|
Name |
Accession |
Description |
Interval |
E-value |
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-252 |
2.50e-171 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 471.91 E-value: 2.50e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 1 MNaaKAQSKDFLLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLK 80
Cdd:COG4674 1 MS--LDTMHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 81 EHQIVHSGVGRKFQTPSVFEDLTVFENLEVSYPQGHSVMGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQ 160
Cdd:COG4674 79 EHEIARLGIGRKFQKPTVFEELTVFENLELALKGDRGVFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 161 WLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVK 240
Cdd:COG4674 159 WLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQ 238
|
250
....*....|..
gi 552559136 241 SDPKVIEVYLGH 252
Cdd:COG4674 239 ADPRVIEVYLGR 250
|
|
| urea_trans_UrtD |
TIGR03411 |
urea ABC transporter, ATP-binding protein UrtD; Members of this protein family are ABC ... |
11-252 |
1.62e-159 |
|
urea ABC transporter, ATP-binding protein UrtD; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274568 [Multi-domain] Cd Length: 242 Bit Score: 442.00 E-value: 1.62e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 11 FLLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVG 90
Cdd:TIGR03411 1 PILYLEGLSVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTMMDVITGKTRPDEGSVLFGGTDLTGLPEHQIARAGIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 RKFQTPSVFEDLTVFENLEVSYPQGHSVMGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQ 170
Cdd:TIGR03411 81 RKFQKPTVFENLTVFENLELALPRDKSVFASLFFRLSAEEKDRIEEVLETIGLADEADRLAGLLSHGQKQWLEIGMLLMQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 171 KPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPKVIEVYL 250
Cdd:TIGR03411 161 DPKLLLLDEPVAGMTDEETEKTAELLKSLAGKHSVVVVEHDMEFVRSIADKVTVLHQGSVLAEGSLDQVQADPRVIEVYL 240
|
..
gi 552559136 251 GH 252
Cdd:TIGR03411 241 GR 242
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
13-245 |
1.39e-111 |
|
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: 320.54 E-value: 1.39e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGRK 92
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENLEVSYP--QGHSVMGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQ 170
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQarTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 171 KPDLLMLDEPVAGMSVAERKKTAELLRRI-TKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPKV 245
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELrERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
12-251 |
2.42e-107 |
|
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: 310.43 E-value: 2.42e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGR 91
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KFQTPSVFEDLTVFENLEVS--YPQGHSVMGAL-----AFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEI 164
Cdd:COG0411 84 TFQNPRLFPELTVLENVLVAahARLGRGLLAALlrlprARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 165 GMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSD 242
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRAD 243
|
....*....
gi 552559136 243 PKVIEVYLG 251
Cdd:COG0411 244 PRVIEAYLG 252
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
12-251 |
1.09e-70 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 217.17 E-value: 1.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGR 91
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KFQTPSVFEDLTVFENLEVSYPQgHSVMGALA--FK----RSAEvVAAVEDVA---ETIFLKDALDQPASLLSHGQKQWL 162
Cdd:PRK11300 85 TFQHVRLFREMTVIENLLVAQHQ-QLKTGLFSglLKtpafRRAE-SEALDRAAtwlERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 163 EIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVK 240
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
250
....*....|.
gi 552559136 241 SDPKVIEVYLG 251
Cdd:PRK11300 243 NNPDVIKAYLG 253
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
12-251 |
5.66e-64 |
|
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: 199.44 E-value: 5.66e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGV-- 89
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIgy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 90 ---GRKfqtpsVFEDLTVFENLEvsypqghsvMGALAFKRSAEVVAAVEDVAEtIF--LKDALDQPASLLSHGQKQWLEI 164
Cdd:COG0410 83 vpeGRR-----IFPSLTVEENLL---------LGAYARRDRAEVRADLERVYE-LFprLKERRRQRAGTLSGGEQQMLAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 165 GMLLIQKPDLLMLDEPVAGMS---VAErkkTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVK 240
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGLApliVEE---IFEIIRRLNREgVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
250
....*....|.
gi 552559136 241 SDPKVIEVYLG 251
Cdd:COG0410 225 ADPEVREAYLG 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-242 |
7.00e-57 |
|
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: 180.71 E-value: 7.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGRK 92
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENLEvsypqghsvMGALAFKRsAEVVAAVEDVAEtIF--LKDALDQPASLLSHGQKQWLEIGMLLIQ 170
Cdd:cd03224 81 PEGRRIFPELTVEENLL---------LGAYARRR-AKRKARLERVYE-LFprLKERRKQLAGTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552559136 171 KPDLLMLDEPVAGMSVAERKKTAELLRRItKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSD 242
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEgvTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
13-241 |
4.19e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 179.49 E-value: 4.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRlkEHQIVHSGVGRK 92
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR--DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENLEvsypqghsVMGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKP 172
Cdd:COG1131 79 PQEPALYPDLTVRENLR--------FFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 173 DLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKS 241
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-247 |
3.41e-47 |
|
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: 156.34 E-value: 3.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSF-DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvHSGVGR 91
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL-RRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KFQTPS--VFEDlTVFEnlEVSYpqghsvmGALAFKRS-AEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLL 168
Cdd:COG1122 80 VFQNPDdqLFAP-TVEE--DVAF-------GPENLGLPrEEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 169 IQKPDLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPKVIE 247
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLE 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-244 |
6.59e-46 |
|
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: 160.07 E-value: 6.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 3 AAKAQSKDFLLAVEGLTVSF-----DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELT 77
Cdd:COG1123 251 APAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 78 RLKEHQI--VHSGVGRKFQTP--SVFEDLTVFEnlEVSYPqghsvMGALAFKRSAEVVAAVEDVAETIFL-KDALDQPAS 152
Cdd:COG1123 331 KLSRRSLreLRRRVQMVFQDPysSLNPRMTVGD--IIAEP-----LRLHGLLSRAERRERVAELLERVGLpPDLADRYPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 153 LLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
250
....*....|....
gi 552559136 231 LSEGSIEHVKSDPK 244
Cdd:COG1123 484 VEDGPTEEVFANPQ 497
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-230 |
3.14e-45 |
|
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: 149.47 E-value: 3.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTrlKEHQIVHSGVGRK 92
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK--KEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENLEvsypqghsvmgalafkrsaevvaavedvaetiflkdaldqpaslLSHGQKQWLEIGMLLIQKP 172
Cdd:cd03230 79 PEEPSLYENLTVRENLK--------------------------------------------LSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 173 DLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
13-251 |
3.44e-45 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 151.34 E-value: 3.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGRK 92
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFEN----LEVSYPQGHsvmgalafKRSAEVVAAVEDvaetiF-LKDALDQPASLLSHGQKQWLEIGML 167
Cdd:COG1137 84 PQEASIFRKLTVEDNilavLELRKLSKK--------EREERLEELLEE-----FgITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 168 LIQKPDLLMLDEPVAG---MSVAERKKTAELLRR------ITkDHTV---LviehdmqfvgDIADRVTVMHQGKVLSEGS 235
Cdd:COG1137 151 LATNPKFILLDEPFAGvdpIAVADIQKIIRHLKErgigvlIT-DHNVretL----------GICDRAYIISEGKVLAEGT 219
|
250
....*....|....*.
gi 552559136 236 IEHVKSDPKVIEVYLG 251
Cdd:COG1137 220 PEEILNNPLVRKVYLG 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
15-240 |
3.58e-45 |
|
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: 150.98 E-value: 3.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 15 VEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRlkEHQIVHSGVGRKFQ 94
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR--EPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 95 TPSVFEDLTVFENLEVsypQG--HSVMGALAFKRSAEVVAAVEdvaetifLKDALDQPASLLSHGQKQWLEIGMLLIQKP 172
Cdd:cd03265 81 DLSVDDELTGWENLYI---HArlYGVPGAERRERIDELLDFVG-------LLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 173 DLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVK 240
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-229 |
6.62e-44 |
|
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: 147.23 E-value: 6.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 15 VEGLTVSFDGF--KAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvHSGVGRK 92
Cdd:cd03225 2 LKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL-RRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQ-------TPSVFEDLtVF--ENLEVSYpqghsvmgalafkrsAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLE 163
Cdd:cd03225 81 FQnpddqffGPTVEEEV-AFglENLGLPE---------------EEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 164 IGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGK 229
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
13-252 |
1.19e-43 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 147.42 E-value: 1.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGRK 92
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENLEVSYpqghSVMGALAFKRSAEvvaAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKP 172
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVL----EIRKDLDRAEREE---RLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 173 DLLMLDEPVAG---MSVAERKKTAELLRriTKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPKVIEVY 249
Cdd:TIGR04406 155 KFILLDEPFAGvdpIAVGDIKKIIKHLK--ERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVY 232
|
...
gi 552559136 250 LGH 252
Cdd:TIGR04406 233 LGE 235
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-251 |
1.21e-43 |
|
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: 147.30 E-value: 1.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGRK 92
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENLevsypqghsvMGALAF--KRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQ 170
Cdd:cd03218 81 PQEASIFRKLTVEENI----------LAVLEIrgLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 171 KPDLLMLDEPVAG---MSVAERKKTAELLRRitKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPKVIE 247
Cdd:cd03218 151 NPKFLLLDEPFAGvdpIAVQDIQKIIKILKD--RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRK 228
|
....
gi 552559136 248 VYLG 251
Cdd:cd03218 229 VYLG 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
13-234 |
1.96e-43 |
|
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: 146.18 E-value: 1.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKeIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKehQIVHSGVGRK 92
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP--QKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENLEvsYpqghsvMGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKP 172
Cdd:cd03264 78 PQEFGVYPNFTVREFLD--Y------IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552559136 173 DLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEG 234
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-241 |
2.59e-43 |
|
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: 146.93 E-value: 2.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHqiVHSGVGR 91
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE--ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KFQTPSVFEDLTVFENLEVSypqghsvmGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQK 171
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYF--------AELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552559136 172 PDLLMLDEPVAGMSVAERKKTAELLRRITK-DHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKS 241
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-239 |
5.53e-43 |
|
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: 146.34 E-value: 5.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvhsgvGR 91
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL-----AR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 K----FQTPSVFEDLTVFENLEvsypqghsvMGALAFKR-----SAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWL 162
Cdd:COG1120 76 RiayvPQEPPAPFGLTVRELVA---------LGRYPHLGlfgrpSAEDREAVEEALERTGLEHLADRPVDELSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 163 EIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHV 239
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-234 |
8.80e-42 |
|
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: 141.89 E-value: 8.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQivhSGVGRK 92
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER---RNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENleVSYPqghsvmGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKP 172
Cdd:cd03259 78 FQDYALFPHLTVAEN--IAFG------LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552559136 173 DLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEG 234
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-244 |
4.68e-41 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 146.97 E-value: 4.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDG--FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICG---KTKATSGSIRFDGKELTRLKEHQIVH 86
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 87 SgVGRKFQTP-------SVFEDLT-VFENLEVSypqghsvmgalafkrSAEVVAAVEDVAETIFLKDALDQPASLLSHGQ 158
Cdd:COG1123 84 R-IGMVFQDPmtqlnpvTVGDQIAeALENLGLS---------------RAEARARVLELLEAVGLERRLDRYPHQLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 159 KQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSI 236
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
....*...
gi 552559136 237 EHVKSDPK 244
Cdd:COG1123 228 EEILAAPQ 235
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
12-245 |
1.12e-40 |
|
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: 139.73 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQI--VHSGV 89
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyeLRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 90 GRKFQTPSVFEDLTVFENleVSYP-QGHSVMG-ALAFKRSAEVVAAVEdvaetifLKDALDQPASLLShGqkqwleiGML 167
Cdd:COG1127 85 GMLFQGGALFDSLTVFEN--VAFPlREHTDLSeAEIRELVLEKLELVG-------LPGAADKMPSELS-G-------GMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 168 --------LIQKPDLLMLDEPVAG----MSvaerKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSE 233
Cdd:COG1127 148 krvalaraLALDPEILLYDEPTAGldpiTS----AVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
250
....*....|....
gi 552559136 234 GSIEHVK--SDPKV 245
Cdd:COG1127 224 GTPEELLasDDPWV 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
15-245 |
1.12e-39 |
|
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: 137.25 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 15 VEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSG--VGRK 92
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRrrMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENleVSYP-QGHSVMGA-LAFKRSAEVVAAVEdvaetifLKDALDQPASLLSHGQKQWLEIGMLLIQ 170
Cdd:cd03261 83 FQSGALFDSLTVFEN--VAFPlREHTRLSEeEIREIVLEKLEAVG-------LRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 171 KPDLLMLDEPVAGMSVAERKKTAELLRRITK--DHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKS--DPKV 245
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAsdDPLV 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-234 |
1.82e-39 |
|
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: 136.48 E-value: 1.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDG----FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQivHS 87
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRL--RK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 88 GVGRKFQTpsVFED--------LTVFENL-EVSYPQGHSVMGALAFKRSAEVVAAVEDVaetiflKDALDQPASLLSHGQ 158
Cdd:cd03257 79 IRRKEIQM--VFQDpmsslnprMTIGEQIaEPLRIHGKLSKKEARKEAVLLLLVGVGLP------EEVLNRYPHELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552559136 159 KQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEG 234
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-182 |
3.09e-39 |
|
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: 133.16 E-value: 3.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 28 VDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRlKEHQIVHSGVGRKFQTPSVFEDLTVFEN 107
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD-DERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552559136 108 LEvsypQGHSVMGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVA 182
Cdd:pfam00005 80 LR----LGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-230 |
7.81e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 135.60 E-value: 7.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSF-----DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHS 87
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 88 gVGRKFQTPSV--FEDLTVFENLEVSYPQGHS--VMGALAFKRSAEVVAAVEDVAetIFLKDALDQPASLLSHGQKQWLE 163
Cdd:COG1101 82 -IGRVFQDPMMgtAPSMTIEENLALAYRRGKRrgLRRGLTKKRRELFRELLATLG--LGLENRLDTKVGLLSGGQRQALS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552559136 164 IGMLLIQKPDLLMLDEPVAgmsvAERKKTAELL-----RRITKDH-TVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTA----ALDPKTAALVlelteKIVEENNlTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-249 |
1.68e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.45 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEH-----QivH 86
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigyvpQ--R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 87 SGVGRKFqtPsvfedLTVFEnlevsypqghsV--MGALA----FKR-SAEVVAAVEDVAETIFLKDALDQPASLLSHGQK 159
Cdd:COG1121 84 AEVDWDF--P-----ITVRD-----------VvlMGRYGrrglFRRpSRADREAVDEALERVGLEDLADRPIGELSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 160 QWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITK-DHTVLVIEHDMQFVGDIADRVTVMHQGkVLSEGSIEH 238
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEE 224
|
250
....*....|.
gi 552559136 239 VKSDPKVIEVY 249
Cdd:COG1121 225 VLTPENLSRAY 235
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-240 |
2.58e-38 |
|
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: 133.01 E-value: 2.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 21 SFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHqiVHSGVGRKFQTPSVFE 100
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA--ARQSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 101 DLTVFENLEVsypqghsvMGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEP 180
Cdd:cd03263 89 ELTVREHLRF--------YARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 181 VAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVK 240
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-234 |
2.38e-37 |
|
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: 129.48 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 14 AVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvhsgvgrkf 93
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 94 qtpsvfedltvfenlevsypqghsvmgalafkrsAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPD 173
Cdd:cd03214 72 ----------------------------------ARKIAYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552559136 174 LLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEG 234
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-234 |
2.92e-37 |
|
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: 130.03 E-value: 2.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEhqiVHSGVGRK 92
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE---ALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENLEVSypqghsvmGALAFKRSAEvvaaVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKP 172
Cdd:cd03268 78 IEAPGFYPNLTARENLRLL--------ARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552559136 173 DLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKVLSEG 234
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-232 |
3.55e-37 |
|
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: 129.96 E-value: 3.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 15 VEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRlkehqiVHSGVGRKFQ 94
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK------ERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 95 TPSVFED--LTVFENLEvsypqghsvMGALAFKR-----SAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGML 167
Cdd:cd03235 76 RRSIDRDfpISVRDVVL---------MGLYGHKGlfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 168 LIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKVLS 232
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVLLLNRTVVAS 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
15-244 |
4.28e-37 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 130.39 E-value: 4.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 15 VEGLTVSFDG----FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVH--SG 88
Cdd:cd03258 4 LKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKarRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 89 VGRKFQTPSVFEDLTVFENleVSYPQghsvmgALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLL 168
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFEN--VALPL------EIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552559136 169 IQKPDLLMLDEPVAGMSVAERKKTAELLRRITK--DHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPK 244
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-239 |
1.72e-36 |
|
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: 128.84 E-value: 1.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICG-----KTKATSGSIRFDGKELTRLKEHQI-VH 86
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVDVLeLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 87 SGVGRKFQTPSVFeDLTVFENleVSYPQGHSVMgalafKRSAEVVAAVEDVAETIFLKDALDQP--ASLLSHGQKQWLEI 164
Cdd:cd03260 81 RRVGMVFQKPNPF-PGSIYDN--VAYGLRLHGI-----KLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552559136 165 GMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHV 239
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-229 |
1.79e-36 |
|
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: 126.59 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 15 VEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQiVHSGVGRKFQ 94
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE-LRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 95 tpsvfedltvfenlevsypqghsvmgalafkrsaevvaavedvaetiflkdaldqpaslLSHGQKQWLEIGMLLIQKPDL 174
Cdd:cd00267 81 -----------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 175 LMLDEPVAGMSVAERKKTAELLRRITKDH-TVLVIEHDMQFVGDIADRVTVMHQGK 229
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-249 |
2.42e-36 |
|
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: 128.84 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSF-DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQI--VHSGV 89
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 90 GRKFQTPSVFEDLTVFENLevsypqghsVMGALAFK---RS-------AEVVAAVEdVAETIFLKDALDQPASLLSHGQK 159
Cdd:cd03256 81 GMIFQQFNLIERLSVLENV---------LSGRLGRRstwRSlfglfpkEEKQRALA-ALERVGLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 160 QWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIE 237
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPA 230
|
250
....*....|..
gi 552559136 238 HVkSDPKVIEVY 249
Cdd:cd03256 231 EL-TDEVLDEIY 241
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-230 |
2.49e-36 |
|
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: 127.76 E-value: 2.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 15 VEGLTVSF-DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKEL---TRLKEHQIVHSGVG 90
Cdd:cd03226 2 IENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakERRKSIGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 RKFQTPSVFEDLTvfenlevsypqghsvmgaLAFKRSAEVVAAVEDVAETIFLKDALDQ-PASlLSHGQKQWLEIGMLLI 169
Cdd:cd03226 82 YQLFTDSVREELL------------------LGLKELDAGNEQAETVLKDLDLYALKERhPLS-LSGGQKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552559136 170 QKPDLLMLDEPVAGMSVAERKKTAELLRRITK-DHTVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-230 |
3.49e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 133.61 E-value: 3.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGR 91
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KFQTPSVFEDLTVFENLevsypqghsVMGA----LAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGML 167
Cdd:COG3845 85 VHQHFMLVPNLTVAENI---------VLGLeptkGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552559136 168 LIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:COG3845 156 LYRGARILILDEPTAVLTPQEADELFEILRRLAAEgKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
12-235 |
1.26e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 129.45 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQ----IVhs 87
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKrnvgMV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 88 gvgrkFQTPSVFEDLTVFENleVSYPqghsvmgaLAFKR--SAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIG 165
Cdd:COG3842 83 -----FQDYALFPHLTVAEN--VAFG--------LRMRGvpKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552559136 166 MLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQ--FVgdIADRVTVMHQGKVLSEGS 235
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEeaLA--LADRIAVMNDGRIEQVGT 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-244 |
1.71e-35 |
|
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: 126.20 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQivhSGVGRK 92
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK---RPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENleVSYPqghsvmgaLAFKRS--AEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQ 170
Cdd:cd03300 78 FQNYALFPHLTVFEN--IAFG--------LRLKKLpkAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 171 KPDLLMLDEPVAGMSVAERKKTAELLRRITKD--HTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPK 244
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKElgITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
12-234 |
2.31e-35 |
|
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: 125.56 E-value: 2.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFD----GFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGkeLTRLKEHQIVHS 87
Cdd:cd03266 1 MITADALTKRFRdvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 88 GVGRKFQTPSVFEDLTVFENLEvsypqghsVMGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGML 167
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLE--------YFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552559136 168 LIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKVLSEG 234
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-230 |
2.55e-35 |
|
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: 125.29 E-value: 2.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDG----FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQ---IV 85
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 86 HSGVGRKFQTPSVFEDLTVFENleVSYPQghsvmgALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIG 165
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALEN--VELPL------LLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 166 MLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKD--HTVLVIEHDMQFVgDIADRVTVMHQGKV 230
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEagTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
15-249 |
9.71e-35 |
|
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: 124.37 E-value: 9.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 15 VEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQivhSGVGRKFQ 94
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---RNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 95 TPSVFEDLTVFENleVSYpqGHSVMGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDL 174
Cdd:cd03296 82 HYALFRHMTVFDN--VAF--GLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 175 LMLDEPVAGMSVAERKKTAELLRRITKD--HTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPKVIEVY 249
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDElhVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVY 234
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-198 |
1.02e-34 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 123.36 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHqiVHSGVGR 91
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED--YRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KFQTPSVFEDLTVFENLEVsypqghsvmgALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQK 171
Cdd:COG4133 80 LGHADGLKPELTVRENLRF----------WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180
....*....|....*....|....*..
