRGQ--ESL---DRFDFQDLMEEKIALLKM----PEDLLTRSVNvG 145
Cdd:cd03257 79 irRKEIQMVFQDP------------MSSLNPRMTIGEQiaEPLrihGKLSKKEARKEAVLLLLVgvglPEEVLNRYPH-E 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 146 FSGGEKKRNDIlQMA-VLEPELCILDESDSGLDIDalkIVAEGVNSLRDGKR----SFIIVTHYQRILDYIKpDYVHVLY 220
Cdd:cd03257 146 LSGGQRQRVAI-ARAlALNPKLLIADEPTSALDVS---VQAQILDLLKKLQEelglTLLFITHDLGVVAKIA-DRVAVMY 220
|
....*...
gi 157083167 221 QGRIVKSG 228
Cdd:cd03257 221 AGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
5.32e-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: 116.93 E-value: 5.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSV--EDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEV-VGGSVEFKGKDLLELSPEDRAG 77
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 78 EgIFMAFQYPveipgvSNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDIL 157
Cdd:COG1123 84 R-IGMVFQDP------MTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGL-ERRLDRYPHQ-LSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157083167 158 QMAVLEPELCILDESDSGLDIDALKIVAEGVNSL-RDGKRSFIIVTHYQRILDYIkPDYVHVLYQGRIVKSGD 229
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEI-ADRVVVMDDGRIVEDGP 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-223 |
9.69e-30 |
|
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: 108.87 E-value: 9.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 3 SIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPEdRAGEGIFM 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGL--LKPTSGEILIDGKDIAKLPLE-ELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 83 AFQypveipgvsnqfflqtalnavrsyrgqesldrfdfqdlmeekiallkmpedlltrsvnvgFSGGEKKRNDILQMAVL 162
Cdd:cd00267 78 VPQ------------------------------------------------------------LSGGQRQRVALARALLL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157083167 163 EPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDYIkPDYVHVLYQGR 223
Cdd:cd00267 98 NPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELA-ADRVIVLKDGK 157
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-238 |
2.78e-29 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 109.73 E-value: 2.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVED-KAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAG--REDyevvGGSVEFKGKDLLELSPED---R 75
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGllKPT----SGEVLVDGKDITKKNLRElrrK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 76 AGegifMAFQYPveipgvSNQFFLQTAL--------------NAVRSyRGQESLDRFDFQDLMEEKIALLkmpedlltrs 141
Cdd:COG1122 77 VG----LVFQNP------DDQLFAPTVEedvafgpenlglprEEIRE-RVEEALELVGLEHLADRPPHEL---------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 142 vnvgfSGGEKKRndiLQMA---VLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYqriLDYIKP--DYV 216
Cdd:COG1122 136 -----SGGQKQR---VAIAgvlAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHD---LDLVAElaDRV 204
|
250 260
....*....|....*....|....*.
gi 157083167 217 HVLYQGRIVKSGD----FTLVKQLEE 238
Cdd:COG1122 205 IVLDDGRIVADGTprevFSDYELLEE 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-228 |
3.26e-28 |
|
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: 107.20 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAG--REDyevvGGSVEFKGKDLLELSPED--RAG 77
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGllRPD----SGEVLIDGEDISGLSEAElyRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 78 EGIFMAFQypveipgvSNQFFlqTALNA-------VRSYRgqeSLDRFDFQDLMEEKIALL-------KMPEDLltrsvn 143
Cdd:cd03261 77 RRMGMLFQ--------SGALF--DSLTVfenvafpLREHT---RLSEEEIREIVLEKLEAVglrgaedLYPAEL------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 144 vgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKR-SFIIVTHYQRILDYIkPDYVHVLYQG 222
Cdd:cd03261 138 ---SGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGlTSIMVTHDLDTAFAI-ADRIAVLYDG 213
|
....*.
gi 157083167 223 RIVKSG 228
Cdd:cd03261 214 KIVAEG 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
17-229 |
7.14e-28 |
|
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: 106.37 E-value: 7.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPEDRAGEGIFMAFQYPVEIPG---- 92
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF--LRPTSGSVLFDGEDITGLPPHEIARLGIGRTFQIPRLFPEltvl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 93 ----VSNQFFLQTALNAVRSYRGQ--------ESLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRndiLQMA 160
Cdd:cd03219 94 envmVAAQARTGSGLLLARARREEreareraeELLERVGLADLADRPAGEL---------------SYGQQRR---LEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157083167 161 ---VLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHyqrILDYIKP--DYVHVLYQGRIVKSGD 229
Cdd:cd03219 156 ralATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEH---DMDVVMSlaDRVTVLDQGRVIAEGT 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-228 |
1.36e-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: 105.71 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVvgGSVEFKGKDLLELSPEDRAGEGI 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS--GSILIDGEDVRKEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FmafqyPVEIPGVSNqfflQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMA 160
Cdd:COG4555 79 L-----PDERGLYDR----LTVRENIRYFAELYGLFDEELKKRIEELIELLGL-EEFLDRRVG-ELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 161 VLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHyqrILDYIKP--DYVHVLYQGRIVKSG 228
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSH---IMQEVEAlcDRVVILHKGKVVAQG 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-203 |
1.69e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 104.51 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYevVGGSVEFKGKDLLELSPED-RAgeGI 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPP--TSGEIYLDGKPLSAMPPPEwRR--QV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQYPVEIPGVsnqffLQTALNAVRSYRgQESLDRFDFQDLMEEkialLKMPEDLLTRSVNvGFSGGEKKRNDILQMA 160
Cdd:COG4619 77 AYVPQEPALWGGT-----VRDNLPFPFQLR-ERKFDRERALELLER----LGLPPDILDKPVE-RLSGGERQRLALIRAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 157083167 161 VLEPELCILDESDSGLDIDALKIVAEGVNSLRDGK-RSFIIVTH 203
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgRAVLWVSH 189
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-229 |
3.29e-27 |
|
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: 105.13 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKDLLELSPEDRAGEgi 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG--LLKPSSGEVLLDGRDLASLSRRELARR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 fMAF--QYPVEIPGVsnqfflqTALNAVRSYR--GQESLDRFDFQD--LMEEKIALLKMpEDLLTRSVNvGFSGGEKkrn 154
Cdd:COG1120 77 -IAYvpQEPPAPFGL-------TVRELVALGRypHLGLFGRPSAEDreAVEEALERTGL-EHLADRPVD-ELSGGER--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 155 dilQMAVL------EPELCILDESDSGLDI----DALKIVAEGVnslRDGKRSFIIVTHYqriLD----YIkpDYVHVLY 220
Cdd:COG1120 144 ---QRVLIaralaqEPPLLLLDEPTSHLDLahqlEVLELLRRLA---RERGRTVVMVLHD---LNlaarYA--DRLVLLK 212
|
....*....
gi 157083167 221 QGRIVKSGD 229
Cdd:COG1120 213 DGRIVAQGP 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-230 |
4.39e-26 |
|
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: 101.59 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAG--REDyevvGGSVEFKGKDLLELSPEDRAG- 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGllRPD----SGEILVDGQDITGLSEKELYEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 78 -EGIFMAFQY-------PVEipgvSN-QFFLqtalnavrsyRGQESLDRFDFQDLMEEKIALL-------KMPEDLltrs 141
Cdd:COG1127 81 rRRIGMLFQGgalfdslTVF----ENvAFPL----------REHTDLSEAEIRELVLEKLELVglpgaadKMPSEL---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 142 vnvgfSGGEKKRndilqmA------VLEPELCILDESDSGLDIDALKIVAEGVNSLRDG-KRSFIIVTHyqrILDYIK-- 212
Cdd:COG1127 143 -----SGGMRKR------ValaralALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTH---DLDSAFai 208
|
250
....*....|....*...
gi 157083167 213 PDYVHVLYQGRIVKSGDF 230
Cdd:COG1127 209 ADRVAVLADGKIIAEGTP 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
4.82e-26 |
|
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: 105.76 E-value: 4.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVS-----VEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDR 75
Cdd:COG1123 260 LLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLL--RPTSGSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 76 A--GEGIFMAFQYPveipgvsnqfflQTALNAVRS--------YRGQESLDRFDFQDLMEEKIALLKMPEDLLTRSVNvG 145
Cdd:COG1123 338 RelRRRVQMVFQDP------------YSSLNPRMTvgdiiaepLRLHGLLSRAERRERVAELLERVGLPPDLADRYPH-E 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLDidaLKIVAEGVNSLRDGKR----SFIIVTHYQRILDYIKpDYVHVLYQ 221
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALD---VSVQAQILNLLRDLQRelglTYLFISHDLAVVRYIA-DRVAVMYD 480
|
....*...
gi 157083167 222 GRIVKSGD 229
Cdd:COG1123 481 GRIVEDGP 488
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-229 |
8.25e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 100.91 E-value: 8.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAG--REDyevvGGSVEFKGKDLLELSPEDRAgeG 79
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGllRPT----SGEVRVLGEDVARDPAEVRR--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 80 IFMAFQYPVEIPGVSnqffLQTALNAVRSYRGqesLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQM 159
Cdd:COG1131 75 IGYVPQEPALYPDLT----VRENLRFFARLYG---LPRKEARERIDELLELFGL-TDAADRKVG-TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157083167 160 AVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHY----QRILdyikpDYVHVLYQGRIVKSGD 229
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYleeaERLC-----DRVAIIDKGRIVADGT 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-229 |
1.11e-25 |
|
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: 100.33 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRED---YEVVGGSVEFKGKDLLELSP---EDR 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipGAPDEGEVLLDGKDIYDLDVdvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 76 AGEGifMAFQYPVEIPGvsnqfflqTALNAVRsY--RGQESLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKR 153
Cdd:cd03260 81 RRVG--MVFQKPNPFPG--------SIYDNVA-YglRLHGIKLKEELDERVEEALRKAALWDEVKDRLHALGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 154 NDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDgKRSFIIVTH----YQRIldyikPDYVHVLYQGRIVKSGD 229
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHnmqqAARV-----ADRTAFLLNGRLVEFGP 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-229 |
1.48e-24 |
|
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: 99.36 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVS--VEDKAI--LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAG-REDYEVVGGSVEFKGKDLLELSPEDR 75
Cdd:COG0444 1 LLEVRNLKVYfpTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGlLPPPGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 76 A---GEGIFMAFQYPveipgvsnqfflQTALNAVRSYRGQ--ESL---DRFDFQDLMEEKIALLKM-----PEDLLTRsv 142
Cdd:COG0444 81 RkirGREIQMIFQDP------------MTSLNPVMTVGDQiaEPLrihGGLSKAEARERAIELLERvglpdPERRLDRyp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 143 nvgFSGGEKKRNDILqMA-VLEPELCILDESDSGLDIDalkIVAEGVNSLRDGKR----SFIIVTHyqrilD-----YIK 212
Cdd:COG0444 149 -heLSGGMRQRVMIA-RAlALEPKLLIADEPTTALDVT---IQAQILNLLKDLQRelglAILFITH-----DlgvvaEIA 218
|
250
....*....|....*..
gi 157083167 213 pDYVHVLYQGRIVKSGD 229
Cdd:COG0444 219 -DRVAVMYAGRIVEEGP 234
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-225 |
3.48e-24 |
|
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: 96.80 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVS----VEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAG--REDyevvGGSVEFKGKDLLELSPED 74
Cdd:COG1124 1 MLEVRNLSVSygqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGleRPW----SGEVTFDGRPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 75 RAGEgIFMAFQYPveipgvsnqfflQTALNAVRSYRGQ--ESLDRFDFQDLMEEKIALLK---MPEDLLTRSVNvGFSGG 149
Cdd:COG1124 77 FRRR-VQMVFQDP------------YASLHPRHTVDRIlaEPLRIHGLPDREERIAELLEqvgLPPSFLDRYPH-QLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 150 EKKRNDILQMAVLEPELCILDESDSGLDIdalkIV-AEGVNSLRDGKR----SFIIVTHYQRILDYIkPDYVHVLYQGRI 224
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDV----SVqAEILNLLKDLREerglTYLFVSHDLAVVAHL-CDRVAVMQNGRI 217
|
.
gi 157083167 225 V 225
Cdd:COG1124 218 V 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-203 |
4.28e-23 |
|
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: 92.93 E-value: 4.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLElsPEDRAGEGI 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLL--PPSAGEVLWNGEPIRD--AREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQYpveiPGVSNQFFLQTALNAVRSYRG--------QESLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKK 152
Cdd:COG4133 78 AYLGHA----DGLKPELTVRENLRFWAALYGlradreaiDEALEAVGLAGLADLPVRQL---------------SAGQKR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 157083167 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH 203
Cdd:COG4133 139 RVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-171 |
8.42e-23 |
|
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: 90.78 E-value: 8.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLLELSPEDRAGEgIFMAFQYPVEIPGVsnq 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT--EGTILLDGQDLTDDERKSLRKE-IGYVFQDPQLFPRL--- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157083167 97 fflqTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:pfam00005 75 ----TVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPgtLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-228 |
9.70e-23 |
|
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: 92.20 E-value: 9.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRageGIF 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLE--RPDSGEILIDGRDVTGVPPERR---NIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 82 MAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEsldrfdfQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAV 161
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLRGVPKAEI-------RARVRELLELVGL-EGLLNRYPH-ELSGGQQQRVALARALA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157083167 162 LEPELCILDESDSGLDID-ALKIVAEGVNSLRDGKRSFIIVTHYQ----RILDYIKpdyvhVLYQGRIVKSG 228
Cdd:cd03259 147 REPSLLLLDEPLSALDAKlREELREELKELQRELGITTIYVTHDQeealALADRIA-----VMNEGRIVQVG 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-228 |
1.32e-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: 92.84 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLsATLAGREDYEVVGGSVEFKGKDLLELSPED-RAGEG 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTL-LSLITGDLPPTYGNDVRLFGERRGGEDVWElRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 80 IF---MAFQYPVEIpgvsnqfflqTALNAVRS-YRGqeSLDRFD-FQDLMEEK----IALLKMpEDLLTRSVNvGFSGGE 150
Cdd:COG1119 82 LVspaLQLRFPRDE----------TVLDVVLSgFFD--SIGLYRePTDEQRERarelLELLGL-AHLADRPFG-TLSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 151 KKRndiLQMA---VLEPELCILDESDSGLDIDALKIVAEGVNSL-RDGKRSFIIVTHYqriLDYIKPDYVHVLY--QGRI 224
Cdd:COG1119 148 QRR---VLIAralVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHH---VEEIPPGITHVLLlkDGRV 221
|
....
gi 157083167 225 VKSG 228
Cdd:COG1119 222 VAAG 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-228 |
2.88e-22 |
|
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: 90.19 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 3 SIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPEDRAGEgifM 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGL--LKPSSGEILLDGKDLASLSPKELARK---I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 83 AfqypveipgvsnqfFLQTALNAVrsyrgqesldrfdfqDLmeekiallkmpEDLLTRSVNVgFSGGEKKRNDILQMAVL 162
Cdd:cd03214 76 A--------------YVPQALELL---------------GL-----------AHLADRPFNE-LSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157083167 163 EPELCILDESDSGLDI----DALKIVAEGVnslRDGKRSFIIVTHYqriLD--YIKPDYVHVLYQGRIVKSG 228
Cdd:cd03214 115 EPPILLLDEPTSHLDIahqiELLELLRRLA---RERGKTVVMVLHD---LNlaARYADRVILLKDGRIVAQG 180
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-224 |
5.62e-22 |
|
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: 88.99 E-value: 5.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPEDRagEGIF 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGL--LKPDSGEIKVLGKDIKKEPEEVK--RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 82 MAFQYPVEIPGVSnqfflqtalnavrsyrGQESLDrfdfqdlmeekiallkmpedlltrsvnvgFSGGEKKRNDILQMAV 161
Cdd:cd03230 77 YLPEEPSLYENLT----------------VRENLK-----------------------------LSGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157083167 162 LEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRI 224
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLC-DRVAILNNGRI 173
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-178 |
8.54e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 90.56 E-value: 8.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKDLLELSPEDRAGE-G 79
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG--ELTPSSGEVRLNGRPLAAWSPWELARRrA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 80 IF-----MAFQYPVE-------IPGvsnqfflqtalnavrsyrgqeSLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFS 147
Cdd:COG4559 79 VLpqhssLAFPFTVEevvalgrAPH---------------------GSSAAQDRQIVREALALVGL-AHLAGRSYQ-TLS 135
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 157083167 148 GGEKKRndiLQMA-VL---------EPELCILDESDSGLDI 178
Cdd:COG4559 136 GGEQQR---VQLArVLaqlwepvdgGPRWLFLDEPTSALDL 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-203 |
9.39e-22 |
|
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: 89.24 E-value: 9.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 3 SIKDLQVSVEDKA-ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDlleLSPEDRAgEGIF 81
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGL--IKESSGSILLNGKP---IKAKERR-KSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 82 MAFQypveipGVSNQFFLQTALNAVR-----SYRGQES----LDRFDFQDLMEekiallKMPEDLltrsvnvgfSGGEKK 152
Cdd:cd03226 75 YVMQ------DVDYQLFTDSVREELLlglkeLDAGNEQaetvLKDLDLYALKE------RHPLSL---------SGGQKQ 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 157083167 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH 203
Cdd:cd03226 134 RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-229 |
1.65e-21 |
|
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: 89.03 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVVGGSVEFKGKDLLELSPEDRAGEGIF 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP--PRSGSIRFDGRDITGLPPHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 82 MAFQypveipgvSNQFF--------LQTALNAVRSYRGQESLDR-FD-FQDLMEEkiallkmpedlltRSVNVG-FSGGE 150
Cdd:cd03224 79 YVPE--------GRRIFpeltveenLLLGAYARRRAKRKARLERvYElFPRLKER-------------RKQLAGtLSGGE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 151 KKrndILQMA---VLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHY-QRILDYIkpDYVHVLYQGRIVK 226
Cdd:cd03224 138 QQ---MLAIAralMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNaRFALEIA--DRAYVLERGRVVL 212
|
...
gi 157083167 227 SGD 229
Cdd:cd03224 213 EGT 215
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-229 |
2.91e-21 |
|
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: 88.89 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKDLLELSPEDRAGEGI 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISG--LLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMA------FqypveiPGVS---NqffLQTALNAVRSYRG-QESLDR-FD-FQDLMEekiaLLKMPEDLLtrsvnvgfSG 148
Cdd:COG0410 81 GYVpegrriF------PSLTveeN---LLLGAYARRDRAEvRADLERvYElFPRLKE----RRRQRAGTL--------SG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 149 GEKkrndilQM-A-----VLEPELCILDESDSGLdidALKIVAE---GVNSLRDGKRSFIIVTHY-QRILDYIkpDYVHV 218
Cdd:COG0410 140 GEQ------QMlAigralMSRPKLLLLDEPSLGL---APLIVEEifeIIRRLNREGVTILLVEQNaRFALEIA--DRAYV 208
|
250
....*....|.
gi 157083167 219 LYQGRIVKSGD 229
Cdd:COG0410 209 LERGRIVLEGT 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-229 |
3.08e-21 |
|
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: 88.94 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVS---VedKAiLRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPEDRAG 77
Cdd:COG0411 4 LLEVRGLTKRfggL--VA-VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF--YRPTSGRILFDGRDITGLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 78 EGIFMAFQYPVEIPGVS-------------NQFFLQTALNAVRSYRG--------QESLDRFDFQDLMEEKIALLkmped 136
Cdd:COG0411 79 LGIARTFQNPRLFPELTvlenvlvaaharlGRGLLAALLRLPRARREereareraEELLERVGLADRADEPAGNL----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 137 lltrsvnvgfSGGEKKRndiLQMA---VLEPELCILDESDSGL---DIDALkivAEGVNSLRDG-KRSFIIVTHyqrILD 209
Cdd:COG0411 154 ----------SYGQQRR---LEIAralATEPKLLLLDEPAAGLnpeETEEL---AELIRRLRDErGITILLIEH---DMD 214
|
250 260
....*....|....*....|..
gi 157083167 210 YIKP--DYVHVLYQGRIVKSGD 229
Cdd:COG0411 215 LVMGlaDRIVVLDFGRVIAEGT 236
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-224 |
3.63e-20 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 85.62 E-value: 3.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSV----EDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVVGGSVEFKGKDLLELSPEDRA- 76
Cdd:cd03255 1 IELKNLSKTYggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR--PTSGEVRVDGTDISKLSEKELAa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 77 --GEGIFMAFQYP-----------VEIPgvsnqFFLQTALNAVRSYRGQESLDRFDFQDLMEekiallKMPEDLltrsvn 143
Cdd:cd03255 79 frRRHIGFVFQSFnllpdltalenVELP-----LLLAGVPKKERRERAEELLERVGLGDRLN------HYPSEL------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 144 vgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSL-RDGKRSFIIVTHYQRILDYIkpDYVHVLYQG 222
Cdd:cd03255 142 ---SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELAEYA--DRIIELRDG 216
|
..
gi 157083167 223 RI 224
Cdd:cd03255 217 KI 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-229 |
4.27e-20 |
|
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: 88.67 E-value: 4.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVS--VEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKDLLELSPEDRAgeg 79
Cdd:COG4987 334 LELEDVSFRypGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR--FLDPQSGSITLGGVDLRDLDEDDLR--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 80 ifmafqypvEIPGVSNQ---FFLQTALNAVRSYRGQ-------ESLDRFDFQDLMEEkiallkMPEDLLTRsvnVG---- 145
Cdd:COG4987 409 ---------RRIAVVPQrphLFDTTLRENLRLARPDatdeelwAALERVGLGDWLAA------LPDGLDTW---LGeggr 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 146 -FSGGEKKRndiLQMA-VL--EPELCILDESDSGLDIDALKIVAEGVNSLRDGkRSFIIVTHYQRILDYIkpDYVHVLYQ 221
Cdd:COG4987 471 rLSGGERRR---LALArALlrDAPILLLDEPTEGLDAATEQALLADLLEALAG-RTVLLITHRLAGLERM--DRILVLED 544
|
....*...
gi 157083167 222 GRIVKSGD 229
Cdd:COG4987 545 GRIVEQGT 552
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-229 |
4.44e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 85.91 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKDLlelspeDRAGEGI 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILG--LLPPTSGTVRLFGKPP------RRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 -----FMAF--QYPVeipgvsnqfflqTALNAVRSYR-GQESLDRF---DFQDLMEEKIALLKMpEDLLTRSVNvGFSGG 149
Cdd:COG1121 78 gyvpqRAEVdwDFPI------------TVRDVVLMGRyGRRGLFRRpsrADREAVDEALERVGL-EDLADRPIG-ELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH-YQRILDYIKpdyvHVLY-QGRIVKS 227
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHdLGAVREYFD----RVLLlNRGLVAH 219
|
..
gi 157083167 228 GD 229
Cdd:COG1121 220 GP 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-203 |
8.57e-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: 8.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEV-VGGSVEFKGKDLLELSPEDRageG 79
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsASGEVLLNGRRLTALPAEQR---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 80 IFMAFQYPVEIPGVS---N-QFFLQTALN-AVRSYRGQESLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRN 154
Cdd:COG4136 78 IGILFQDDLLFPHLSvgeNlAFALPPTIGrAQRRARVEQALEEAGLAGFADRDPATL---------------SGGQRARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157083167 155 DILQMAVLEPELCILDESDSGLDIDalkivaegvnsLRDGKRSF------------IIVTH 203
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAA-----------LRAQFREFvfeqirqrgipaLLVTH 192
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-223 |
4.89e-19 |
|
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: 81.28 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 12 EDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKDLLELSPEdragegifmafqypveip 91
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR--LYDPTSGEILIDGVDLRDLDLE------------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 92 gvsnqfflqtalnavrSYRgqesldrfdfqdlmeEKIALLkmPED--LLTRSV--NVgFSGGEKKRNDILQMAVLEPELC 167
Cdd:cd03228 73 ----------------SLR---------------KNIAYV--PQDpfLFSGTIreNI-LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 157083167 168 ILDESDSGLDIDALKIVAEGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGR 223
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKG-KTVIVIAH--RLSTIRDADRIIVLDDGR 171
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-228 |
9.97e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.51 E-value: 9.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKDLLELSPEDRAG--- 77
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG--ELSPDSGEVRLNGRPLADWSPAELARrra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 78 ---EGIFMAFQYPVE-------IPGVSNQFFLQTALNAVrsyrgqesLDRFDFQDLMEEKIALLkmpedlltrsvnvgfS 147
Cdd:PRK13548 80 vlpQHSSLSFPFTVEevvamgrAPHGLSRAEDDALVAAA--------LAQVDLAHLAGRDYPQL---------------S 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 148 GGEKKRndiLQMA-VL--------EPELCILDESDSGLDI----DALKIVAEGVnslRDGKRSFIIVTH-------YQri 207
Cdd:PRK13548 137 GGEQQR---VQLArVLaqlwepdgPPRWLLLDEPTSALDLahqhHVLRLARQLA---HERGLAVIVVLHdlnlaarYA-- 208
|
250 260
....*....|....*....|.
gi 157083167 208 ldyikpDYVHVLYQGRIVKSG 228
Cdd:PRK13548 209 ------DRIVLLHQGRLVADG 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-248 |
1.95e-18 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 84.12 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 12 EDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKDLLELSPEDRAgEGIFMAFQypveip 91
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG--LYEPTSGRILIDGIDLRQIDPASLR-RQIGVVLQ------ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 92 gvSNQFFLQTALNAVRSYRgqeslDRFDFQDLME--------EKIAllKMPEDLLTRsvnVG-----FSGGEKKRndiLQ 158
Cdd:COG2274 557 --DVFLFSGTIRENITLGD-----PDATDEEIIEaarlaglhDFIE--ALPMGYDTV---VGeggsnLSGGQRQR---LA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 159 MA---VLEPELCILDESDSGLDIDALKIVAEGVNSLRDGkRSFIIVTHYQRILDYIkpDYVHVLYQGRIVKSGDFtlvKQ 235
Cdd:COG2274 622 IAralLRNPRILILDEATSALDAETEAIILENLRRLLKG-RTVIIIAHRLSTIRLA--DRIIVLDKGRIVEDGTH---EE 695
|
250
....*....|....*
gi 157083167 236 LEEQG--YGWLTEQQ 248
Cdd:COG2274 696 LLARKglYAELVQQQ 710
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-228 |
2.29e-18 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 80.49 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKA----ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAG--REDyevvGGSVEFKGKDLLELSPED 74
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGllEPD----AGFATVDGFDVVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 75 RAGEGIFmafqypveiPGVSNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRN 154
Cdd:cd03266 77 RRRLGFV---------SDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGM-EELLDRRVG-GFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157083167 155 DILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHyqrILDYIKP--DYVHVLYQGRIVKSG 228
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTH---IMQEVERlcDRVVVLHRGRVVYEG 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-231 |
2.54e-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: 83.65 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVS-VEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPEDRAgEGI 80
Cdd:COG4988 337 IELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF--LPPYSGSILINGVDLSDLDPASWR-RQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQYPVEIPG------------VSNQfFLQTALNAVRsyrgqesLDRFdfqdlmeekIALLkmPEDLLTR--SVNVGF 146
Cdd:COG4988 414 AWVPQNPYLFAGtirenlrlgrpdASDE-ELEAALEAAG-------LDEF---------VAAL--PDGLDTPlgEGGRGL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVK 226
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG-RTVILITH--RLALLAQADRILVLDDGRIVE 551
|
....*
gi 157083167 227 SGDFT 231
Cdd:COG4988 552 QGTHE 556
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-227 |
3.14e-18 |
|
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: 79.01 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKDLLELSPEDRAGEGIF 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSG--LYKPDSGEILVDGKEVSFASPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 82 MAFQYPVeipgvsnqfflqtalnavrsyrgqesldrfdfqdlmeekiallkmpedlltrsvnvgfsgGEKKRNDILQMAV 161
Cdd:cd03216 79 MVYQLSV------------------------------------------------------------GERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157083167 162 LEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYqriLDYIKP--DYVHVLYQGRIVKS 227
Cdd:cd03216 99 RNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHR---LDEVFEiaDRVTVLRDGRVVGT 163
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-228 |
3.21e-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: 79.52 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVE------DKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVVGGSVEFKGKDLLELSPEDR 75
Cdd:cd03213 4 LSFRNLTVTVKsspsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 76 AG----EGIFMAFqypveipgvsnqfflQTAlnavrsyrgQESLdrfDFQdlmeekiALLKmpedlltrsvnvGFSGGEK 151
Cdd:cd03213 84 IGyvpqDDILHPT---------------LTV---------RETL---MFA-------AKLR------------GLSGGER 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157083167 152 KRNDI-LQMaVLEPELCILDESDSGLD-IDALKIVaEGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:cd03213 118 KRVSIaLEL-VSNPSLLFLDEPTSGLDsSSALQVM-SLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-226 |
3.64e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 80.09 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKA----ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLLELSPEDRA 76
Cdd:COG1136 4 LLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPT--SGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 77 ---GEGIFMAFQYP-----------VEIPGVsnqffLQTALNAVRSYRGQESLDRFDFQDLMEekiallKMPEDLltrsv 142
Cdd:COG1136 82 rlrRRHIGFVFQFFnllpeltalenVALPLL-----LAGVSRKERRERARELLERVGLGDRLD------HRPSQL----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 143 nvgfSGGEKKRndilqMA-----VLEPELCILDE------SDSGLDI-DALKIVAegvnslRDGKRSFIIVTHYQRILDY 210
Cdd:COG1136 146 ----SGGQQQR-----VAiaralVNRPKLILADEptgnldSKTGEEVlELLRELN------RELGTTIVMVTHDPELAAR 210
|
250
....*....|....*.
gi 157083167 211 IkpDYVHVLYQGRIVK 226
Cdd:COG1136 211 A--DRVIRLRDGRIVS 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-203 |
7.30e-18 |
|
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: 79.11 E-value: 7.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLLELSPE-DRAGEGI 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD--SGTIIIDGLKLTDDKKNiNELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQypveipgvsnQFFL---QTALnavrsyrgqesldrfdfQDLMEEKIALLKMP--------EDLLTRsvnVG---- 145
Cdd:cd03262 79 GMVFQ----------QFNLfphLTVL-----------------ENITLAPIKVKGMSkaeaeeraLELLEK---VGladk 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157083167 146 -------FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH 203
Cdd:cd03262 129 adaypaqLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-203 |
7.39e-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: 78.62 E-value: 7.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 12 EDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLlelsPEDRAG-----EGIFMAFQY 86
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGL--LRPQSGAVLIDGEPL----DYSRKGllerrQRVGLVFQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 87 PveipgvSNQFFLQTA--------LN------AVRSyRGQESLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKK 152
Cdd:TIGR01166 77 P------DDQLFAADVdqdvafgpLNlglseaEVER-RVREALTAVGASGLRERPTHCL---------------SGGEKK 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 157083167 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH 203
Cdd:TIGR01166 135 RVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-228 |
8.69e-18 |
|
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: 78.80 E-value: 8.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAG--REDyevvGGSVEFKGKDLLEL-SPEDRAGE 78
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGliKPD----SGEITFDGKSYQKNiEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 79 GIfmafQYPVEIPGVSNQFFLQTALNA--VRSYRGQESLDRFDFQDLMEEKIAllkmpedlltrsvnvGFSGGEKKRNDI 156
Cdd:cd03268 77 LI----EAPGFYPNLTARENLRLLARLlgIRKKRIDEVLDVVGLKDSAKKKVK---------------GFSLGMKQRLGI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157083167 157 LQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDYIKPDYVhVLYQGRIVKSG 228
Cdd:cd03268 138 ALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIG-IINKGKLIEEG 208
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-248 |
9.90e-18 |
|
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: 79.12 E-value: 9.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 16 ILRGLDLDVRPGEVHAIMGPNGSGKSTLsATLAGREdYEVVGGSVEFKGKDLLELSPEDRAGEgIFMAFQYPVeipgvsn 95
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTV-VSLLERF-YDPTSGEILLDGVDIRDLNLRWLRSQ-IGLVSQEPV------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 96 qFFLQTALNAVRsyrgqesLDRFDFQDLMEEKIALL--------KMPEDLLTRSVNVGF--SGGEKKRNDILQMAVLEPE 165
Cdd:cd03249 88 -LFDGTIAENIR-------YGKPDATDEEVEEAAKKanihdfimSLPDGYDTLVGERGSqlSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 166 LCILDESDSGLDIDALKIVAEGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF-TLVKQleEQGYGWL 244
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKG-RTTIVIAH--RLSTIRNADLIAVLQNGQVVEQGTHdELMAQ--KGVYAKL 234
|
....
gi 157083167 245 TEQQ 248
Cdd:cd03249 235 VKAQ 238
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-229 |
1.48e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 80.53 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRageGI 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFE--TPDSGRILLDGRDVTGLPPEKR---NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQ---------------YPVEIPGVSnqfflqtalNAVRSYRGQESLDRFDFQDLMEekiallKMPEDLltrsvnvg 145
Cdd:COG3842 80 GMVFQdyalfphltvaenvaFGLRMRGVP---------KAEIRARVAELLELVGLEGLAD------RYPHQL-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 146 fSGGEKKRndilqMA-----VLEPELCILDESDSGLDidalkivaegvNSLRDG-----KR-------SFIIVTHYQ--- 205
Cdd:COG3842 137 -SGGQQQR-----VAlaralAPEPRVLLLDEPLSALD-----------AKLREEmreelRRlqrelgiTFIYVTHDQeea 199
|
250 260
....*....|....*....|....*....
gi 157083167 206 -----RILdyikpdyvhVLYQGRIVKSGD 229
Cdd:COG3842 200 laladRIA---------VMNDGRIEQVGT 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
14-226 |
2.66e-17 |
|
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: 78.69 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 14 KAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRAgegifmAFQYPVeipgv 93
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLE--KPAQGTVSFRGQDLYQLDRKQRR------AFRRDV----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 94 snQFFLQTALNAV--RSYRGQ------ESLDRFDFQDLMEEKIALLKM----PEDLltRSVNVGFSGGEKKRNDILQMAV 161
Cdd:TIGR02769 91 --QLVFQDSPSAVnpRMTVRQiigeplRHLTSLDESEQKARIAELLDMvglrSEDA--DKLPRQLSGGQLQRINIARALA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157083167 162 LEPELCILDESDSGLDIDALKIVAEGVNSLR-DGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVK 226
Cdd:TIGR02769 167 VKPKLIVLDEAVSNLDMVLQAVILELLRKLQqAFGTAYLFITHDLRLVQSFC-QRVAVMDKGQIVE 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-203 |
3.43e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 78.28 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDY--EV-VGGSVEFKGK-------DLLEL 70
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpEVtITGSIVYNGHniysprtDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 71 SPEdragegIFMAFQYPveipgvsNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKI---ALLKMPEDLLTRSVnVGFS 147
Cdd:PRK14239 85 RKE------IGMVFQQP-------NPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLkgaSIWDEVKDRLHDSA-LGLS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157083167 148 GGEKKRNDILQMAVLEPELCILDESDSGLD-IDALKIvAEGVNSLRDgKRSFIIVTH 203
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDpISAGKI-EETLLGLKD-DYTMLLVTR 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-228 |
3.64e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.03 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLaGR--EDYEV--VGGSVEFKGKDLLELsPEDRAG 77
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-NRliELYPEarVSGEVYLDGQDIFKM-DVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 78 EGIFMAFQYPVEIPGVSnqFFLQTALNA-----VRSYRGQESLDRFDFQ--DLMEEKIALLKMPEDLLtrsvnvgfSGGE 150
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLS--IFENVALGLklnrlVKSKKELQERVRWALEkaQLWDEVKDRLDAPAGKL--------SGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157083167 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDgKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFPQQAARIS-DYVAFLYKGQIVEWG 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
4.39e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.11 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVS--VEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELS-PEDRAG 77
Cdd:PRK13632 7 MIKVENVSFSypNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGL--LKPQSGEIKIDGITISKENlKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 78 EGIFmaFQYPveipgvSNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDIL 157
Cdd:PRK13632 85 IGII--FQNP------DNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGM-EDYLDKEPQ-NLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157083167 158 QMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRD-GKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGD 229
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtRKKTLISITH--DMDEAILADKVIVFSEGKLIAQGK 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-203 |
4.57e-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: 76.80 E-value: 4.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 3 SIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKDLLELSpeDRAGegiFM 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILG--LLKPTSGSIRVFGKPLEKER--KRIG---YV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 83 A------FQYPVEIPGVsnqfflqTALNAVRSYRGQESLDRFDFQDLME--EKIALLKMPEDLLTRsvnvgFSGGEKKRN 154
Cdd:cd03235 74 PqrrsidRDFPISVRDV-------VLMGLYGHKGLFRRLSKADKAKVDEalERVGLSELADRQIGE-----LSGGQQQRV 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157083167 155 DILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH 203
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTH 190
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
17-228 |
1.33e-16 |
|
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: 75.87 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPEDRAGEGIfmAFQYPV---EIPGV 93
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTL--LKPTSGRATVAGHDVVREPREVRRRIGI--VFQDLSvddELTGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 94 SNqFFLQTALNAVRSYRGQESLDR-FDFQDLMEEKIALLKMpedlltrsvnvgFSGGEKKRNDILQMAVLEPELCILDES 172
Cdd:cd03265 92 EN-LYIHARLYGVPGAERRERIDElLDFVGLLEAADRLVKT------------YSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157083167 173 DSGLDIDALKIVAEGVNSL-RDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLC-DRVAIIDHGRIIAEG 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-229 |
1.48e-16 |
|
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: 78.19 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSV----EDKAILRGLDLDVRPGEVHAIMGPNGSGKS--TLSAT--LAgrEDYEVVGGSVEFKGKDLLELSP 72
Cdd:COG4172 6 LLSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSvtALSILrlLP--DPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 73 ED-RA--GEGIFMAFQYPveipgvsnqfflQTALNAVRSYRGQ--ESL---DRFDFQDLMEEKIALLKM-----PEDLLT 139
Cdd:COG4172 84 RElRRirGNRIAMIFQEP------------MTSLNPLHTIGKQiaEVLrlhRGLSGAAARARALELLERvgipdPERRLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 140 RsvnvgF----SGGEKKRNDIlQMAVL-EPELCILDESDSGLDIdalKIVAEGVNSLRDGKRS------FI-----IVTH 203
Cdd:COG4172 152 A-----YphqlSGGQRQRVMI-AMALAnEPDLLIADEPTTALDV---TVQAQILDLLKDLQRElgmallLIthdlgVVRR 222
|
250 260
....*....|....*....|....*.
gi 157083167 204 YQrildyikpDYVHVLYQGRIVKSGD 229
Cdd:COG4172 223 FA--------DRVAVMRQGEIVEQGP 240
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-203 |
1.56e-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: 78.48 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDK-AILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPEDRaGEGI 80
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF--VDPTEGSIAVNGVPLADADADSW-RDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQYPveipgvsnQFFLQTALNAVRSYRG-------QESLDRFDFQDLMEEkiallkMPEDLLTR--SVNVGFSGGEK 151
Cdd:TIGR02857 399 AWVPQHP--------FLFAGTIAENIRLARPdasdaeiREALERAGLDEFVAA------LPQGLDTPigEGGAGLSGGQA 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 157083167 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGkRSFIIVTH 203
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG-RTVLLVTH 515
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-228 |
4.08e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.47 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGR-EDYEV---VGGSVEFKGKDLLELSPEDRA 76
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSkikVDGKVLYFGKDIFQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 77 GEgIFMAFQYPVEIPGVSnqfflqTALNAVRSYRGQESLDRFDFQDLMEE---KIALLKMPEDLLTRSVNvGFSGGEKKR 153
Cdd:PRK14246 90 KE-VGMVFQQPNPFPHLS------IYDNIAYPLKSHGIKEKREIKKIVEEclrKVGLWKEVYDRLNSPAS-QLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157083167 154 NDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDgKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKN-EIAIVIVSHNPQQVARVA-DYVAFLYNGELVEWG 234
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-223 |
8.81e-16 |
|
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: 72.60 E-value: 8.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRAGEG-I 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE--EPDSGSILIDGEDLTDLEDELPPLRRrI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQYPVEIPGVSnqfflqtalnaVRsyrgqesldrfdfqdlmeEKIALlkmpedlltrsvnvGFSGGEKKRNDILQMA 160
Cdd:cd03229 79 GMVFQDFALFPHLT-----------VL------------------ENIAL--------------GLSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157083167 161 VLEPELCILDESDSGLDIDALKIVAEGVNSLRDG-KRSFIIVTHYQRILDYIKpDYVHVLYQGR 223
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLA-DRVVVLRDGK 178
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-203 |
9.76e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.87 E-value: 9.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFkGK---------DLLELS 71
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGEL--EPDSGTVKL-GEtvkigyfdqHQEELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 72 PEDRagegifmAFQYPVEI-PGVSNQFflqtalnaVRSYrgqesLDRFDFQdlmeekiallkmPEDLLTRsVNVgFSGGE 150
Cdd:COG0488 392 PDKT-------VLDELRDGaPGGTEQE--------VRGY-----LGRFLFS------------GDDAFKP-VGV-LSGGE 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 157083167 151 KKRndiLQMAVL---EPELCILDESDSGLDIDALKIVAEGvnsLRDGKRSFIIVTH 203
Cdd:COG0488 438 KAR---LALAKLllsPPNVLLLDEPTNHLDIETLEALEEA---LDDFPGTVLLVSH 487
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-228 |
1.63e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 75.20 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 12 EDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPED-RagEGIFMAFQypvei 90
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF--YDPTSGRILIDGVDIRDLTLESlR--RQIGVVPQ----- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 91 pgvsnQFFL--QTALNAVRSYRGQESLDRfdfqdlMEE--KIA-----LLKMPEDLLT----RSVNvgFSGGEKKRNDIL 157
Cdd:COG1132 422 -----DTFLfsGTIRENIRYGRPDATDEE------VEEaaKAAqahefIEALPDGYDTvvgeRGVN--LSGGQRQRIAIA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157083167 158 QMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFII------VTHYQRILdyikpdyvhVLYQGRIVKSG 228
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIahrlstIRNADRIL---------VLDDGRIVEQG 556
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
12-240 |
1.97e-15 |
|
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: 73.62 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 12 EDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLleLSPE------DRAGegifMAFQ 85
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPT--SGKVTVDGLDT--LDEEnlweirKKVG----MVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 86 YPveipgvSNQF----------F----LQTALNAVRSyRGQESLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEK 151
Cdd:TIGR04520 85 NP------DNQFvgatveddvaFglenLGVPREEMRK-RVDEALKLVGMEDFRDREPHLL---------------SGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSL-RDGKRSFIIVTHYqrILDYIKPDYVHVLYQGRIVKSGD- 229
Cdd:TIGR04520 143 QRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHD--MEEAVLADRVIVMNKGKIVAEGTp 220
|
250
....*....|....
gi 157083167 230 ---FTLVKQLEEQG 240
Cdd:TIGR04520 221 reiFSQVELLKEIG 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-229 |
2.07e-15 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 73.00 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKA----ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLLELSPEDR- 75
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPT--SGSVLVDGTDLTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 76 -AGEGIFMAFQ---------------YPVEIPGVSnqfflqtalnavRSYRGQESLDRFDFQDLMEEKIAllkMPEDLlt 139
Cdd:cd03258 79 kARRRIGMIFQhfnllssrtvfenvaLPLEIAGVP------------KAEIEERVLELLELVGLEDKADA---YPAQL-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 140 rsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLD------IDALkivaegvnsLRDGKRSF----IIVTHYqriLD 209
Cdd:cd03258 142 -------SGGQKQRVGIARALANNPKVLLCDEATSALDpettqsILAL---------LRDINRELgltiVLITHE---ME 202
|
250 260
....*....|....*....|..