gi 552559136 172 PDLLMLDEPVAGMSVAERKKTAELLRR 198
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-230 |
5.71e-34 |
|
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: 121.59 E-value: 5.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHqivHSGVGRK 92
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK---DRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENLEVSYPQGHSvmgalafkRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKP 172
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKV--------PKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 173 DLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLgtTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-229 |
2.09e-33 |
|
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: 119.21 E-value: 2.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRL-KEHQIVHSGVGR 91
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLeDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KFQTPSVFEDLTVFENleVSYPqghsvmgalafkrsaevvaavedvaetiflkdaldqpaslLSHGQKQWLEIGMLLIQK 171
Cdd:cd03229 81 VFQDFALFPHLTVLEN--IALG----------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 172 PDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGK 229
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-239 |
4.50e-32 |
|
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: 123.79 E-value: 4.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 20 VSF----DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLkEHQIVHSGVGRKFQT 95
Cdd:COG2274 479 VSFrypgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI-DPASLRRQIGVVLQD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 96 PSVFEDlTVFENLEVSYPQghsvMGALAFKRSAEVVAAVEDVAEtifLKDALDQP----ASLLSHGQKQWLEIGMLLIQK 171
Cdd:COG2274 558 VFLFSG-TIRENITLGDPD----ATDEEIIEAARLAGLHDFIEA---LPMGYDTVvgegGSNLSGGQRQRLAIARALLRN 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552559136 172 PDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDiADRVTVMHQGKVLSEGSIEHV 239
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEEL 696
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-249 |
6.06e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.57 E-value: 6.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIV-HSGVG 90
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELArRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 RkfQTPSVFEDLTVfenLEVsypqghsV-MGALAF----KRSAEVVAAVEDVAETIFLKDaLDQPAslLSHGQKQWLEIG 165
Cdd:PRK13548 82 P--QHSSLSFPFTV---EEV-------VaMGRAPHglsrAEDDALVAAALAQVDLAHLAG-RDYPQ--LSGGEQQRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 166 MLLIQ------KPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDM----QFvgdiADRVTVMHQGKVLSE 233
Cdd:PRK13548 147 RVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLnlaaRY----ADRIVLLHQGRLVAD 222
|
250
....*....|....*.
gi 552559136 234 GSIEHVKSDPKVIEVY 249
Cdd:PRK13548 223 GTPAEVLTPETLRRVY 238
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
13-235 |
9.52e-32 |
|
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: 122.17 E-value: 9.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSF-DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVH--SGV 89
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRqiAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 90 GrkfQTPSVFEDlTVFENLEVSYPQ--GHSVMGALAFKRSAEVVAAvedvaetifLKDALDQP----ASLLSHGQKQWLE 163
Cdd:COG4988 417 P---QNPYLFAG-TIRENLRLGRPDasDEELEAALEAAGLDEFVAA---------LPDGLDTPlgegGRGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552559136 164 IGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVgDIADRVTVMHQGKVLSEGS 235
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALL-AQADRILVLDDGRIVEQGT 554
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-249 |
9.93e-32 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 117.14 E-value: 9.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQI-VHSGVG 90
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELaRRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 RKfQTPSVFeDLTVfenLEVsypqghsV-MGALA-FKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLL 168
Cdd:COG4559 81 PQ-HSSLAF-PFTV---EEV-------VaLGRAPhGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 169 IQ-------KPDLLMLDEPVAGMSVAERKKTAELLRRITKDH-TVLVIEHD----MQFvgdiADRVTVMHQGKVLSEGSI 236
Cdd:COG4559 149 AQlwepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGgGVVAVLHDlnlaAQY----ADRILLLHQGRLVAQGTP 224
|
250
....*....|...
gi 552559136 237 EHVKSDPKVIEVY 249
Cdd:COG4559 225 EEVLTDELLERVY 237
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
13-251 |
1.34e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.01 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFylDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQivhsgvgRK 92
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFDLTI--AAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-------RP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 ----FQTPSVFEDLTVFENLevsypqghsvmgALAF----KRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEI 164
Cdd:COG3840 73 vsmlFQENNLFPHLTVAQNI------------GLGLrpglKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 165 GMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHV--K 240
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALldG 220
|
250
....*....|.
gi 552559136 241 SDPKVIEVYLG 251
Cdd:COG3840 221 EPPPALAAYLG 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-233 |
1.35e-31 |
|
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: 115.65 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDG----FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRlkehqiVHSG 88
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG------PGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 89 VGRKFQTPSVFEDLTVFENlevsypqghsVMGALAFKR--SAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGM 166
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDN----------VALGLELQGvpKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552559136 167 LLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQ---FVgdiADRVTVMHQ--GKVLSE 233
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeavFL---ADRVVVLSArpGRIVAE 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
15-230 |
1.87e-31 |
|
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: 115.32 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 15 VEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELT-RLKEHQIVHSGVGRKF 93
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTdDKKNINELRQKVGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 94 QTPSVFEDLTVFENlevsypqghsVMGAL--AFKRS-AEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQ 170
Cdd:cd03262 83 QQFNLFPHLTVLEN----------ITLAPikVKGMSkAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552559136 171 KPDLLMLDEPVAGMSVAERKKTAELLRRITKDH-TVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
13-248 |
2.67e-31 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 115.51 E-value: 2.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKaVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQivhSGVGRK 92
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK---RDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENLEVSypqghsvMGALAFKRsAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKP 172
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYG-------LKKRKVDK-KEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552559136 173 DLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPKVIEV 248
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFV 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-239 |
1.26e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.58 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 10 DFLLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGV 89
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 90 GRKFQTPSVFEDLTVFENLEVsypqGHSVMGALAFKRsAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLI 169
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFL----GREPRRGGLIDW-RAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552559136 170 QKPDLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHV 239
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQgVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
13-248 |
1.70e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 115.94 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQivhSGVGRK 92
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---RNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENLevSYPqghsvmgaLAFKR--SAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQ 170
Cdd:COG3839 81 FQSYALYPHMTVYENI--AFP--------LKLRKvpKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 171 KPDLLMLDEPV----AGMSVAERKKTAELLRRItkDHTVLVIEHD----MQFvgdiADRVTVMHQGKVLSEGSIEHVKSD 242
Cdd:COG3839 151 EPKVFLLDEPLsnldAKLRVEMRAEIKRLHRRL--GTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEELYDR 224
|
....*.
gi 552559136 243 PKVIEV 248
Cdd:COG3839 225 PANLFV 230
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
12-233 |
1.75e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 112.83 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFD----GFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIV-- 85
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 86 ---HSG-VgrkFQTPSVFEDLTVFENLEVsyPQghsvmgALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQW 161
Cdd:COG1136 84 rrrHIGfV---FQFFNLLPELTALENVAL--PL------LLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 162 LEIGMLLIQKPDLLMLDEP------VAGMSVaerkktAELLRRITKDH--TVLVIEHDMQfVGDIADRVTVMHQGKVLSE 233
Cdd:COG1136 153 VAIARALVNRPKLILADEPtgnldsKTGEEV------LELLRELNRELgtTIVMVTHDPE-LAARADRVIRLRDGRIVSD 225
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-251 |
6.90e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 111.91 E-value: 6.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGR 91
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KFQTPSVFEDLTVFENLEVSYPQGHSVMGALAFKRSAEVVAAVedvaETIFLKDALDQPaslLSHGQKQWLEIGMLLIQK 171
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEF----HIEHLRDSMGQS---LSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 172 PDLLMLDEPVAG---MSVAERKKTAELLRriTKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPKVIEV 248
Cdd:PRK10895 156 PKFILLDEPFAGvdpISVIDIKRIIEHLR--DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRV 233
|
...
gi 552559136 249 YLG 251
Cdd:PRK10895 234 YLG 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
26-234 |
8.34e-30 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 111.14 E-value: 8.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 26 KAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLkEHQIVHSGVGRKFQTPSVFEDlTVF 105
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL-DPADLRRNIGYVPQDVTLFYG-TLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 106 ENLEVSYPqghsvmgalaFKRSAEVVAAVEDVAETIFLKdalDQPASL----------LSHGQKQWLEIGMLLIQKPDLL 175
Cdd:cd03245 96 DNITLGAP----------LADDERILRAAELAGVTDFVN---KHPNGLdlqigergrgLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 176 MLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVgDIADRVTVMHQGKVLSEG 234
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
15-244 |
1.00e-29 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 113.63 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 15 VEGLTVSFDG----FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVH--SG 88
Cdd:COG1135 4 LENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAarRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 89 VGRKFQTPSVFEDLTVFENleVSYP---QGHSvmgalafkrSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIG 165
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAEN--VALPleiAGVP---------KAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 166 MLLIQKPDLLMLDEPVAGM------SVaerkktAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIE 237
Cdd:COG1135 153 RALANNPKVLLCDEATSALdpettrSI------LDLLKDINRELglTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVL 226
|
....*..
gi 552559136 238 HVKSDPK 244
Cdd:COG1135 227 DVFANPQ 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-244 |
1.12e-29 |
|
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: 115.94 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSF-----------DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTT----VLDLIcgktkATSGSIRFDGKEL 76
Cdd:COG4172 275 LLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 77 TRLKEH---------QIVhsgvgrkFQTP--------SVFEdlTVFENLEVSYPQghsvMGALAfkRSAEVVAAVEDVAe 139
Cdd:COG4172 350 DGLSRRalrplrrrmQVV-------FQDPfgslsprmTVGQ--IIAEGLRVHGPG----LSAAE--RRARVAEALEEVG- 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 140 tiflkdaLDqPASL------LSHGQKQWLEIGMLLIQKPDLLMLDEPVAG--MSVaeRKKTAELLRRITKDH--TVLVIE 209
Cdd:COG4172 414 -------LD-PAARhrypheFSGGQRQRIAIARALILEPKLLVLDEPTSAldVSV--QAQILDLLRDLQREHglAYLFIS 483
|
250 260 270
....*....|....*....|....*....|....*
gi 552559136 210 HDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPK 244
Cdd:COG4172 484 HDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQ 518
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-230 |
1.52e-29 |
|
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: 108.67 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGRK 92
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQtpsvfedltvfenlevsypqghsvmgalafkrsaevvaavedvaetiflkdaldqpaslLSHGQKQWLEIGMLLIQKP 172
Cdd:cd03216 81 YQ-----------------------------------------------------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 173 DLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
13-229 |
2.72e-29 |
|
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: 108.24 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGF--KAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvHSGVG 90
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL-RKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 RKFQTPSVFEDlTVFENlevsypqghsvmgalafkrsaevvaavedvaetiflkdaldqpasLLSHGQKQWLEIGMLLIQ 170
Cdd:cd03228 80 YVPQDPFLFSG-TIREN---------------------------------------------ILSGGQRQRIAIARALLR 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 171 KPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVgDIADRVTVMHQGK 229
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
27-234 |
3.39e-29 |
|
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: 110.11 E-value: 3.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 27 AVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGV--GRKFQtpsVFEDLTV 104
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVvfGQKTQ---LWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 105 FEnlevsypqGHSVMGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGM 184
Cdd:cd03267 113 ID--------SFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 552559136 185 SVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEG 234
Cdd:cd03267 185 DVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
12-251 |
1.08e-28 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 108.81 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGR 91
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KFQTPSVFEDLTVFENLevsypqghsVMGALAFKRSA--EVVAAVEDVAETIFLKDAldQPASLLSHGQKQWLEIGMLLI 169
Cdd:PRK11614 85 VPEGRRVFSRMTVEENL---------AMGGFFAERDQfqERIKWVYELFPRLHERRI--QRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 170 QKPDLLMLDEPVAGMS---VAERKKTAELLRRitKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPKVI 246
Cdd:PRK11614 154 SQPRLLLLDEPSLGLApiiIQQIFDTIEQLRE--QGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVR 231
|
....*
gi 552559136 247 EVYLG 251
Cdd:PRK11614 232 SAYLG 236
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-244 |
1.32e-28 |
|
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: 110.14 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDG----FKAVDDLSFYLDPKEIRVIIGPNGAGKTT----VLDLIcGKTKATSGSIRFDGKELTRLKEHQ 83
Cdd:COG0444 1 LLEVRNLKVYFPTrrgvVKAVDGVSFDVRRGETLGLVGESGSGKSTlaraILGLL-PPPGITSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 84 IvhSGV-GRKFQTpsVFED--------LTVF----ENLEVsypqgHSVM-GALAFKRSAEVVAAVEdvaetiflkdaLDQ 149
Cdd:COG0444 80 L--RKIrGREIQM--IFQDpmtslnpvMTVGdqiaEPLRI-----HGGLsKAEARERAIELLERVG-----------LPD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 150 PASL-------LSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIAD 220
Cdd:COG0444 140 PERRldrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEIAD 219
|
250 260
....*....|....*....|....
gi 552559136 221 RVTVMHQGKVLSEGSIEHVKSDPK 244
Cdd:COG0444 220 RVAVMYAGRIVEEGPVEELFENPR 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
23-234 |
1.45e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 107.83 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 23 DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHsgVGRK----FQTPSV 98
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPY--LRRRigvvFQDFRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 99 FEDLTVFENleVSYPQghSVMGalafKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLD 178
Cdd:COG2884 91 LPDRTVYEN--VALPL--RVTG----KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 179 EPVAGMSVAERKKTAELLRRITKDH-TVLVIEHDMQFVGDIADRVTVMHQGKVLSEG 234
Cdd:COG2884 163 EPTGNLDPETSWEIMELLEEINRRGtTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-250 |
2.08e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 109.79 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 8 SKDFLLAV--EGLTVSFDGF--------KAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDG---- 73
Cdd:COG4586 8 SKTYRVYEkePGLKGALKGLfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 74 KELTRLKeHQIvhsGV--GRKFQtpsVFEDLTVFENLEVsypqghsvMGAL------AFKRSaevvaaVEDVAETIFLKD 145
Cdd:COG4586 88 KRRKEFA-RRI---GVvfGQRSQ---LWWDLPAIDSFRL--------LKAIyripdaEYKKR------LDELVELLDLGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 146 ALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVT 223
Cdd:COG4586 147 LLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALCDRVI 226
|
250 260 270
....*....|....*....|....*....|
gi 552559136 224 VMHQGKVLSEGSIEHVK---SDPKVIEVYL 250
Cdd:COG4586 227 VIDHGRIIYDGSLEELKerfGPYKTIVLEL 256
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
13-243 |
7.28e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.02 E-value: 7.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRL--KEHQivhsgVG 90
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLhaRDRK-----VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 RKFQTPSVFEDLTVFENleVSYpqGHSVMGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQ 170
Cdd:PRK10851 78 FVFQHYALFRHMTVFDN--IAF--GLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552559136 171 KPDLLMLDEPVAGMSVAERKktaELLRRITKDH-----TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDP 243
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRK---ELRRWLRQLHeelkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-242 |
8.21e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 107.89 E-value: 8.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvhsgvG-- 90
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRI-----Gyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 ---RkfqtpSVFEDLTVFENLEvsYpqghsvMGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGML 167
Cdd:COG4152 77 peeR-----GLYPKMKVGEQLV--Y------LARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 168 LIQKPDLLMLDEPVAGM-SVAerkktAELLRRITKDH-----TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKS 241
Cdd:COG4152 144 LLHDPELLILDEPFSGLdPVN-----VELLKDVIRELaakgtTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRR 218
|
.
gi 552559136 242 D 242
Cdd:COG4152 219 Q 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-242 |
9.40e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 110.64 E-value: 9.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGR 91
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KFQTPSVFEDLTVFENLEVSYPQGHSVMGA-LAFKRSAEVVAAVedVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQ 170
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKVCGVnIIDWREMRVRAAM--MLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552559136 171 KPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLV-IEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSD 242
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-239 |
1.47e-27 |
|
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: 105.39 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 20 VSF---DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQiVHSGVGRKFQTP 96
Cdd:cd03254 8 VNFsydEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS-LRSMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 97 SVFEDlTVFENLEVSYPQGhsvmgalafkRSAEVVAAVEDVAETIF---LKDALD----QPASLLSHGQKQWLEIGMLLI 169
Cdd:cd03254 87 FLFSG-TIMENIRLGRPNA----------TDEEVIEAAKEAGAHDFimkLPNGYDtvlgENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 170 QKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDiADRVTVMHQGKVLSEGSIEHV 239
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-244 |
1.75e-27 |
|
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: 109.77 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDG----FKAVDDLSFYLDPKEIRVIIGPNGAGKT----TVLDLICGKTKATSGSIRFDGKELTRLKEHQ 83
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 84 IvhSGV-GRK----FQTPsvfedLT-----------VFENLEVsypqgHSVMGALAfkRSAEVVAAVEDVAetiflkdaL 147
Cdd:COG4172 86 L--RRIrGNRiamiFQEP-----MTslnplhtigkqIAEVLRL-----HRGLSGAA--ARARALELLERVG--------I 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 148 DQPASL-------LSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDI 218
Cdd:COG4172 144 PDPERRldayphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVRRF 223
|
250 260
....*....|....*....|....*.
gi 552559136 219 ADRVTVMHQGKVLSEGSIEHVKSDPK 244
Cdd:COG4172 224 ADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
10-247 |
3.44e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.59 E-value: 3.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 10 DFLLAVEGLTVSF-DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEhQIVHSG 88
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENE-KWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 89 VGRKFQTP--SVFEDlTVFEnlEVSYpqGHSVMGAlafkRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGM 166
Cdd:PRK13647 81 VGLVFQDPddQVFSS-TVWD--DVAF--GPVNMGL----DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 167 LLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEhVKSDPKV 245
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS-LLTDEDI 230
|
..
gi 552559136 246 IE 247
Cdd:PRK13647 231 VE 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-244 |
4.24e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 104.73 E-value: 4.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 1 MNAAkAQSKDFLLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVL-------DLICGKTkaTSGSIRFDG 73
Cdd:COG1117 1 MTAP-ASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGAR--VEGEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 74 KE-------LTRLKEHqivhsgVGRKFQTPSVFEdLTVFENleVSYpqGHSVMGalaFKRSAEVVAAVE----DVA---E 139
Cdd:COG1117 78 EDiydpdvdVVELRRR------VGMVFQKPNPFP-KSIYDN--VAY--GLRLHG---IKSKSELDEIVEeslrKAAlwdE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 140 tifLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEP------VAGMSVaErkktaELLRRITKDHTVLVIEHDMQ 213
Cdd:COG1117 144 ---VKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPtsaldpISTAKI-E-----ELILELKKDYTIVIVTHNMQ 214
|
250 260 270
....*....|....*....|....*....|.
gi 552559136 214 FVGDIADRVTVMHQGKVLSEGSIEHVKSDPK 244
Cdd:COG1117 215 QAARVSDYTAFFYLGELVEFGPTEQIFTNPK 245
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-234 |
6.37e-27 |
|
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: 103.53 E-value: 6.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 19 TVSFDGFKAVDDLSFYLD---PKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKEL--TRLKEHQIVHS-GVGRK 92
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdSRKKINLPPQQrKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENLEVsypqghsvmgALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKP 172
Cdd:cd03297 81 FQQYALFPHLNVRENLAF----------GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552559136 173 DLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEG 234
Cdd:cd03297 151 ELLLLDEPFSALDRALRLQLLPELKQIKKNLniPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
30-231 |
7.33e-27 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 103.56 E-value: 7.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 30 DLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVH--SGVGRKFQTPSVFEDLTVFEN 107
Cdd:TIGR02982 23 DINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQlrRRIGYIFQAHNLLGFLTARQN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 108 LEvsypqghsvMGA--LAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMS 185
Cdd:TIGR02982 103 VQ---------MALelQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 552559136 186 VAERKKTAELLRRITKDH--TVLVIEHDMQFVgDIADRVTVMHQGKVL 231
Cdd:TIGR02982 174 SKSGRDVVELMQKLAKEQgcTILMVTHDNRIL-DVADRILQMEDGKLL 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
24-230 |
2.35e-26 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 101.72 E-value: 2.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 24 GFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQI--VHSGVGRKFQTPSVFED 101
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpyLRRKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 102 LTVFEN----LEVSYpqghsVMGALAFKRsaevvaaVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLML 177
Cdd:cd03292 93 RNVYENvafaLEVTG-----VPPREIRKR-------VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 552559136 178 DEPVAGMSVAERKKTAELLRRITK-DHTVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-240 |
3.39e-26 |
|
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: 101.06 E-value: 3.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICG--KTKATSGSIRFDGKELTRLKEHQIVHSGVG 90
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 RKFQTPSVFEDLTVFEnlevsypqghsvmgalaFKRsaevvaaveDVAETiflkdaldqpaslLSHGQKQWLEIGMLLIQ 170
Cdd:cd03217 81 LAFQYPPEIPGVKNAD-----------------FLR---------YVNEG-------------FSGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552559136 171 KPDLLMLDEPVAGMSVAERKKTAELLRRI-TKDHTVLVIEHDMQFVGDI-ADRVTVMHQGKVLSEGSIEHVK 240
Cdd:cd03217 122 EPDLAILDEPDSGLDIDALRLVAEVINKLrEEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELAL 193
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
13-234 |
3.71e-26 |
|
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: 101.20 E-value: 3.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvhsgvGRK 92
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRI-----GYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENLevSYpqghsvMGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKP 172
Cdd:cd03269 76 PEERGLYPKMKVIDQL--VY------LAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 173 DLLMLDEPVAGMSVAERK--KTA--ELLRRITkdhTVLVIEHDMQFVGDIADRVTVMHQGKVLSEG 234
Cdd:cd03269 148 ELLILDEPFSGLDPVNVEllKDVirELARAGK---TVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
25-252 |
6.81e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 101.31 E-value: 6.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 25 FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGK-----ELtrlkehqivhsGVGrkFQtpsvf 99
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallEL-----------GAG--FH----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 100 EDLTVFENLEVSypqGhSVMGalaFKRS--AEVVAAVEDVAEtifLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLML 177
Cdd:COG1134 101 PELTGRENIYLN---G-RLLG---LSRKeiDEKFDEIVEFAE---LGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 178 DEPVAGMSVAERKKTAELLRRITKDH-TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEhvksdpKVIEVYLGH 252
Cdd:COG1134 171 DEVLAVGDAAFQKKCLARIRELRESGrTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE------EVIAAYEAL 240
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
12-243 |
1.38e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 103.38 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQivhSGVGR 91
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ---RPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KFQTPSVFEDLTVFENLEVSYPQGHsvmgaLAfkrSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQK 171
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGLKQDK-----LP---KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 172 PDLLMLDEPVAGMSVAERKK----TAELLRRITKdhTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDP 243
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRmqleVVDILERVGV--TCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-244 |
5.96e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.56 E-value: 5.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 4 AKAQSKDFLLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRL-KEH 82
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 83 QIVHSgvgrKFQTPSVFEDLTVFENleVSYpqghsvmgALAFKR--SAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQ 160
Cdd:PRK09452 86 RHVNT----VFQSYALFPHMTVFEN--VAF--------GLRMQKtpAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 161 WLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEH 238
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
....*.