gi 157083167 210 YIKP--DYVHVLYQGRIVKSGD 229
Cdd:cd03258 203 VVKRicDRVAVMEKGEVVEEGT 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-229 |
2.29e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 73.99 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVE----DKAILRGLDLDVRPGEVHAIMGPNGSGKS----TLSATLA--GRedyevVGGSVEFKGKDLLEL 70
Cdd:PRK09473 12 LLDVKDLRVTFStpdgDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGR-----IGGSATFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 71 sPED-----RAgEGIFMAFQYPVeipgvsnqfflqTALNAVRSYRGQ--ESL---DRFDFQDLMEEKIALL---KMPEdl 137
Cdd:PRK09473 87 -PEKelnklRA-EQISMIFQDPM------------TSLNPYMRVGEQlmEVLmlhKGMSKAEAFEESVRMLdavKMPE-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 138 LTRSVNV---GFSGGEKKRNDIlQMAVL-EPELCILDESDSGLDIdalKIVAEGVNSLRDGKRSF----IIVTHYQRILD 209
Cdd:PRK09473 151 ARKRMKMyphEFSGGMRQRVMI-AMALLcRPKLLIADEPTTALDV---TVQAQIMTLLNELKREFntaiIMITHDLGVVA 226
|
250 260
....*....|....*....|
gi 157083167 210 YIkPDYVHVLYQGRIVKSGD 229
Cdd:PRK09473 227 GI-CDKVLVMYAGRTMEYGN 245
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-240 |
3.08e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.13 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVED--KAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLLELSPED-RAGE 78
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE--AGTITVGGMVLSEETVWDvRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 79 GifMAFQYPveipgvSNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQ 158
Cdd:PRK13635 84 G--MVFQNP------DNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGM-EDFLNREPH-RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 159 MAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFII-VTHyqRILDYIKPDYVHVLYQGRIVKSGD----FTLV 233
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLsITH--DLDEAAQADRVIVMNKGEILEEGTpeeiFKSG 231
|
....*..
gi 157083167 234 KQLEEQG 240
Cdd:PRK13635 232 HMLQEIG 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-228 |
3.15e-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: 72.26 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 12 EDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELsPEDRAGEGIFMAFQYPVEIP 91
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF--YDPQKGQILIDGIDIRDI-SRKSLRSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 92 GvsnqfflqTALNAVRsyrgqesLDRFDFQDLMEEKIA--------LLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAV 161
Cdd:cd03254 91 G--------TIMENIR-------LGRPNATDEEVIEAAkeagahdfIMKLPNGYDTVLGENGgnLSQGERQLLAIARAML 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157083167 162 LEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDyikPDYVHVLYQGRIVKSG 228
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKN---ADKILVLDDGKIIEEG 219
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
10-225 |
3.33e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 10 SVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVVGGSVEfkgkdllelspedragegiFMAFQYPVE 89
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-------------------VPDNQFGRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 90 IPGVSNQFFLQTALNAVrsyrgqESLDRFDFQDlmeeKIALLKMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCIL 169
Cdd:COG2401 100 ASLIDAIGRKGDFKDAV------ELLNAVGLSD----AVLWLRRFKEL---------STGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 157083167 170 DESDSGLDIDALKIVAEGVNSL-RDGKRSFIIVTHYQRILDYIKPD-YVHVLYQGRIV 225
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATHHYDVIDDLQPDlLIFVGYGGVPE 218
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
17-228 |
3.50e-15 |
|
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: 73.19 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAG--REDyevvGGSVEFKGKDLLELSPEDRagEGIFMAFQYPV---EIP 91
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTllRPT----SGTARVAGYDVVREPRKVR--RSIGIVPQYASvdeDLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 92 GVSNQFF---LQTALNAVRSYRGQESLDRFDFQDLMEEKIAllkmpedlltrsvnvGFSGGEKKRNDILQMAVLEPELCI 168
Cdd:TIGR01188 83 GRENLEMmgrLYGLPKDEAEERAEELLELFELGEAADRPVG---------------TYSGGMRRRLDIAASLIHQPDVLF 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 169 LDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:TIGR01188 148 LDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLC-DRIAIIDHGRIIAEG 206
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-240 |
3.54e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.37 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 13 DKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLagREDYEVVGGSVEFKGKDLLELspedragegifmafqypveipg 92
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL--QNLYQPTGGQVLLDGVPLVQY---------------------- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 93 vsNQFFLQTALNAVrsyrGQE--------------SLDRFDFQDLMEEKIA------LLKMPEDLLTrsvNVG-----FS 147
Cdd:TIGR00958 549 --DHHYLHRQVALV----GQEpvlfsgsvreniayGLTDTPDEEIMAAAKAanahdfIMEFPNGYDT---EVGekgsqLS 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSlrdGKRSFIIVTHYQRILDyiKPDYVHVLYQGRIVKS 227
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR---ASRTVLLIAHRLSTVE--RADQILVLKKGSVVEM 694
|
250
....*....|...
gi 157083167 228 GDFtlvKQLEEQG 240
Cdd:TIGR00958 695 GTH---KQLMEDQ 704
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-228 |
4.16e-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: 71.56 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 20 LDLDVrPGEVHAIMGPNGSGKSTLSATLAGREDYE----VVGGSVEFKGKDLLELSPEDRageGIFMAFQYPVEIPGVS- 94
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDggtiVLNGTVLFDSRKKINLPPQQR---KIGLVFQQYALFPHLNv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 95 --N-QFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:cd03297 93 reNlAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQL---------------SGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157083167 172 SDSGLDiDALKIVAEgvNSLRDGKRSF----IIVTHYQRILDYIKPDYVhVLYQGRIVKSG 228
Cdd:cd03297 158 PFSALD-RALRLQLL--PELKQIKKNLnipvIFVTHDLSEAEYLADRIV-VMEDGRLQYIG 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-85 |
5.13e-15 |
|
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: 71.70 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKA----ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVVGGSVEFKGKDLLELSPEDRA 76
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDR--PTSGTVRLAGQDLFALDEDARA 85
|
90
....*....|....*
gi 157083167 77 ---GEGI---FMAFQ 85
Cdd:COG4181 86 rlrARHVgfvFQSFQ 100
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-230 |
5.25e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.20 E-value: 5.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQV--SVED------------KAIlRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKD 66
Cdd:PRK15079 8 LLEVADLKVhfDIKDgkqwfwqppktlKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGL--VKATDGEVAWLGKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 67 LLELSPEDR--AGEGIFMAFQYPVeipgvsnqfflqTALNA-----------VRSYRGQesLDRFDFQD---LMEEKIAL 130
Cdd:PRK15079 85 LLGMKDDEWraVRSDIQMIFQDPL------------ASLNPrmtigeiiaepLRTYHPK--LSRQEVKDrvkAMMLKVGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 131 LkmpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIdalKIVAEGVNSLRDGKR----SFIIVTHYQR 206
Cdd:PRK15079 151 L---PNLINRYPH-EFSGGQCQRIGIARALILEPKLIICDEPVSALDV---SIQAQVVNLLQQLQRemglSLIFIAHDLA 223
|
250 260
....*....|....*....|....
gi 157083167 207 ILDYIKpDYVHVLYQGRIVKSGDF 230
Cdd:PRK15079 224 VVKHIS-DRVLVMYLGHAVELGTY 246
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-225 |
5.89e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 72.04 E-value: 5.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQV-----SVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKDLLELSPEDR 75
Cdd:COG1101 1 MLELKNLSKtfnpgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAG--SLPPDSGSILIDGKDVTKLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 76 AGegiFMA--FQYPVeipgvsnqffLQTALN-------AVRSYRGQE-----SLDRfDFQDLMEEKIALLKMP-EDLLTr 140
Cdd:COG1101 79 AK---YIGrvFQDPM----------MGTAPSmtieenlALAYRRGKRrglrrGLTK-KRRELFRELLATLGLGlENRLD- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 141 sVNVGF-SGGEkkRNDI-LQMAVL-EPELCILDESDSGLD------IDAL--KIVAEgvnslrdGKRSFIIVTH-YQRIL 208
Cdd:COG1101 144 -TKVGLlSGGQ--RQALsLLMATLtKPKLLLLDEHTAALDpktaalVLELteKIVEE-------NNLTTLMVTHnMEQAL 213
|
250 260
....*....|....*....|.
gi 157083167 209 DY----IkpdyvhVLYQGRIV 225
Cdd:COG1101 214 DYgnrlI------MMHEGRII 228
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-228 |
7.41e-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: 71.36 E-value: 7.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 16 ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPED-RAGEGIFMAfqypveipgvS 94
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF--YVPENGRVLVDGHDLALADPAWlRRQVGVVLQ----------E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 95 NQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIA-LLKMPE--DLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:cd03252 85 NVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDfISELPEgyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157083167 172 SDSGLDIDALKIVAEGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDICAG-RTVIIIAH--RLSTVKNADRIIVMEKGRIVEQG 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-228 |
8.36e-15 |
|
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: 71.11 E-value: 8.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 13 DKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRageGIFMAFQYPVEIPG 92
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFE--TPTSGEILLDGKDITNLPPHKR---PVNTVFQNYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 93 VS---N-QFFLQTAlnavrsyrgqeSLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCI 168
Cdd:cd03300 87 LTvfeNiAFGLRLK-----------KLPKAEIKERVAEALDLVQL-EGYANRKPS-QLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157083167 169 LDESDSGLDidaLKIVAEGVNSLRDGKRS----FIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:cd03300 154 LDEPLGALD---LKLRKDMQLELKRLQKElgitFVFVTHDQEEALTMS-DRIAVMNKGKIQQIG 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-229 |
8.56e-15 |
|
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: 71.11 E-value: 8.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 12 EDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLsATLAGREdYEVVGGSVEFKGKDLLELSpedragegifmafqypveip 91
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTL-VNLIPRF-YDVDSGRILIDGHDVRDYT-------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 92 gvsnqfflqtaLNAVRSYRGQESLDRFDFQDLMEEKIA-----------------------LLKMPEDLLT----RSVNV 144
Cdd:cd03251 71 -----------LASLRRQIGLVSQDVFLFNDTVAENIAygrpgatreeveeaaraanahefIMELPEGYDTvigeRGVKL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 145 gfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFII------VTHYQRILdyikpdyvhV 218
Cdd:cd03251 140 --SGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIahrlstIENADRIV---------V 208
|
250
....*....|.
gi 157083167 219 LYQGRIVKSGD 229
Cdd:cd03251 209 LEDGKIVERGT 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-225 |
1.06e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.64 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 14 KAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRAgegifmAFQYPVeipgv 93
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLE--SPSQGNVSWRGEPLAKLNRAQRK------AFRRDI----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 94 snQFFLQTALNAV-----------RSYRGQESLDRFDFQDLMEEKIALLKMPEDLLTRsVNVGFSGGEKKRNDILQMAVL 162
Cdd:PRK10419 92 --QMVFQDSISAVnprktvreiirEPLRHLLSLDKAERLARASEMLRAVDLDDSVLDK-RPPQLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157083167 163 EPELCILDESDSGLDidaLKIVAEGVNSLRDGKR----SFIIVTHYQRILDYIkPDYVHVLYQGRIV 225
Cdd:PRK10419 169 EPKLLILDEAVSNLD---LVLQAGVIRLLKKLQQqfgtACLFITHDLRLVERF-CQRVMVMDNGQIV 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-203 |
1.08e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.90 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVvgGSVEFKGKDLLELSPEdRAGEGI 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTS--GTLLFEGEDISTLKPE-IYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQYPVeIPGVS---NQFF-LQTALNAVRSYRGQESLDRFDfqdlmeekiallkMPEDLLTRSVNvGFSGGEKKRNDI 156
Cdd:PRK10247 84 SYCAQTPT-LFGDTvydNLIFpWQIRNQQPDPAIFLDDLERFA-------------LPDTILTKNIA-ELSGGEKQRISL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 157083167 157 LQMAVLEPELCILDESDSGLDIDALKIVAEGVNSL-RDGKRSFIIVTH 203
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTH 196
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-228 |
1.16e-14 |
|
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: 70.36 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRageGIF 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLE--EPTSGRIYIGGRDVTDLPPKDR---DIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 82 MAFQ----YPveipgvSNQFFLQTALNAVRSYRGQESLDRfdfqdLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDIL 157
Cdd:cd03301 76 MVFQnyalYP------HMTVYDNIAFGLKLRKVPKDEIDE-----RVREVAELLQI-EHLLDRKPK-QLSGGQRQRVALG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157083167 158 QMAVLEPELCILDESDSGLDIDA-LKIVAEGVNSLRDGKRSFIIVTHyqrilDYIKP----DYVHVLYQGRIVKSG 228
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLrVQMRAELKRLQQRLGTTTIYVTH-----DQVEAmtmaDRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
1.16e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 71.65 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVED-KAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKG-------KDLLELsp 72
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGI--LKPTSGEVLIKGepikydkKSLLEV-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 73 edRAGEGIfmAFQYPveipgvSNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEkiALLKMPEDLLTRSVNVGFSGGEKK 152
Cdd:PRK13639 77 --RKTVGI--VFQNP------DDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKE--ALKAVGMEGFENKPPHHLSGGQKK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157083167 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHyQRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTH-DVDLVPVYADKVYVMSDGKIIKEG 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
13-241 |
1.38e-14 |
|
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: 72.44 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 13 DKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVVGGSVEFKGKDLLELSPED-RAgegifmafqypvEIP 91
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIP--RFYEPDSGQILLDGHDLADYTLASlRR------------QVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 92 GVSNQFFL--QTALNAVRsYRGQESLDRFDFQDLMEEKIALL---KMPEDLLTrsvNVG-----FSGGEKKRNDILQMAV 161
Cdd:TIGR02203 410 LVSQDVVLfnDTIANNIA-YGRTEQADRAEIERALAAAYAQDfvdKLPLGLDT---PIGengvlLSGGQRQRLAIARALL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 162 LEPELCILDESDSGLDIDALKIVAEGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGdfTLVKQLEEQGY 241
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLMQG-RTTLVIAH--RLSTIEKADRIVVMDDGRIVERG--THNELLARNGL 560
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-228 |
1.55e-14 |
|
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: 69.98 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 16 ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGR-EDYEVVGGSVEFKGKDLLElspedragegifMAFQYPVEIpgvs 94
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtEGNVSVEGDIHYNGIPYKE------------FAEKYPGEI---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 95 nqfflqtalnavrSYRGQEslDRFDFQDLMEEKI-ALLKMPEDLLTRsvnvGFSGGEKKRNDILQMAVLEPELCILDESD 173
Cdd:cd03233 86 -------------IYVSEE--DVHFPTLTVRETLdFALRCKGNEFVR----GISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157083167 174 SGLD-IDALKIvaegVNSLR---DGKRSFIIVTHYQ---RILDYIkpDYVHVLYQGRIVKSG 228
Cdd:cd03233 147 RGLDsSTALEI----LKCIRtmaDVLKTTTFVSLYQasdEIYDLF--DKVLVLYEGRQIYYG 202
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-228 |
2.09e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.92 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 20 LDLDVRPGEVHAIMGPNGSGKSTLSATLAG----REDYEVVGGSVEFKGKDLLELSPEDRAgegIFMAFQYPveipgvSN 95
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGllqpTEGKVTVGDIVVSSTSKQKEIKPVRKK---VGVVFQFP------ES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 96 QFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMPEDLLTRSvNVGFSGGEKKRNDILQMAVLEPELCILDESDSG 175
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKS-PFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 157083167 176 LDIDALKIVAEGVNSLRDGKRSFIIVTH-YQRILDYikPDYVHVLYQGRIVKSG 228
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHlMDDVADY--ADYVYLLEKGHIISCG 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-223 |
3.80e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.45 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 3 SIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVVGGSVEFKGKDLLELSPEdRAGegiFM 82
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILK-RTG---FV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 83 AfQYPVEIPGVSnqffLQTALNAVRSYRGQESLDRFDFQDLMEEKIA---LLKMPEDLLTRSVNVGFSGGEKKRNDILQM 159
Cdd:PLN03211 146 T-QDDILYPHLT----VRETLVFCSLLRLPKSLTKQEKILVAESVISelgLTKCENTIIGNSFIRGISGGERKRVSIAHE 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157083167 160 AVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGR 223
Cdd:PLN03211 221 MLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-228 |
4.92e-14 |
|
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: 68.11 E-value: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSV--EDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKDLLELspedrageg 79
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQQGEITLDGVPVSDL--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 80 ifmafqypveipgvsnqfflqtalnavrsyrgqesldrfdfQDLMEEKIALLKMPEDLLTRSV--NVG--FSGGEKKRND 155
Cdd:cd03247 70 -----------------------------------------EKALSSLISVLNQRPYLFDTTLrnNLGrrFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157083167 156 ILQMAVLEPELCILDESDSGLD-IDALKIVAEGVNSLRDgkRSFIIVTHYQRILDYIkpDYVHVLYQGRIVKSG 228
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDpITERQLLSLIFEVLKD--KTLIWITHHLTGIEHM--DKILFLENGKIIMQG 178
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-228 |
5.00e-14 |
|
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: 68.76 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGeVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPEDRAGEGiF 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATL--TPPSSGTIRIDGQDVLKQPQKLRRRIG-Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 82 MAFQYPVeIPGVSNQFFL--QTALNAVRSYRGQESLDRfdfqdlMEEKIALlkmpEDLLTRSVNvGFSGGEKKRNDILQM 159
Cdd:cd03264 77 LPQEFGV-YPNFTVREFLdyIAWLKGIPSKEVKARVDE------VLELVNL----GDRAKKKIG-SLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157083167 160 AVLEPELCILDESDSGLDIDA-------LKIVAEGvnslrdgkRSFIIVTHyqrILDYIKP--DYVHVLYQGRIVKSG 228
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEErirfrnlLSELGED--------RIVILSTH---IVEDVESlcNQVAVLNKGKLVFEG 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-229 |
6.37e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.01 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLagredyevvggsvefkgkDLLElSPED---RAG 77
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI------------------NLLE-QPEAgtiRVG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 78 EgifmafqypVEIpgvsnqfflqtalNAVRSYRGQESLDR-------FDFQ------------DLMEEKIALLKMPED-- 136
Cdd:PRK11264 64 D---------ITI-------------DTARSLSQQKGLIRqlrqhvgFVFQnfnlfphrtvleNIIEGPVIVKGEPKEea 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 137 ------LLTRsvnVG-----------FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFI 199
Cdd:PRK11264 122 tarareLLAK---VGlagketsyprrLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMV 198
|
250 260 270
....*....|....*....|....*....|
gi 157083167 200 IVTHYQRILDYIKpDYVHVLYQGRIVKSGD 229
Cdd:PRK11264 199 IVTHEMSFARDVA-DRAIFMDQGRIVEQGP 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-203 |
9.47e-14 |
|
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: 68.08 E-value: 9.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELS-------PED 74
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGI--ILPDSGEVLFDGKPLDIAArnrigylPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 75 RA---GEGIFMAFQYPVEIPGVSnqffLQTALNAVRSYrgqesLDRFDFQDLMEEKIallkmpEDLltrsvnvgfSGGEK 151
Cdd:cd03269 79 RGlypKMKVIDQLVYLAQLKGLK----KEEARRRIDEW-----LERLELSEYANKRV------EEL---------SKGNQ 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 157083167 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH 203
Cdd:cd03269 135 QKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTH 186
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-228 |
1.06e-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: 68.03 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 13 DKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVVGGSVEFKGKDLLELSPED-RAGEGIFmafqyPVEIP 91
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF--RFYDVSSGSILIDGQDIREVTLDSlRRAIGVV-----PQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 92 gvsnqFFLQTALNAVRSYRgqesLDRFDFQdlMEE--KIA-----LLKMPEDLLTRsvnVG-----FSGGEKKRNDILQM 159
Cdd:cd03253 86 -----LFNDTIGYNIRYGR----PDATDEE--VIEaaKAAqihdkIMRFPDGYDTI---VGerglkLSGGEKQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157083167 160 AVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSfIIVTHyqRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTT-IVIAH--RLSTIVNADKIIVLKDGRIVERG 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-228 |
1.67e-13 |
|
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: 67.53 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDL--QVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLelSPEDRAGEG 79
Cdd:cd03263 1 LQIRNLtkTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL--RPTSGTAYINGYSIR--TDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 80 IFMAFQYPVEIPGVsnqfflqTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMPEDLLTRSVNvgFSGGEKKRndiLQ- 158
Cdd:cd03263 77 LGYCPQFDALFDEL-------TVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRART--LSGGMKRK---LSl 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157083167 159 -MAVL-EPELCILDESDSGLDIDALKIVAEGVNSLRDGkRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:cd03263 145 aIALIgGPSVLLLDEPTSGLDPASRRAIWDLILEVRKG-RSIILTTHSMDEAEALC-DRIAIMSDGKLRCIG 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-229 |
2.10e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPEDRAGEGIFMAFQYPVEIPGVSNQ 96
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI--HEPTKGTITINNINYNKLDHKLAAQLGIGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 97 FFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSggEKKRNDILQMAVLEPELCILDESDSGL 176
Cdd:PRK09700 99 ENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSIS--HKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 157083167 177 ---DIDALKIVaegVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGD 229
Cdd:PRK09700 177 tnkEVDYLFLI---MNQLRKEGTAIVYISHKLAEIRRIC-DRYTVMKDGSSVCSGM 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-85 |
2.33e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.89 E-value: 2.33e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKDLLELSPEDRAGEGIFMAFQ 85
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSG--VYQPDSGEILLDGEPVRFRSPRDAQAAGIAIIHQ 86
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-242 |
2.42e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 67.85 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGR----------EDYEVVGGSvefKGKDLLELspedRAGEGifMAFQY 86
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLhvptqgsvrvDDTLITSTS---KNKDIKQI----RKKVG--LVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 87 PveipgvSNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMPEDLLTRSvNVGFSGGEKKRNDILQMAVLEPEL 166
Cdd:PRK13649 94 P------ESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKN-PFELSGGQMRRVAIAGILAMEPKI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 167 CILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH-YQRILDYikPDYVHVLYQGRIVKSGD----FTLVKQLEEQGY 241
Cdd:PRK13649 167 LVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlMDDVANY--ADFVYVLEKGKLVLSGKpkdiFQDVDFLEEKQL 244
|
.