gi 552559136 239 VKSDPK 244
Cdd:PRK09452 232 IYEEPK 237
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-239 |
6.21e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.32 E-value: 6.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvhsgvGRK 92
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL-----ARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 F----QTPSVFEDLTVFEnlEVSYpqGHSVMGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLL 168
Cdd:PRK11231 78 LallpQHHLTPEGITVRE--LVAY--GRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552559136 169 IQKPDLLMLDEPVAGMSVAERKKTAELLRRI-TKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHV 239
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-249 |
6.64e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 100.26 E-value: 6.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGRK 92
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQtpSVFEDLTVFENLEVsypqghsvmgalaFKR-----SAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGML 167
Cdd:PRK13537 88 FD--NLDPDFTVRENLLV-------------FGRyfglsAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 168 LIQKPDLLMLDEPVAGMSVAERKKTAELLRRI-TKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGS----IEH-VKS 241
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAphalIESeIGC 232
|
....*...
gi 552559136 242 DpkVIEVY 249
Cdd:PRK13537 233 D--VIEIY 238
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-244 |
7.38e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.83 E-value: 7.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLD----LICGKTKA-TSGSIRFDGKELTRLKEHQIvHS 87
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEArVSGEVYLDGQDIFKMDVIEL-RR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 88 GVGRKFQTPSVFEDLTVFENLEVSYPQGHSVmgalafKRSAEVVAAVEDVAETIFL----KDALDQPASLLSHGQKQWLE 163
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLKLNRLV------KSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 164 IGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDP 243
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
.
gi 552559136 244 K 244
Cdd:PRK14247 237 R 237
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-230 |
9.30e-25 |
|
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: 96.73 E-value: 9.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSfdgfKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGR 91
Cdd:cd03215 4 VLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 kfqtpsVFEDltvfenlevsypqghsvmgalafkRSAEVVAAVEDVAETIFLkdaldqpASLLSHGQKQWLEIGMLLIQK 171
Cdd:cd03215 80 ------VPED------------------------RKREGLVLDLSVAENIAL-------SSLLSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 172 PDLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
13-225 |
1.24e-24 |
|
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: 101.98 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDG-FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvHSGVGR 91
Cdd:TIGR02857 322 LEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KFQTPSVFEDlTVFENLEVSYPQGhsvmGALAFKRSAEVVAAVEDVAEtifLKDALDQP----ASLLSHGQKQWLEIGML 167
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARPDA----SDAEIREALERAGLDEFVAA---LPQGLDTPigegGAGLSGGQAQRLALARA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552559136 168 LIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDiADRVTVM 225
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-239 |
1.50e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 98.55 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFK--AVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTrlkEHQI--VHS 87
Cdd:PRK13635 5 IIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS---EETVwdVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 88 GVGRKFQTP------SVFEDLTVF--ENLEVSYPQghsvMgalaFKRsaeVVAAVEDVAETIFLKdalDQPASlLSHGQK 159
Cdd:PRK13635 82 QVGMVFQNPdnqfvgATVQDDVAFglENIGVPREE----M----VER---VDQALRQVGMEDFLN---REPHR-LSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 160 QWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRIT--KDHTVLVIEHDMQFVGDiADRVTVMHQGKVLSEGSIE 237
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPE 225
|
..
gi 552559136 238 HV 239
Cdd:PRK13635 226 EI 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
24-244 |
3.60e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 98.72 E-value: 3.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 24 GFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHS--GVGRKFQTPSVFED 101
Cdd:PRK11153 17 TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArrQIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 102 LTVFENleVSYPQghsvmgALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPV 181
Cdd:PRK11153 97 RTVFDN--VALPL------ELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552559136 182 AGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPK 244
Cdd:PRK11153 169 SALDPATTRSILELLKDINRELglTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPK 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
26-239 |
4.02e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.81 E-value: 4.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 26 KAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELT----RLKEhqiVHSGVGRKFQTP--SVF 99
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSD---IRKKVGLVFQYPeyQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 100 EDlTVFENLEVsypqGHSVMGALAFKRSAEVVAAVEDVAetIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDE 179
Cdd:PRK13637 98 EE-TIEKDIAF----GPINLGLSEEEIENRVKRAMNIVG--LDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552559136 180 PVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHV 239
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
23-247 |
8.18e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 96.69 E-value: 8.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 23 DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQI-VHSGVGRKFQ------- 94
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLeVRKTVGIVFQnpddqlf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 95 TPSVFEDLTvFENLEVSYPQghsvmgalafkrsAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDL 174
Cdd:PRK13639 93 APTVEEDVA-FGPLNLGLSK-------------EEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552559136 175 LMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIE-HDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPKVIE 247
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
10-246 |
9.08e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 96.84 E-value: 9.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 10 DFLLAVEGLTVSF-DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQI-VHS 87
Cdd:PRK13636 3 DYILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMkLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 88 GVGRKFQTP-------SVFEDLTvFENLEVSYPQghsvmgalafkrsAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQ 160
Cdd:PRK13636 83 SVGMVFQDPdnqlfsaSVYQDVS-FGAVNLKLPE-------------DEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 161 WLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITK--DHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEH 238
Cdd:PRK13636 149 RVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKE 228
|
....*...
gi 552559136 239 VKSDPKVI 246
Cdd:PRK13636 229 VFAEKEML 236
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-244 |
1.03e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.39 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFK-----------AVDDLSFYLDPKEIRVIIGPNGAGKTT----VLDLIcgktkATSGSIRFDGKEL 76
Cdd:PRK15134 275 LLDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 77 TRLKEHQIVhsGVGRKFQTpsVFED--------LTVF----ENLEVSYPQghsvmgALAFKRSAEVVAAVEDVAetifLK 144
Cdd:PRK15134 350 HNLNRRQLL--PVRHRIQV--VFQDpnsslnprLNVLqiieEGLRVHQPT------LSAAQREQQVIAVMEEVG----LD 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 145 DALDQ--PASLlSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTV--LVIEHDMQFVGDIAD 220
Cdd:PRK15134 416 PETRHryPAEF-SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCH 494
|
250 260
....*....|....*....|....
gi 552559136 221 RVTVMHQGKVLSEGSIEHVKSDPK 244
Cdd:PRK15134 495 QVIVLRQGEVVEQGDCERVFAAPQ 518
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
16-243 |
1.07e-23 |
|
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: 95.45 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 16 EGLTVSF-DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSgVGRKFQ 94
Cdd:cd03295 4 ENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK-IGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 95 TPSVFEDLTVFENLEVsYPQGHSVMGALAFKRSAEVVAAVeDVAETIFLKDALDQpaslLSHGQKQWLEIGMLLIQKPDL 174
Cdd:cd03295 83 QIGLFPHMTVEENIAL-VPKLLKWPKEKIRERADELLALV-GLDPAEFADRYPHE----LSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552559136 175 LMLDEPVAGMSVAERKKTAELLRRITKD--HTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDP 243
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
17-251 |
2.38e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.44 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 17 GLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRlkEHQIVHSGVGRKFQTP 96
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA--RARLARARIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 97 SVFEDLTVFENLevsypqghSVMGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLM 176
Cdd:PRK13536 124 NLDLEFTVRENL--------LVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 177 LDEPVAGMSVAERKKTAELLRR-ITKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSI-----EHVKSDpkVIEVYL 250
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPhalidEHIGCQ--VIEIYG 273
|
.
gi 552559136 251 G 251
Cdd:PRK13536 274 G 274
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-244 |
2.51e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.84 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVL-------DLICGKTkaTSGSIRFDGKELTRLKEHQI 84
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLrsinrmnDLNPEVT--ITGSIVYNGHNIYSPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 85 -VHSGVGRKFQTPSVFEdLTVFENleVSYpqGHSVMGalaFKRSAEVVAAVED--VAETIF--LKDALDQPASLLSHGQK 159
Cdd:PRK14239 83 dLRKEIGMVFQQPNPFP-MSIYEN--VVY--GLRLKG---IKDKQVLDEAVEKslKGASIWdeVKDRLHDSALGLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 160 QWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHV 239
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
....*
gi 552559136 240 KSDPK 244
Cdd:PRK14239 235 FMNPK 239
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-244 |
3.25e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 94.73 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 1 MNAAKaqSKDFLLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLK 80
Cdd:PRK14246 1 MEAGK--SAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 81 E-HQI----VHSGVGRKFQTPSVFEDLTVFENleVSYPqghsvMGALAFKRSAEVVAAVEDVAETIFL----KDALDQPA 151
Cdd:PRK14246 79 DiFQIdaikLRKEVGMVFQQPNPFPHLSIYDN--IAYP-----LKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 152 SLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIADRVTVMHQGKVL 231
Cdd:PRK14246 152 SQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
250
....*....|...
gi 552559136 232 SEGSIEHVKSDPK 244
Cdd:PRK14246 232 EWGSSNEIFTSPK 244
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-235 |
3.30e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 97.93 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 20 VSF---DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQiVHSGVGRKFQTP 96
Cdd:COG1132 345 VSFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES-LRRQIGVVPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 97 SVFEDlTVFENlevsypqghsvmgaLAFKRS----AEVVAA-----VEDVAETifLKDALDQP----ASLLSHGQKQWLE 163
Cdd:COG1132 424 FLFSG-TIREN--------------IRYGRPdatdEEVEEAakaaqAHEFIEA--LPDGYDTVvgerGVNLSGGQRQRIA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552559136 164 IGMLLIQKPDLLMLDEPVAGM-SVAERK-KTAelLRRITKDHTVLVIEHDMQFVGDiADRVTVMHQGKVLSEGS 235
Cdd:COG1132 487 IARALLKDPPILILDEATSALdTETEALiQEA--LERLMKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
26-242 |
4.01e-23 |
|
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: 97.57 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 26 KAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFD-GKELTRLKEHQIVHSG-----VGRKFQTPSVF 99
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPDGRGrakryIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 100 EDLTVFENLE----VSYPQGHSVMGALAfkrSAEVVAAVEDVAETIflkdaLDQPASLLSHGQKQWLEIGMLLIQKPDLL 175
Cdd:TIGR03269 378 PHRTVLDNLTeaigLELPDELARMKAVI---TLKMVGFDEEKAEEI-----LDKYPDELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 176 MLDEPVAGMSVAERKKTAE--LLRRITKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSD 242
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHsiLKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-230 |
5.64e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 5.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 15 VEGLTVSFDGFKAVDDLSFYLDPKEiRV-IIGPNGAGKTTVLDLICGKTKATSGSIRFD-GKELTRLKehqivhsgvgrk 92
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGD-RIgLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLP------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 fQTPSVFEDLTVFENLEVSYPQGHSVMGALAF------------KRSAEVVAAVEDV--------AETI-----FLKDAL 147
Cdd:COG0488 68 -QEPPLDDDLTVLDTVLDGDAELRALEAELEEleaklaepdedlERLAELQEEFEALggweaearAEEIlsglgFPEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 148 DQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPvagmsvaerkkT-----------AELLRRitKDHTVLVIEHDMQFVG 216
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEP-----------TnhldlesiewlEEFLKN--YPGTVLVVSHDRYFLD 213
|
250
....*....|....
gi 552559136 217 DIADRVTVMHQGKV 230
Cdd:COG0488 214 RVATRILELDRGKL 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-230 |
8.07e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.67 E-value: 8.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFdgkeltrlkehqivhsGVGR 91
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL----------------GETV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KF----QTPSVF-EDLTVFENLEVSYPQG-----HSVMGALAFKRsaevvaavedvaetiflkDALDQPASLLSHGQKQW 161
Cdd:COG0488 379 KIgyfdQHQEELdPDKTVLDELRDGAPGGteqevRGYLGRFLFSG------------------DDAFKPVGVLSGGEKAR 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552559136 162 LEIGMLLIQKPDLLMLDEP-----VAGMSVAErkktaELLrrITKDHTVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPtnhldIETLEALE-----EAL--DDFPGTVLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-197 |
8.46e-23 |
|
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: 92.04 E-value: 8.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEH---QIVHSGv 89
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpheNILYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 90 grkfQTPSVFEDLTVFENLEVSYP--QGHSVMgalafkrsaevvaaVEDVAETIFLKDALDQPASLLSHGQKQWLEIGML 167
Cdd:TIGR01189 80 ----HLPGLKPELSALENLHFWAAihGGAQRT--------------IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARL 141
|
170 180 190
....*....|....*....|....*....|
gi 552559136 168 LIQKPDLLMLDEPVAGMSVAERKKTAELLR 197
Cdd:TIGR01189 142 WLSRRPLWILDEPTTALDKAGVALLAGLLR 171
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
25-234 |
1.08e-22 |
|
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: 92.60 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 25 FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKeltrlkehqiVHS--GVGRKFQtpsvfEDL 102
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR----------VSSllGLGGGFN-----PEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 103 TVFENLEVSypqgHSVMGaLAFKRSAEVVAAVEDVAEtifLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVA 182
Cdd:cd03220 100 TGRENIYLN----GRLLG-LSRKEIDEKIDEIIEFSE---LGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552559136 183 GMSVAERKKTAELLR-RITKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEG 234
Cdd:cd03220 172 VGDAAFQEKCQRRLReLLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
6-244 |
1.36e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 94.39 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 6 AQSKDFLLAVEGLTVSFD-------------GFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFD 72
Cdd:PRK15079 2 TEGKKVLLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 73 GKELTRLKEHQI--VHSGVGRKFQTP--SVFEDLTV----FENLEVSYPQghsvMGALAFKRsaEVVAAVEDVAetiFLK 144
Cdd:PRK15079 82 GKDLLGMKDDEWraVRSDIQMIFQDPlaSLNPRMTIgeiiAEPLRTYHPK----LSRQEVKD--RVKAMMLKVG---LLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 145 DALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRV 222
Cdd:PRK15079 153 NLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRV 232
|
250 260
....*....|....*....|..
gi 552559136 223 TVMHQGKVLSEGSIEHVKSDPK 244
Cdd:PRK15079 233 LVMYLGHAVELGTYDEVYHNPL 254
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
9-248 |
1.89e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 92.75 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 9 KDFLLAVEGLTVSFDGFK--AVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvH 86
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI-R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 87 SGVGRKFQTP------SVFEDLTVF--ENLEVSypqghsvmgalafkrSAEVVAAVEDVAETIFLKDALDQPASLLSHGQ 158
Cdd:PRK13632 83 KKIGIIFQNPdnqfigATVEDDIAFglENKKVP---------------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 159 KQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRI--TKDHTVLVIEHDMQFVgDIADRVTVMHQGKVLSEGSI 236
Cdd:PRK13632 148 KQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKP 226
|
250
....*....|..
gi 552559136 237 EHVKSDPKVIEV 248
Cdd:PRK13632 227 KEILNNKEILEK 238
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-247 |
3.30e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.47 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 3 AAKAQSKDFLLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVL-------DLICGKTkaTSGSIRFDGKE 75
Cdd:PRK14271 12 AADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmnDKVSGYR--YSGDVLLGGRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 76 LTRLKEHQIVHSGVGRKFQTPSVFEdLTVFENLeVSYPQGHSVMGALAFKRSAEvvAAVEDVAETIFLKDALDQPASLLS 155
Cdd:PRK14271 90 IFNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNV-LAGVRAHKLVPRKEFRGVAQ--ARLTEVGLWDAVKDRLSDSPFRLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 156 HGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGS 235
Cdd:PRK14271 166 GGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGP 245
|
250
....*....|..
gi 552559136 236 IEHVKSDPKVIE 247
Cdd:PRK14271 246 TEQLFSSPKHAE 257
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
30-230 |
3.75e-22 |
|
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: 90.99 E-value: 3.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 30 DLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTrLKEHQIVHSGVGRKFQTPSVFEDlTVFENle 109
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHKYLHSKVSLVGQEPVLFAR-SLQDN-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 110 VSYPqghsvMGALAFKRSAEvvAAVEDVAETIFLKDAL------DQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAG 183
Cdd:cd03248 108 IAYG-----LQSCSFECVKE--AAQKAHAHSFISELASgydtevGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 552559136 184 MSVAERKKTAELLRRITKDHTVLVIEHDMQFVgDIADRVTVMHQGKV 230
Cdd:cd03248 181 LDAESEQQVQQALYDWPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-243 |
4.13e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 92.87 E-value: 4.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 1 MNAAKAQSKDFLLAVEGLTVSF---DG-FKAVDDLSFYLDPKEIRVIIGPNGAGKT-TVLDL--ICGKTKATSGSIRFDG 73
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTFstpDGdVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALmgLLAANGRIGGSATFNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 74 KELTRLKEHQIVHSgvgRKFQTPSVFEDLTVFEN--LEVsypqGHSVMGALAFKRSAEVVAAVEdvaETIFLKDALDQPA 151
Cdd:PRK09473 81 REILNLPEKELNKL---RAEQISMIFQDPMTSLNpyMRV----GEQLMEVLMLHKGMSKAEAFE---ESVRMLDAVKMPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 152 SL---------LSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIAD 220
Cdd:PRK09473 151 ARkrmkmypheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICD 230
|
250 260
....*....|....*....|...
gi 552559136 221 RVTVMHQGKVLSEGSIEHVKSDP 243
Cdd:PRK09473 231 KVLVMYAGRTMEYGNARDVFYQP 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-230 |
4.24e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 94.31 E-value: 4.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSfdgfKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVG- 90
Cdd:COG1129 256 VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAy 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 ----RKFQtpSVFEDLTVFENLEVSYPQGHSVMGALafkRSAEVVAAVEDVAETIFLK-DALDQPASLLSHGQKQWLEIG 165
Cdd:COG1129 332 vpedRKGE--GLVLDLSIRENITLASLDRLSRGGLL---DRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLA 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 166 MLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:COG1129 407 KWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEgKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-249 |
6.63e-22 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 90.76 E-value: 6.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 31 LSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKAtSGSIRFDGKELTRLKEHQIVHSgvgRKF---QTPSVFEdLTVFEN 107
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARH---RAYlsqQQTPPFA-MPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 108 LEVSYPQGhsvmgalafKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQ-----KPD--LLMLDEP 180
Cdd:PRK03695 90 LTLHQPDK---------TRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 181 VAGMSVAERKKTAELLRRI-TKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPKVIEVY 249
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
15-239 |
7.19e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 90.91 E-value: 7.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 15 VEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvhsgvGRKF- 93
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSREL-----AKRLa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 94 ---QTPSVFEDLTVFEnLeVS---YPqgHSvMGALafkrSAEVVAAVEDVAETIFLKDA----LDQpaslLSHGQKQWLE 163
Cdd:COG4604 79 ilrQENHINSRLTVRE-L-VAfgrFP--YS-KGRL----TAEDREIIDEAIAYLDLEDLadryLDE----LSGGQRQRAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 164 IGMLLIQKPDLLMLDEP---------VAGMSvaerkktaeLLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLS 232
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPlnnldmkhsVQMMK---------LLRRLADELgkTVVIVLHDINFASCYADHIVAMKDGRVVA 216
|
....*..