gi 157083167 242 G 242
Cdd:PRK13649 245 G 245
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-203 |
2.46e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 66.49 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRAgegifmafqypveipgVSNQ 96
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL--RPTSGTVRRAGGARVAYVPQRSE----------------VPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 97 FFLqTALNAVRSYRGQE--SLDRFDFQDLMEEKIALLKMP-EDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESD 173
Cdd:NF040873 70 LPL-TVRDLVAMGRWARrgLWRRLTRDDRAAVDDALERVGlADLAGRQLG-ELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|
gi 157083167 174 SGLDIDALKIVAEGVNSLRDGKRSFIIVTH 203
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTH 177
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
13-228 |
2.81e-13 |
|
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: 66.91 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 13 DKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGR-EDYEVVGGSVEFKGKdllELSPEdragegifmafQYPVEIP 91
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvEGGGTTSGQILFNGQ---PRKPD-----------QFQKCVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 92 GVSNQFFLQTALnAVRSY-------RGQESLDrfDFQDLMEEKIALLKMPEDLLTRSVNV-GFSGGEKKRNDILQMAVLE 163
Cdd:cd03234 85 YVRQDDILLPGL-TVRETltytailRLPRKSS--DAIRKKRVEDVLLRDLALTRIGGNLVkGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157083167 164 PELCILDESDSGLD-IDALKIVAEGVNSLRDGKrsFIIVTHYQ------RILDYIKpdyvhVLYQGRIVKSG 228
Cdd:cd03234 162 PKVLILDEPTSGLDsFTALNLVSTLSQLARRNR--IVILTIHQprsdlfRLFDRIL-----LLSSGEIVYSG 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-246 |
4.17e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.95 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAG--REDYEVV---GGSVEFKGKDLLELSPEdr 75
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGllRPQKGAVlwqGKPLDYSKRGLLALRQQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 76 agegIFMAFQYPveipgvSNQFFlqtalnavrsYRGQESLDRFDFQDL--MEEKIAllKMPEDLLTRSVNVGF------- 146
Cdd:PRK13638 79 ----VATVFQDP------EQQIF----------YTDIDSDIAFSLRNLgvPEAEIT--RRVDEALTLVDAQHFrhqpiqc 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 147 -SGGEKKRNDILQMAVLEPELCILDESDSGLD-------IDALK-IVAEGvnslrdgkrSFIIVTHYQRILDYIKPDYVH 217
Cdd:PRK13638 137 lSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagrtqmIAIIRrIVAQG---------NHVIISSHDIDLIYEISDAVY 207
|
250 260 270
....*....|....*....|....*....|....*
gi 157083167 218 VLYQGRIVKSGD----FTLVKQLEEQGYG--WLTE 246
Cdd:PRK13638 208 VLRQGQILTHGApgevFACTEAMEQAGLTqpWLVK 242
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-203 |
5.07e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.78 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 4 IKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEF-KGKDL------LELSPEDRA 76
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPD--SGEVSIpKGLRIgylpqePPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 77 GEGIFMAFQYPVEipgvsnqffLQTALNAVRSYRGQESLDRFDFQDLMEEKIAL---------------LKMPEDLLTRS 141
Cdd:COG0488 79 LDTVLDGDAELRA---------LEAELEELEAKLAEPDEDLERLAELQEEFEALggweaearaeeilsgLGFPEEDLDRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157083167 142 VNVgFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDAlkiVA--EGVnsLRDGKRSFIIVTH 203
Cdd:COG0488 150 VSE-LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEF--LKNYPGTVLVVSH 207
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-203 |
5.63e-13 |
|
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: 64.39 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFkgkdllelspedragegif 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGEL--EPDEGIVTW------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 82 mafqypveIPGVSNQFFLQtalnavrsyrgqesldrfdfqdlmeekiallkmpedlltrsvnvgFSGGEKKRNDILQMAV 161
Cdd:cd03221 60 --------GSTVKIGYFEQ---------------------------------------------LSGGEKMRLALAKLLL 86
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 157083167 162 LEPELCILDESDSGLDIDALKIVAEGvnsLRDGKRSFIIVTH 203
Cdd:cd03221 87 ENPNLLLLDEPTNHLDLESIEALEEA---LKEYPGTVILVSH 125
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-231 |
5.92e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 66.60 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLaGR--EDYEV--VGGSVEFKGKDLL--ELSPED- 74
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL-NRmnDLIPGarVEGEILLDGEDIYdpDVDVVEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 75 --RAGegifMAFQYPveipgvsNQFFLQTALNAVRSYRGQESLDRFDFQDLMEE---KIAL---LKmpeDLLTRSVnVGF 146
Cdd:COG1117 91 rrRVG----MVFQKP-------NPFPKSIYDNVAYGLRLHGIKSKSELDEIVEEslrKAALwdeVK---DRLKKSA-LGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 147 SGGEKKRndiLQMA---VLEPELCILDESDSGLD-IDALKIvAEGVNSLRDgKRSFIIVTH--YQ--RIldyikPDYVHV 218
Cdd:COG1117 156 SGGQQQR---LCIAralAVEPEVLLMDEPTSALDpISTAKI-EELILELKK-DYTIVIVTHnmQQaaRV-----SDYTAF 225
|
250
....*....|....*..
gi 157083167 219 LYQGRIVKSGD----FT 231
Cdd:COG1117 226 FYLGELVEFGPteqiFT 242
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-229 |
1.27e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 65.90 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKdllELSPEDRAGEG- 79
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD--SGEVLWDGE---PLDPEDRRRIGy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 80 -----------------IFMAfqypvEIPGVSnqffLQTALNAVRSYrgqesLDRFDFQDLMEEKIallkmpEDLltrsv 142
Cdd:COG4152 76 lpeerglypkmkvgeqlVYLA-----RLKGLS----KAEAKRRADEW-----LERLGLGDRANKKV------EEL----- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 143 nvgfSGGEKKRndiLQM--AVL-EPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHyqrILDYIKP--DYVH 217
Cdd:COG4152 131 ----SKGNQQK---VQLiaALLhDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSH---QMELVEElcDRIV 200
|
250
....*....|..
gi 157083167 218 VLYQGRIVKSGD 229
Cdd:COG4152 201 IINKGRKVLSGS 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-229 |
1.42e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 65.16 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAiLRgLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRageGI 80
Cdd:COG3840 1 MLRLDDLTYRYGDFP-LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFL--PPDSGRILWNGQDLTALPPAER---PV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQypveipgvSNQFF--LQTA------------LNAVRSYRGQESLDRFDFQDLMEekiallKMPEDLltrsvnvgf 146
Cdd:COG3840 74 SMLFQ--------ENNLFphLTVAqniglglrpglkLTAEQRAQVEQALERVGLAGLLD------RLPGQL--------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIdALKivAEG---VNSL-RDGKRSFIIVTHY----QRIldyikPDYVHV 218
Cdd:COG3840 131 SGGQRQRVALARCLVRKRPILLLDEPFSALDP-ALR--QEMldlVDELcRERGLTVLMVTHDpedaARI-----ADRVLL 202
|
250
....*....|.
gi 157083167 219 LYQGRIVKSGD 229
Cdd:COG3840 203 VADGRIAADGP 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
12-228 |
1.47e-12 |
|
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: 64.92 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 12 EDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPED-RAGEGIFMafQYPVEI 90
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL--YKPTSGSVLLDGTDIRQLDPADlRRNIGYVP--QDVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 91 PGvsnqfflqtalnAVRS---YRGQESLDrfdfQDLME--------EKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQM 159
Cdd:cd03245 91 YG------------TLRDnitLGAPLADD----ERILRaaelagvtDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157083167 160 AVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKrSFIIVTHYQRILDYIkpDYVHVLYQGRIVKSG 228
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK-TLIIITHRPSLLDLV--DRIIVMDSGRIVADG 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-203 |
1.80e-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: 66.23 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAI-LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVVGGSVEFKGKDLLELSPEDRAgegi 80
Cdd:TIGR02868 335 LELRDLSAGYPGAPPvLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD--PLQGEVTLDGVPVSSLDQDEVR---- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 fmafqypvEIPGVSNQ---FFLQTALNAVRSYRGQ-------ESLDRFDFQDLMEEkiallkMPEDLLTRSVNVG--FSG 148
Cdd:TIGR02868 409 --------RRVSVCAQdahLFDTTVRENLRLARPDatdeelwAALERVGLADWLRA------LPDGLDTVLGEGGarLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 157083167 149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSfIIVTH 203
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTV-VLITH 528
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-241 |
2.18e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.29 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 14 KAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRED--YEVVGGSVEFKGKDLLELSPEDRaGEGIFMAfQYPVEIP 91
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfHIGVEGVITYDGITPEEIKKHYR-GDVVYNA-ETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 92 GVSNQFFLQTALNAVRSYRGQESLDRFDFQdlmeEKIALLKMPEDLL--TRSVNV------GFSGGEKKRNDILQMAVLE 163
Cdd:TIGR00956 152 HLTVGETLDFAARCKTPQNRPDGVSREEYA----KHIADVYMATYGLshTRNTKVgndfvrGVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 164 PELCILDESDSGLD-------IDALKIVAEGVNSLrdgkrsfIIVTHYQRILD-YIKPDYVHVLYQGRIVKSGDFTLVKQ 235
Cdd:TIGR00956 228 AKIQCWDNATRGLDsatalefIRALKTSANILDTT-------PLVAIYQCSQDaYELFDKVIVLYEGYQIYFGPADKAKQ 300
|
....*..
gi 157083167 236 -LEEQGY 241
Cdd:TIGR00956 301 yFEKMGF 307
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
17-229 |
2.36e-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: 64.28 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPEDRageGIFMAFQYPVEIPGVSNQ 96
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGF--IKPDSGKILLNGKDITNLPPEKR---DISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 97 FFLQTALNAVRSYRGQesldrfdfqdlMEEKI----ALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDES 172
Cdd:cd03299 90 KNIAYGLKKRKVDKKE-----------IERKVleiaEMLGI-DHLLNRKPET-LSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157083167 173 DSGLDIdalKIVAEGVNSLRDGKRSF----IIVTHYQ---RILDyikpDYVHVLYQGRIVKSGD 229
Cdd:cd03299 157 FSALDV---RTKEKLREELKKIRKEFgvtvLHVTHDFeeaWALA----DKVAIMLNGKLIQVGK 213
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
8-178 |
2.49e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.57 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 8 QVSVEDKaiLRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvgGSVEFKGKDLLELSPEDRAGEGIFMA---- 83
Cdd:PRK03695 5 DVAVSTR--LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS---GSIQFAGQPLEAWSAAELARHRAYLSqqqt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 84 --FQYPVeipgvsnqF-FLQTALNAvrsyrgqeSLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKR----NDI 156
Cdd:PRK03695 80 ppFAMPV--------FqYLTLHQPD--------KTRTEAVASALNEVAEALGL-DDKLGRSVN-QLSGGEWQRvrlaAVV 141
|
170 180
....*....|....*....|....*
gi 157083167 157 LQMA-VLEPE--LCILDESDSGLDI 178
Cdd:PRK03695 142 LQVWpDINPAgqLLLLDEPMNSLDV 166
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-229 |
3.99e-12 |
|
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: 65.15 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 12 EDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPEDRaGEGIfmafQY-PVEI 90
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGV--WPPTAGSVRLDGADLSQWDREEL-GRHI----GYlPQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 91 pgvsnQFFLQT-ALNAVRsyrgqesldrfdFQDLMEEKI-----------ALLKMPEDLLTRsvnVG-----FSGGEKKR 153
Cdd:COG4618 416 -----ELFDGTiAENIAR------------FGDADPEKVvaaaklagvheMILRLPDGYDTR---IGeggarLSGGQRQR 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157083167 154 ndI-LQMAVL-EPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDYIkpDYVHVLYQGRIVKSGD 229
Cdd:COG4618 476 --IgLARALYgDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAV--DKLLVLRDGRVQAFGP 549
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-229 |
4.71e-12 |
|
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: 63.72 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAG--REDyevvGGSVEFKGKDLLELSPEDRAGEG 79
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlvKPD----SGKILLDGQDITKLPMHKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 80 IfmafQY-PVEiPGVSNQFFLQTALNAVRSYRGqesLDRFDFQDLMEEKIALLKMPEdlLTRSVNVGFSGGEKKRNDILQ 158
Cdd:cd03218 77 I----GYlPQE-ASIFRKLTVEENILAVLEIRG---LSKKEREEKLEELLEEFHITH--LRKSKASSLSGGERRRVEIAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157083167 159 MAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQR-ILDYIkpDYVHVLYQGRIVKSGD 229
Cdd:cd03218 147 ALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVReTLSIT--DRAYIIYEGKVLAEGT 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-203 |
5.32e-12 |
|
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: 63.26 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKA----ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLLELSPeDRAg 77
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT--SGEVLVDGEPVTGPGP-DRG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 78 egifMAFQ---------------YPVEIPGVSnqfflqtalNAVRSYRGQESLDRFDFQDlmeekiALLKMPEDLltrsv 142
Cdd:cd03293 77 ----YVFQqdallpwltvldnvaLGLELQGVP---------KAEARERAEELLELVGLSG------FENAYPHQL----- 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157083167 143 nvgfSGGEKKRNDILQMAVLEPELCILDESDSGLD-IDALKIVAEGVNSLRDGKRSFIIVTH 203
Cdd:cd03293 133 ----SGGMRQRVALARALAVDPDVLLLDEPFSALDaLTREQLQEELLDIWRETGKTVLLVTH 190
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-228 |
1.14e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.94 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSAT---LAGREDYEVVGGSVEFKGKDLL--ELSP-EDR 75
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEARVEGEVRLFGRNIYspDVDPiEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 76 AGEGifMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQESLDRFDFQDLmeEKIALLKMPEDLLtRSVNVGFSGGEKKRND 155
Cdd:PRK14267 85 REVG--MVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWAL--KKAALWDEVKDRL-NDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157083167 156 ILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDgKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPAQAARVS-DYVAFLYLGKLIEVG 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-228 |
1.21e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.19 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 6 DLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRED----YE-----VVGGSVEFKGKDLLELspEDRA 76
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgYRysgdvLLGGRSIFNYRDVLEF--RRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 77 GegifMAFQYPveipgvsNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGF--SGGEKKRN 154
Cdd:PRK14271 104 G----MLFQRP-------NPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFrlSGGQQQLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157083167 155 DILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDgKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAD-RLTVIIVTHNLAQAARIS-DRAALFFDGRLVEEG 244
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
8-178 |
1.40e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.55 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 8 QVSVEDKaiLRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvgGSVEFKGKDLLELSPedragegifmafqyp 87
Cdd:COG4138 5 DVAVAGR--LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ---GEILLNGRPLSDWSA--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 88 veipgvsnqfflqTALNAVRSYRGQESLDRFD---FQ----------------DLMEEKIALLKMpEDLLTRSVNvGFSG 148
Cdd:COG4138 65 -------------AELARHRAYLSQQQSPPFAmpvFQylalhqpagasseaveQLLAQLAEALGL-EDKLSRPLT-QLSG 129
|
170 180 190
....*....|....*....|....*....|....*....
gi 157083167 149 GEKKRndILQMAVL---------EPELCILDESDSGLDI 178
Cdd:COG4138 130 GEWQR--VRLAAVLlqvwptinpEGQLLLLDEPMNSLDV 166
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-228 |
1.62e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.34 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVVGGSVEFKGKDLLELSPEDRAGEGI 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA--RLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQYPVeiP-GVSNQFFLQTALNAVRSYRGQESL-DRFDFQDLMeEKIALLKMPEDLLTRsvnvgFSGGEKKRNDILQ 158
Cdd:PRK11231 80 LLPQHHLT--PeGITVRELVAYGRSPWLSLWGRLSAeDNARVNQAM-EQTRINHLADRRLTD-----LSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157083167 159 MAVLEPELCILDESDSGLDI----DALKIVAEgvnsLRDGKRSFIIVTH-YQRILDYIkpDYVHVLYQGRIVKSG 228
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDInhqvELMRLMRE----LNTQGKTVVTVLHdLNQASRYC--DHLVVLANGHVMAQG 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-84 |
2.05e-11 |
|
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: 60.91 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVsvedKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKDLLELS--------- 71
Cdd:cd03215 4 VLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFG--LRPPASGEITLDGKPVTRRSprdairagi 77
|
90
....*....|....*.
gi 157083167 72 ---PEDRAGEGIFMAF 84
Cdd:cd03215 78 ayvPEDRKREGLVLDL 93
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-229 |
2.16e-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: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPEDRAGEGIFMAFQYPVEIP----- 91
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGL--YQPDSGEILIDGKPVRIRSPRDAIALGIGMVHQHFMLVPnltva 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 92 -----GVSNQFFLQTALNAVRSyRGQESLDRFDFqdlmeeKIALLKMPEDLltrSVnvgfsgGEKKRNDILQMAVLEPEL 166
Cdd:COG3845 99 enivlGLEPTKGGRLDRKAARA-RIRELSERYGL------DVDPDAKVEDL---SV------GEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157083167 167 CILDESDSGL---DIDAL-KIVAEgvnsLRDGKRSFIIVTHYqriLDYIKP--DYVHVLYQGRIVKSGD 229
Cdd:COG3845 163 LILDEPTAVLtpqEADELfEILRR----LAAEGKSIIFITHK---LREVMAiaDRVTVLRRGKVVGTVD 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-203 |
2.21e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 61.65 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDR----- 75
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLE--EITSGDLIVDGLKVNDPKVDERlirqe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 76 AGegifMAFQypveipgvsnQFFL---QTALNAV----RSYRGQESLDrfdfqdlmEEKIAllkmpEDLLTRsvnVG--- 145
Cdd:PRK09493 79 AG----MVFQ----------QFYLfphLTALENVmfgpLRVRGASKEE--------AEKQA-----RELLAK---VGlae 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157083167 146 --------FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH 203
Cdd:PRK09493 129 rahhypseLSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-203 |
3.27e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.66 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDllelSPEDRAGEgi 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGL--LPPAAGTIKLDGGD----IDDPDVAE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 fmAFQYpveipgVSNQFFLQTALNAV------RSYRGQ------ESLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSG 148
Cdd:PRK13539 74 --ACHY------LGHRNAMKPALTVAenlefwAAFLGGeeldiaAALEAVGLAPLAHLPFGYL---------------SA 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 157083167 149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH 203
Cdd:PRK13539 131 GQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
15-203 |
4.61e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.56 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 15 AILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLLELSPEDRA---GEGIFMAFQypveip 91
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS--SGEVSLVGQPLHQMDEEARAklrAKHVGFVFQ------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 92 gvsnQFFLQTALNAVRS------YRGQ-ESLDRFDFQDLMEE---KIALLKMPEDLltrsvnvgfSGGEKKRNDILQMAV 161
Cdd:PRK10584 96 ----SFMLIPTLNALENvelpalLRGEsSRQSRNGAKALLEQlglGKRLDHLPAQL---------SGGEQQRVALARAFN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 157083167 162 LEPELCILDESDSGLDIDALKIVAEGVNSL-RDGKRSFIIVTH 203
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTH 205
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-186 |
4.70e-11 |
|
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: 60.06 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEdrAGEGIF 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLL--RPDSGEVRWNGTPLAEQRDE--PHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 82 mafqYPVEIPGVSNQFflqTALNAVRSYR---GQESLDRFDFQDLMEekialLKMPEDLLTRSVnvgfSGGEKKRNDILQ 158
Cdd:TIGR01189 77 ----YLGHLPGLKPEL---SALENLHFWAaihGGAQRTIEDALAAVG-----LTGFEDLPAAQL----SAGQQRRLALAR 140
|
170 180
....*....|....*....|....*...
gi 157083167 159 MAVLEPELCILDESDSGLDIDALKIVAE 186
Cdd:TIGR01189 141 LWLSRRPLWILDEPTTALDKAGVALLAG 168
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-228 |
5.72e-11 |
|
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: 61.76 E-value: 5.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 13 DKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPED-RAGEGIFmafqyPVEI- 90
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF--YDVTSGRILIDGQDIRDVTQASlRAAIGIV-----PQDTv 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 91 --------------PGVSNQFFLQTALNAvrsyrgqeSLDRFdfqdlmeekIALLkmPEDLLTRsvnVG-----FSGGEK 151
Cdd:COG5265 443 lfndtiayniaygrPDASEEEVEAAARAA--------QIHDF---------IESL--PDGYDTR---VGerglkLSGGEK 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 152 KRNDILQMAVLEPELCILDESDSGLD------I-DALKIVAEGVNSLrdgkrsfII------VTHYQRILdyikpdyvhV 218
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALDsrteraIqAALREVARGRTTL-------VIahrlstIVDADEIL---------V 564
|
250
....*....|
gi 157083167 219 LYQGRIVKSG 228
Cdd:COG5265 565 LEAGRIVERG 574
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-220 |
6.37e-11 |
|
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: 60.84 E-value: 6.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 24 VRPGEVHAIMGPNGSGKSTLSATLAGR-----------EDY-EVVGgsvEFKGKDLLELSPEDRAGE-GIFMAFQYPVEI 90
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKlkpnlgkfddpPDWdEILD---EFRGSELQNYFTKLLEGDvKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 91 PgvsnqfflqtalNAVRSYRGqESLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILD 170
Cdd:cd03236 100 P------------KAVKGKVG-ELLKKKDERGKLDELVDQLEL-RHVLDRNID-QLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 157083167 171 ESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLY 220
Cdd:cd03236 165 EPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLS-DYIHCLY 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
16-176 |
6.79e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 16 ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLLELSPEDRAGEGIFMAFQYPVEIPgvsN 95
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD--SGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFP---N 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 96 QFFLQTALnaVRSYRGQESLDRfdfqdlMEEKIALLKMPEDL--LTRSVNVgfsgGEKKRNDILQMAVLEPELCILDESD 173
Cdd:PRK15439 101 LSVKENIL--FGLPKRQASMQK------MKQLLAALGCQLDLdsSAGSLEV----ADRQIVEILRGLMRDSRILILDEPT 168
|
...
gi 157083167 174 SGL 176
Cdd:PRK15439 169 ASL 171
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-184 |
7.52e-11 |
|
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: 60.27 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVS-VEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPED----RA 76
Cdd:cd03256 1 IEVENLSKTyPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLV--EPTSGSVLIDGTDINKLKGKAlrqlRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 77 GEG-IFMAFQYPVEIPGVSNqfFLQTALNAVRSYRGqeSLDRFDFQDLmEEKIALLK---MPEDLLTRSVNVgfSGGEKK 152
Cdd:cd03256 79 QIGmIFQQFNLIERLSVLEN--VLSGRLGRRSTWRS--LFGLFPKEEK-QRALAALErvgLLDKAYQRADQL--SGGQQQ 151
|
170 180 190
....*....|....*....|....*....|..
gi 157083167 153 RNDILQMAVLEPELCILDESDSGLDIDALKIV 184
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQV 183
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-228 |
7.97e-11 |
|
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: 60.35 E-value: 7.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPED-RA--GEGIFMAFQ-------- 85
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRL--IEPTSGKVLIDGQDIAAMSRKElRElrRKKISMVFQsfallphr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 86 -------YPVEIPGVSNQfflqtalnaVRSYRGQESLDRFDFQDLMEekiallKMPEDLltrsvnvgfSGGEKKRNDILQ 158
Cdd:cd03294 118 tvlenvaFGLEVQGVPRA---------EREERAAEALELVGLEGWEH------KYPDEL---------SGGMQQRVGLAR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 159 MAVLEPELCILDESDSGLD--IDA------LKIVAEgvnslrdGKRSFIIVTH----YQRILDYIKpdyvhVLYQGRIVK 226
Cdd:cd03294 174 ALAVDPDILLMDEAFSALDplIRRemqdelLRLQAE-------LQKTIVFITHdldeALRLGDRIA-----IMKDGRLVQ 241
|
..
gi 157083167 227 SG 228
Cdd:cd03294 242 VG 243
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-228 |
7.99e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 60.32 E-value: 7.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGK-----DLLELSPEDR 75
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSAR--LAPDAGEVHYRMRdgqlrDLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 76 --------------AGEGIFMAfqypveipgVSNQFFLQTALNAV--RSY---RGQESldrfdfqDLMEE-KIALLKMpe 135
Cdd:PRK11701 84 rrllrtewgfvhqhPRDGLRMQ---------VSAGGNIGERLMAVgaRHYgdiRATAG-------DWLERvEIDAARI-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 136 DLLTRSvnvgFSGGEKKRndiLQMA---VLEPELCILDESDSGLDIDA----LKIVAEGVNSLRdgkRSFIIVTH---YQ 205
Cdd:PRK11701 146 DDLPTT----FSGGMQQR---LQIArnlVTHPRLVFMDEPTGGLDVSVqarlLDLLRGLVRELG---LAVVIVTHdlaVA 215
|
250 260
....*....|....*....|...
gi 157083167 206 RILdyikPDYVHVLYQGRIVKSG 228
Cdd:PRK11701 216 RLL----AHRLLVMKQGRVVESG 234
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-229 |
9.02e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 60.86 E-value: 9.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKA----ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRA 76
Cdd:COG1135 1 MIELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLE--RPTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 77 GE--GIFMAFQ---------------YPVEIPGVSnqfflqtalNAVRSYRGQESLDRFDfqdlMEEKIAllKMPEDLlt 139
Cdd:COG1135 79 AArrKIGMIFQhfnllssrtvaenvaLPLEIAGVP---------KAEIRKRVAELLELVG----LSDKAD--AYPSQL-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 140 rsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLD------IDALkivaegvnsLRDGKRSF----IIVTH----YQ 205
Cdd:COG1135 142 -------SGGQKQRVGIARALANNPKVLLCDEATSALDpettrsILDL---------LKDINRELgltiVLITHemdvVR 205
|
250 260
....*....|....*....|....
gi 157083167 206 RILdyikpDYVHVLYQGRIVKSGD 229
Cdd:COG1135 206 RIC-----DRVAVLENGRIVEQGP 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-224 |
9.12e-11 |
|
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: 59.79 E-value: 9.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 13 DKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLagREDYEVVGGSVEFKGKDlLELSPEDRAGEGIFMAFQYPVEIPG 92
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL--ENFYQPQGGQVLLDGKP-ISQYEHKYLHSKVSLVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 93 vSNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEkiallkMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILD 170
Cdd:cd03248 103 -SLQDNIAYGLQSCSFECVKEAAQKAHAHSFISE------LASGYDTEVGEKGsqLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 157083167 171 ESDSGLDIDALKIVAEgvnSLRDG--KRSFIIVTHyqRILDYIKPDYVHVLYQGRI 224
Cdd:cd03248 176 EATSALDAESEQQVQQ---ALYDWpeRRTVLVIAH--RLSTVERADQILVLDGGRI 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-229 |
9.70e-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: 61.24 E-value: 9.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVS-----------VEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvgGSVEFKGKDLLEL 70
Cdd:COG4172 276 LEARDLKVWfpikrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE---GEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 71 SPED----RAgeGIFMAFQYPveipgvsnqfflqtalnavrsYRgqeSLD-RFDFQDLMEEKIALLKMP----------E 135
Cdd:COG4172 353 SRRAlrplRR--RMQVVFQDP---------------------FG---SLSpRMTVGQIIAEGLRVHGPGlsaaerrarvA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 136 DLLTRsvnVG------------FSGGEKKRNDILQMAVLEPELCILDESDSGLDidaLKIVAEGVNSLRDGKR----SFI 199
Cdd:COG4172 407 EALEE---VGldpaarhrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALD---VSVQAQILDLLRDLQRehglAYL 480
|
250 260 270
....*....|....*....|....*....|
gi 157083167 200 IVTHYQRILDYIKpDYVHVLYQGRIVKSGD 229
Cdd:COG4172 481 FISHDLAVVRALA-HRVMVMKDGKVVEQGP 509
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-210 |
9.98e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.05 E-value: 9.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEV---VGGSVEFKGKDLLELSPE-DRAG 77
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrVEGRVEFFNQNIYERRVNlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 78 EGIFMAFQYPveipgvsNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMPEDL---LTRSVnVGFSGGEKKRN 154
Cdd:PRK14258 88 RQVSMVHPKP-------NLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIkhkIHKSA-LDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157083167 155 DILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLR-DGKRSFIIVTH----YQRILDY 210
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHnlhqVSRLSDF 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-225 |
1.07e-10 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 59.68 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 13 DKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKDLLELSPEDRA------GegifMAFQ- 85
Cdd:COG2884 14 GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG--EERPTSGQVLVNGQDLSRLKRREIPylrrriG----VVFQd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 86 --------------YPVEIPGVSnqfflqtalNAVRSYRGQESLDRFDFQDLMEekiallKMPEDLltrsvnvgfSGGEK 151
Cdd:COG2884 88 frllpdrtvyenvaLPLRVTGKS---------RKEIRRRVREVLDLVGLSDKAK------ALPHEL---------SGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157083167 152 KRNDILQMAVLEPELCILDESDSGLDID-ALKIVA--EGVNslRDGKrSFIIVTHYQRILDYIkPDYVHVLYQGRIV 225
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPEtSWEIMEllEEIN--RRGT-TVLIATHDLELVDRM-PKRVLELEDGRLV 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-230 |
1.12e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.13 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLagREDYEVVGGSVEFKGKDLLELSpedRAG--EGIFMAFQYPveipGVS 94
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLL--QRVFDPQSGRILIDGTDIRTVT---RASlrRNIAVVFQDA----GLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 95 NqfflqtalnavRSYRGQESLDRFDFQDlmEEKIALLKMPE--DLLTRS-----VNVG-----FSGGEKKRNDILQmAVL 162
Cdd:PRK13657 422 N-----------RSIEDNIRVGRPDATD--EEMRAAAERAQahDFIERKpdgydTVVGergrqLSGGERQRLAIAR-ALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157083167 163 -EPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFII------VTHYQRILdyikpdyvhVLYQGRIVKSGDF 230
Cdd:PRK13657 488 kDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIahrlstVRNADRIL---------VFDNGRVVESGSF 553
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-224 |
1.30e-10 |
|
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: 58.38 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVED--KAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDrageg 79
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLL--RPTSGRVRLDGADISQWDPNE----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 80 ifmafqypveipgvsnqfflqtalnavrsYRGQesldrfdfqdlmeekIALLkmPED--LLTRSV--NVgFSGGEKKRnd 155
Cdd:cd03246 74 -----------------------------LGDH---------------VGYL--PQDdeLFSGSIaeNI-LSGGQRQR-- 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157083167 156 ILQMAVL--EPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDYIkpDYVHVLYQGRI 224
Cdd:cd03246 105 LGLARALygNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA--DRILVLEDGRV 173
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-229 |
1.32e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.00 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLLELS--PEDRAGEGIfmAFQYPveipgvS 94
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ--KGKVLVSGIDTGDFSklQGIRKLVGI--VFQNP------E 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 95 NQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDS 174
Cdd:PRK13644 88 TQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGL-EKYRHRSPKT-LSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 157083167 175 GLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDyiKPDYVHVLYQGRIVKSGD 229
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELH--DADRIIVMDRGKIVLEGE 218
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-73 |
1.51e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.05 E-value: 1.51e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAG--REDyevvGGSVEFKGKDLLELSPE 73
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGlaRPD----AGEVLWQGEPIRRQRDE 71
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
1.55e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.86 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKA-ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKdllelsPEDRAGEG 79
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGI--LKPSSGRILFDGK------PIDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 80 IF-------MAFQYPveipgvSNQFFLQTAlnavrsyrgqesldrfdFQDLMEEKIAlLKMPEDLLTRSVNVG------- 145
Cdd:PRK13636 77 LMklresvgMVFQDP------DNQLFSASV-----------------YQDVSFGAVN-LKLPEDEVRKRVDNAlkrtgie 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 146 ---------FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDG-KRSFIIVTHYQRILDyIKPDY 215
Cdd:PRK13636 133 hlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVP-LYCDN 211
|
250
....*....|...
gi 157083167 216 VHVLYQGRIVKSG 228
Cdd:PRK13636 212 VFVMKEGRVILQG 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-193 |
1.68e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 59.62 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPEDRAGEGI 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGF--YKPTGGTILLRGQHIEGLPGHQIARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQY--------PVEIPGVSNQFFLQT----ALNAVRSYR--GQESLDRFDFqdlMEEKIALLkmpeDLLTRSV-NVG 145
Cdd:PRK11300 83 VRTFQHvrlfremtVIENLLVAQHQQLKTglfsGLLKTPAFRraESEALDRAAT---WLERVGLL----EHANRQAgNLA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 157083167 146 FsgGEKKRNDILQMAVLEPELCILDESDSGL------DIDALkivaegVNSLRD 193
Cdd:PRK11300 156 Y--GQQRRLEIARCMVTQPEILMLDEPAAGLnpketkELDEL------IAELRN 201
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-228 |
1.97e-10 |
|
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: 58.66 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 20 LDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLLELSPEDRAgegIFMAFQypveipgvSNQFFL 99
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQ--SGRVLINGVDVTAAPPADRP---VSMLFQ--------ENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 100 QTA--------------LNAVRSYRGQESLDRFDFQDLMeekialLKMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPE 165
Cdd:cd03298 84 HLTveqnvglglspglkLTAEDRQAIEVALARVGLAGLE------KRLPGEL---------SGGERQRVALARVLVRDKP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157083167 166 LCILDESDSGLD----IDALKIVAEgvnSLRDGKRSFIIVTHYQRILDYIKPDYVHvLYQGRIVKSG 228
Cdd:cd03298 149 VLLLDEPFAALDpalrAEMLDLVLD---LHAETKMTVLMVTHQPEDAKRLAQRVVF-LDNGRIAAQG 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-229 |
2.29e-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: 60.20 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYE--------------------------- 54
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptsgriiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 55 ---VVGGSVEFKGKDLLELSPEDRAG--EGIFMAFQYPVEIPGvsNQFFLQTALNAVRS--YRGQESLDRfdfqdlmeeK 127
Cdd:TIGR03269 81 pcpVCGGTLEPEEVDFWNLSDKLRRRirKRIAIMLQRTFALYG--DDTVLDNVLEALEEigYEGKEAVGR---------A 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 128 IALLKMPEdLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSL-RDGKRSFIIVTHY 204
Cdd:TIGR03269 150 VDLIEMVQ-LSHRITHIArdLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHW 228
|
250 260
....*....|....*....|....*
gi 157083167 205 QRILDYIKpDYVHVLYQGRIVKSGD 229
Cdd:TIGR03269 229 PEVIEDLS-DKAIWLENGEIKEEGT 252
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-205 |
2.33e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 59.96 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRAgegIF 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFE--TPDSGRIMLDGQDITHVPAENRH---VN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 82 MAFQYPVEIPGVS---NQFF---LQTALNAVRSYRGQESLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRND 155
Cdd:PRK09452 90 TVFQSYALFPHMTvfeNVAFglrMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQL---------------SGGQQQRVA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 157083167 156 ILQMAVLEPELCILDESDSGLDidaLKIVAEGVNSLRDGKR----SFIIVTHYQ 205
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALD---YKLRKQMQNELKALQRklgiTFVFVTHDQ 205
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-229 |
2.44e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.33 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 4 IKDLQVSVEDKAiLRGLDLDVRPGEVHAIMGPNGSGKST----LSATLAGREdyevvgGSVEFKGKD---------LLEL 70
Cdd:PRK13651 11 IFNKKLPTELKA-LDNVSVEINQGEFIAIIGQTGSGKTTfiehLNALLLPDT------GTIEWIFKDeknkkktkeKEKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 71 SPEDRAGEGIFMAFQYPVEIP---GVSNQF-----FLQTALNAV----RSY--RGQESLDRfdfqdlMEEKIALLKMPED 136
Cdd:PRK13651 84 LEKLVIQKTRFKKIKKIKEIRrrvGVVFQFaeyqlFEQTIEKDIifgpVSMgvSKEEAKKR------AAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 137 LLTRSvNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH-YQRILDYIKpdY 215
Cdd:PRK13651 158 YLQRS-PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHdLDNVLEWTK--R 234
|
250
....*....|....
gi 157083167 216 VHVLYQGRIVKSGD 229
Cdd:PRK13651 235 TIFFKDGKIIKDGD 248
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-205 |
2.67e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 59.66 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 3 SIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVVGGSVEFKGKDLLELSPEDRageGIFM 82
Cdd:PRK11000 5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGDLFIGEKRMNDVPPAER---GVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 83 AFQ----YPvEIPGVSNQFF---LQTALNAVRSYRGQESLDRFDFQDLMEEKiallkmPEDLltrsvnvgfSGGEKKRND 155
Cdd:PRK11000 80 VFQsyalYP-HLSVAENMSFglkLAGAKKEEINQRVNQVAEVLQLAHLLDRK------PKAL---------SGGQRQRVA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 157083167 156 ILQMAVLEPELCILDESDSGLDIdALKIV--AEGVNSLRDGKRSFIIVTHYQ 205
Cdd:PRK11000 144 IGRTLVAEPSVFLLDEPLSNLDA-ALRVQmrIEISRLHKRLGRTMIYVTHDQ 194
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-228 |
2.99e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.88 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKST----LSATLAGREDYEVVGGSV---EFKGKDLLELspedRAGEGIfmAFQYPve 89
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTllqhLNGLLQPTSGTVTIGERVitaGKKNKKLKPL----RKKVGI--VFQFP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 90 ipgvSNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMPEDLLTRSvNVGFSGGEKKRNDILQMAVLEPELCIL 169
Cdd:PRK13634 95 ----EHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARS-PFELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157083167 170 DESDSGLDIDALKIVAEGVNSL-RDGKRSFIIVTH-YQRILDYikPDYVHVLYQGRIVKSG 228
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHsMEDAARY--ADQIVVMHKGTVFLQG 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
17-228 |
3.22e-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: 58.50 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLLELSPEDRageGIFMAFQYPVEIPgvsnq 96
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD--SGTILFGGEDATDVPVQER---NVGFVFQHYALFR----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 97 fFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMPE-DLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDSG 175
Cdd:cd03296 88 -HMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQlDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 157083167 176 LDIdalKIVAEGVNSLR----DGKRSFIIVTHYQ-RILDYikPDYVHVLYQGRIVKSG 228
Cdd:cd03296 167 LDA---KVRKELRRWLRrlhdELHVTTVFVTHDQeEALEV--ADRVVVMNKGRIEQVG 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-239 |
3.41e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 58.59 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 4 IKDLQVSVED--KAiLRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKdllELSPED----RAG 77
Cdd:PRK13647 7 VEDLHFRYKDgtKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI--YLPQRGRVKVMGR---EVNAENekwvRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 78 EGifMAFQYPveipgvSNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDIL 157
Cdd:PRK13647 81 VG--LVFQDP------DDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRM-WDFRDKPPY-HLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 158 QMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYqriLDYIK--PDYVHVLYQGRIVKSGDFTLV-- 233
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHD---VDLAAewADQVIVLKEGRVLAEGDKSLLtd 227
|
....*.
gi 157083167 234 KQLEEQ 239
Cdd:PRK13647 228 EDIVEQ 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-211 |
4.83e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 58.66 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLLELSPEDRAGEGIF 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPD--AGSISLCGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 82 MAFQypveipGVSNQFFLQTALNAVRSYRGQESLD-RFDFQDLMEekIALLKMPEDLLTRSVnvgfSGGEKKRNDILQMA 160
Cdd:PRK13537 86 PQFD------NLDPDFTVRENLLVFGRYFGLSAAAaRALVPPLLE--FAKLENKADAKVGEL----SGGMKRRLTLARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 157083167 161 VLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHY----QRILDYI 211
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFmeeaERLCDRL 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-228 |
5.10e-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: 57.73 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 12 EDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAG--REDyevvGGSVEFKGKDLLELSPEDRAGEGIFMA--FQYP 87
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGllQPT----SGEVRVAGLVPWKRRKKFLRRIGVVFGqkTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 88 VEIPGVSNQFFLQtalnavRSYRgqesLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELC 167
Cdd:cd03267 108 WDLPVIDSFYLLA------AIYD----LPPARFKKRLDELSELLDL-EELLDTPVR-QLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157083167 168 ILDESDSGLDIDALKIVAEGVNSL-RDGKRSFIIVTHYQRILDYIkPDYVHVLYQGRIVKSG 228
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEAL-ARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
31-228 |
6.01e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 58.28 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 31 AIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELS-PEDRAGEGIfmAFQYPveipgvSNQFFLQTALNAVRSY 109
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGI--LKPTSGSVLIRGEPITKENiREVRKFVGL--VFQNP------DDQIFSPTVEQDIAFG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 110 RGQESLDRFDFQDLMEEKIALLKMpEDLLTRsVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVN 189
Cdd:PRK13652 104 PINLGLDEETVAHRVSSALHMLGL-EELRDR-VPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLN 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 157083167 190 SLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:PRK13652 182 DLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYG 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-205 |
7.03e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.31 E-value: 7.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRAgegI 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE--QPTAGQIMLDGVDLSHVPPYQRP---I 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQYPVEIPGVSNQFFLQTALNavrsyrgQESLDRFDFQDLMEEKIALLKMPEdlLTRSVNVGFSGGEKKRNDILQMA 160
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLK-------QDKLPKAEIASRVNEMLGLVHMQE--FAKRKPHQLSGGQRQRVALARSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 157083167 161 VLEPELCILDESDSGLDI---DALKIvaEGVNSLRDGKRSFIIVTHYQ 205
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKklrDRMQL--EVVDILERVGVTCVMVTHDQ 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-84 |
7.05e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.50 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAI-LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAG-RedyEVVGGSVEFKGKDLLELS-------- 71
Cdd:COG3845 258 LEVENLSVRDDRGVPaLKDVSLEVRAGEILGIAGVAGNGQSELAEALAGlR---PPASGSIRLDGEDITGLSprerrrlg 334
|
90
....*....|....*..
gi 157083167 72 ----PEDRAGEGIFMAF 84
Cdd:COG3845 335 vayiPEDRLGRGLVPDM 351
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-75 |
7.75e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 58.23 E-value: 7.75e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRE--DyevvGGSVEFKGKDLL-ELSPEDR 75
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLEtpD----SGRIVLNGRDLFtNLPPRER 75
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-248 |
8.68e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 58.32 E-value: 8.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQV-SVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvgGSVEFKGKDLLELSPED-RA--- 76
Cdd:PRK11174 350 IEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ---GSLKINGIELRELDPESwRKhls 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 77 --GegifmafQYPveipgvsnQFFLQTALNAVRsyRGQESLDRFDFQDLME-----EKIALLKMPEDLLTRSVNVGFSGG 149
Cdd:PRK11174 427 wvG-------QNP--------QLPHGTLRDNVL--LGNPDASDEQLQQALEnawvsEFLPLLPQGLDTPIGDQAAGLSVG 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 150 EKKRndI-LQMAVLEP-ELCILDESDSGLDIDALKIVAEGVNSLRDGKrSFIIVTHyqRILDYIKPDYVHVLYQGRIVKS 227
Cdd:PRK11174 490 QAQR--LaLARALLQPcQLLLLDEPTASLDAHSEQLVMQALNAASRRQ-TTLMVTH--QLEDLAQWDQIWVMQDGQIVQQ 564
|
250 260
....*....|....*....|....