gi 552559136 233 EGSIEHV 239
Cdd:COG4604 217 QGTPEEI 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-235 |
1.40e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 91.70 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 7 QSKDFLLaVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTrlkEHQIVH 86
Cdd:PRK11432 2 TQKNFVV-LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT---HRSIQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 87 SGVGRKFQTPSVFEDLTVFENleVSYpqGHSVMGALAFKRSAEVVAAVEDVAETIFLKDALDQpaslLSHGQKQWLEIGM 166
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGEN--VGY--GLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQ----ISGGQQQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552559136 167 LLIQKPDLLMLDEPV----AGMSVAERKKTAELLRRItkDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGS 235
Cdd:PRK11432 150 ALILKPKVLLFDEPLsnldANLRRSMREKIRELQQQF--NITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGS 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-235 |
1.53e-21 |
|
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: 89.60 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 20 VSF----DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvHSGVGRKFQT 95
Cdd:cd03251 6 VTFrypgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL-RRQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 96 PSVFEDlTVFENlevsypqghsvmgaLAFKRSAEVVAAVEDVAET-------IFLKDALDQP----ASLLSHGQKQWLEI 164
Cdd:cd03251 85 VFLFND-TVAEN--------------IAYGRPGATREEVEEAARAanahefiMELPEGYDTVigerGVKLSGGQRQRIAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552559136 165 GMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDiADRVTVMHQGKVLSEGS 235
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGT 219
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
12-243 |
1.58e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 89.99 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGK-----ELTRLKEHQ--- 83
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAErrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 84 -------IVHsgvgrkfQTP------SVFEDLTVFENLEVsypQGHSVMGALAfKRSAEVVAAVEDVAETIflkDalDQP 150
Cdd:PRK11701 86 llrtewgFVH-------QHPrdglrmQVSAGGNIGERLMA---VGARHYGDIR-ATAGDWLERVEIDAARI---D--DLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 151 ASlLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQG 228
Cdd:PRK11701 150 TT-FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARLLAHRLLVMKQG 228
|
250
....*....|....*
gi 552559136 229 KVLSEGSIEHVKSDP 243
Cdd:PRK11701 229 RVVESGLTDQVLDDP 243
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-242 |
3.09e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.04 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRL---KEHQIvhsG 88
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtpaKAHQL---G 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 89 VGRKFQTPSVFEDLTVFENLEVSYPQghsvmGALAFKRSAEVVAAVedvaeTIFLKdaLDQPASLLSHGQKQWLEIGMLL 168
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGLPK-----RQASMQKMKQLLAAL-----GCQLD--LDSSAGSLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552559136 169 IQKPDLLMLDEPVAGMSVAErkkTAELLRRI----TKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSD 242
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAE---TERLFSRIrellAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-245 |
4.51e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 89.05 E-value: 4.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 6 AQSKDFLLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIV 85
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 86 HSgvgRK-----FQTPSVFEDLTVFENleVSYP-QGHSVMGALAFKRSaeVVAAVEDVAetifLKDALDQPASLLSHGQK 159
Cdd:PRK11831 81 TV---RKrmsmlFQSGALFTDMNVFDN--VAYPlREHTQLPAPLLHST--VMMKLEAVG----LRGAAKLMPSELSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 160 QWLEIGMLLIQKPDLLMLDEPVAG-----MSVaerkktaeLLRRITK-DH----TVLVIEHDMQFVGDIADRVTVMHQGK 229
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGqdpitMGV--------LVKLISElNSalgvTCVVVSHDVPEVLSIADHAYIVADKK 221
|
250
....*....|....*...
gi 552559136 230 VLSEGSIE--HVKSDPKV 245
Cdd:PRK11831 222 IVAHGSAQalQANPDPRV 239
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
13-235 |
5.21e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 91.70 E-value: 5.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAV-DDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLkEHQIVHSGVGR 91
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL-SHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KFQTPSVFEDlTVFENL----EVSYPQghsVMGALAFKRSAEVVAAVEDVAETIflkdaLDQPASLLSHGQKQWLEIGML 167
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVtlgrDISEEQ---VWQALETVQLAELARSLPDGLYTP-----LGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552559136 168 LIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDiADRVTVMHQGKVLSEGS 235
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGT 557
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-198 |
5.85e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.24 E-value: 5.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGK--ELTRLKE--HQIVHsg 88
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiDDPDVAEacHYLGH-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 89 vgRKFQTPSvfedLTVFENLEvsypqghsvmGALAFKRSAE--VVAAVEDVAetifLKDALDQPASLLSHGQKQWLEIGM 166
Cdd:PRK13539 81 --RNAMKPA----LTVAENLE----------FWAAFLGGEEldIAAALEAVG----LAPLAHLPFGYLSAGQKRRVALAR 140
|
170 180 190
....*....|....*....|....*....|..
gi 552559136 167 LLIQKPDLLMLDEPVAGMSVAERKKTAELLRR 198
Cdd:PRK13539 141 LLVSNRPIWILDEPTAALDAAAVALFAELIRA 172
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
31-249 |
6.57e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 88.36 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 31 LSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTkATSGSIRFDGKELTRLKEHQIVHSgvgRKF---QTPSVFeDLTVFEN 107
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARH---RAYlsqQQSPPF-AMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 108 LEVSYPQGHSvmgalafkrSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQ-----KPD--LLMLDEP 180
Cdd:COG4138 90 LALHQPAGAS---------SEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 181 VAGMSVAERKKTAELLRRIT-KDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPKVIEVY 249
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELCqQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVF 230
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
24-230 |
8.87e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.24 E-value: 8.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 24 GFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQI--VHSGVGRKFQTPSVFED 101
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 102 LTVFENleVSYPQghSVMGALAFKRSAEVVAAVEDVAetiFLKDALDQPASlLSHGQKQWLEIGMLLIQKPDLLMLDEPV 181
Cdd:PRK10908 94 RTVYDN--VAIPL--IIAGASGDDIRRRVSAALDKVG---LLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 552559136 182 AGMSVAERKKTAELLRRITK-DHTVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:PRK10908 166 GNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
12-244 |
1.14e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 89.03 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDG----FKAVDDLSFYLDPKEIRVIIGPNGAGKT----TVLDLICGKTKATSGSIRFDGKELTRLKE-- 81
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEke 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 82 -HQIVHSGVGRKFQTPsvfedltvFENLEVSYPQGHSVMGALAFKRSAEVVAAVEDVAETIFLKDALDqPASL------- 153
Cdd:PRK11022 83 rRNLVGAEVAMIFQDP--------MTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPD-PASRldvyphq 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 154 LSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITK--DHTVLVIEHDMQFVGDIADRVTVMHQGKVL 231
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
250
....*....|...
gi 552559136 232 SEGSIEHVKSDPK 244
Cdd:PRK11022 234 ETGKAHDIFRAPR 246
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-246 |
1.34e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.94 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDG-FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQiVHSGVG 90
Cdd:PRK13652 3 LIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE-VRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 RKFQTPsvfEDLTVFENLEVSYPQGHSVMGAlafkRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQ 170
Cdd:PRK13652 82 LVFQNP---DDQIFSPTVEQDIAFGPINLGL----DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552559136 171 KPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPKVI 246
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLL 232
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-243 |
2.05e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 88.42 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDG----FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTK----ATSGSIRFDGKELTRL---K 80
Cdd:COG4170 3 LLDIRNLTIEIDTpqgrVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLsprE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 81 EHQIVHSGVGRKFQTPSVFED--LTVFENLEVSYPQgHSVMG---ALAFKRSAEVVAAVEDVAetifLKDALDQPASL-- 153
Cdd:COG4170 83 RRKIIGREIAMIFQEPSSCLDpsAKIGDQLIEAIPS-WTFKGkwwQRFKWRKKRAIELLHRVG----IKDHKDIMNSYph 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 154 -LSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:COG4170 158 eLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQgtSILLISHDLESISQWADTITVLYCGQT 237
|
250
....*....|...
gi 552559136 231 LSEGSIEHVKSDP 243
Cdd:COG4170 238 VESGPTEQILKSP 250
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-244 |
2.36e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 86.82 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 9 KDFLLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLD-----LICGKTKATSGSIRFDGKELTRLKEHQ 83
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 84 I-VHSGVGRKFQTPSVFEDLTVFENLEVSYPQGHSVMGAlafKRSAEVVA-AVEDVAETIFLKDALDQPASLLSHGQKQW 161
Cdd:PRK14267 81 IeVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSK---KELDERVEwALKKAALWDEVKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 162 LEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKS 241
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
...
gi 552559136 242 DPK 244
Cdd:PRK14267 238 NPE 240
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-235 |
2.75e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.17 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 32 SFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQivhSGVGRKFQTPSVFEDLTVFENLEVS 111
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR---RPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 112 YPQGhsvmgalaFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKK 191
Cdd:PRK10771 96 LNPG--------LKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 552559136 192 TAELLRRI--TKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGS 235
Cdd:PRK10771 168 MLTLVSQVcqERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
13-239 |
3.31e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 88.91 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSfdgfkAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQ-----IVHS 87
Cdd:PRK10762 258 LKVDNLSGP-----GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 88 GVGRKfqTPSVFEDLTVFENLEV-SYPQGHSVMGALafKRSAEvVAAVEDVAETIFLKD-ALDQPASLLSHGQKQWLEIG 165
Cdd:PRK10762 333 SEDRK--RDGLVLGMSVKENMSLtALRYFSRAGGSL--KHADE-QQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIA 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552559136 166 MLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH-TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHV 239
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGlSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQA 482
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
28-232 |
3.77e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 86.71 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 28 VDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSgVGRKFQTP------SVFED 101
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK-IGMVFQNPdnqfvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 102 LTVF--ENLEVSYpqghsvmgalafkrsAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDE 179
Cdd:PRK13650 102 DVAFglENKGIPH---------------EEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 552559136 180 PVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGdIADRVTVMHQGKVLS 232
Cdd:PRK13650 167 ATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVA-LSDRVLVMKNGQVES 220
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-243 |
3.92e-20 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 87.55 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSF---DG-FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTK----ATSGSIRFDGKELTRL---K 80
Cdd:PRK15093 3 LLDIRNLTIEFktsDGwVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLsprE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 81 EHQIVHSGVGRKFQTPSvfedltvfENLEVSYPQGHSVMGAL---AFK------------RSAEVVAAVEdvaetifLKD 145
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQ--------SCLDPSERVGRQLMQNIpgwTYKgrwwqrfgwrkrRAIELLHRVG-------IKD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 146 ALDQPASL---LSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIAD 220
Cdd:PRK15093 148 HKDAMRSFpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQWAD 227
|
250 260
....*....|....*....|...
gi 552559136 221 RVTVMHQGKVLSEGSIEHVKSDP 243
Cdd:PRK15093 228 KINVLYCGQTVETAPSKELVTTP 250
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-234 |
5.21e-20 |
|
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: 84.52 E-value: 5.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGF------KAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTK--ATSGSIRFDGKELTRLKEHQI 84
Cdd:cd03213 4 LSFRNLTVTVKSSpsksgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 85 vhsgVGRKFQTPSVFEDLTVFENLEVSypqghsvmgalAFKRSaevvaavedvaetiflkdaldqpaslLSHGQKQWLEI 164
Cdd:cd03213 84 ----IGYVPQDDILHPTLTVRETLMFA-----------AKLRG--------------------------LSGGERKRVSI 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552559136 165 GMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH-TVLVIEHdmQFVGDI---ADRVTVMHQGKVLSEG 234
Cdd:cd03213 123 ALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGrTIICSIH--QPSSEIfelFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-247 |
6.16e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.21 E-value: 6.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvhsgvGR 91
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLL-----AL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KFQTPSVFEDltvfENLEVSYPQGHSvmgALAFKRSAEVVAAVE---DVAETIFLKDAL---DQPASLLSHGQKQWLEIG 165
Cdd:PRK13638 76 RQQVATVFQD----PEQQIFYTDIDS---DIAFSLRNLGVPEAEitrRVDEALTLVDAQhfrHQPIQCLSHGQKKRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 166 MLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRIT-KDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPK 244
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTE 228
|
...
gi 552559136 245 VIE 247
Cdd:PRK13638 229 AME 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-230 |
6.39e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.18 E-value: 6.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 5 KAQSKDF-LLAVEGLTvsFDGFKavdDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQ 83
Cdd:PRK15439 260 RQQAAGApVLTVEDLT--GEGFR---NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 84 IVHSGV-----GRkfQTPSVFEDLTVFENLeVSYPqgHSVMGAlaFKRSAEVVAAVEDVAETIFLK-DALDQPASLLSHG 157
Cdd:PRK15439 335 RLARGLvylpeDR--QSSGLYLDAPLAWNV-CALT--HNRRGF--WIKPARENAVLERYRRALNIKfNHAEQAARTLSGG 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552559136 158 QKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHT-VLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:PRK15439 408 NQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
13-222 |
6.73e-20 |
|
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: 84.47 E-value: 6.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEhqIVHSGVGRK 92
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD--SIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENLEvsypqghsvmgalaFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKP 172
Cdd:cd03231 79 GHAPGIKTTLSVLENLR--------------FWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 173 DLLMLDEPVAGMSVAERKKTAELLRRitkdHT------VLVIEHDMQFVGDIADRV 222
Cdd:cd03231 145 PLWILDEPTTALDKAGVARFAEAMAG----HCarggmvVLTTHQDLGLSEAGAREL 196
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-247 |
7.15e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.52 E-value: 7.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRL-KEHQIVhsgvg 90
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgAERGVV----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 rkFQTPSVFEDLTVFENLEVsypqGHSVMGALAFKRSAEVVAAVEDVAetifLKDALDQPASLLSHGQKQWLEIGMLLIQ 170
Cdd:PRK11248 76 --FQNEGLLPWRNVQDNVAF----GLQLAGVEKMQRLEIAHQMLKKVG----LEGAEKRYIWQLSGGQRQRVGIARALAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 171 KPDLLMLDEPVAGMSVAERKKTAELLRRITKD--HTVLVIEHDMQ---FV-----------GDIADRVTVMHQGKVLSEG 234
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITHDIEeavFMatelvllspgpGRVVERLPLNFARRFVAGE 225
|
250
....*....|...
gi 552559136 235 SIEHVKSDPKVIE 247
Cdd:PRK11248 226 SSRSIKSDPQFIA 238
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-235 |
7.67e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 88.09 E-value: 7.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 19 TVSFDGFK-AVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSgVGRKFQTPS 97
Cdd:PRK13657 341 SFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN-IAVVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 98 VFeDLTVFENLEVSYPQGhsvmgalafkRSAEVVAAVEDVAETIFLKDALD-------QPASLLSHGQKQWLEIGMLLIQ 170
Cdd:PRK13657 420 LF-NRSIEDNIRVGRPDA----------TDEEMRAAAERAQAHDFIERKPDgydtvvgERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552559136 171 KPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDiADRVTVMHQGKVLSEGS 235
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGS 552
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
16-235 |
8.40e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 88.26 E-value: 8.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 16 EGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKEL------TRLKehqivhsgV 89
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdagdiaTRRR--------V 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 90 GRKFQTPSVFEDLTVFENLEVsypqgHsvmgALAFKRSAEVVAA-VEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLL 168
Cdd:NF033858 342 GYMSQAFSLYGELTVRQNLEL-----H----ARLFHLPAAEIAArVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAV 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552559136 169 IQKPDLLMLDEPVAGMSVAER----KKTAELLRRitkDH-TVLVIEHDMqfvgDIA---DRVTVMHQGKVLSEGS 235
Cdd:NF033858 413 IHKPELLILDEPTSGVDPVARdmfwRLLIELSRE---DGvTIFISTHFM----NEAercDRISLMHAGRVLASDT 480
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-249 |
8.58e-20 |
|
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: 85.14 E-value: 8.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 10 DFLLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKT-KATSGSIRFDGKELTR-----LKEHQ 83
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERRGGedvweLRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 84 -IVHSGVGRKFQtpsvfEDLTVFENLeVSypqG-HSVMGaLAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQW 161
Cdd:COG1119 81 gLVSPALQLRFP-----RDETVLDVV-LS---GfFDSIG-LYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 162 LEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKD---HTVLVIEHdmqfVGDIAD---RVTVMHQGKVLSEGS 235
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgapTLVLVTHH----VEEIPPgitHVLLLKDGRVVAAGP 226
|
250
....*....|....
gi 552559136 236 IEHVKSDPKVIEVY 249
Cdd:COG1119 227 KEEVLTSENLSEAF 240
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-224 |
9.21e-20 |
|
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: 87.92 E-value: 9.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 18 LTVSFDGFKavddLSfyLDPKEIRV-----IIGPNGAGKTTVLDLICGKTKATSGSIRFDGKeltrlkehqivhsgVGRK 92
Cdd:COG1245 347 LTKSYGGFS----LE--VEGGEIREgevlgIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--------------ISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENLEVSYPQGhsvMGALAFKrsaevvaavEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKP 172
Cdd:COG1245 407 PQYISPDYDGTVEEFLRSANTDD---FGSSYYK---------TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDA 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 552559136 173 DLLMLDEPVAGMSVAERKKTAELLRRIT--KDHTVLVIEHDMQFVGDIADRVTV 224
Cdd:COG1245 475 DLYLLDEPSAHLDVEQRLAVAKAIRRFAenRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-239 |
1.23e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.82 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvhsgvGRK 92
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA-----SRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 F----QTPSVFEDLTVFENLEVSYPQGHSVMGALAFKRSAEVVAAVEDVAETIFlkdaLDQPASLLSHGQKQWLEIGMLL 168
Cdd:PRK09536 79 VasvpQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQF----ADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552559136 169 IQKPDLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHV 239
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-244 |
1.27e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.65 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 26 KAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELT------RLKEhqiVHSGVGRKFQTPSV- 98
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKK---LRKKVSLVFQFPEAq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 99 -FEDlTVFENLEvsypqghsvMGALAFKRSAEVV--AAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLL 175
Cdd:PRK13641 98 lFEN-TVLKDVE---------FGPKNFGFSEDEAkeKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 176 MLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPK 244
Cdd:PRK13641 168 CLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
39-234 |
1.37e-19 |
|
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: 84.08 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 39 EIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLkehQIVHSGVGRKFQTPSVFEDLTVFENLEVSYPQGhsv 118
Cdd:cd03298 25 EITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA---PPADRPVSMLFQENNLFAHLTVEQNVGLGLSPG--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 119 mgalaFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRR 198
Cdd:cd03298 99 -----LKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 552559136 199 ITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEG 234
Cdd:cd03298 174 LHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-243 |
2.11e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 86.82 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 16 EGLTV-SFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATsGSIRFDGKELTRLKE----HQIvhSGVG 90
Cdd:PRK11174 353 EDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPeswrKHL--SWVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 rkfQTPSVFEDlTVFENLEVSYPQG--HSVMGALAFKRSAEVVAAvedvaetifLKDALDQP----ASLLSHGQKQWLEI 164
Cdd:PRK11174 430 ---QNPQLPHG-TLRDNVLLGNPDAsdEQLQQALENAWVSEFLPL---------LPQGLDTPigdqAAGLSVGQAQRLAL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 165 GMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIaDRVTVMHQGKVLSEGSIEHVKSDP 243
Cdd:PRK11174 497 ARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
43-243 |
2.79e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 84.69 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 43 IIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELT---RLKEHQIVHSGVGRKFQTP--SVFEDlTVFENLEVSyPQGHS 117
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkKNKKLKPLRKKVGIVFQFPehQLFEE-TVEKDICFG-PMNFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 118 VMGALAFKRSAEVVAAV---EDVaetiflkdaLDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAE 194
Cdd:PRK13634 116 VSEEDAKQKAREMIELVglpEEL---------LARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMME 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 552559136 195 LLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDP 243
Cdd:PRK13634 187 MFYKLHKEKglTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
8-247 |
3.27e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 84.47 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 8 SKDFLLAVEGLTVSFDGFK--AVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICG---KTKATSGSIRFDGKELTRlKEH 82
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllPDDNPNSKITVDGITLTA-KTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 83 QIVHSGVGRKFQTP------SVFEDLTVF--ENLEVSYPqghsvmgalafkrsaEVVAAVEDVAETIFLKDALDQPASLL 154
Cdd:PRK13640 80 WDIREKVGIVFQNPdnqfvgATVGDDVAFglENRAVPRP---------------EMIKIVRDVLADVGMLDYIDSEPANL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 155 SHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQfVGDIADRVTVMHQGKVLS 232
Cdd:PRK13640 145 SGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDID-EANMADQVLVLDDGKLLA 223
|
250
....*....|....*
gi 552559136 233 EGSIEHVKSDPKVIE 247
Cdd:PRK13640 224 QGSPVEIFSKVEMLK 238
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
13-229 |
3.31e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.12 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGRK 92
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSVFEDLTVFENLevsypqghsVMGAL----AFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLL 168
Cdd:PRK11288 85 YQELHLVPEMTVAENL---------YLGQLphkgGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552559136 169 IQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTV-LVIEHDMQFVGDIADRVTVMHQGK 229
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRViLYVSHRMEEIFALCDAITVFKDGR 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
8-247 |
4.86e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.52 E-value: 4.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 8 SKDFLLAVEGLTVSFDG-----FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIR---------FDG 73
Cdd:PRK13631 17 SDDIILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiyigdkKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 74 KELT------RLKEHQIVHSGVGRKFQTP--SVFEDlTVFENLevsypqghsVMGALAFKRSAEvvAAVEDVA---ETIF 142
Cdd:PRK13631 97 HELItnpyskKIKNFKELRRRVSMVFQFPeyQLFKD-TIEKDI---------MFGPVALGVKKS--EAKKLAKfylNKMG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 143 LKDA-LDQPASLLSHGQKQWLEI-GMLLIQkPDLLMLDEPVAGMSVAERKKTAELLRRITKDH-TVLVIEHDMQFVGDIA 219
Cdd:PRK13631 165 LDDSyLERSPFGLSGGQKRRVAIaGILAIQ-PEILIFDEPTAGLDPKGEHEMMQLILDAKANNkTVFVITHTMEHVLEVA 243
|
250 260
....*....|....*....|....*...