gi 157083167 228 GDF-TLVKQleeQG--YGWLTEQQ 248
Cdd:PRK11174 565 GDYaELSQA---GGlfATLLAHRQ 585
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-230 |
9.75e-10 |
|
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: 56.01 E-value: 9.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVED-KAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGredyevvggsvefkgkdlleLSPedrAGEGI 80
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG--------------------LWP---WGSGR 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 fmafqypVEIPGVSNQFFL-QtalnavRSYRGQESLdrfdfqdlmeeKIALLKMPEDLLtrsvnvgfSGGEKKRNDILQM 159
Cdd:cd03223 58 -------IGMPEGEDLLFLpQ------RPYLPLGTL-----------REQLIYPWDDVL--------SGGEQQRLAFARL 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157083167 160 AVLEPELCILDESDSGLDIDALKIVAEgvnSLRDGKRSFIIVTHYQRILDYikpdYVHVLyqgRIVKSGDF 230
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQ---LLKELGITVISVGHRPSLWKF----HDRVL---DLDGEGGW 166
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-241 |
1.76e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 57.36 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 14 KAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEV-VGGSVEFKGKDLleLSPEDRAGEGIFMafQYPVEIPG 92
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkGSGSVLLNGMPI--DAKEMRAISAYVQ--QDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 93 --VSNQFFLQTALNAVRSYRGQESLDRFDfqDLMEEkIALLKMpEDLLTRSVNV--GFSGGEKKRNDILQMAVLEPELCI 168
Cdd:TIGR00955 114 ltVREHLMFQAHLRMPRRVTKKEKRERVD--EVLQA-LGLRKC-ANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 169 LDESDSGLD-------IDALKIVAEgvnslrdgKRSFIIVTHYQ---RILDYIkpDYVHVLYQGRIVKSGDFT-LVKQLE 237
Cdd:TIGR00955 190 CDEPTSGLDsfmaysvVQVLKGLAQ--------KGKTIICTIHQpssELFELF--DKIILMAEGRVAYLGSPDqAVPFFS 259
|
....
gi 157083167 238 EQGY 241
Cdd:TIGR00955 260 DLGH 263
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-49 |
2.01e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.37 E-value: 2.01e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAG 49
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG 49
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-203 |
2.02e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 6 DLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVVGGSVEFKGKDLLELSPEDRAGegifMAFQ 85
Cdd:TIGR00956 768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRPLDSSFQRSIG----YVQQ 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 86 YPVEIPGVSnqffLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMPE--DLLTRSVNVGFSGGEKKRNDILQMAVLE 163
Cdd:TIGR00956 844 QDLHLPTST----VRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESyaDAVVGVPGEGLNVEQRKRLTIGVELVAK 919
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 157083167 164 PELCI-LDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH 203
Cdd:TIGR00956 920 PKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-220 |
2.46e-09 |
|
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: 57.10 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 25 RPGEVHAIMGPNGSGKSTLSATLAGRE-----DYEVVGGSVE----FKGKDLLELSPEDRAGEgIFMAF--QYPVEIPgv 93
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELkpnlgDYDEEPSWDEvlkrFRGTELQDYFKKLANGE-IKVAHkpQYVDLIP-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 94 snqfflqtalnavRSYRG--QESLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:COG1245 174 -------------KVFKGtvRELLEKVDERGKLDELAEKLGL-ENILDRDISE-LSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157083167 172 SDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLY 220
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLA-DYVHILY 286
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-228 |
2.64e-09 |
|
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: 55.62 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKD--LLELSpedrage 78
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI--YPPDSGTVTVRGRVssLLGLG------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 79 gifMAFQYpvEIPGVSNQFFLQTALNAVRSYRGQESLDRFDFQDLmeekiallkmpEDLLTRSVNVgFSGGEKKRndiLQ 158
Cdd:cd03220 93 ---GGFNP--ELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSEL-----------GDFIDLPVKT-YSSGMKAR---LA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157083167 159 MAV---LEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYqriLDYIKP--DYVHVLYQGRIVKSG 228
Cdd:cd03220 153 FAIataLEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHD---PSSIKRlcDRALVLEKGKIRFDG 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-87 |
3.21e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 56.39 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKA-ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRageG 79
Cdd:PRK11650 3 GLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLE--RITSGEIWIGGRVVNELEPADR---D 77
|
90
....*....|..
gi 157083167 80 IFMAFQ----YP 87
Cdd:PRK11650 78 IAMVFQnyalYP 89
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-228 |
3.32e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 56.29 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSV-EDKAILRGLD---LDVRPGEVHAIMGPNGSGKSTLSATLAGREDY--EVVGGSVEFKGKDLLELSPED 74
Cdd:PRK11022 3 LLNVDKLSVHFgDESAPFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYpgRVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 75 R---AGEGIFMAFQYPVEI--PGVSNQFFLQTALNA----VRSYRGQESLDRFDFQDLMEEKIALLKMPEDLltrsvnvg 145
Cdd:PRK11022 83 RrnlVGAEVAMIFQDPMTSlnPCYTVGFQIMEAIKVhqggNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQL-------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 146 fSGGEKKRNDILQMAVLEPELCILDESDSGLDIdalKIVAEGVNSLRDGKR----SFIIVTH--------YQRILdyikp 213
Cdd:PRK11022 155 -SGGMSQRVMIAMAIACRPKLLIADEPTTALDV---TIQAQIIELLLELQQkenmALVLITHdlalvaeaAHKII----- 225
|
250
....*....|....*
gi 157083167 214 dyvhVLYQGRIVKSG 228
Cdd:PRK11022 226 ----VMYAGQVVETG 236
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-184 |
4.44e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKdllelsPEDRAGEGI 80
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVE--SGQIQIDGK------TATRGDRSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAfqYPVEIPG-------VSNQFFlqtaLNAVRSYRGQEsldrfdfqdLMEEKIALLKMP--EDLLTRSVnvgfSGGEK 151
Cdd:PRK13543 83 FMA--YLGHLPGlkadlstLENLHF----LCGLHGRRAKQ---------MPGSALAIVGLAgyEDTLVRQL----SAGQK 143
|
170 180 190
....*....|....*....|....*....|...
gi 157083167 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIV 184
Cdd:PRK13543 144 KRLALARLWLSPAPLWLLDEPYANLDLEGITLV 176
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-229 |
4.60e-09 |
|
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: 56.35 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 19 GLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFK-GK---DLLELSPED--RAGEGIFMAFQ----YP- 87
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGV--LEPTSGEVNVRvGDewvDMTKPGPDGrgRAKRYIGILHQeydlYPh 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 88 ------------VEIPgvsNQFFLQTALNAVRSyrgqesldrFDFQDLMEEKIaLLKMPEDLltrsvnvgfSGGEKKRND 155
Cdd:TIGR03269 380 rtvldnlteaigLELP---DELARMKAVITLKM---------VGFDEEKAEEI-LDKYPDEL---------SEGERHRVA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157083167 156 ILQMAVLEPELCILDESDSGLDIDALKIVAEGV-NSLRDGKRSFIIVTHYqriLDYIKP--DYVHVLYQGRIVKSGD 229
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlKAREEMEQTFIIVSHD---MDFVLDvcDRAALMRDGKIVKIGD 511
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-243 |
4.67e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 56.26 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSV-EDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSpEDRAGEGI 80
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGY--YPLTEGEIRLDGRPLSSLS-HSVLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQYPVEIpgvSNQFFLQTALnavrsyrGQESLDRFDFQDLMEEKIALL--KMPEDLLTRSVNVG--FSGGEKKrndI 156
Cdd:PRK10790 418 AMVQQDPVVL---ADTFLANVTL-------GRDISEEQVWQALETVQLAELarSLPDGLYTPLGEQGnnLSVGQKQ---L 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 157 LQMA---VLEPELCILDESDSGLDIDALKIVAEGVNSLRDgKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGdfTLV 233
Cdd:PRK10790 485 LALArvlVQTPQILILDEATANIDSGTEQAIQQALAAVRE-HTTLVVIAH--RLSTIVEADTILVLHRGQAVEQG--THQ 559
|
250
....*....|
gi 157083167 234 KQLEEQGYGW 243
Cdd:PRK10790 560 QLLAAQGRYW 569
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-226 |
7.82e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 54.71 E-value: 7.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKdllELSPED--RAGEGIFMAFQYPveipgvS 94
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGL--FEEFEGKVKIDGE---LLTAENvwNLRRKIGMVFQNP------D 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 95 NQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMpEDLLTRSvNVGFSGGEKKRNDILQMAVLEPELCILDESDS 174
Cdd:PRK13642 92 NQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNM-LDFKTRE-PARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 157083167 175 GLDIDALKIVAEGVNSLRDgKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVK 226
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKE-KYQLTVLSITHDLDEAASSDRILVMKAGEIIK 220
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-228 |
8.11e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.51 E-value: 8.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSatlagredYEVVG------GSVEFKGKDLLELSPEDR 75
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTF--------YMVVGivprdaGNIIIDDEDISLLPLHAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 76 AGEGIFMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQESLDRFDfqDLMEE-KIALLKmpeDLLTRSVnvgfSGGEKKRN 154
Cdd:PRK10895 76 ARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRAN--ELMEEfHIEHLR---DSMGQSL----SGGERRRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157083167 155 DILQMAVLEPELCILDESDSGLD----IDALKIVAEgvnsLRDGKRSFIIVTHYQR-ILDYIKPDYvhVLYQGRIVKSG 228
Cdd:PRK10895 147 EIARALAANPKFILLDEPFAGVDpisvIDIKRIIEH----LRDSGLGVLITDHNVReTLAVCERAY--IVSQGHLIAHG 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-228 |
8.25e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 55.23 E-value: 8.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELS--------- 71
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGT--LTPTAGTVLVAGDDVEALSaraasrrva 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 72 --PEDRAgegifMAFQYPVE-------IPGVSnQFFLQTALN--AVRSYRGQESLDRFDFQDLMEekiallkmpedlltr 140
Cdd:PRK09536 81 svPQDTS-----LSFEFDVRqvvemgrTPHRS-RFDTWTETDraAVERAMERTGVAQFADRPVTS--------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 141 svnvgFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYqriLD----YIkpDYV 216
Cdd:PRK09536 140 -----LSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHD---LDlaarYC--DEL 209
|
250
....*....|..
gi 157083167 217 HVLYQGRIVKSG 228
Cdd:PRK09536 210 VLLADGRVRAAG 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-177 |
8.48e-09 |
|
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: 54.39 E-value: 8.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPeDRagegiFMAFQYPVEIPGVSNQ 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLA--QPTSGGVILEGKQITEPGP-DR-----MVVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 97 FFLQTALNAVRSyrgqeSLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDILQMAVLEPELCILDESDSGL 176
Cdd:TIGR01184 73 ENIALAVDRVLP-----DLSKSERRAIVEEHIALVGLTEAADKRPGQL--SGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
.
gi 157083167 177 D 177
Cdd:TIGR01184 146 D 146
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-228 |
8.53e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 54.76 E-value: 8.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 27 GEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLLELSPED-RAGEGIfmAFQYPveipgvSNQFflqtaLNA 105
Cdd:PRK13648 35 GQWTSIVGHNGSGKSTIAKLMIGIEKVK--SGEIFYNNQAITDDNFEKlRKHIGI--VFQNP------DNQF-----VGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 106 VRSYRGQESLDRFDF-QDLMEEKIALLKMPEDLLTR--SVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALK 182
Cdd:PRK13648 100 IVKYDVAFGLENHAVpYDEMHRRVSEALKQVDMLERadYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 157083167 183 IVAEGVNSLRDGKRSFII-VTHyqRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIIsITH--DLSEAMEADHVIVMNKGTVYKEG 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-235 |
9.96e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 54.84 E-value: 9.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 10 SVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVvgGSVEFKGKDLLELSPEDRAGEGIFMAFQypve 89
Cdd:PRK13536 50 SYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA--GKITVLGVPVPARARLARARIGVVPQFD---- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 90 ipGVSNQFFLQTALNAVRSYRGQESLDrfdfqdlMEEKI-ALLKMPEdlLTRSVNV---GFSGGEKKRNDILQMAVLEPE 165
Cdd:PRK13536 124 --NLDLEFTVRENLLVFGRYFGMSTRE-------IEAVIpSLLEFAR--LESKADArvsDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157083167 166 LCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDYIkPDYVHVLYQGR-IVKSGDFTLVKQ 235
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERL-CDRLCVLEAGRkIAEGRPHALIDE 262
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-178 |
1.23e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.02 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 3 SIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLaGREdYEVVGGSVEFKGKDLLELSPEDRAGEGIFM 82
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRH-QPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 83 AFQYPvEIPGVSNQfflqtALNAVRSYRGQESLDRFDFQDL--MEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMA 160
Cdd:PRK10575 91 PQQLP-AAEGMTVR-----ELVAIGRYPWHGALGRFGAADRekVEEAISLVGL-KPLAHRLVD-SLSGGERQRAWIAMLV 162
|
170
....*....|....*...
gi 157083167 161 VLEPELCILDESDSGLDI 178
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDI 180
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-220 |
1.39e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 24 VRPGEVHAIMGPNGSGKSTLSATLAGR-----EDYEVVGGSVE----FKGKDLLELSPEDRAGE-GIFMAFQYPVEIPgv 93
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGElipnlGDYEEEPSWDEvlkrFRGTELQNYFKKLYNGEiKVVHKPQYVDLIP-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 94 snqfflqtalnavRSYRGQ--ESLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:PRK13409 174 -------------KVFKGKvrELLKKVDERGKLDEVVERLGL-ENILDRDISE-LSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157083167 172 SDSGLDIDALKIVAEGVNSLRDGKrSFIIVTHYQRILDYIKpDYVHVLY 220
Cdd:PRK13409 239 PTSYLDIRQRLNVARLIRELAEGK-YVLVVEHDLAVLDYLA-DNVHIAY 285
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-76 |
1.48e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 53.93 E-value: 1.48e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLsATLAGREDyEVVGGSVEFKGKDLLELSPEDRA 76
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTL-LSMISRLL-PPDSGEVLVDGLDVATTPSRELA 74
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-229 |
1.63e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.09 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 16 ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGR----------EDYeVVGGSVEFKGKDLLELSPE----DRAGEGIF 81
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDI-YIGDKKNNHELITNPYSKKiknfKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 82 MAFQYPveipgvSNQFFLQTALNAVRSyrGQESLDRFDFQDLMEEKIALLKM--PEDLLTRSvNVGFSGGEKKRNDILQM 159
Cdd:PRK13631 120 MVFQFP------EYQLFKDTIEKDIMF--GPVALGVKKSEAKKLAKFYLNKMglDDSYLERS-PFGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157083167 160 AVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH-YQRILDYikPDYVHVLYQGRIVKSGD 229
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHtMEHVLEV--ADEVIVMDKGKILKTGT 259
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-71 |
1.75e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 53.55 E-value: 1.75e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157083167 10 SVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKD--LLELS 71
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG--ILEPTSGRVEVNGRVsaLLELG 96
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-241 |
1.81e-08 |
|
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: 54.36 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 16 ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELspeDRAGEGIFMAF--QYPVEIPGV 93
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGF--FQARSGEILLNGFSLKDI---DRHTLRQFINYlpQEPYIFSGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 94 snqfFLQTALNAVRSYRGQESLDRFdfQDLMEEKIALLKMPEDLLTR--SVNVGFSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:TIGR01193 564 ----ILENLLLGAKENVSQDEIWAA--CEIAEIKDDIENMPLGYQTElsEEGSSISGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157083167 172 SDSGLD-IDALKIVAEGVNsLRDgkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGdfTLVKQLEEQGY 241
Cdd:TIGR01193 638 STSNLDtITEKKIVNNLLN-LQD--KTIIFVAH--RLSVAKQSDKIIVLDHGKIIEQG--SHDELLDRNGF 701
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-210 |
1.95e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 53.48 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAG--------REDYEVVGGSVEFKGKDLLELSp 72
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksaGSHIELLGRTVQREGRLARDIR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 73 EDRAGEG-IFMAFQY--------PVEIPGVSNQFFLQTAL---NAVRSYRGQESLDRFDFQDLMEEKIALLkmpedlltr 140
Cdd:PRK09984 83 KSRANTGyIFQQFNLvnrlsvleNVLIGALGSTPFWRTCFswfTREQKQRALQALTRVGMVHFAHQRVSTL--------- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 141 svnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQriLDY 210
Cdd:PRK09984 154 ------SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQ--VDY 215
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-203 |
3.08e-08 |
|
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: 52.50 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedyevvggSVEFKGKDLLELSPEDRAGEGIF 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGL--------SPPLAGRVLLNGGPLDFQRDSIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 82 MAFQYPVEIPGVsnqfflQTALNAVRSYRgqeSLDRFDFQDLMEEKIAL--LKMPEDLLTRSVnvgfSGGEKKRNDILQM 159
Cdd:cd03231 73 RGLLYLGHAPGI------KTTLSVLENLR---FWHADHSDEQVEEALARvgLNGFEDRPVAQL----SAGQQRRVALARL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 157083167 160 AVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH 203
Cdd:cd03231 140 LLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-228 |
4.40e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.32 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 23 DVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVVGGSVEFKGK--DLLELSPEDRAGEGIFMAFQYPVEI--PGVSNQFF 98
Cdd:PRK10261 346 DLWPGETLSLVGESGSGKSTTGRALL--RLVESQGGEIIFNGQriDTLSPGKLQALRRDIQFIFQDPYASldPRQTVGDS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 99 LQTALNAVRSYRGQESLDRFDFqdlMEEKIALLkmPEDLLTRSVNvgFSGGEKKRNDILQMAVLEPELCILDESDSGLDI 178
Cdd:PRK10261 424 IMEPLRVHGLLPGKAAAARVAW---LLERVGLL--PEHAWRYPHE--FSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 157083167 179 dalKIVAEGVNSLRDGKR----SFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:PRK10261 497 ---SIRGQIINLLLDLQRdfgiAYLFISHDMAVVERIS-HRVAVMYLGQIVEIG 546
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-225 |
4.40e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.17 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSV----EDKAILRGLDLDVRPGEVHAIMGPNGSGKS--TLSAT-LAGREDYEVVGGSVEFKGKDLLELS-P 72
Cdd:PRK15134 5 LLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvtALSILrLLPSPPVVYPSGDIRFHGESLLHASeQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 73 EDRA--GEGIFMAFQYP-VEIPGVSNqffLQTALNAVRS-YRGQ-------ESLDRFDFQDLMEEKIALLKMPEDLltrs 141
Cdd:PRK15134 85 TLRGvrGNKIAMIFQEPmVSLNPLHT---LEKQLYEVLSlHRGMrreaargEILNCLDRVGIRQAAKRLTDYPHQL---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 142 vnvgfSGGEKKRNDIlQMAVL-EPELCILDESDSGLDIdalKIVAEGVNSLRDGKR----SFIIVTHYQRILDYIKpDYV 216
Cdd:PRK15134 158 -----SGGERQRVMI-AMALLtRPELLIADEPTTALDV---SVQAQILQLLRELQQelnmGLLFITHNLSIVRKLA-DRV 227
|
....*....
gi 157083167 217 HVLYQGRIV 225
Cdd:PRK15134 228 AVMQNGRCV 236
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-205 |
4.90e-08 |
|
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: 51.48 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLdLD-----VRPGEVHAIMGPNGSGKSTLSATLAGREDYEVVGGSVEFKGKDLLElspedra 76
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRQL-LNnisgyVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRPLDK------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 77 gegifmAFQypvEIPGVSNQFFLQTALNAVRsyrgqESLdRFDfqdlmeekiALLKmpedlltrsvnvGFSGGEKKRNDI 156
Cdd:cd03232 76 ------NFQ---RSTGYVEQQDVHSPNLTVR-----EAL-RFS---------ALLR------------GLSVEQRKRLTI 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157083167 157 LQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSfIIVTHYQ 205
Cdd:cd03232 120 GVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQA-ILCTIHQ 167
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-87 |
5.13e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 52.60 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVED-KAILRGLD---LDVRPGEVHAIMGPNGSGKSTLSATLAG--REDYEVVGGSVEFKGKDLLELSPED 74
Cdd:COG4170 3 LLDIRNLTIEIDTpQGRVKAVDrvsLTLNEGEIRGLVGESGSGKSLIAKAICGitKDNWHVTADRFRWNGIDLLKLSPRE 82
|
90
....*....|....*.
gi 157083167 75 R---AGEGIFMAFQYP 87
Cdd:COG4170 83 RrkiIGREIAMIFQEP 98
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-229 |
6.02e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 51.95 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSatlagredYEVVG------GSVEFKGKDLLELSPED 74
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTF--------YMIVGlvkpdsGRIFLDGEDITHLPMHK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 75 RAGEGI------------------FMAfqypveipgvsnqfFLQTalnavRSYRGQESLDRFDfqDLMEE-KIA-LLKMP 134
Cdd:COG1137 75 RARLGIgylpqeasifrkltvednILA--------------VLEL-----RKLSKKEREERLE--ELLEEfGIThLRKSK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 135 EDLLtrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLD----IDALKIVAEgvnsLRD---GkrsfIIVT--HYQ 205
Cdd:COG1137 134 AYSL--------SGGERRRVEIARALATNPKFILLDEPFAGVDpiavADIQKIIRH----LKErgiG----VLITdhNVR 197
|
250 260
....*....|....*....|....
gi 157083167 206 RILDYIkpDYVHVLYQGRIVKSGD 229
Cdd:COG1137 198 ETLGIC--DRAYIISEGKVLAEGT 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-229 |
6.05e-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: 52.90 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVVGGSVEFKGKDLLELSPEDRAGEGI 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQYPVEIP--GVSNQFFLQTALnAVRSYRGQESLDRFDFQDLMEEkialLKMPEDLLTRSVNvGFSGGEKKRNDILQ 158
Cdd:TIGR02633 81 VIIHQELTLVPelSVAENIFLGNEI-TLPGGRMAYNAMYLRAKNLLRE----LQLDADNVTRPVG-DYGGGQQQLVEIAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157083167 159 MAVLEPELCILDESDSGLDIDALKIVaegVNSLRDGKRSFIIVTHYQRILDYIKP--DYVHVLYQGRIVKSGD 229
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEIL---LDIIRDLKAHGVACVYISHKLNEVKAvcDTICVIRDGQHVATKD 224
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-243 |
7.26e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.79 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 13 DKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLagREDYEVVGGSVEFKGKDLLELspedragegifmafqypveipg 92
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI--QRHFDVSEGDIRFHDIPLTKL---------------------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 93 vsnqfflqtALNAVRSYRGQESLDRFDFQDLMEEKIAL-----------------------LKMPEDLLTR--SVNVGFS 147
Cdd:PRK10789 383 ---------QLDSWRSRLAVVSQTPFLFSDTVANNIALgrpdatqqeiehvarlasvhddiLRLPQGYDTEvgERGVMLS 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKS 227
Cdd:PRK10789 454 GGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG-RTVIISAH--RLSALTEASEILVMQHGHIAQR 530
|
250
....*....|....*.