gi 552559136 220 DRVTVMHQGKVLSEGSIEHVKSDPKVIE 247
Cdd:PRK13631 244 DEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-211 |
4.94e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.84 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEhQIVHSGVGR 91
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KFQTPSVFEDlTVFENLEVSYpqghsvmgaLAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQK 171
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIFPW---------QIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 552559136 172 PDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVI--EHD 211
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHD 197
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
39-230 |
5.11e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 84.70 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 39 EIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKeltRLKEHQIVHSGVGRKFQTPSVFEDLTVFENLevsypqghSV 118
Cdd:PRK11000 30 EFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---RMNDVPPAERGVGMVFQSYALYPHLSVAENM--------SF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 119 MGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPV----AGMSVAERKKTAE 194
Cdd:PRK11000 99 GLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLsnldAALRVQMRIEISR 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 552559136 195 LLRRITKdhTVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:PRK11000 179 LHKRLGR--TMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-235 |
5.15e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 83.68 E-value: 5.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 25 FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKEL---TRLKEHQIVHSGVGRKFQTP--SVF 99
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthkTKDKYIRPVRKRIGMVFQFPesQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 100 EDlTVFENLEvsypqghsvMGALAFKRSAEVVA--AVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLML 177
Cdd:PRK13646 100 ED-TVEREII---------FGPKNFKMNLDEVKnyAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 178 DEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGS 235
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQTDEnkTIILVSHDMNEVARYADEVIVMKEGSIVSQTS 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-211 |
5.92e-19 |
|
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: 85.49 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 3 AAKAQSKDFLLAVEGLTVSFDGFKAV-DDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKE 81
Cdd:TIGR02868 325 AGAVGLGKPTLELRDLSAGYPGAPPVlDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 82 HQiVHSGVGRKFQTPSVFeDLTVFENLEVSYPQ--GHSVMGALAFKRSAEVVAAVEDVAETIflkdaLDQPASLLSHGQK 159
Cdd:TIGR02868 405 DE-VRRRVSVCAQDAHLF-DTTVRENLRLARPDatDEELWAALERVGLADWLRALPDGLDTV-----LGEGGARLSGGER 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 552559136 160 QWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHD 211
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-242 |
8.29e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.88 E-value: 8.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 20 VSF----DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRF-----DGKELTRLKEHqivhsgVG 90
Cdd:PRK13648 13 VSFqyqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYnnqaiTDDNFEKLRKH------IG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 RKFQTP-SVFEDLTV-------FENLEVSYPQGHSvmgalafkrsaEVVAAVEDVAetiFLKDALDQPASLlSHGQKQWL 162
Cdd:PRK13648 87 IVFQNPdNQFVGSIVkydvafgLENHAVPYDEMHR-----------RVSEALKQVD---MLERADYEPNAL-SGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 163 EIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRI--TKDHTVLVIEHDMQFVGDiADRVTVMHQGKVLSEGSIEHVK 240
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
..
gi 552559136 241 SD 242
Cdd:PRK13648 231 DH 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-244 |
8.82e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.98 E-value: 8.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 10 DFLLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICG--KTKATSGSIRFDGKELT----RLKEHQ 83
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIFEGEELQasniRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 84 ---IVHsgvgrkfQTPSVFEDLTVFENLEV-SYPQGHSVMGALA-FKRSAEVVAAVE---DVAetiflkdaldQPASLLS 155
Cdd:PRK13549 83 giaIIH-------QELALVKELSVLENIFLgNEITPGGIMDYDAmYLRAQKLLAQLKldiNPA----------TPVGNLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 156 HGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAErkkTAELLRRIT--KDHTV--LVIEHDMQFVGDIADRVTVMHQGKvl 231
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASLTESE---TAVLLDIIRdlKAHGIacIYISHKLNEVKAISDTICVIRDGR-- 220
|
250
....*....|...
gi 552559136 232 segsieHVKSDPK 244
Cdd:PRK13549 221 ------HIGTRPA 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
44-235 |
1.14e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 82.87 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 44 IGPNGAGKTTVLDLICGKTKATSGSIRFDGKELT---RLKEHQIVHSGVGRKFQTP--SVFEDlTVFENLEVSyPQGHSV 118
Cdd:PRK13649 39 IGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsKNKDIKQIRKKVGLVFQFPesQLFEE-TVLKDVAFG-PQNFGV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 119 MGALAFKRSAEVVAAVeDVAETIFLKDALDqpaslLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRR 198
Cdd:PRK13649 117 SQEEAEALAREKLALV-GISESLFEKNPFE-----LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKK 190
|
170 180 190
....*....|....*....|....*....|....*...
gi 552559136 199 ITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGS 235
Cdd:PRK13649 191 LHQSgMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
13-230 |
1.22e-18 |
|
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: 80.34 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKA--VDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQI-VHSGV 89
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELgDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 90 grkfqtpsVFEDLTVFENlevsypqghsvmgalafkrsaevvaaveDVAETIflkdaldqpaslLSHGQKQWLEIGMLLI 169
Cdd:cd03246 81 --------LPQDDELFSG----------------------------SIAENI------------LSGGQRQRLGLARALY 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552559136 170 QKPDLLMLDEPVAGMSVAERKKTAELLRRITK-DHTVLVIEHDMQFVgDIADRVTVMHQGKV 230
Cdd:cd03246 113 GNPRILVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
15-244 |
1.39e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.11 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 15 VEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIR-----FDG-------KELTR-LKE 81
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditIDTarslsqqKGLIRqLRQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 82 HqivhsgVGRKFQTPSVFEDLTVFENLevsypqghsVMGALAFKRS--AEVVAAVEDVAETIFLKDALDQPASLLSHGQK 159
Cdd:PRK11264 86 H------VGFVFQNFNLFPHRTVLENI---------IEGPVIVKGEpkEEATARARELLAKVGLAGKETSYPRRLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 160 QWLEIGMLLIQKPDLLMLDEPVAGMS---VAERKKTAELLRRitKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSI 236
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDpelVGEVLNTIRQLAQ--EKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
|
....*...
gi 552559136 237 EHVKSDPK 244
Cdd:PRK11264 229 KALFADPQ 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
21-243 |
1.49e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 81.68 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 21 SFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELT--RLKEHQIVHSGvGRKFQTPSV 98
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA-GMVFQQFYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 99 FEDLTVFENlevsypqghsVM-GALAFKRSAEvvAAVEDVAETIFLKDALDQPA----SLLSHGQKQWLEIGMLLIQKPD 173
Cdd:PRK09493 89 FPHLTALEN----------VMfGPLRVRGASK--EEAEKQARELLAKVGLAERAhhypSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552559136 174 LLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDP 243
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-251 |
1.54e-18 |
|
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: 84.11 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICG--KTKATSGSIRFDGKELTRLKEHQIVHSGV 89
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 90 GRKFQTPSVFEDLTVFENL----EVSYPqGHSVMGALAFKRSAEVVAAVEDVAetiflkDALDQPASLLSHGQKQWLEIG 165
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIflgnEITLP-GGRMAYNAMYLRAKNLLRELQLDA------DNVTRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 166 MLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRItKDHTV--LVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVkSDP 243
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVacVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM-SED 231
|
....*...
gi 552559136 244 KVIEVYLG 251
Cdd:TIGR02633 232 DIITMMVG 239
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
27-246 |
2.17e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 82.06 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 27 AVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGRKFQTP------SVFE 100
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPdnqivaTIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 101 DLTVF--ENLEVSypqghsvmgalafkrSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLD 178
Cdd:PRK13633 105 EDVAFgpENLGIP---------------PEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 179 EPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDiADRVTVMHQGKVLSEGSIEHVKSDPKVI 246
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMM 238
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
12-217 |
2.33e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 80.23 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKE--HQIV---- 85
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeyHQDLlylg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 86 -HSGVGRkfqtpsvfeDLTVFENLEVSYPQGHSVmgalafkRSAEVVAAVEDVAetifLKDALDQPASLLSHGQKQWLEI 164
Cdd:PRK13538 81 hQPGIKT---------ELTALENLRFYQRLHGPG-------DDEALWEALAQVG----LAGFEDVPVRQLSAGQQRRVAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 165 GMLLIQKPDLLMLDEPVagmsVAERKKTAELLRRITKDHT------VLVIEHDMQFVGD 217
Cdd:PRK13538 141 ARLWLTRAPLWILDEPF----TAIDKQGVARLEALLAQHAeqggmvILTTHQDLPVASD 195
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-235 |
2.53e-18 |
|
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: 80.62 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 27 AVDDLSFYLDPKEiRV-IIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvhsgvgRKF-----QTPSVFE 100
Cdd:cd03244 19 VLKNISFSIKPGE-KVgIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL------RSRisiipQDPVLFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 101 DlTVFENLEvsyPQG-HSvmgalafkrSAEVVAAVEDVAetifLKDALDQPA-----------SLLSHGQKQWLEIGMLL 168
Cdd:cd03244 92 G-TIRSNLD---PFGeYS---------DEELWQALERVG----LKEFVESLPggldtvveeggENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 169 IQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDiADRVTVMHQGKVLSEGS 235
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
13-229 |
2.67e-18 |
|
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: 78.64 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDgkeltrlkehqivhsgvgrk 92
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 fqtpsvfedltvfENLEVSYpqghsvmgalafkrsaevvaavedvaetiflkdaLDQpaslLSHGQKQWLEIGMLLIQKP 172
Cdd:cd03221 61 -------------STVKIGY----------------------------------FEQ----LSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 173 DLLMLDEPVAGMSVAERKKTAELLRriTKDHTVLVIEHDMQFVGDIADRVTVMHQGK 229
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEALK--EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
30-245 |
2.92e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 83.62 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 30 DLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLkEHQIVHSGVGRKFQTPSVFEDlTVFENle 109
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY-DHHYLHRQVALVGQEPVLFSG-SVREN-- 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 110 VSYpqghsvmgALAFKRSAEVVA-AVEDVAETIFLKDA------LDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVA 182
Cdd:TIGR00958 575 IAY--------GLTDTPDEEIMAaAKAANAHDFIMEFPngydteVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552559136 183 GMSVAERKKTAELLRRitKDHTVLVIEHDMQFVGDiADRVTVMHQGKVLSEGSIEHVKSDPKV 245
Cdd:TIGR00958 647 ALDAECEQLLQESRSR--ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
5-224 |
3.16e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 83.32 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 5 KAQSKDFLLAVEGLTVSFDGFKavddLSfyLDPKEIRV-----IIGPNGAGKTTVLDLICGKTKATSGSIRFDGKeltrl 79
Cdd:PRK13409 333 DESERETLVEYPDLTKKLGDFS----LE--VEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK----- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 80 kehqivhsgVGRKFQTPSVFEDLTVFENLEVSYPQGHSVMgalaFKrsaevvaavEDVAETIFLKDALDQPASLLSHGQK 159
Cdd:PRK13409 402 ---------ISYKPQYIKPDYDGTVEDLLRSITDDLGSSY----YK---------SEIIKPLQLERLLDKNVKDLSGGEL 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 160 QWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRIT--KDHTVLVIEHDMQFVGDIADRVTV 224
Cdd:PRK13409 460 QRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAeeREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-220 |
3.28e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 81.37 E-value: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 3 AAKAQSKDFLLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVL-------DLICGKTkaTSGSIRFDGKE 75
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFR--VEGKVTFHGKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 76 LTRLKEHQI-VHSGVGRKFQTPSVFEDlTVFENleVSY-PQGHSVMGAL--AFKRSAEVVAAVEDVaetiflKDALDQPA 151
Cdd:PRK14243 79 LYAPDVDPVeVRRRIGMVFQKPNPFPK-SIYDN--IAYgARINGYKGDMdeLVERSLRQAALWDEV------KDKLKQSG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 152 SLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIAD 220
Cdd:PRK14243 150 LSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSD 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-244 |
3.37e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.37 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDG----FKAVDDLSFYLDPKEIRVIIGPNGAGKT-TVLDLIcgKTKATSGSIRFDGKELTRLKEHQIVH 86
Cdd:PRK10261 12 VLAVENLNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM--RLLEQAGGLVQCDKMLLRRRSRQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 87 SG--------------VGRKFQTP--SVFEDLTVFENL--EVSYPQGHSVMGALA-FKRSAEVVAAVEdvAETIflkdaL 147
Cdd:PRK10261 90 LSeqsaaqmrhvrgadMAMIFQEPmtSLNPVFTVGEQIaeSIRLHQGASREEAMVeAKRMLDQVRIPE--AQTI-----L 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 148 DQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHT--VLVIEHDMQFVGDIADRVTVM 225
Cdd:PRK10261 163 SRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVM 242
|
250
....*....|....*....
gi 552559136 226 HQGKVLSEGSIEHVKSDPK 244
Cdd:PRK10261 243 YQGEAVETGSVEQIFHAPQ 261
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-251 |
4.64e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.80 E-value: 4.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 16 EGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSgVGRKFQT 95
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 96 PSVFEDLTVFENLEVS-YPqgHSVMgalaFKR-SAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPD 173
Cdd:PRK10253 90 ATTPGDITVQELVARGrYP--HQPL----FTRwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 174 LLMLDEPVAGMSVAERKKTAELLRRI--TKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSdPKVIEVYLG 251
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT-AELIERIYG 242
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
25-235 |
9.19e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.44 E-value: 9.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 25 FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSG-SIRFDGK---ELTRLKEHQIVHSGVGRKFQTP--SV 98
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAipaNLKKIKEVKRLRKEIGLVFQFPeyQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 99 FEDltvfeNLEVSYPQGHSVMGA---LAFKRSAEVVAAVEdvaetiFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLL 175
Cdd:PRK13645 104 FQE-----TIEKDIAFGPVNLGEnkqEAYKKVPELLKLVQ------LPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552559136 176 MLDEPVAGMSVAERKKTAELLRRITKDHT--VLVIEHDMQFVGDIADRVTVMHQGKVLSEGS 235
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-230 |
9.93e-18 |
|
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: 82.10 E-value: 9.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKA--VDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvhsgvG 90
Cdd:COG4618 331 LSVENLTVVPPGSKRpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL-----G 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 RKF----QTPSVFEDlTVFENLevsypqghSVMGALafkRSAEVVAAVE--DVAETIF-LKDALDQP----ASLLSHGQK 159
Cdd:COG4618 406 RHIgylpQDVELFDG-TIAENI--------ARFGDA---DPEKVVAAAKlaGVHEMILrLPDGYDTRigegGARLSGGQR 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552559136 160 QwlEIGM--LLIQKPDLLMLDEPVAGM-SVAERKktaeLLRRIT--KDH--TVLVIEHDMQFVGdIADRVTVMHQGKV 230
Cdd:COG4618 474 Q--RIGLarALYGDPRLVVLDEPNSNLdDEGEAA----LAAAIRalKARgaTVVVITHRPSLLA-AVDKLLVLRDGRV 544
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
20-235 |
1.51e-17 |
|
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: 78.81 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 20 VSF---DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQiVHSGVGRKFQTP 96
Cdd:cd03253 6 VTFaydPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS-LRRAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 97 SVFEDlTVFENLEVSYPqghsvmgalafkrSA---EVVAAVE--DVAETIF-LKDALD----QPASLLSHGQKQWLEIGM 166
Cdd:cd03253 85 VLFND-TIGYNIRYGRP-------------DAtdeEVIEAAKaaQIHDKIMrFPDGYDtivgERGLKLSGGEKQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 167 LLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDiADRVTVMHQGKVLSEGS 235
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-235 |
7.55e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 79.67 E-value: 7.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 24 GFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKEL-TRLkehQIVHSGVGRKFQTPSVFEDL 102
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNL---DAVRQSLGMCPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 103 TVFENLeVSYPQghsvmgaLAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVA 182
Cdd:TIGR01257 1019 TVAEHI-LFYAQ-------LKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552559136 183 GMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGS 235
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-241 |
9.38e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 79.67 E-value: 9.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 8 SKDFLLAVEGLTVSFDGFK--AVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKE-LTRLKEhqi 84
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISD--- 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 85 VHSGVGRKFQTPSVFEDLTVFENLEVsYPQGHSVmgalafkrSAEVVAAVEDVA-ETIFLKDALDQPASLLSHGQKQWLE 163
Cdd:TIGR01257 2010 VHQNMGYCPQFDAIDDLLTGREHLYL-YARLRGV--------PAEEIEKVANWSiQSLGLSLYADRLAGTYSGGNKRKLS 2080
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 164 IGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKS 241
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREgRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKS 2159
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
5-243 |
1.78e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.77 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 5 KAQSKDFLLAVEGLTVsfdgfkAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKE--- 81
Cdd:PRK10070 27 QGLSKEQILEKTGLSL------GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDael 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 82 HQIVHSGVGRKFQTPSVFEDLTVFENLEVsypqGHSVMGALAFKRSAEVVAAVEDVAETIFLKDALDQpaslLSHGQKQW 161
Cdd:PRK10070 101 REVRRKKIAMVFQSFALMPHMTVLDNTAF----GMELAGINAEERREKALDALRQVGLENYAHSYPDE----LSGGMRQR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 162 LEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHV 239
Cdd:PRK10070 173 VGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHqrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
....
gi 552559136 240 KSDP 243
Cdd:PRK10070 253 LNNP 256
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-235 |
1.87e-16 |
|
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: 75.99 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 23 DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTrLKEHQIVHSGVGRKFQTPSVFeDL 102
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA-LADPAWLRRQVGVVLQENVLF-NR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 103 TVFENLEVSYPQG--HSVMGALAFKRSAEVVAAVEDVAETIflkdaLDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEP 180
Cdd:cd03252 91 SIRDNIALADPGMsmERVIEAAKLAGAHDFISELPEGYDTI-----VGEQGAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 552559136 181 VAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDiADRVTVMHQGKVLSEGS 235
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGS 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
13-235 |
2.03e-16 |
|
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: 75.14 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSF--DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQiVHSGVG 90
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED-LRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 RKFQTPSVFeDLTVFENLEvsyPQGH----SVMGALAFKRSAEVvaavedvaetiflkdaldqpaslLSHGQKQWLEIGM 166
Cdd:cd03369 86 IIPQDPTLF-SGTIRSNLD---PFDEysdeEIYGALRVSEGGLN-----------------------LSQGQRQLLCLAR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 167 LLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIaDRVTVMHQGKVLSEGS 235
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-230 |
2.49e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.76 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 4 AKAQSKDFLLAVEGLTV-SFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEH 82
Cdd:COG3845 249 APAEPGEVVLEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 83 QIVHSGVGRkfqtpsVFED---------LTVFENLEVSYpQGHSVMGALAFKRSAEVVAAVEDVAETiF--LKDALDQPA 151
Cdd:COG3845 329 ERRRLGVAY------IPEDrlgrglvpdMSVAENLILGR-YRRPPFSRGGFLDRKAIRAFAEELIEE-FdvRTPGPDTPA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 152 SLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAerkkTAELLRRITKDH-----TVLVIEHDMQFVGDIADRVTVMH 226
Cdd:COG3845 401 RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVG----AIEFIHQRLLELrdagaAVLLISEDLDEILALSDRIAVMY 476
|
....
gi 552559136 227 QGKV 230
Cdd:COG3845 477 EGRI 480
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
26-235 |
4.76e-16 |
|
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: 74.88 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 26 KAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvHSGVGRKFQTPSVFeDLTVF 105
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL-RSQIGLVSQEPVLF-DGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 106 ENLEVSYPQGHSVmgalafkrsaEVVAAVEDVAETIF---LKDALD----QPASLLSHGQKQWLEIGMLLIQKPDLLMLD 178
Cdd:cd03249 95 ENIRYGKPDATDE----------EVEEAAKKANIHDFimsLPDGYDtlvgERGSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 179 EPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDiADRVTVMHQGKVLSEGS 235
Cdd:cd03249 165 EATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
26-235 |
4.97e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.54 E-value: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 26 KAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELT---RLKEHQIVHSGVGRKFQTP--SVFE 100
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstsKQKEIKPVRKKVGVVFQFPesQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 101 DlTVFENLEVSyPQGHSVMgalafKRSAEVVAAvEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEP 180
Cdd:PRK13643 100 E-TVLKDVAFG-PQNFGIP-----KEKAEKIAA-EKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 181 VAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGS 235
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
12-245 |
5.82e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.41 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSF-DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVG 90
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 RKFQTPSV-FEDLTVFENLevSYPQGHSVMGALAFKRSAEVVaavedVAETIFLKDALDQPASLlSHGQKQWLEIGMLLI 169
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDL--AFGPENLCLPPIEIRKRVDRA-----LAEIGLEKYRHRSPKTL-SGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 170 QKPDLLMLDEpVAGMSVAERKKTaeLLRRITKDH----TVLVIEHDMQFVGDiADRVTVMHQGKVLSEGSIEHVKSDPKV 245
Cdd:PRK13644 153 MEPECLIFDE-VTSMLDPDSGIA--VLERIKKLHekgkTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSL 228
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
8-237 |
9.43e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 74.29 E-value: 9.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 8 SKDFLLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICG--KTKATSGSIRFDGKELTRLKEHQIV 85
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 86 HSGVGRKFQTPSVFEDLTVFENLEVSYPQGHSVMG-----ALAFkrsAEVVAAVEDVA--ETIFLKDALDQPaslLSHGQ 158
Cdd:CHL00131 83 HLGIFLAFQYPIEIPGVSNADFLRLAYNSKRKFQGlpeldPLEF---LEIINEKLKLVgmDPSFLSRNVNEG---FSGGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 159 KQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRI-TKDHTVLVIEHdMQFVGD--IADRVTVMHQGKVLSEGS 235
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLmTSENSIILITH-YQRLLDyiKPDYVHVMQNGKIIKTGD 235
|
..
gi 552559136 236 IE 237
Cdd:CHL00131 236 AE 237
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-242 |
1.40e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.89 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVL----DLICGKtKATSGSIRFDGKELTR----LKEHQ 83
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGD-KSAGSHIELLGRTVQRegrlARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 84 IVHSGVGRKFQTPSVFEDLTVFENLEV----SYPQGHSVMGALAFKRSAEVVAAVEDVAETIFLKdaldQPASLLSHGQK 159
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIgalgSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAH----QRVSTLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 160 QWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIE 237
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
....*
gi 552559136 238 HVKSD 242
Cdd:PRK09984 239 QFDNE 243
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-239 |
1.51e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.91 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 35 LDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRlkehqiVHSGVgrkFQTPS------VFEDLTVFenl 108
Cdd:PRK11144 21 LPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFD------AEKGI---CLPPEkrrigyVFQDARLF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 109 evsyPQgHSVMGALAFKRSAEVVAAVEDVAETIFLKDALDQ-PASLlSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVA 187
Cdd:PRK11144 89 ----PH-YKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRyPGSL-SGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 188 eRKKtaEL---LRRITKDHT--VLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHV 239
Cdd:PRK11144 163 -RKR--ELlpyLERLAREINipILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
24-235 |
1.80e-15 |
|
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: 75.55 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 24 GFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvhsgvgRKF-----QTPSV 98
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL------RQFinylpQEPYI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 99 FeDLTVFENLEVSYPQGHSVMGALAFKRSAEVVAAVEDVAETifLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLD 178
Cdd:TIGR01193 560 F-SGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLG--YQTELSEEGSSISGGQKQRIALARALLTDSKVLILD 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 179 EPVAGMSVAERKKTAELLRRItKDHTVLVIEHDMQfVGDIADRVTVMHQGKVLSEGS 235
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGS 691
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-250 |
2.79e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.84 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 37 PKEIRV--IIGPNGAGKTTVLDLICGKTKATSGSI-----------RFDGKEL----TRLKEHQIvhsGVGRKFQ----T 95
Cdd:PRK13409 96 PKEGKVtgILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkRFRGTELqnyfKKLYNGEI---KVVHKPQyvdlI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 96 PSVFeDLTVFENLEVSYPQGhsvmgalafkrsaevvaAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLL 175
Cdd:PRK13409 173 PKVF-KGKVRELLKKVDERG-----------------KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552559136 176 MLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIADRVTVMHqGKVLSEGSIEHVKSDPKVIEVYL 250
Cdd:PRK13409 235 FFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDYLADNVHIAY-GEPGAYGVVSKPKGVRVGINEYL 308
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-234 |
3.32e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 72.30 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 26 KAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGK---TKATSGSIRFDGKELTRLKEHQIVhsGVGRKFQTpsVFEDL 102
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKPDQFQKCV--AYVRQDDI--LLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 103 TVFENLevsYPQGHSVMGALafKRSAEVVAAVEDVAetifLKDALDQPA-----SLLSHGQKQWLEIGMLLIQKPDLLML 177
Cdd:cd03234 97 TVRETL---TYTAILRLPRK--SSDAIRKKRVEDVL----LRDLALTRIggnlvKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552559136 178 DEPVAGMSVAERKKTAELLRRI-TKDHTVLVIEH----DMqFvgDIADRVTVMHQGKVLSEG 234
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLaRRNRIVILTIHqprsDL-F--RLFDRILLLSSGEIVYSG 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-249 |
3.86e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.90 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 5 KAQSKDFLLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQI 84
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 85 VHSGVGRKFQTPSVfEDLTVFENLEVS-YPQgHSVMGALAFKRSAEVVAAVEDVAETIFLKDALDQpaslLSHGQKQWLE 163
Cdd:PRK10575 84 ARKVAYLPQQLPAA-EGMTVRELVAIGrYPW-HGALGRFGAADREKVEEAISLVGLKPLAHRLVDS----LSGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 164 IGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKS 241
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
....*...
gi 552559136 242 DPKVIEVY 249
Cdd:PRK10575 238 GETLEQIY 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-243 |
4.21e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.36 E-value: 4.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSF----DGFKAVDDLSFYLDPKEIRVIIGPNGAGKT----TVLDLICGKTKA-TSGSIRFDGKELTRLKEH 82
Cdd:PRK15134 5 LLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 83 QIVH---SGVGRKFQTPSVfeDLTVFENLEVSYPQG---HSVMGALAFKrsAEVVAAVEDVAETIFLKDALDQPASLlSH 156
Cdd:PRK15134 85 TLRGvrgNKIAMIFQEPMV--SLNPLHTLEKQLYEVlslHRGMRREAAR--GEILNCLDRVGIRQAAKRLTDYPHQL-SG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 157 GQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITK--DHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEG 234
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQN 239
|
....*....
gi 552559136 235 SIEHVKSDP 243
Cdd:PRK15134 240 RAATLFSAP 248
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
12-243 |
5.06e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.51 E-value: 5.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSF---------DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTrLKEH 82
Cdd:PRK15112 4 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 83 QIVHSGVGRKFQTPSV----------FEDLTVFENLEVSYPQghsvmgalafkRSAEVVAAVEDVAetiFLKDALDQPAS 152
Cdd:PRK15112 83 SYRSQRIRMIFQDPSTslnprqrisqILDFPLRLNTDLEPEQ-----------REKQIIETLRQVG---LLPDHASYYPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 153 LLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHT---VLVIEHdMQFVGDIADRVTVMHQGK 229
Cdd:PRK15112 149 MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGisyIYVTQH-LGMMKHISDQVLVMHQGE 227
|
250
....*....|....
gi 552559136 230 VLSEGSIEHVKSDP 243
Cdd:PRK15112 228 VVERGSTADVLASP 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
43-244 |
6.06e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 72.31 E-value: 6.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 43 IIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRL------------KEHQIVHSGVGRKFQTPSVFEDLTVFENLEV 110
Cdd:PRK10619 36 IIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadkNQLRLLRTRLTMVFQHFNLWSHMTVLENVME 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 111 SYPQGHSVMGALAFKRsaevvaAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMsvaERK 190
Cdd:PRK10619 116 APIQVLGLSKQEARER------AVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSAL---DPE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552559136 191 KTAELLRRITK----DHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPK 244
Cdd:PRK10619 187 LVGEVLRIMQQlaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQ 244
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
12-249 |
7.39e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 7.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRfdgkeltrlKEHQIVHSGVGR 91
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KFQTPSVFEdLTVfenlevsypqgHSVMGALAFKRSAEVVAAVEDVAETiflkDALDQPASLLSHGQKQWLEIGMLLIQK 171
Cdd:PRK09544 75 KLYLDTTLP-LTV-----------NRFLRLRPGTKKEDILPALKRVQAG----HLIDAPMQKLSGGETQRVLLARALLNR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 172 PDLLMLDEPVAGMSVAERKKTAELLRRITK--DHTVLVIEHDMQFVGDIADRVTVMHQgKVLSEGSIEHVKSDPKVIEVY 249
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHPEFISMF 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-224 |
7.40e-15 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 71.67 E-value: 7.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 39 EIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKEltrlkehqivhsgVGRKFQTPSVFEDLTVFENLevsypqgHSV 118
Cdd:cd03237 26 EVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-------------VSYKPQYIKADYEGTVRDLL-------SSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 119 ---MGALAFKRSaevvaaveDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAEL 195
Cdd:cd03237 86 tkdFYTHPYFKT--------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180 190
....*....|....*....|....*....|.
gi 552559136 196 LRRITKDH--TVLVIEHDMQFVGDIADRVTV 224
Cdd:cd03237 158 IRRFAENNekTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-226 |
9.13e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.61 E-value: 9.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLIcGKTKATSGSIRFDGK-------------ELTRL 79
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRveffnqniyerrvNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 80 KEHqivhsgVGRKFQTPSVFEdLTVFENleVSYpqGHSVMGalaFKRSAEVVAAVEDVAETIFL----KDALDQPASLLS 155
Cdd:PRK14258 87 RRQ------VSMVHPKPNLFP-MSVYDN--VAY--GVKIVG---WRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552559136 156 HGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLR--RITKDHTVLVIEHDMQFVGDIADRVTVMH 226
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFK 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-230 |
1.04e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.63 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRF------DGKELTRLKehqivh 86
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAgtaplaEAREDTRLM------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 87 sgvgrkFQTPSVFEDLTVFENlevsypqghsVMGALAFKRSAEVVAAVEDVAetifLKD-ALDQPASLlSHGQKQWLEIG 165
Cdd:PRK11247 87 ------FQDARLLPWKKVIDN----------VGLGLKGQWRDAALQALAAVG----LADrANEWPAAL-SGGQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 166 MLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-250 |
1.29e-14 |
|
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: 71.24 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 37 PKEIRV--IIGPNGAGKTTVLDLICGKTKATSGSIR-----------FDGKEL----TRLKEHQIvhsGVGRKFQ----T 95
Cdd:cd03236 23 PREGQVlgLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELqnyfTKLLEGDV---KVIVKPQyvdlI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 96 PSVFeDLTVFENLEVSYPQGhsvmgalafkrsaevvaAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLL 175
Cdd:cd03236 100 PKAV-KGKVGELLKKKDERG-----------------KLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 176 MLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHqGKVLSEGSIEHVKSDPKVIEVYL 250
Cdd:cd03236 162 FFDEPSSYLDIKQRLNAARLIRELAEDdNYVLVVEHDLAVLDYLSDYIHCLY-GEPGAYGVVTLPKSVREGINEFL 236
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
15-252 |
1.87e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.43 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 15 VEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTT---VLDLIcgkTKATSGSI-----RFDGKELTRLKEHQIVH 86
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLL---EMPRSGTLniagnHFDFSKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 87 SGVGRKFQTPSVFEDLTVFENLeVSYPqghsvMGALAFKRsAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGM 166
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNL-IEAP-----CRVLGLSK-DQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 167 LLIQKPDLLMLDEPVAGMsvaERKKTAELLrRITKDH-----TVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVkS 241
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAAL---DPEITAQIV-SIIRELaetgiTQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCF-T 229
|
250
....*....|...
gi 552559136 242 DPKVIEV--YLGH 252
Cdd:PRK11124 230 QPQTEAFknYLSH 242
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
12-195 |
2.91e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.49 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRL-KEHQIVHSGvg 90
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGdRSRFMAYLG-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 rkfQTPSVFEDLTVFENLEvsYPQGHSVMGALAFKRSAEVVAAVEDVAETIFLKdaldqpaslLSHGQKQWLEIGMLLIQ 170
Cdd:PRK13543 89 ---HLPGLKADLSTLENLH--FLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQ---------LSAGQKKRLALARLWLS 154
|
170 180 190
....*....|....*....|....*....|
gi 552559136 171 KPDLLMLDEPVA-----GMSVAERKKTAEL 195
Cdd:PRK13543 155 PAPLWLLDEPYAnldleGITLVNRMISAHL 184
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-244 |
5.48e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.04 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 27 AVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvhSGVGRKFQTpsVFEDltVFE 106
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKL--QALRRDIQF--IFQD--PYA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 107 NLEVSYPQGHSVMGALAFKRSAEVVAAVEDVA---ETIFLK--DALDQPASLlSHGQKQWLEIGMLLIQKPDLLMLDEPV 181
Cdd:PRK10261 413 SLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAwllERVGLLpeHAWRYPHEF-SGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552559136 182 AGMSVAERKKTAELLRRITKDHTV--LVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDPK 244
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
30-233 |
5.91e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.07 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 30 DLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLK---EHQIVHSGVGRKFQTPSVFEDLTVFE 106
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 107 NLEVSYPQGHsVMGALAFKRSAEVVAAVedvaetiflkdALDQPA----SLLSHGQKQWLEIGMLLIQKPDLLMLDEPVA 182
Cdd:PRK11629 107 NVAMPLLIGK-KKPAEINSRALEMLAAV-----------GLEHRAnhrpSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552559136 183 GMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIaDRVTVMHQGKVLSE 233
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-252 |
1.16e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.03 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGR 91
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KFQTPSVFEDLTVFENL----EVSYPqghsvMGALAFKRsaeVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGML 167
Cdd:PRK10762 84 IHQELNLIPQLTIAENIflgrEFVNR-----FGRIDWKK---MYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 168 LIQKPDLLMLDEPVAGMSVAErkkTAELLRRIT----KDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDp 243
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTE---TESLFRVIRelksQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTED- 231
|
....*....
gi 552559136 244 KVIEVYLGH 252
Cdd:PRK10762 232 SLIEMMVGR 240
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-226 |
1.19e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.81 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 37 PKEIRV--IIGPNGAGKTTVLDLICGKTKATSGSI-----------RFDGKEL----TRLKEHQIvhsGVGRKFQ----T 95
Cdd:COG1245 96 PKKGKVtgILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGTELqdyfKKLANGEI---KVAHKPQyvdlI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 96 PSVFeDLTVFENLEvsypqghsvmgalafkrSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLL 175
Cdd:COG1245 173 PKVF-KGTVRELLE-----------------KVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 552559136 176 MLDEPVAGMSVAERKKTAELLRRITK-DHTVLVIEHDMQFVGDIADRVTVMH 226
Cdd:COG1245 235 FFDEPSSYLDIYQRLNVARLIRELAEeGKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-222 |
1.35e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.92 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKeltrlkehqivhSGVGRK 92
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN------------ANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 93 FQTPSV-FE-DLTVFENLEVSYPQGH---SVMGALafkrsaevvaavedvAETIFLKDALDQPASLLSHGQKQWLEIGML 167
Cdd:PRK15064 388 AQDHAYdFEnDLTLFDWMSQWRQEGDdeqAVRGTL---------------GRLLFSQDDIKKSVKVLSGGEKGRMLFGKL 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 168 LIQKPDLLMLDEPVAGMSVaerkKTAELLRRITKDH--TVLVIEHDMQFVGDIADRV 222
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDM----ESIESLNMALEKYegTLIFVSHDREFVSSLATRI 505
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
27-243 |
3.24e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.59 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 27 AVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKehqiVHSGVGRKF---QTPSVFEDlT 103
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ----LDSWRSRLAvvsQTPFLFSD-T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 104 VFENLEVSYPQghsvmgalAFKRSAEVVAAVEDVAETIF-LKDALD----QPASLLSHGQKQWLEIGMLLIQKPDLLMLD 178
Cdd:PRK10789 405 VANNIALGRPD--------ATQQEIEHVARLASVHDDILrLPQGYDtevgERGVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552559136 179 EPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDiADRVTVMHQGKVLSEGSIEHVKSDP 243
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-235 |
3.52e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.61 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 15 VEGLTVSFDGFKAVDDLSFYLdPKEIRV-IIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHS------ 87
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDI-PAGCMVgLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPriaymp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 88 -GVGRkfqtpSVFEDLTVFENLEVsypqghsvMGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGM 166
Cdd:NF033858 83 qGLGK-----NLYPTLSVFENLDF--------FGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 167 LLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH---TVLV----IEHDMQFvgdiaDRVTVMHQGKVLSEGS 235
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLVatayMEEAERF-----DWLVAMDAGRVLATGT 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-235 |
4.60e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.31 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 2 NAAKAQSKDFLLAVEGLTVSFDG--FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRL 79
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 80 KEHQI-----VHSgvgrkfQTPSVFEDlTVFENLEVSYPQGHsvmgalafkrSAEVVAAVEDVAetifLKDALDQPASL- 153
Cdd:PRK11160 408 SEAALrqaisVVS------QRVHLFSA-TLRDNLLLAAPNAS----------DEALIEVLQQVG----LEKLLEDDKGLn 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 154 ---------LSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDM----QFvgdiaD 220
Cdd:PRK11160 467 awlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLtgleQF-----D 541
|
250
....*....|....*
gi 552559136 221 RVTVMHQGKVLSEGS 235
Cdd:PRK11160 542 RICVMDNGQIIEQGT 556
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
12-235 |
5.24e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.04 E-value: 5.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDL---SFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIvHSG 88
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNL-RRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 89 VGRKFQTP------SVFEDLTVFENLEVSYPQghsvmgalafkrsAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWL 162
Cdd:PRK13642 83 IGMVFQNPdnqfvgATVEDDVAFGMENQGIPR-------------EEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552559136 163 EIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDiADRVTVMHQGKVLSEGS 235
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAA 223
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
12-247 |
6.50e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.77 E-value: 6.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKAT--------SGSIRFDGKELTRLKEHQ 83
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 84 IVHsgvgRKFQTPSVFEDLTVFENLEV----SYPqgHSVMGALAFKRSAEVVAAVEDVAETiflkDALD-QPASLLSHGQ 158
Cdd:PRK13547 81 LAR----LRAVLPQAAQPAFAFSAREIvllgRYP--HARRAGALTHRDGEIAWQALALAGA----TALVgRDVTTLSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 159 KQWLEIGMLLIQ---------KPDLLMLDEPVAGMSVAERKKTAELLRRITKDHT--VLVIEHDMQFVGDIADRVTVMHQ 227
Cdd:PRK13547 151 LARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNLAARHADRIAMLAD 230
|
250 260
....*....|....*....|
gi 552559136 228 GKVLSEGSIEHVKSdPKVIE 247
Cdd:PRK13547 231 GAIVAHGAPADVLT-PAHIA 249
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
13-237 |
9.60e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.06 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSF-DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTR-LKEHQIVHSGVG 90
Cdd:PRK15056 7 IVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQaLQKNLVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 RK--FQTPSVFEDLTVFENLevsypqGHsvMGALAfKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLL 168
Cdd:PRK15056 87 EEvdWSFPVLVEDVVMMGRY------GH--MGWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 169 IQKPDLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADrVTVMHQGKVLSEGSIE 237
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTE 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
12-232 |
1.24e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.74 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATS--GSIRFDGKELT----RLKEHQ-- 83
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRfkdiRDSEALgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 84 -IVHsgvgrkfQTPSVFEDLTVFENLEVSYPQGHSvmGAL----AFKRSAEVVAAVEdvaetifLKDALDQPASLLSHGQ 158
Cdd:NF040905 81 vIIH-------QELALIPYLSIAENIFLGNERAKR--GVIdwneTNRRARELLAKVG-------LDESPDTLVTDIGVGK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 159 KQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRItKDH--TVLVIEHDMQFVGDIADRVTVMHQGKVLS 232
Cdd:NF040905 145 QQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQgiTSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-230 |
1.38e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.68 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 7 QSKDFLLAVEGLTVSFDgfKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVH 86
Cdd:PRK10982 245 KPGEVILEVRNLTSLRQ--PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAIN 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 87 SG---VGRKFQTPSVFEDLTV-FENLEVSYPQGHSVMGALAFKRsaeVVAAVEDVAETIFLKDALDQPA-SLLSHGQKQW 161
Cdd:PRK10982 323 HGfalVTEERRSTGIYAYLDIgFNSLISNIRNYKNKVGLLDNSR---MKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQK 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 162 LEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRIT-KDHTVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:PRK10982 400 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
26-244 |
1.93e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.76 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 26 KAVDDLSFYLDPKEIRVIIGPNGAGKTTV---LDLIcgkTKATSGSIRFDGKELT---------RLKEHQIVhsgvgrkF 93
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLarlLTMI---ETPTGGELYYQGQDLLkadpeaqklLRQKIQIV-------F 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 94 QTPsvFEDL--------TVFENLEVsypqgHSVMGAlafkrsAEVVAAVEDVAETIFLK-DALDQPASLLSHGQKQWLEI 164
Cdd:PRK11308 99 QNP--YGSLnprkkvgqILEEPLLI-----NTSLSA------AERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 165 GMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLV-IEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSD 242
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVfISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNN 245
|
..
gi 552559136 243 PK 244
Cdd:PRK11308 246 PR 247
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-215 |
2.40e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 15 VEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGK-ELTRLKEHQivhsgvgrkf 93
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFDQHR---------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 94 qtpsvfEDL----TVFENL-----EVsypqghSVMGalafkRSAEVVAAVEDvaetiFL---KDALdQPASLLSHGQKQW 161
Cdd:PRK11147 392 ------AELdpekTVMDNLaegkqEV------MVNG-----RPRHVLGYLQD-----FLfhpKRAM-TPVKALSGGERNR 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 162 LEIGMLLIQKPDLLMLDEPVAGMSVaerkKTAELLRRITKDH--TVLVIEHDMQFV 215
Cdd:PRK11147 449 LLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYqgTVLLVSHDRQFV 500
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-244 |
2.61e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.72 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGfKAVDDLSFYLDPKEIRVIIGPNGAGKT----TVLDLICGKTKATSGSIRFDGKEltrlkehqIVHSG 88
Cdd:PRK10418 5 IELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKP--------VAPCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 89 V-GRK----FQTP-SVFEDLTVFENlevsypqgHSVMGALAFKRS---AEVVAAVEDVAetiflkdaLDQPASLL----- 154
Cdd:PRK10418 76 LrGRKiatiMQNPrSAFNPLHTMHT--------HARETCLALGKPaddATLTAALEAVG--------LENAARVLklypf 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 155 --SHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHT--VLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:PRK10418 140 emSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRI 219
|
250
....*....|....
gi 552559136 231 LSEGSIEHVKSDPK 244
Cdd:PRK10418 220 VEQGDVETLFNAPK 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-233 |
2.95e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 25 FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGrkFQTPS-----VF 99
Cdd:PRK09700 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMA--YITESrrdngFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 100 EDLTVFENLEVS-YPQGHSVMGALAFKRSAEVVAAVEDVAETIFLK-DALDQPASLLSHGQKQWLEIGMLLIQKPDLLML 177
Cdd:PRK09700 354 PNFSIAQNMAISrSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 178 DEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKVLSE 233
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
12-240 |
3.34e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.43 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKT--KATSGSIRFDGKELTRLKEHQIVHSGV 89
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 90 GRKFQTPSVFEDLTVFENLEVSYPQGHSVMGALAFKRSaevvaaveDVAETIFLKDA-LDQPASLL--------SHGQKQ 160
Cdd:PRK09580 81 FMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRF--------DFQDLMEEKIAlLKMPEDLLtrsvnvgfSGGEKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 161 WLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDI--ADRVTVMHQGKVLSEGSIEH 238
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYikPDYVHVLYQGRIVKSGDFTL 232
|
..