gi 157083167 228 GDftlVKQLEEQGyGW 243
Cdd:PRK10789 531 GN---HDQLAQQS-GW 542
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-180 |
7.46e-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: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVED-KAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGredyevvggsvefkgkdlleLSPedrAGEG 79
Cdd:COG4178 362 ALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG--------------------LWP---YGSG 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 80 IfmafqypVEIPGVSNQFFL-QtalnavRSYRGQESL----------DRFDFQDLME--EKIALlkmpEDLLTRsVNVG- 145
Cdd:COG4178 419 R-------IARPAGARVLFLpQ------RPYLPLGTLreallypataEAFSDAELREalEAVGL----GHLAER-LDEEa 480
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 157083167 146 -----FSGGEKKRndiLQMA---VLEPELCILDESDSGLDIDA 180
Cdd:COG4178 481 dwdqvLSLGEQQR---LAFArllLHKPDWLFLDEATSALDEEN 520
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
16-177 |
8.80e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 52.01 E-value: 8.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 16 ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLLELSPEDRAGEGIFMAFQYPVEIPGVSN 95
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT--SGHIRFHGTDVSRLHARDRKVGFVFQHYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 96 QFFLQTALnavrsyrgqESLDRFDFQDLMEEKIALLKMPEdlLTRSVN---VGFSGGEKKRNDILQMAVLEPELCILDES 172
Cdd:PRK10851 95 IAFGLTVL---------PRRERPNAAAIKAKVTQLLEMVQ--LAHLADrypAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
....*
gi 157083167 173 DSGLD 177
Cdd:PRK10851 164 FGALD 168
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-203 |
9.68e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 51.71 E-value: 9.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDY---EVVGGSVEFKGKDLL--ELSP-EDR 75
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgFRVEGKVTFHGKNLYapDVDPvEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 76 AGEGifMAFQYPVEIPgvsNQFFLQTALNA-VRSYRGqesldrfDFQDLMEEKI---ALLKMPEDLLTRSvNVGFSGGEK 151
Cdd:PRK14243 91 RRIG--MVFQKPNPFP---KSIYDNIAYGArINGYKG-------DMDELVERSLrqaALWDEVKDKLKQS-GLSLSGGQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 157083167 152 KRNDILQMAVLEPELCILDESDSGLD-IDALKIvAEGVNSLRDgKRSFIIVTH 203
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDpISTLRI-EELMHELKE-QYTIIIVTH 208
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
16-229 |
1.00e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 51.17 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 16 ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRE-----DYEVVGGSVEFKG----KDLLELspedRAGEGifMAFQ- 85
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEmprsgTLNIAGNHFDFSKtpsdKAIREL----RRNVG--MVFQq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 86 Y---------------PVEIPGVSNQFFLQTALNAVRSYRGQESLDRFDFQdlmeekiallkmpedlltrsvnvgFSGGE 150
Cdd:PRK11124 91 YnlwphltvqqnlieaPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLH------------------------LSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 151 KKRNDILQMAVLEPELCILDESDSGLDIDalkIVAEGVNSLRDGKRSFI---IVTHYqriLDYIKPDYVHVLY--QGRIV 225
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPE---ITAQIVSIIRELAETGItqvIVTHE---VEVARKTASRVVYmeNGHIV 220
|
....
gi 157083167 226 KSGD 229
Cdd:PRK11124 221 EQGD 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-65 |
1.18e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 1.18e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGK 65
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSG--NYQPDAGSILIDGQ 66
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-228 |
1.31e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.34 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVED--KAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAG------REDYEVVGGSVEFKGKDLLELspE 73
Cdd:PRK13640 6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddNPNSKITVDGITLTAKTVWDI--R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 74 DRAGegifMAFQYPveipgvSNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKR 153
Cdd:PRK13640 84 EKVG----IVFQNP------DNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANL--SGGQKQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157083167 154 NDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFII-VTHyqRILDYIKPDYVHVLYQGRIVKSG 228
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVIsITH--DIDEANMADQVLVLDDGKLLAQG 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-229 |
1.44e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.63 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVS-----------VEDKAILRGLDLDVRPGEVHAIMGPNGSGKST----LSATLAGRedyevvgGSVEFKGK 65
Cdd:PRK15134 275 LLDVEQLQVAfpirkgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-------GEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 66 DLLELS-----PEDRAgegIFMAFQYPveipgvsnqfflQTALNAvrsyrgqesldRFDFQDLMEEKIA----------- 129
Cdd:PRK15134 348 PLHNLNrrqllPVRHR---IQVVFQDP------------NSSLNP-----------RLNVLQIIEEGLRvhqptlsaaqr 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 130 ----LLKMPE---DLLTRSVNVG-FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKR-SFII 200
Cdd:PRK15134 402 eqqvIAVMEEvglDPETRHRYPAeFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLF 481
|
250 260
....*....|....*....|....*....
gi 157083167 201 VTHYQRILDYIkPDYVHVLYQGRIVKSGD 229
Cdd:PRK15134 482 ISHDLHVVRAL-CHQVIVLRQGEVVEQGD 509
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
14-229 |
1.81e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.12 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 14 KAiLRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRAG--EGIFMAFQYP---- 87
Cdd:PRK11308 29 KA-LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIE--TPTGGELYYQGQDLLKADPEAQKLlrQKIQIVFQNPygsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 88 ---------VEIPGVSNqfflqTALNAV-RSYRGQEsldrfdfqdlMEEKIALlkMPEDLlTRSVNVgFSGGEKKRNDIL 157
Cdd:PRK11308 106 nprkkvgqiLEEPLLIN-----TSLSAAeRREKALA----------MMAKVGL--RPEHY-DRYPHM-FSGGQRQRIAIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157083167 158 QMAVLEPELCILDESDSGLDIdalKIVAEGVNSLRDGKR----SFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGD 229
Cdd:PRK11308 167 RALMLDPDVVVADEPVSALDV---SVQAQVLNLMMDLQQelglSYVFISHDLSVVEHIA-DEVMVMYLGRCVEKGT 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-82 |
1.84e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.17 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVsvedKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDL------------L 68
Cdd:COG1129 256 VLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGAD--PADSGEIRLDGKPVrirsprdairagI 329
|
90
....*....|....
gi 157083167 69 ELSPEDRAGEGIFM 82
Cdd:COG1129 330 AYVPEDRKGEGLVL 343
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
12-240 |
2.28e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.47 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 12 EDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLS----ATLAGREdyevvgGSVEFKGKDLLELSP----EDRAGegifMA 83
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAkhmnALLIPSE------GKVYVDGLDTSDEENlwdiRNKAG----MV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 84 FQYPveipgvSNQFF--------------LQTALNAVRSyRGQESLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGG 149
Cdd:PRK13633 91 FQNP------DNQIVativeedvafgpenLGIPPEEIRE-RVDESLKKVGMYEYRRHAPHLL---------------SGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKivaEGVNSLRDGKRSF----IIVTHYQRilDYIKPDYVHVLYQGRIV 225
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR---EVVNTIKELNKKYgitiILITHYME--EAVEADRIIVMDSGKVV 223
|
250
....*....|....*....
gi 157083167 226 KSGD----FTLVKQLEEQG 240
Cdd:PRK13633 224 MEGTpkeiFKEVEMMKKIG 242
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-226 |
2.47e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.60 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 18 RGLD---LDVRPGEVHAIMGPNGSGKSTL-----SATLAGREDYEVVGGSV--EFKGKDLLELSPEdragegIFMAFQYP 87
Cdd:PRK13641 21 KGLDnisFELEEGSFVALVGHTGSGKSTLmqhfnALLKPSSGTITIAGYHItpETGNKNLKKLRKK------VSLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 88 veipgvSNQFFLQTALNAVRSyrGQESldrFDFQDlMEEKIALLK------MPEDLLTRSvNVGFSGGEKKRNDILQMAV 161
Cdd:PRK13641 95 ------EAQLFENTVLKDVEF--GPKN---FGFSE-DEAKEKALKwlkkvgLSEDLISKS-PFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157083167 162 LEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH-YQRILDYikPDYVHVLYQGRIVK 226
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHnMDDVAEY--ADDVLVLEHGKLIK 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-229 |
2.62e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 50.35 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELspEDRAGE--- 78
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLE--KPSEGSIVVNGQTINLV--RDKDGQlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 79 -----------GIFMAFQY----------------PVEIPGVSNQfflqtalnaVRSYRGQESLDRFDFQDLmeekiALL 131
Cdd:PRK10619 82 adknqlrllrtRLTMVFQHfnlwshmtvlenvmeaPIQVLGLSKQ---------EARERAVKYLAKVGIDER-----AQG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 132 KMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDYI 211
Cdd:PRK10619 148 KYPVHL---------SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHV 218
|
250
....*....|....*...
gi 157083167 212 KpDYVHVLYQGRIVKSGD 229
Cdd:PRK10619 219 S-SHVIFLHQGKIEEEGA 235
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-223 |
3.10e-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: 49.39 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 8 QVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKdllelspedragegifMAFqyp 87
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG--ELEKLSGSVSVPGS----------------IAY--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 88 veipgVSNQFFLQTAlnavrSYR-----GQEsldrFDFQDLME--EKIALLK----MPEDLLT----RSVNVgfSGGEKK 152
Cdd:cd03250 71 -----VSQEPWIQNG-----TIRenilfGKP----FDEERYEKviKACALEPdleiLPDGDLTeigeKGINL--SGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157083167 153 RndI-LQMAVL-EPELCILDESDSGLDID-ALKIVAEGVNSLRDGKRSFIIVTHYqriLDYIKP-DYVHVLYQGR 223
Cdd:cd03250 135 R--IsLARAVYsDADIYLLDDPLSAVDAHvGRHIFENCILGLLLNNKTRILVTHQ---LQLLPHaDQIVVLDNGR 204
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
12-207 |
3.83e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.61 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 12 EDK-AILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVVGGSVEFKG-----------------KDLleLSPE 73
Cdd:PLN03140 890 EDRlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGfpkkqetfarisgyceqNDI--HSPQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 74 DRAGEG-IFMAF-QYPVEipgVSNQfflqtalnavrsyrgqeslDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEK 151
Cdd:PLN03140 968 VTVRESlIYSAFlRLPKE---VSKE-------------------EKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQR 1025
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 157083167 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRI 207
Cdd:PLN03140 1026 KRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
12-224 |
3.92e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 49.73 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 12 EDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLLELSPEDRAGEgIFMAFQYPveip 91
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE--SGQIIIDGDLLTEENVWDIRHK-IGMVFQNP---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 92 gvSNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMpEDLLTRSvNVGFSGGEKKRNDILQMAVLEPELCILDE 171
Cdd:PRK13650 91 --DNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGM-QDFKERE-PARLSGGQKQRVAIAGAVAMRPKIIILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 157083167 172 SDSGLDIDALKIVAEGVNSLRDGKRSFII-VTHYqriLDYIK-PDYVHVLYQGRI 224
Cdd:PRK13650 167 ATSMLDPEGRLELIKTIKGIRDDYQMTVIsITHD---LDEVAlSDRVLVMKNGQV 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-203 |
5.15e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 49.04 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 16 ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRA---GEGIFMAFQYPVEIPG 92
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLD--TPTSGDVIFNGQPMSKLSSAAKAelrNQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 93 VsnqfflqTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDILQMAVLEPELCILDES 172
Cdd:PRK11629 102 F-------TALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSEL--SGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|...
gi 157083167 173 DSGLDIDALKIVAEGVNSL--RDGKrSFIIVTH 203
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELnrLQGT-AFLVVTH 204
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-229 |
5.22e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.24 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDK----AILRGLDLDVRPGEVHAIMGPNGSGKSTlsATLAGREDYEVVGGSVEF-------KGKDLLE 69
Cdd:PRK10261 12 VLAVENLNIAFMQEqqkiAAVRNLSFSLQRGETLAIVGESGSGKSV--TALALMRLLEQAGGLVQCdkmllrrRSRQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 70 LSPEDRA------GEGIFMAFQYPVeipgvsnqfflqTALNAV--------RSYRGQESLDRFDFQDLMEEKIALLKMPE 135
Cdd:PRK10261 90 LSEQSAAqmrhvrGADMAMIFQEPM------------TSLNPVftvgeqiaESIRLHQGASREEAMVEAKRMLDQVRIPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 136 --DLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSL-RDGKRSFIIVTHYQRILDYIK 212
Cdd:PRK10261 158 aqTILSRYPH-QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIA 236
|
250
....*....|....*..
gi 157083167 213 pDYVHVLYQGRIVKSGD 229
Cdd:PRK10261 237 -DRVLVMYQGEAVETGS 252
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
12-242 |
5.36e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 49.28 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 12 EDKAiLRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDL----LELSpEDRAGEGIfmAFQYP 87
Cdd:PRK13637 19 EKKA-LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGL--LKPTSGKIIIDGVDItdkkVKLS-DIRKKVGL--VFQYP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 88 veipgvSNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMP-EDLLTRSvNVGFSGGEKKRNDILQMAVLEPEL 166
Cdd:PRK13637 93 ------EYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKS-PFELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 167 CILDESDSGLDIDALKIVAEGVNSLRDG-KRSFIIVTHYQRilDYIK-PDYVHVLYQGRIVKSGD----FTLVKQLEEQG 240
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSME--DVAKlADRIIVMNKGKCELQGTprevFKEVETLESIG 243
|
..
gi 157083167 241 YG 242
Cdd:PRK13637 244 LA 245
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-65 |
1.16e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 1.16e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 157083167 14 KAiLRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVVGGSVEFKGK 65
Cdd:NF040905 15 KA-LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEILFDGE 65
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-228 |
1.21e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.47 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTL------------SATLAGreDYEVVGGSVefKGKDLLELSPEdragegIFMAF 84
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMiqltngliisetGQTIVG--DYAIPANLK--KIKEVKRLRKE------IGLVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 85 QYPveipgvSNQFFLQTALNAVRSYRGQESLDRFDFQDLMEEKIALLKMPEDLLTRSvNVGFSGGEKKRNDILQMAVLEP 164
Cdd:PRK13645 97 QFP------EYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRS-PFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157083167 165 ELCILDESDSGLDIDALKIVAEGVNSL-RDGKRSFIIVTH-YQRILDYikPDYVHVLYQGRIVKSG 228
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHnMDQVLRI--ADEVIVMHEGKVISIG 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-67 |
1.55e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.39 E-value: 1.55e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVVGGSVEFKGKDL 67
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEEL 71
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-43 |
2.61e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 2.61e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 157083167 4 IKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTL 43
Cdd:PRK10938 263 LNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTL 302
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-85 |
2.62e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 2.62e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPEDRAGEGIFMAFQ 85
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGI--YQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-80 |
2.83e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 7 LQVSVEDKAI-----LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPED--RAGEG 79
Cdd:PRK10762 5 LQLKGIDKAFpgvkaLSGAALNVYPGRVMALVGENGAGKSTMMKVLTGI--YTRDAGSILYLGKEVTFNGPKSsqEAGIG 82
|
.
gi 157083167 80 I 80
Cdd:PRK10762 83 I 83
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-241 |
3.51e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 46.80 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKDLLELSPEDRAGEGI 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG--DPRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMafqypveIPGVSNQFFLQTAlnavrsyrgQESL-------DRFDFQDLMEEKIALLkmPEDLLTRSVNVG-FSGGEKK 152
Cdd:PRK11614 83 AI-------VPEGRRVFSRMTV---------EENLamggffaERDQFQERIKWVYELF--PRLHERRIQRAGtMSGGEQQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLR-DGKRSFIIVTHYQRILDYikPDYVHVLYQGRIV--KSGD 229
Cdd:PRK11614 145 MLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLReQGMTIFLVEQNANQALKL--ADRGYVLENGHVVleDTGD 222
|
250
....*....|..
gi 157083167 230 FTLVKQLEEQGY 241
Cdd:PRK11614 223 ALLANEAVRSAY 234
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-243 |
4.97e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 47.13 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKA--ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAgREdYEVVGGSVEFKGKDLLELSPED-RAGe 78
Cdd:PRK11160 339 LTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-RA-WDPQQGEILLNGQPIADYSEAAlRQA- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 79 gifMAFqypveipgVSNQ--FF-------LQTALNAVRSYRGQESLDRFDFQDLMEEKIALlkmpeDLLTRSVNVGFSGG 149
Cdd:PRK11160 416 ---ISV--------VSQRvhLFsatlrdnLLLAAPNASDEALIEVLQQVGLEKLLEDDKGL-----NAWLGEGGRQLSGG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 150 EKKRNDILQmAVLEP-ELCILDESDSGLD-------IDALKIVAEGvnslrdgkRSFIIVTHYQRILDYIkpDYVHVLYQ 221
Cdd:PRK11160 480 EQRRLGIAR-ALLHDaPLLLLDEPTEGLDaeterqiLELLAEHAQN--------KTVLMITHRLTGLEQF--DRICVMDN 548
|
250 260
....*....|....*....|..
gi 157083167 222 GRIVKSGDFTLVkqLEEQGYGW 243
Cdd:PRK11160 549 GQIIEQGTHQEL--LAQQGRYY 568
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-203 |
5.91e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.03 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 12 EDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLaGREDyEVVGGSVEFKGKDLLELSPEDRAG---EGIFMAFQ--- 85
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLD-KPTSGTYRVAGQDVATLDADALAQlrrEHFGFIFQryh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 86 --------YPVEIPGVsnqfFLQTALNAvRSYRGQESLDRFDFQDLMEEKiallkmPEDLltrsvnvgfSGGEKKRNDIL 157
Cdd:PRK10535 97 llshltaaQNVEVPAV----YAGLERKQ-RLLRAQELLQRLGLEDRVEYQ------PSQL---------SGGQQQRVSIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 157083167 158 QMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH 203
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-60 |
8.42e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 8.42e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSV 60
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG--ELEPDSGTV 376
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-211 |
1.15e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 24 VRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKgkdlLELS--PedragegifmafQYPVEIPGVSNQFFLQT 101
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVL--KPDEGEVDPE----LKISykP------------QYIKPDYDGTVEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 102 ALNAVR-SYRGQESLDRFDFQDLMEEKIallkmpEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDA 180
Cdd:PRK13409 424 ITDDLGsSYYKSEIIKPLQLERLLDKNV------KDL---------SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 488
|
170 180 190
....*....|....*....|....*....|..
gi 157083167 181 LKIVAEGVNSLRDGKR-SFIIVTHYQRILDYI 211
Cdd:PRK13409 489 RLAVAKAIRRIAEEREaTALVVDHDIYMIDYI 520
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
144-209 |
1.71e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 1.71e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 144 VGFSGGEKKRND---ILQMAVLEPE-LCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILD 209
Cdd:cd03227 76 LQLSGGEKELSAlalILALASLKPRpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAE 145
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-177 |
1.78e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 44.69 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKdllelsPEDRAGEGI 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ--HGSITLDGK------PVEGPGAER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 FMAFQYPVEIPGVSNQ----FFLQTA--LNAVRSYRGQESLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRN 154
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQdnvaFGLQLAgvEKMQRLEIAHQMLKKVGLEGAEKRYIWQL---------------SGGQRQRV 137
|
170 180
....*....|....*....|...
gi 157083167 155 DILQMAVLEPELCILDESDSGLD 177
Cdd:PRK11248 138 GIARALAANPQLLLLDEPFGALD 160
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
2-203 |
1.90e-05 |
|
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: 44.18 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAI-LRGLDLDvrpgEVHAIMGPNGSGKSTL--SATLA-----GREDYEVVGGSVEFKGKDLLELSPE 73
Cdd:cd03279 6 LELKNFGPFREEQVIdFTGLDNN----GLFLICGPTGAGKSTIldAITYAlygktPRYGRQENLRSVFAPGEDTAEVSFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 74 DRAGEGIFMAFQYPveipGVSNQFFLQTALNAvrsyrgQESLDRFdfqdlmeekiallkmpedlLTRSVNvGFSGGEKKR 153
Cdd:cd03279 82 FQLGGKKYRVERSR----GLDYDQFTRIVLLP------QGEFDRF-------------------LARPVS-TLSGGETFL 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 154 NDI-LQMAVLEP---------ELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH 203
Cdd:cd03279 132 ASLsLALALSEVlqnrggarlEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISH 191
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
14-87 |
2.08e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.79 E-value: 2.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157083167 14 KAILRgLDLDVRPGEVHAIMGPNGSGKSTLSATLAG--REDYEVVGGSVEFKGKDLLELSPEDR---AGEGIFMAFQYP 87
Cdd:PRK15093 21 KAVDR-VSMTLTEGEIRGLVGESGSGKSLIAKAICGvtKDNWRVTADRMRFDDIDLLRLSPRERrklVGHNVSMIFQEP 98
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-85 |
3.08e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 43.80 E-value: 3.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157083167 21 DLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLLELSPEDRAgegIFMAFQ 85
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPA--SGSLTLNGQDHTTTPPSRRP---VSMLFQ 78
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-209 |
3.15e-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: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 13 DKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDyevvggsvEFKGkdllelspEDRAGEGIFMAF--QYPVEI 90
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK--------DFNG--------EARPQPGIKVGYlpQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 91 P----------GVSNQFFLQTALNAVRSYRGQESLdrfDFQDLMEEKIAL---------------LKMPEDLL-----TR 140
Cdd:TIGR03719 81 PtktvrenveeGVAEIKDALDRFNEISAKYAEPDA---DFDKLAAEQAELqeiidaadawdldsqLEIAMDALrcppwDA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157083167 141 SVNVgFSGGEKKRNDILQMAVLEPELCILDESDSGLDidalkivAEGV----NSLRDGKRSFIIVTHYQRILD 209
Cdd:TIGR03719 158 DVTK-LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD-------AESVawleRHLQEYPGTVVAVTHDRYFLD 222
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-228 |
3.97e-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: 43.25 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVED--KAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKDLLELSPED-RAge 78
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRL--VELSSGSILIDGVDISKIGLHDlRS-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 79 giFMAF--QYPVEIPGvsnqfflqtalnAVRsyrgqESLDRFDFQDlmEEKI-----------ALLKMPEDLLTRSVNVG 145
Cdd:cd03244 79 --RISIipQDPVLFSG------------TIR-----SNLDPFGEYS--DEELwqalervglkeFVESLPGGLDTVVEEGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 146 --FSGGEK----------KRNDILqmavlepelcILDESDSGLDIDALKIVAEGVNSLRDGkRSFIIVTHyqR---ILDY 210
Cdd:cd03244 138 enLSVGQRqllclarallRKSKIL----------VLDEATASVDPETDALIQKTIREAFKD-CTVLTIAH--RldtIIDS 204
|
250
....*....|....*...