gi 552559136 239 VK 240
Cdd:PRK09580 233 VK 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
9-230 |
3.59e-12 |
|
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: 65.62 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 9 KDFLLAVEGLT---VSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTK-ATSGSIRFDGKELTRLKEHQI 84
Cdd:TIGR02633 254 GDVILEARNLTcwdVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNPAQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 85 VHSGVG-----RKFQtpSVFEDLTVFENLEVSYPQGHSVMGALafKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQK 159
Cdd:TIGR02633 334 IRAGIAmvpedRKRH--GIVPILGVGKNITLSVLKSFCFKMRI--DAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552559136 160 QWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH-TVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:TIGR02633 410 QKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGvAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-239 |
1.21e-11 |
|
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: 64.05 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICG--KTKATSGSI----------------RFDGK 74
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 75 ELTR----LKEHQI--------VHSGVGRK----FQ-TPSVFEDLTVFENLEVSYPQ-GHSvmGALAFKRSAEVVAAVEd 136
Cdd:TIGR03269 81 PCPVcggtLEPEEVdfwnlsdkLRRRIRKRiaimLQrTFALYGDDTVLDNVLEALEEiGYE--GKEAVGRAVDLIEMVQ- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 137 vaetifLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQF 214
Cdd:TIGR03269 158 ------LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEV 231
|
250 260
....*....|....*....|....*
gi 552559136 215 VGDIADRVTVMHQGKVLSEGSIEHV 239
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
25-244 |
1.46e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.18 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 25 FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRF---DGKELTRLKEHQIVHSG------------- 88
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEKVLEKlviqktrfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 89 -------VGRKFQtpsvFEDLTVFE-NLEVSYPQGHSVMG---ALAFKRSAEVVAAVeDVAETIFLKDALDqpaslLSHG 157
Cdd:PRK13651 100 ikeirrrVGVVFQ----FAEYQLFEqTIEKDIIFGPVSMGvskEEAKKRAAKYIELV-GLDESYLQRSPFE-----LSGG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 158 QKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSI 236
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDT 249
|
....*...
gi 552559136 237 EHVKSDPK 244
Cdd:PRK13651 250 YDILSDNK 257
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
31-219 |
2.66e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.03 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 31 LSFYLDPKeIRVIiGPNGAGKTTVLDLICGKTKATSGSIRFDgKELTrlkehqivhsgVGRKFQTPSVFEDLTVFENL-- 108
Cdd:TIGR03719 26 LSFFPGAK-IGVL-GLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGIK-----------VGYLPQEPQLDPTKTVRENVee 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 109 -------------EVS--YPQGHSVMGALAfKRSAEVVAAVE-----DVAETIFLK-DAL-----DQPASLLSHGQKQWL 162
Cdd:TIGR03719 92 gvaeikdaldrfnEISakYAEPDADFDKLA-AEQAELQEIIDaadawDLDSQLEIAmDALrcppwDADVTKLSGGERRRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 163 EIGMLLIQKPDLLMLDEPVAGMSvAErkkTAELLRRITKDH--TVLVIEHDMQFVGDIA 219
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHLD-AE---SVAWLERHLQEYpgTVVAVTHDRYFLDNVA 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-219 |
3.75e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.65 E-value: 3.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 10 DFLLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFdGKELtrlkehQIVHSGV 89
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV------KLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 90 GRKFQTPsvfeDLTVFEnlEVSYPQGHSVMGALAFKRSAEVVAavedvaetiFLKDALDQ--PASLLSHGQKQWLEIGML 167
Cdd:TIGR03719 393 SRDALDP----NKTVWE--EISGGLDIIKLGKREIPSRAYVGR---------FNFKGSDQqkKVGQLSGGERNRVHLAKT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 168 LIQKPDLLMLDEPVAGMSVaerkktaELLRRITK-----DHTVLVIEHDMQFVGDIA 219
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDV-------ETLRALEEallnfAGCAVVISHDRWFLDRIA 507
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
39-233 |
6.16e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.85 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 39 EIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGV-----GRKFQtpSVFEDLTVFENLEVSYP 113
Cdd:PRK11288 280 EIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGImlcpeDRKAE--GIIPVHSVADNINISAR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 114 QGHSVMGALaFKRSAEvvaavEDVAETiFLKD------ALDQPASLLSHGQKQ------WLEIGMlliqkpDLLMLDEPV 181
Cdd:PRK11288 358 RHHLRAGCL-INNRWE-----AENADR-FIRSlniktpSREQLIMNLSGGNQQkailgrWLSEDM------KVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552559136 182 AGMSVAERKKTAELLRRITKDH-TVLVIEHDMQFVGDIADRVTVMHQGKVLSE 233
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELAAQGvAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-233 |
6.65e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.86 E-value: 6.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGL-----TVSFDGFKA----VDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEH 82
Cdd:PRK10419 3 LLNVSGLshhyaHGGLSGKHQhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 83 QIvhsgvgRKFQ--TPSVFED--------LTVFENLevSYPQGH--SVMGALAFKRSAEVVAAVEDVAEtiflkDALDQP 150
Cdd:PRK10419 83 QR------KAFRrdIQMVFQDsisavnprKTVREII--REPLRHllSLDKAERLARASEMLRAVDLDDS-----VLDKRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 151 ASLlSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITK--DHTVLVIEHDMQFVGDIADRVTVMHQG 228
Cdd:PRK10419 150 PQL-SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNG 228
|
....*
gi 552559136 229 KVLSE 233
Cdd:PRK10419 229 QIVET 233
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
37-216 |
6.91e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.18 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 37 PKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQ---IVHSGVGRKFQTPSVFEDLTVFENLEVSyp 113
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKHVGFVFQSFMLIPTLNALENVELP-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 114 qghsvmGALAFKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTA 193
Cdd:PRK10584 113 ------ALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
|
170 180
....*....|....*....|....*
gi 552559136 194 ELLRRITKDH--TVLVIEHDMQFVG 216
Cdd:PRK10584 187 DLLFSLNREHgtTLILVTHDLQLAA 211
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-210 |
7.13e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 61.75 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 6 AQSKDFLLAVEGLTVSF-DGFKAVDDLSFYLDPKEiRV-IIGPNGAGKTTVLDLICGKTKATSGSIRF-DGKELTrlkeh 82
Cdd:COG4178 356 ETSEDGALALEDLTLRTpDGRPLLEDLSLSLKPGE-RLlITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL----- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 83 qivhsgvgrkF--QTPSVFEDlTVFENLevSYPQGHSVMGalafkrSAEVVAAVEDV--AEtifLKDALDQPAS---LLS 155
Cdd:COG4178 430 ----------FlpQRPYLPLG-TLREAL--LYPATAEAFS------DAELREALEAVglGH---LAERLDEEADwdqVLS 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 552559136 156 HGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEH 210
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
24-230 |
7.56e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.40 E-value: 7.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 24 GFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRL--KEHQI--VhsgvgrkFQTPSVF 99
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELepADRDIamV-------FQNYALY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 100 EDLTVFENLEvsYpqghsvmgALAFKR--SAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLML 177
Cdd:PRK11650 89 PHMSVRENMA--Y--------GLKIRGmpKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552559136 178 DEPV----AGMSVAERKKTAELLRRITKdhTVLVIEHD----MQfvgdIADRVTVMHQGKV 230
Cdd:PRK11650 159 DEPLsnldAKLRVQMRLEIQRLHRRLKT--TSLYVTHDqveaMT----LADRVVVMNGGVA 213
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-230 |
7.92e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.48 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 26 KAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTK-ATSGSIRFDGKELTRLKEHQIVHSGVG-----RKFQtpSVF 99
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGIAmvpedRKRD--GIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 100 EDLTVFENLEVSYPQGHSVMGALafKRSAEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDE 179
Cdd:PRK13549 354 PVMGVGKNITLAALDRFTGGSRI--DDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 552559136 180 PVAGMSVAERKKTAELLRRITKDH-TVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:PRK13549 432 PTRGIDVGAKYEIYKLINQLVQQGvAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-251 |
9.60e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 9.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 16 EGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGRKFQT 95
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 96 PSVFEDLTVFENLEVS-YP-QGHSVMGALAFKRSaevvaavedvaETIFlkDALD------QPASLLSHGQKQWLEIGML 167
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGrYPtKGMFVDQDKMYRDT-----------KAIF--DELDididprAKVATLSVSQMQMIEIAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 168 LIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLV-IEHDMQFVGDIADRVTVMHQGKVLSEGSIEHVKSDpKVI 246
Cdd:PRK10982 149 FSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVyISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMD-KII 227
|
....*
gi 552559136 247 EVYLG 251
Cdd:PRK10982 228 AMMVG 232
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
28-184 |
1.06e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 28 VDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTR-LKEHQIVHSGVGRKfqtPSVFEDLTVFE 106
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGHR---SGINPYLTLRE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552559136 107 NlevSYPQGHSVMGALafkrsaevvaAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGM 184
Cdd:PRK13540 94 N---CLYDIHFSPGAV----------GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-70 |
1.71e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 1.71e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 15 VEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIR 70
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK 382
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-232 |
2.08e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 60.51 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSF----DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIR--------FDGKELTRL 79
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRvagqdvatLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 80 -KEHqivhsgVGRKFQTPSVFEDLTVFENLEVsyPQGHSvmGALAFKRSAEVVAAVEDVAetifLKDALDQPASLLSHGQ 158
Cdd:PRK10535 84 rREH------FGFIFQRYHLLSHLTAAQNVEV--PAVYA--GLERKQRLLRAQELLQRLG----LEDRVEYQPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552559136 159 KQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRI-TKDHTVLVIEHDMQfVGDIADRVTVMHQGKVLS 232
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEIVR 223
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-239 |
4.40e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.52 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 27 AVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKEltrlkehQIVHSGVGRKFQtpsvfedLTVFE 106
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-------ALIAISSGLNGQ-------LTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 107 NLEVSypqghSVMGALAFKRSAEVVAAVEDVAEtifLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEpvaGMSV 186
Cdd:PRK13545 105 NIELK-----GLMMGLTKEKIKEIIPEIIEFAD---IGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE---ALSV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 187 AERKKTAELLRRIT----KDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHV 239
Cdd:PRK13545 174 GDQTFTKKCLDKMNefkeQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-199 |
8.33e-10 |
|
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: 56.48 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 29 DDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKA--TSGSIRFDGKELTR-------LKEHQIVHSGVgrkfqtpsvf 99
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDKnfqrstgYVEQQDVHSPN---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 100 edLTVFENLEVSypqghsvmgalAFKRSaevvaavedvaetiflkdaldqpaslLSHGQKQWLEIGMLLIQKPDLLMLDE 179
Cdd:cd03232 94 --LTVREALRFS-----------ALLRG--------------------------LSVEQRKRLTIGVELAAKPSILFLDE 134
|
170 180
....*....|....*....|
gi 552559136 180 PVAGMSVAERKKTAELLRRI 199
Cdd:cd03232 135 PTSGLDSQAAYNIVRFLKKL 154
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
31-241 |
1.17e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 31 LSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTR------------LKEHQIVHSGVGRKFQTP-S 97
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgltdlrrvlsiIPQSPVLFSGTVRFNIDPfS 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 98 VFEDLTVFENLEVSYPQghSVMGALAFKRSAEVVAAVEDvaetiflkdaldqpaslLSHGQKQWLEIGMLLIQKPDLLML 177
Cdd:PLN03232 1335 EHNDADLWEALERAHIK--DVIDRNPFGLDAEVSEGGEN-----------------FSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552559136 178 DEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDiADRVTVMHQGKVLSEGSIEHVKS 241
Cdd:PLN03232 1396 DEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-233 |
1.33e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.06 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 24 GFkAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELT--RLKEHQIVHSgvgrkfqtpSVFED 101
Cdd:PRK10522 336 GF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaeQPEDYRKLFS---------AVFTD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 102 LTVFENLevSYPQGHSVMGALafkrsaevvaaVEDVAETIFLKDALD----QPASL-LSHGQKQWLEIGMLLIQKPDLLM 176
Cdd:PRK10522 406 FHLFDQL--LGPEGKPANPAL-----------VEKWLERLKMAHKLEledgRISNLkLSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 177 LDEPVAGMSVAERKK-TAELLRRI-TKDHTVLVIEHDMQFVgDIADRVTVMHQGKvLSE 233
Cdd:PRK10522 473 LDEWAADQDPHFRREfYQVLLPLLqEMGKTIFAISHDDHYF-IHADRLLEMRNGQ-LSE 529
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-240 |
1.71e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 19 TVSFDGFKAVDDLsfyLDPKEIRVIIGPNGAGKTTVLDLICGKT----KATSGSIRFDGKELTRLKEH---QIVHSGvgr 91
Cdd:TIGR00956 71 TKTFDILKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGITPEEIKKHyrgDVVYNA--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 kfQTPSVFEDLTVFENLEVSY----PQgHSVMGAlafkrSAEVVAA-VEDVAETIFlkdALDQPASL---------LSHG 157
Cdd:TIGR00956 145 --ETDVHFPHLTVGETLDFAArcktPQ-NRPDGV-----SREEYAKhIADVYMATY---GLSHTRNTkvgndfvrgVSGG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 158 QKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLR---RITKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEG 234
Cdd:TIGR00956 214 ERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKtsaNILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFG 293
|
....*.
gi 552559136 235 SIEHVK 240
Cdd:TIGR00956 294 PADKAK 299
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
27-235 |
2.43e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.95 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 27 AVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGK-----ELTRLKEHQIVHSgvgrkfQTPSVFED 101
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdyTLASLRNQVALVS------QNVHLFND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 102 lTVFENleVSYPQGHSvmgalaFKRsAEVVAAVEDVAETIF---LKDALD----QPASLLSHGQKQWLEIGMLLIQKPDL 174
Cdd:PRK11176 432 -TIANN--IAYARTEQ------YSR-EQIEEAARMAYAMDFinkMDNGLDtvigENGVLLSGGQRQRIAIARALLRDSPI 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552559136 175 LMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVgDIADRVTVMHQGKVLSEGS 235
Cdd:PRK11176 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTI-EKADEILVVEDGEIVERGT 561
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
132-241 |
2.52e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.67 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 132 AAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKD-HTVLVIEH 210
Cdd:NF000106 123 ARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQ 202
|
90 100 110
....*....|....*....|....*....|.
gi 552559136 211 DMQFVGDIADRVTVMHQGKVLSEGSIEHVKS 241
Cdd:NF000106 203 YMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
30-190 |
2.66e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.26 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 30 DLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSG--VGRKFqtpsvfeDLTVFEN 107
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGhnLGLKL-------EMTVFEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 108 LevsypqghsVMGALAFKRSAEVVAAVedvaeTIF-LKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSV 186
Cdd:PRK13541 91 L---------KFWSEIYNSAETLYAAI-----HYFkLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK 156
|
....
gi 552559136 187 AERK 190
Cdd:PRK13541 157 ENRD 160
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-233 |
8.16e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.19 E-value: 8.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 17 GLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTrlkehqivhsgvgrkfqtp 96
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ------------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 97 sVFEDLTVFENLevsYPQGhsvmgalAFKRSAEVVAAVEDVAETIFLKdaldqPASLLSHGQKQWLEIGMLLIQKPDLLM 176
Cdd:COG2401 96 -FGREASLIDAI---GRKG-------DFKDAVELLNAVGLSDAVLWLR-----RFKELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 177 LDEPVAGMSVAERKKTAELLRRITKDH--TVLVIEHDMQFVGDIA-DRVTVMHQGKVLSE 233
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKLARRAgiTLVVATHHYDVIDDLQpDLLIFVGYGGVPEE 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
37-238 |
1.11e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 55.05 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 37 PKEIRVIIGPNGAGKTTVLDLICGKTKA---TSGSIRFDGKELTRLKEHQIvhSGVGRKFQ--TPSvfedLTVFENLEVs 111
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAI--SAYVQQDDlfIPT----LTVREHLMF- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 112 ypQGHSVMGALAFKRsaEVVAAVEDVAETIFLKDALD----QPASL--LSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMS 185
Cdd:TIGR00955 123 --QAHLRMPRRVTKK--EKRERVDEVLQALGLRKCANtrigVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 186 VAERKKTAELLRRI-TKDHTVLVIEHdmQFVGDIA---DRVTVMHQGKVLSEGSIEH 238
Cdd:TIGR00955 199 SFMAYSVVQVLKGLaQKGKTIICTIH--QPSSELFelfDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
25-239 |
1.94e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.67 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 25 FKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGkeltrlkEHQIVHSGVGRKFQtpsvfedLTV 104
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-------EVSVIAISAGLSGQ-------LTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 105 FENLEVSypqghsvMGALAFKRSaEVVAAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEpvaGM 184
Cdd:PRK13546 103 IENIEFK-------MLCMGFKRK-EIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---AL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 185 SVAERKKTAELLRRI----TKDHTVLVIEHDMQFVGDIADRVTVMHQGKVLSEGSIEHV 239
Cdd:PRK13546 172 SVGDQTFAQKCLDKIyefkEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
31-219 |
4.32e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 31 LSFYLDPKeIRVIiGPNGAGKTTVLDLICGKTKATSGSIRFDgKELTrlkehqivhsgVGRKFQTPSVFEDLTVFENLE- 109
Cdd:PRK11819 28 LSFFPGAK-IGVL-GLNGAGKSTLLRIMAGVDKEFEGEARPA-PGIK-----------VGYLPQEPQLDPEKTVRENVEe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 110 ----------------VSYPQGHSVMGALAfKRSAEVVAAVE-----------DVAetiflKDAL-----DQPASLLSHG 157
Cdd:PRK11819 94 gvaevkaaldrfneiyAAYAEPDADFDALA-AEQGELQEIIDaadawdldsqlEIA-----MDALrcppwDAKVTKLSGG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 158 QKQWLEIGMLLIQKPDLLMLDEPVAGM---SVA--ERkktaeLLRRITKdhTVLVIEHDMQFVGDIA 219
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLdaeSVAwlEQ-----FLHDYPG--TVVAVTHDRYFLDNVA 227
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
106-212 |
6.89e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 51.85 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 106 ENLEVSYpQGHSVMGALAF--KRSAEVVAAVEDVAETI-FLKDA------LDQPASLLSHGQKQWLEIGMLLiQKPD--- 173
Cdd:cd03271 114 ETLEVRY-KGKSIADVLDMtvEEALEFFENIPKIARKLqTLCDVglgyikLGQPATTLSGGEAQRIKLAKEL-SKRStgk 191
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 552559136 174 -LLMLDEPVAGMSVAERKKTAELLRRIT-KDHTVLVIEHDM 212
Cdd:cd03271 192 tLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNL 232
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
147-222 |
1.82e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.75 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 147 LDQPASLLSHGQKQWLEIGMLLI---QKPDLLMLDEPVAGMSVAERKKTAELLRRIT-KDHTVLVIEHDMQFVgDIADRV 222
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVV-KVADYV 881
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
22-230 |
2.03e-07 |
|
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: 49.95 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 22 FDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTK---ATSGSIRFDG---KELTRLKEHQIVHSGvgrkfQT 95
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGipyKEFAEKYPGEIIYVS-----EE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 96 PSVFEDLTVFENLEVSYP-QGHsvmgalafkrsaEVVAAVedvaetiflkdaldqpasllSHGQKQWLEIGMLLIQKPDL 174
Cdd:cd03233 92 DVHFPTLTVRETLDFALRcKGN------------EFVRGI--------------------SGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 175 LMLDEPVAG---MSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:cd03233 140 LCWDNSTRGldsSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-230 |
2.60e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRF-DGKELTRLKEHQIVHSgvg 90
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQLEFL--- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 RKFQTPsvFEDLTVFENLEVSyPQGHSVMGALAFKrsaevvaavedvaetiflKDALDQPASLLSHGQKQWLEIGMLLIQ 170
Cdd:PRK10636 389 RADESP--LQHLARLAPQELE-QKLRDYLGGFGFQ------------------GDKVTEETRRFSGGEKARLVLALIVWQ 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 171 KPDLLMLDEPVAGMSVAERKKTAELLrrITKDHTVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:PRK10636 448 RPNLLLLDEPTNHLDLDMRQALTEAL--IDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-233 |
2.79e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 25 FKAVDDLSFYLDPKEIR-----VIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSgVGRKFQ----- 94
Cdd:PRK10938 11 FRLSDTKTLQLPSLTLNagdswAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL-VSDEWQrnntd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 95 TPSVFEDLTvfenlevsypqGHSVmgalafkrsAEVV-------AAVEDVAETIFLKDALDQPASLLSHGQKQWLEIGML 167
Cdd:PRK10938 90 MLSPGEDDT-----------GRTT---------AEIIqdevkdpARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552559136 168 LIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLV--------IEHDMQFVGDIADRvTVMHQGK---VLSE 233
Cdd:PRK10938 150 LMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVlvlnrfdeIPDFVQFAGVLADC-TLAETGEreeILQQ 225
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
20-58 |
4.51e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 49.61 E-value: 4.51e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 552559136 20 VSFDGFKAVDDLSFYLDPKE-IRVIIGPNGAGKTTVLDLI 58
Cdd:COG3950 6 LTIENFRGFEDLEIDFDNPPrLTVLVGENGSGKTTLLEAI 45
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
13-210 |
4.55e-07 |
|
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: 48.30 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTV-SFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIrfdgkeltrlkehqIVHSGVGR 91
Cdd:cd03223 1 IELENLSLaTPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------------GMPEGEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 KF--QTPsvfedltvfenlevsY-PQGHsvmgalafkrsaevvaavedvaetifLKDALDQP-ASLLSHGQKQWLEIGML 167
Cdd:cd03223 67 LFlpQRP---------------YlPLGT--------------------------LREQLIYPwDDVLSGGEQQRLAFARL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 552559136 168 LIQKPDLLMLDEPVAGMSVAerkkTAELLRRITKDH--TVLVIEH 210
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEE----SEDRLYQLLKELgiTVISVGH 146
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-184 |
4.96e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 29 DDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKA---TSGSIRFDGKEL-------TRLKEHQIVHSgvgrkfqtpsv 98
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLdssfqrsIGYVQQQDLHL----------- 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 99 fEDLTVFENLEVSypqghsvmgalAFKR-SAEV--------VAAVEDVAETIFLKDAL-DQPASLLSHGQKQWLEIGMLL 168
Cdd:TIGR00956 849 -PTSTVRESLRFS-----------AYLRqPKSVsksekmeyVEEVIKLLEMESYADAVvGVPGEGLNVEQRKRLTIGVEL 916
|
170
....*....|....*..