gi 157083167 211 ikpDYVHVLYQGRIVKSG 228
Cdd:cd03244 205 ---DRILVLDKGRVVEFD 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-211 |
5.27e-05 |
|
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: 44.00 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 22 LDVRPGEVH-----AIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKgkdlLELS--PedragegifmafQYPVEIPGVS 94
Cdd:COG1245 356 LEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVL--KPDEGEVDED----LKISykP------------QYISPDYDGT 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 95 NQFFLQTALNAV--RSYRGQESLDRFDFQDLMEEKIallkmpEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILDES 172
Cdd:COG1245 418 VEEFLRSANTDDfgSSYYKTEIIKPLGLEKLLDKNV------KDL---------SGGELQRVAIAACLSRDADLYLLDEP 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 157083167 173 DSGLDID-------ALKIVAEGvnslrdGKRSFIIVTHYQRILDYI 211
Cdd:COG1245 483 SAHLDVEqrlavakAIRRFAEN------RGKTAMVVDHDIYLIDYI 522
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-229 |
6.12e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 43.15 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVeDKAILRGLDLDVRPGEVHAIMGPNGSGKS-TLSATL----AGredYEVVGGSVEFKGKdllELSPEDRA 76
Cdd:PRK10418 5 IELRNIALQA-AQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAG---VRQTAGRVLLDGK---PVAPCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 77 GEGIFMAFQYPveipgvsnqfflQTALNAVRSYR--GQESL-------DRFDFQDLMEEkiALLKMPEDLLtRSVNVGFS 147
Cdd:PRK10418 78 GRKIATIMQNP------------RSAFNPLHTMHthARETClalgkpaDDATLTAALEA--VGLENAARVL-KLYPFEMS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 148 GGEKKRNDIlQMAVL-EPELCILDESDSGLDIDA----LKIVAEGVnslRDGKRSFIIVTHYQRILDYIKpDYVHVLYQG 222
Cdd:PRK10418 143 GGMLQRMMI-ALALLcEAPFIIADEPTTDLDVVAqariLDLLESIV---QKRALGMLLVTHDMGVVARLA-DDVAVMSHG 217
|
....*..
gi 157083167 223 RIVKSGD 229
Cdd:PRK10418 218 RIVEQGD 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-239 |
6.64e-05 |
|
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: 43.66 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 24 VRPGEVHAIMGPNGSGKSTLSATLAGRedYE-VVGGSVEFKGKDL------------LELSPEDRAGEGIfmafqypVEI 90
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALFGA--YPgKFEGNVFINGKPVdirnpaqairagIAMVPEDRKRHGI-------VPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 91 PGVSNQFflqtALNAVRSYRGQESLDRFDFQDLMEEKIALLKM----PEDLLTRsvnvgFSGGEKKRNDILQMAVLEPEL 166
Cdd:TIGR02633 354 LGVGKNI----TLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVktasPFLPIGR-----LSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157083167 167 CILDESDSGLDIDALKIVAEGVNSL-RDGKRSFIIVTHYQRILDYikPDYVHVLYQGRIvkSGDFTLVKQLEEQ 239
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGL--SDRVLVIGEGKL--KGDFVNHALTQEQ 494
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-211 |
6.86e-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: 43.39 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFkgKDLLELSPEDRAGEGIF 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQE--QPDSGTIEI--GETVKLAYVDQSRDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 82 MAFQYPVEIPGVSNQFFLQTALNAVRSYRGqesldRFDFQDLMEEKiallkmpedlltrsvNVG-FSGGEKKRndiLQMA 160
Cdd:TIGR03719 399 PNKTVWEEISGGLDIIKLGKREIPSRAYVG-----RFNFKGSDQQK---------------KVGqLSGGERNR---VHLA 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 157083167 161 VLEPE---LCILDESDSGLDIDALKivaegvnSLRDGKRSF----IIVTHYQRILDYI 211
Cdd:TIGR03719 456 KTLKSggnVLLLDEPTNDLDVETLR-------ALEEALLNFagcaVVISHDRWFLDRI 506
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
17-85 |
7.22e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 43.25 E-value: 7.22e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPED--RAGEGIFMAFQ 85
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLE--RPTSGRVLVDGQDLTALSEKElrKARRQIGMIFQ 89
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-76 |
8.70e-05 |
|
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: 43.25 E-value: 8.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 157083167 20 LDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKdllELSPEDRA 76
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGL--YRPESGEILLDGQ---PVTADNRE 402
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-216 |
9.62e-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: 42.40 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 23 DVRPGEVHAIMGPNGSGKSTLSATLAGR-----EDYEVVGGSVEFKGKdllELSPEDragEGIFMAFQYPVeIPGVSNQF 97
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVlkpdeGDIEIELDTVSYKPQ---YIKADY---EGTVRDLLSSI-TKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 98 FLQTalnavrsyrgqesldrfdfqdlmeEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESDSGLD 177
Cdd:cd03237 94 YFKT------------------------EIAKPLQI-EQILDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 157083167 178 IDALKIVAEGVNSLRD-GKRSFIIVTHyqrilDYIKPDYV 216
Cdd:cd03237 148 VEQRLMASKVIRRFAEnNEKTAFVVEH-----DIIMIDYL 182
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-43 |
1.03e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 42.41 E-value: 1.03e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTL 43
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTL 46
|
|
| 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 157083167 14 KAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLagREDYEVVGGSVEFKGKDLLELSP-EDRAGEGifmafqYPVEIPG 92
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI--NRLIEPTSGEIFIDGEDIREQDPvELRRKIG------YVIQQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 93 VSNQFFLQTALNAVRSYRGQESLDRfdfQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDES 172
Cdd:cd03295 86 LFPHMTVEENIALVPKLLKWPKEKI---RERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 157083167 173 DSGLD-IDALKIVAEGVNSLRDGKRSFIIVTHyqRILDYIK-PDYVHVLYQGRIVKSG 228
Cdd:cd03295 163 FGALDpITRDQLQEEFKRLQQELGKTIVFVTH--DIDEAFRlADRIAIMKNGEIVQVG 218
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-248 |
1.73e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 13 DKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEF-KGKDL-------LELSpedRAGEGifmAF 84
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--ELAPVSGEIGLaKGIKLgyfaqhqLEFL---RADES---PL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 85 QYPVEI-PGVSNQfflqtalnAVRSYRGQesldrFDFQ-DLMEEKIALlkmpedlltrsvnvgFSGGEKKRNDILQMAVL 162
Cdd:PRK10636 396 QHLARLaPQELEQ--------KLRDYLGG-----FGFQgDKVTEETRR---------------FSGGEKARLVLALIVWQ 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 163 EPELCILDESDSGLDIDALKIVAEgvnSLRDGKRSFIIVTHyQRILDYIKPDYVHVLYQGRI-VKSGDFTLVKQleeqgy 241
Cdd:PRK10636 448 RPNLLLLDEPTNHLDLDMRQALTE---ALIDFEGALVVVSH-DRHLLRSTTDDLYLVHDGKVePFDGDLEDYQQ------ 517
|
....*..
gi 157083167 242 gWLTEQQ 248
Cdd:PRK10636 518 -WLSDVQ 523
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-228 |
1.76e-04 |
|
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: 41.24 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 16 ILRGLDLDVRPGEVHAIMGPNGSGKSTLsaTLAGREDYEVVGGSVEFKGKDLLELSPED-RAGEGIFMafQYPVEIPGvs 94
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLEAEEGKIEIDGIDISTIPLEDlRSSLTIIP--QDPTLFSG-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 95 nqfflqtalnAVRSyrgqeSLDRFDFQDlmEEKI-ALLKMPEDLLTrsvnvgFSGGEKKRNDILQMAVLEPELCILDESD 173
Cdd:cd03369 97 ----------TIRS-----NLDPFDEYS--DEEIyGALRVSEGGLN------LSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 157083167 174 SGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDYikpDYVHVLYQGRIVKSG 228
Cdd:cd03369 154 ASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDY---DKILVMDAGEVKEYD 205
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-80 |
1.91e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.96 E-value: 1.91e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157083167 18 RGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRAGEGI 80
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLR--PARGGRIMLNGKEINALSTAQRLARGL 340
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-51 |
2.04e-04 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 41.59 E-value: 2.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRE 51
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLE 62
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
143-219 |
2.49e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 143 NVG-----FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRD-GKRSFIIVTHyqRILDYIKPDYV 216
Cdd:PTZ00265 1351 NVGpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkADKTIITIAH--RIASIKRSDKI 1428
|
...
gi 157083167 217 HVL 219
Cdd:PTZ00265 1429 VVF 1431
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-248 |
2.57e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGK-DLLELSPEDRAGEg 79
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKN--EISADGGSYTFPGNwQLAWVNQETPALP- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 80 iFMAFQYPVEIPGVSNQF--FLQTAL-----NAVRSYRGQesLDRFDFQDLMEEKIALLK---MPEDLLTRSVNvGFSGG 149
Cdd:PRK10636 78 -QPALEYVIDGDREYRQLeaQLHDANerndgHAIATIHGK--LDAIDAWTIRSRAASLLHglgFSNEQLERPVS-DFSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALkIVAEgvNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGD 229
Cdd:PRK10636 154 WRMRLNLAQALICRSDLLLLDEPTNHLDLDAV-IWLE--KWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGN 230
|
250
....*....|....*....
gi 157083167 230 FTlvkQLEEQGYGWLTEQQ 248
Cdd:PRK10636 231 YS---SFEVQRATRLAQQQ 246
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-188 |
2.71e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.01 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVVGGSVEFKGKDLLELSPEDRA--GEGIFMAFQ--------- 85
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIE--RPSAGKIWFSGHDITRLKNREVPflRRQIGMIFQdhhllmdrt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 86 ------YPVEIPGVSNQfflqtalnAVRSyRGQESLDrfdfqdlmeeKIALLKMpedllTRSVNVGFSGGEKKRNDILQM 159
Cdd:PRK10908 96 vydnvaIPLIIAGASGD--------DIRR-RVSAALD----------KVGLLDK-----AKNFPIQLSGGEQQRVGIARA 151
|
170 180
....*....|....*....|....*....
gi 157083167 160 AVLEPELCILDESDSGLDiDALkivAEGV 188
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLD-DAL---SEGI 176
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
123-216 |
2.88e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 123 LMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGK-RSFIIV 201
Cdd:PTZ00265 557 LIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEnRITIII 636
|
90
....*....|....*
gi 157083167 202 THYQRILDYIKPDYV 216
Cdd:PTZ00265 637 AHRLSTIRYANTIFV 651
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
24-228 |
2.91e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 41.31 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 24 VRPGEVHAIMGPNGSGKSTLSATLAgredyevvgGSVEFKGKDLL----ELSPEDRA--GEGIFMAFQYPveipgvsnqf 97
Cdd:PRK15112 36 LREGQTLAIIGENGSGKSTLAKMLA---------GMIEPTSGELLiddhPLHFGDYSyrSQRIRMIFQDP---------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 98 flQTALNAvRSYRGQeSLD-------RFDFQDLMEEKIALLKMPeDLLTRSVNV---GFSGGEKKRNDILQMAVLEPELC 167
Cdd:PRK15112 97 --STSLNP-RQRISQ-ILDfplrlntDLEPEQREKQIIETLRQV-GLLPDHASYyphMLAPGQKQRLGLARALILRPKVI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157083167 168 ILDESDSGLDIDALKIVAEGVNSLRDGKR-SFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
Cdd:PRK15112 172 IADEALASLDMSMRSQLINLMLELQEKQGiSYIYVTQHLGMMKHIS-DQVLVMHQGEVVERG 232
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-171 |
3.49e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.50 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 2 LSIKDLQVSVEDKAILRG-LDLDVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVVGGSVEFKGKdllELSPEDRAgegi 80
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEILLDGK---PVTAEQPE---- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 fmafQYPVEIPGVSNQFFLQTAL-----NAVRSYRGQESLDRFDfqdlMEEKIALlkmpEDLltRSVNVGFSGGEKKRND 155
Cdd:PRK10522 394 ----DYRKLFSAVFTDFHLFDQLlgpegKPANPALVEKWLERLK----MAHKLEL----EDG--RISNLKLSKGQKKRLA 459
|
170
....*....|....*..
gi 157083167 156 ILqMAVLEP-ELCILDE 171
Cdd:PRK10522 460 LL-LALAEErDILLLDE 475
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-239 |
3.54e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGredyevvggsvefkgkDLLELSPEDRAGegi 80
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAG----------------ELPLLSGERQSQ--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 81 fmaFQYPVEIPgvsnqfF--LQTALNAV--RSYRGQESLDRFDF--------QD------LMEEKIALLKMpEDLLTRSV 142
Cdd:PRK10938 64 ---FSHITRLS------FeqLQKLVSDEwqRNNTDMLSPGEDDTgrttaeiiQDevkdpaRCEQLAQQFGI-TALLDRRF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 143 NVgFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFI-IVTHYQRILDYIkpDYVHVLyq 221
Cdd:PRK10938 134 KY-LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDFV--QFAGVL-- 208
|
250
....*....|....*...
gi 157083167 222 grivksGDFTLVKQLEEQ 239
Cdd:PRK10938 209 ------ADCTLAETGERE 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-177 |
3.81e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 40.90 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 1 MLSIKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvvGGSVEFKGKDLLELSPED--RAGE 78
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD--HGEILFDGENIPAMSRSRlyTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 79 GIFMAFQ---------------YPV----EIPGVSNQFFLQTALNAVrSYRGQESLdrfdfqdlmeekiallkMPEDLlt 139
Cdd:PRK11831 85 RMSMLFQsgalftdmnvfdnvaYPLrehtQLPAPLLHSTVMMKLEAV-GLRGAAKL-----------------MPSEL-- 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 157083167 140 rsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLD 177
Cdd:PRK11831 145 -------SGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
29-63 |
4.20e-04 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 39.60 E-value: 4.20e-04
10 20 30
....*....|....*....|....*....|....*
gi 157083167 29 VHAIMGPNGSGKSTLSATLAGREDYEVVGGSVEFK 63
Cdd:pfam13671 1 LILLVGLPGSGKSTLARRLLEELGAVRLSSDDERK 35
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-229 |
5.06e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 11 VEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVefkgkdLLELSpedragegifmafqypveI 90
Cdd:PTZ00243 670 LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS--QFEISEGRV------WAERS------------------I 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 91 PGVSNQFFLQTAlnAVRS---YRGQEslDRFDFQDL-----MEEKIALLK--MPEDLLTRSVNVgfSGGEKKRNDILQMA 160
Cdd:PTZ00243 724 AYVPQQAWIMNA--TVRGnilFFDEE--DAARLADAvrvsqLEADLAQLGggLETEIGEKGVNL--SGGQKARVSLARAV 797
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157083167 161 VLEPELCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDyiKPDYVHVLYQGRIVKSGD 229
Cdd:PTZ00243 798 YANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVP--RADYVVALGDGRVEFSGS 864
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
19-43 |
7.73e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.81 E-value: 7.73e-04
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-43 |
7.93e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 40.07 E-value: 7.93e-04
10 20
....*....|....*....|....*..
gi 157083167 17 LRGLDLDVRPGEVHAIMGPNGSGKSTL 43
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTT 64
|
|
| PRK06547 |
PRK06547 |
hypothetical protein; Provisional |
32-56 |
1.03e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235825 Cd Length: 172 Bit Score: 38.96 E-value: 1.03e-03
10 20
....*....|....*....|....*
gi 157083167 32 IMGPNGSGKSTLSATLAGREDYEVV 56
Cdd:PRK06547 20 IDGRSGSGKTTLAGALAARTGFQLV 44
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
109-239 |
1.75e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 109 YRGQESLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAegv 188
Cdd:PLN03073 309 YKRLELIDAYTAEARAASILAGLSFTPEMQVKATKT-FSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLE--- 384
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 157083167 189 NSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDF-TLVKQLEEQ 239
Cdd:PLN03073 385 TYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYdTFERTREEQ 436
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-231 |
1.87e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.22 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 23 DVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKDLLELSP------------EDRAGEGIFMAFQypvei 90
Cdd:PRK10762 274 TLRKGEILGVSGLMGAGRTELMKVLYG--ALPRTSGYVTLDGHEVVTRSPqdglangivyisEDRKRDGLVLGMS----- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 91 pgVSNQFFLqTALNAVRSYRGQesLDRFDFQDLMEEKIAL--LKMPedllTRSVNVGF-SGGEKKRNDILQMAVLEPELC 167
Cdd:PRK10762 347 --VKENMSL-TALRYFSRAGGS--LKHADEQQAVSDFIRLfnIKTP----SMEQAIGLlSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157083167 168 ILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTH--------YQRILdyikpdyvhVLYQGRIvkSGDFT 231
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSempevlgmSDRIL---------VMHEGRI--SGEFT 478
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-248 |
2.61e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 38.80 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 13 DKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGredyevvggsvefkgkdllELSPEDRAGEGIFMAFQYPVEIPG 92
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-------------------ELSHAETSSVVIRGSVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 93 VSN-----QFFLQTALNAVRSYRG------QESLDRFDFQDLMEekiallkmpedLLTRSVNVgfSGGEKKRNDILQMAV 161
Cdd:PLN03232 690 IFNatvreNILFGSDFESERYWRAidvtalQHDLDLLPGRDLTE-----------IGERGVNI--SGGQKQRVSMARAVY 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 162 LEPELCILDESDSGLDIDALKIVAEgvNSLRDGKR--SFIIVTHYQRILDYIkpDYVHVLYQGRIVKSGDF-------TL 232
Cdd:PLN03232 757 SNSDIYIFDDPLSALDAHVAHQVFD--SCMKDELKgkTRVLVTNQLHFLPLM--DRIILVSEGMIKEEGTFaelsksgSL 832
|
250
....*....|....*.
gi 157083167 233 VKQLEEQGyGWLTEQQ 248
Cdd:PLN03232 833 FKKLMENA-GKMDATQ 847
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
147-210 |
3.49e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 37.30 E-value: 3.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157083167 147 SGGEKKRNDILQMAVLEPE--LCILDESDSGLDIDALKIVAEGVNSLRDGKRSFIIVTHYQRILDY 210
Cdd:cd03238 89 SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS 154
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-51 |
3.54e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.18 E-value: 3.54e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 157083167 5 KDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGRE 51
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQE 374
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-67 |
4.98e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.22 E-value: 4.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 157083167 16 ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVVGGSVEFKGKDL 67
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFM--RMVEVCGGEIRVNGREI 1374
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
21-43 |
5.32e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.60 E-value: 5.32e-03
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-177 |
5.36e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.90 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 16 ILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGREDYEV-VGGSVEFKGKDLLELSP--------EDRAGEGIFM---A 83
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLkVSGEITYNGYRLNEFVPrktsayisQNDVHVGVMTvkeT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 84 FQYPVEIPGVSNQFFLQTALNAVRSYRG---QESLDRFDFQDLMEE-----------KIALLKMPED-LLTRSVNVGFSG 148
Cdd:PLN03140 260 LDFSARCQGVGTRYDLLSELARREKDAGifpEAEVDLFMKATAMEGvksslitdytlKILGLDICKDtIVGDEMIRGISG 339
|
170 180
....*....|....*....|....*....
gi 157083167 149 GEKKRNDILQMAVLEPELCILDESDSGLD 177
Cdd:PLN03140 340 GQKKRVTTGEMIVGPTKTLFMDEISTGLD 368
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
110-177 |
6.30e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 37.80 E-value: 6.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157083167 110 RGQESLDRFDFQDLMEEkiallkMPEDL-LtrsvnvgfsgGEKKRndiLQMAVL---EPELCILDESDSGLD 177
Cdd:NF033858 377 RVAEMLERFDLADVADA------LPDSLpL----------GIRQR---LSLAVAvihKPELLILDEPTSGVD 429
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-203 |
8.35e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 37.24 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 4 IKDLQVSVEDKAILRGLDLDVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVVGGSVEFKGKdlLE----------LSPE 73
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLG--QLQADSGRIHCGTK--LEvayfdqhraeLDPE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157083167 74 ----DRAGEGifmafQYPVEIPGVSNQfflqtalnaVRSYrgqesldrfdFQD-LMEEKIALlkMPEDLLtrsvnvgfSG 148
Cdd:PRK11147 398 ktvmDNLAEG-----KQEVMVNGRPRH---------VLGY----------LQDfLFHPKRAM--TPVKAL--------SG 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 157083167 149 GEKKRndiLQMA--VLEP-ELCILDESDSGLDIDALKIVAEgvnSLRDGKRSFIIVTH 203
Cdd:PRK11147 444 GERNR---LLLArlFLKPsNLLILDEPTNDLDVETLELLEE---LLDSYQGTVLLVSH 495
|
|
| |