gi 552559136 169 IQKPDLLM-LDEPVAGM 184
Cdd:TIGR00956 917 VAKPKLLLfLDEPTSGL 933
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
147-239 |
8.94e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 49.63 E-value: 8.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 147 LDQPASLLSHGQKQWLEIGMLLiQKPD----LLMLDEPVAGMSVAERKKTAELLRR-ITKDHTVLVIEHDMQFVgDIADR 221
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKEL-SKRStgrtLYILDEPTTGLHFDDIKKLLEVLQRlVDKGNTVVVIEHNLDVI-KTADY 900
|
90 100
....*....|....*....|....
gi 552559136 222 VTVM------HQGKVLSEGSIEHV 239
Cdd:TIGR00630 901 IIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-242 |
9.61e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 48.70 E-value: 9.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSF--DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICgKTKATSGSIRFDGKELTRLKEHQIvHSGVG 90
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSWNSVPLQKW-RKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 RKFQTPSVFEDlTVFENLEvsyPQGhsvmgalafKRSAEvvaAVEDVAETIFLKDALDQ-PASL----------LSHGQK 159
Cdd:cd03289 81 VIPQKVFIFSG-TFRKNLD---PYG---------KWSDE---EIWKVAEEVGLKSVIEQfPGQLdfvlvdggcvLSHGHK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 160 QWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDiADRVTVMHQGKVLSEGSIEHV 239
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKL 223
|
...
gi 552559136 240 KSD 242
Cdd:cd03289 224 LNE 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
31-242 |
1.41e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 31 LSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDG------------KELTRLKEHQIVHSGVGRKFQTP-S 97
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmdlrKVLGIIPQAPVLFSGTVRFNLDPfN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 98 VFEDLTVFENLEVSYPQghSVMGALAFKRSAEVVAAVEDvaetiflkdaldqpaslLSHGQKQWLEIGMLLIQKPDLLML 177
Cdd:PLN03130 1338 EHNDADLWESLERAHLK--DVIRRNSLGLDAEVSEAGEN-----------------FSVGQRQLLSLARALLRRSKILVL 1398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552559136 178 DEPVAGMSV---AERKKTaelLRRITKDHTVLVIEHDMQFVGDiADRVTVMHQGKVLSEGSIEHVKSD 242
Cdd:PLN03130 1399 DEATAAVDVrtdALIQKT---IREEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
19-217 |
1.44e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 19 TVSFDGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICG-KTKATS------GSIRFDGKELTRLKEHqivhsgVGr 91
Cdd:PRK10938 267 VVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQGYSndltlfGRRRGSGETIWDIKKH------IG- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 92 kfqtpsvfedlTVFENLEVSYPQGHSVMGAL--AFKRSAEVVAAVEDVA--------ETIFLKDAL-DQPASLLSHGQKQ 160
Cdd:PRK10938 340 -----------YVSSSLHLDYRVSTSVRNVIlsGFFDSIGIYQAVSDRQqklaqqwlDILGIDKRTaDAPFHSLSWGQQR 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552559136 161 WLEIGMLLIQKPDLLMLDEPVAGMSVAERKktaeLLRR-----ITKDHTVLV------------IEHDMQFVGD 217
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRQ----LVRRfvdvlISEGETQLLfvshhaedapacITHRLEFVPD 478
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-213 |
1.69e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.75 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSF--DGFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICgKTKATSGSIRFDG------------KELTR 78
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvswnsvtlqtwrKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 79 LKEHQIVHSGVGRKFQTP-SVFEDLTVFEnlevsypqghsvmgalafkrsaevvaavedVAETIFLKDALDQ-PASL--- 153
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNLDPyEQWSDEEIWK------------------------------VAEEVGLKSVIEQfPDKLdfv 1346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552559136 154 -------LSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAerkkTAELLRRITK----DHTVLVIEHDMQ 213
Cdd:TIGR01271 1347 lvdggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPV----TLQIIRKTLKqsfsNCTVILSEHRVE 1413
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-235 |
2.00e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.40 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 30 DLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDG------------KELTRLKEHQIVHSGVGRKFQTP- 96
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglhdlrFKITIIPQDPVLFSGSLRMNLDPf 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 97 SVFEDLTVFENLEVSYPqgHSVMGALAFKRSAEVVAAVEDvaetiflkdaldqpaslLSHGQKQWLEIGMLLIQKPDLLM 176
Cdd:TIGR00957 1384 SQYSDEEVWWALELAHL--KTFVSALPDKLDHECAEGGEN-----------------LSVGQRQLVCLARALLRKTKILV 1444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552559136 177 LDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIAdRVTVMHQGKVLSEGS 235
Cdd:TIGR00957 1445 LDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGA 1502
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
39-226 |
3.97e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.03 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 39 EIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGkeltrlkehqivhsgvgrkfQTPSVfedltvfenlevsYPQGHSv 118
Cdd:cd03222 26 EVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG--------------------ITPVY-------------KPQYID- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 119 mgalafkrsaevvaavedvaetiflkdaldqpaslLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSVAERKKTAELLRR 198
Cdd:cd03222 72 -----------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180 190
....*....|....*....|....*....|
gi 552559136 199 ITK--DHTVLVIEHDMQFVGDIADRVTVMH 226
Cdd:cd03222 117 LSEegKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
30-230 |
5.36e-06 |
|
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: 47.10 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 30 DLSFYldPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELT-----RLKEHqivhsgvgrkFQTpsVFEDLTV 104
Cdd:COG4615 352 DLTIR--RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTadnreAYRQL----------FSA--VFSDFHL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 105 FENLevsypqghsvMGALAFKRSAEV-----------VAAVEDvaetiflkDALDQPAslLSHGQKQWLE-IGMLLIQKP 172
Cdd:COG4615 418 FDRL----------LGLDGEADPARArellerleldhKVSVED--------GRFSTTD--LSQGQRKRLAlLVALLEDRP 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552559136 173 dLLMLDE------PVAgmsvaeRKK-TAELL---RRITKdhTVLVIEHDMQFVgDIADRVTVMHQGKV 230
Cdd:COG4615 478 -ILVFDEwaadqdPEF------RRVfYTELLpelKARGK--TVIAISHDDRYF-DLADRVLKMDYGKL 535
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-235 |
6.36e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 16 EGLTVSFDGfkavddLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTR--LKEhqivhsgVGRKF 93
Cdd:PTZ00243 1320 EGLPLVLRG------VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRE-------LRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 94 ----QTPSVFeDLTVFEN----LEVSypqghsvmgalafkrSAEVVAAVEDV-------AETIFLKDALDQPASLLSHGQ 158
Cdd:PTZ00243 1387 smipQDPVLF-DGTVRQNvdpfLEAS---------------SAEVWAALELVglrervaSESEGIDSRVLEGGSNYSVGQ 1450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552559136 159 KQWLEIGMLLIQK-PDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVIEHDMQFVGDIaDRVTVMHQGKVLSEGS 235
Cdd:PTZ00243 1451 RQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGS 1527
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
19-56 |
6.78e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 46.46 E-value: 6.78e-06
10 20 30
....*....|....*....|....*....|....*...
gi 552559136 19 TVSFDGFKAVDDLSFYLDPkeIRVIIGPNGAGKTTVLD 56
Cdd:COG4637 4 RIRIKNFKSLRDLELPLGP--LTVLIGANGSGKSNLLD 39
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-228 |
9.25e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.44 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 30 DLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRfdgkeltrlkehqivHSG-VGRKFQTPSVFEDlTVFENL 108
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK---------------HSGrISFSPQTSWIMPG-TIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 109 --EVSYPQGH--SVMGALAFKRSAEVVAAVEdvaetiflKDALDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGM 184
Cdd:TIGR01271 508 ifGLSYDEYRytSVIKACQLEEDIALFPEKD--------KTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 552559136 185 SVAERKKTAE-LLRRITKDHTVLVIEHDMQFVGDiADRVTVMHQG 228
Cdd:TIGR01271 580 DVVTEKEIFEsCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
37-234 |
1.03e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.03 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 37 PKEIRVIIGPNGAGKTTVLDLICGKTKATS--GSIRFDGKELTRlkehQIVHSgVGRKFQTPSVFEDLTVFENL------ 108
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK----QILKR-TGFVTQDDILYPHLTVRETLvfcsll 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 109 --------EVSYPQGHSVMGALAFKRSAEVVAAvedvaeTIFLKDaldqpaslLSHGQKQWLEIGMLLIQKPDLLMLDEP 180
Cdd:PLN03211 168 rlpksltkQEKILVAESVISELGLTKCENTIIG------NSFIRG--------ISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 181 VAGM-SVAERKKTAELLRRITKDHTVLVIEHD-MQFVGDIADRVTVMHQGKVLSEG 234
Cdd:PLN03211 234 TSGLdATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
147-234 |
1.08e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.62 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 147 LDQPASLLSHGQKQWLEIGMLLIQ--KPDLLMLDEPVAGMSVAERKKTAELLRR-ITKDHTVLVIEHDMQFVgDIADRVT 223
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQLLEVIKGlIDLGNTVILIEHNLDVL-SSADWII 159
|
90
....*....|....*..
gi 552559136 224 VM------HQGKVLSEG 234
Cdd:cd03238 160 DFgpgsgkSGGKVVFSG 176
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
20-59 |
1.95e-05 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 44.02 E-value: 1.95e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 552559136 20 VSFDGFKAVDDLSFYLDPKeIRVIIGPNGAGKTTVLDLIC 59
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKG-LTLITGPNGSGKTTILDAIK 39
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
20-208 |
2.85e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.61 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 20 VSFDGFKAVDDLSFYLDPKeIRVIIGPNGAGKTTVLD---LICGKTKATSGSIR-FDGKELTRLKEHQIVH------SGV 89
Cdd:COG3593 6 IKIKNFRSIKDLSIELSDD-LTVLVGENNSGKSSILEalrLLLGPSSSRKFDEEdFYLGDDPDLPEIEIELtfgsllSRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 90 GRKFQTPSVFEDL-TVFENLEVSYPQG--------HSVMGALAFKRSAEVVAAVEDVAE-----TIFLKDALDQPASLLS 155
Cdd:COG3593 85 LRLLLKEEDKEELeEALEELNEELKEAlkalnellSEYLKELLDGLDLELELSLDELEDllkslSLRIEDGKELPLDRLG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 156 HGQKQWLEIGMLLI-------QKPDLLMLDEPVAGMSVAERKKTAELLRRITKDHTVLVI 208
Cdd:COG3593 165 SGFQRLILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVII 224
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
30-241 |
3.66e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 44.08 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 30 DLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRfdgkeltrlkehqivHSG-VGRKFQTPSVFEDlTVFENL 108
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK---------------HSGrISFSSQFSWIMPG-TIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 109 --EVSYPQGH--SVMGALAFKrsaEVVAAVEDVAETIflkdaLDQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGM 184
Cdd:cd03291 119 ifGVSYDEYRykSVVKACQLE---EDITKFPEKDNTV-----LGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552559136 185 SVAERKKTAE-LLRRITKDHTVLVIEHDMQFVgDIADRVTVMHQGKVLSEGSIEHVKS 241
Cdd:cd03291 191 DVFTEKEIFEsCVCKLMANKTRILVTSKMEHL-KKADKILILHEGSSYFYGTFSELQS 247
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-232 |
3.95e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 12 LLAVEGLTVSFDGFKAVDDLSFYLDPKEiRV-IIGPNGAGKTTVLDLICGKTKATSGSIRFDgKELTrlkehqivhsgVG 90
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNE-RVcLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLI-----------VA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 91 RKFQTPSVFEDLTVF-----------ENLEVSYPQGHSVMGALA---FKRSAEVVAAVE------------DVAETIFLk 144
Cdd:PRK11147 70 RLQQDPPRNVEGTVYdfvaegieeqaEYLKRYHDISHLVETDPSeknLNELAKLQEQLDhhnlwqlenrinEVLAQLGL- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 145 DAlDQPASLLSHGqkqWLE---IGMLLIQKPDLLMLDEPVAGMSVAerkkTAELLRRITKDH--TVLVIEHDMQFVGDIA 219
Cdd:PRK11147 149 DP-DAALSSLSGG---WLRkaaLGRALVSNPDVLLLDEPTNHLDIE----TIEWLEGFLKTFqgSIIFISHDRSFIRNMA 220
|
250
....*....|...
gi 552559136 220 DRVTVMHQGKVLS 232
Cdd:PRK11147 221 TRIVDLDRGKLVS 233
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-244 |
5.37e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 142 FLKD------ALDQPASLLSHGQKQWL----EIGMLLIQKpdLLMLDEPVAGMSVAERKKTAELLRRItKD--HTVLVIE 209
Cdd:TIGR00630 471 FLIDvgldylSLSRAAGTLSGGEAQRIrlatQIGSGLTGV--LYVLDEPSIGLHQRDNRRLINTLKRL-RDlgNTLIVVE 547
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 552559136 210 HDMQFVgDIADRVTVM------HQGKVLSEGSIEHVKSDPK 244
Cdd:TIGR00630 548 HDEDTI-RAADYVIDIgpgageHGGEVVASGTPEEILANPD 587
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
13-229 |
8.26e-05 |
|
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: 42.46 E-value: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 13 LAVEGLTVSFD-----GFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRfdgkeltrlkehqiVHS 87
Cdd:cd03250 1 ISVEDASFTWDsgeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS--------------VPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 88 GVGRKFQTPSVFEDlTVFENLEVSYPqghsvmgaLAFKRSAEVVAA---VEDVAetIFlkDALDQP-----ASLLSHGQK 159
Cdd:cd03250 67 SIAYVSQEPWIQNG-TIRENILFGKP--------FDEERYEKVIKAcalEPDLE--IL--PDGDLTeigekGINLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552559136 160 QWLEIGMLLIQKPDLLMLDEPVAG--MSVAeRKKTAELLRRITKDH-TVLVIEHDMQFVGDiADRVTVMHQGK 229
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAvdAHVG-RHIFENCILGLLLNNkTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
229-252 |
9.92e-05 |
|
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00005. There is a conserved AYLG sequence motif. This family is the C terminal of an ATP dependent branched-chain amino acid transporter. This domain is essential for LPS transport, through critical interactions with Walker A and switch helix domains.
Pssm-ID: 463560 Cd Length: 25 Bit Score: 38.39 E-value: 9.92e-05
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
29-235 |
1.19e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.58 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 29 DDLSFYLDPKEIRVIIGPNGAGKTTVLDLICgktkatsgsirfdgkeltrlkehqivhSGVGRKFqtpsvfedltvfenl 108
Cdd:cd03227 12 VPNDVTFGEGSLTIITGPNGSGKSTILDAIG---------------------------LALGGAQ--------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 109 evsypqghSVMGALAFKRSAEVVAAVEdvAETIFLkdaLDQpaslLSHGQKQWLEIGMLL----IQKPDLLMLDEPVAGM 184
Cdd:cd03227 50 --------SATRRRSGVKAGCIVAAVS--AELIFT---RLQ----LSGGEKELSALALILalasLKPRPLYILDEIDRGL 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 552559136 185 SVAERKKTAELLRRIT-KDHTVLVIEHDMQFvgdIADRVTVMHQGKVLSEGS 235
Cdd:cd03227 113 DPRDGQALAEAILEHLvKGAQVIVITHLPEL---AELADKLIHIKKVITGVY 161
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-227 |
1.62e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 28 VDDLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDG--------KELTRLKEHQIVHsgvgrkfqtpsVF 99
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQPALEY-----------VI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 100 EDLTVFENLEVSYPQ------GHSVmGALAFKRSAEVVAAVEDVAETI-----FLKDALDQPASLLSHGQKQWLEIGMLL 168
Cdd:PRK10636 86 DGDREYRQLEAQLHDanerndGHAI-ATIHGKLDAIDAWTIRSRAASLlhglgFSNEQLERPVSDFSGGWRMRLNLAQAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552559136 169 IQKPDLLMLDEPVAGMSVaerkKTAELLRRITKDH--TVLVIEHDMQFVGDIADRVTVMHQ 227
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLDL----DAVIWLEKWLKSYqgTLILISHDRDFLDPIVDKIIHIEQ 221
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
6-184 |
1.74e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 6 AQSKDFLLAVEGLTVSFDgfkavdDLSFYLD-PKEIR-------------------------VIIGPNGAGKTTVLDLIC 59
Cdd:PLN03140 854 APKRGMVLPFTPLAMSFD------DVNYFVDmPAEMKeqgvtedrlqllrevtgafrpgvltALMGVSGAGKTTLMDVLA 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 60 GKTKA--TSGSIRFDG-----KELTRLK---EHQIVHSgvgrkfqtPSVfedlTVFENLEVSypqghsvmgalAFKRSAE 129
Cdd:PLN03140 928 GRKTGgyIEGDIRISGfpkkqETFARISgycEQNDIHS--------PQV----TVRESLIYS-----------AFLRLPK 984
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 130 VVAA------VEDVAETIFLKDALDQPASL-----LSHGQKQWLEIGMLLIQKPDLLMLDEPVAGM 184
Cdd:PLN03140 985 EVSKeekmmfVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
24-215 |
1.97e-04 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 41.14 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 24 GFKAVDDLSFYLDPKEIRVIIGPNGAGKTTVLDLIC----GKTKAtsgsirfdgkeLTRLKEHQIVHSGVGRKFQTPSVf 99
Cdd:cd03239 8 NFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICfvlgGKAAK-----------LRRGSLLFLAGGGVKAGINSASV- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 100 edltvfenlEVSYPQGHSVMGAlafkrsaevvaavEDVAEtiflkdaldqpasLLSHGQKQWLEIGMLL----IQKPDLL 175
Cdd:cd03239 76 ---------EITFDKSYFLVLQ-------------GKVEQ-------------ILSGGEKSLSALALIFalqeIKPSPFY 120
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 552559136 176 MLDEPVAGMSVAERKKTAELLRRITKdhtvlvieHDMQFV 215
Cdd:cd03239 121 VLDEIDAALDPTNRRRVSDMIKEMAK--------HTSQFI 152
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-230 |
3.27e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 30 DLSFYLDPKEIRVIIGPNGAGKTTVLDLICGKTKATSGSIRFDGK-ELTRLKEHQIvhSGVgrkfqtpsvfeDLTVFENL 108
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvRMAVFSQHHV--DGL-----------DLSSNPLL 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 109 EVS--YPqghsvmGALAFKRSAEVVAAveDVAETIFLkdaldQPASLLSHGQKQWLEIGMLLIQKPDLLMLDEPVAGMSV 186
Cdd:PLN03073 594 YMMrcFP------GVPEQKLRAHLGSF--GVTGNLAL-----QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL 660
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 552559136 187 AERKKTAELLrrITKDHTVLVIEHDMQFVGDIADRVTVMHQGKV 230
Cdd:PLN03073 661 DAVEALIQGL--VLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-222 |
3.82e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 40.28 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 38 KEIRVIIGPNGAGKTTVLDLI---CGKTKATSGSIRFDGKELTRLKE-----HQIVHSGVGRKFQtpsVFEDLTVFENle 109
Cdd:cd03240 22 SPLTLIVGQNGAGKTTIIEALkyaLTGELPPNSKGGAHDPKLIREGEvraqvKLAFENANGKKYT---ITRSLAILEN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 110 VSY-PQGHSvmgalafkrsaevvaavedvaetiflKDALDQPASLLSHGQKQW------LEIGMLLIQKPDLLMLDEPVA 182
Cdd:cd03240 97 VIFcHQGES--------------------------NWPLLDMRGRCSGGEKVLasliirLALAETFGSNCGILALDEPTT 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 552559136 183 GMSvAERKKTAelLRRITKDHT------VLVIEHDMQFVgDIADRV 222
Cdd:cd03240 151 NLD-EENIEES--LAEIIEERKsqknfqLIVITHDEELV-DAADHI 192
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
22-66 |
6.74e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 6.74e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 552559136 22 FDGFKAVDDLSFyldPKEIRVIIGPNGAGKTTVLDLIC----GKTKATS 66
Cdd:COG0419 10 FRSYRDTETIDF---DDGLNLIVGPNGAGKSTILEAIRyalyGKARSRS 55
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
22-104 |
8.41e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 22 FDGFKAVDDLSFYLDPKeIRVIIGPNGAGKTTVLDLIC----GKTKATSGSIRFDGKELTRLKEHQIVHSGVGRKFQTPS 97
Cdd:TIGR00618 11 FGSYKGTHTIDFTALGP-IFLICGKTGAGKTTLLDAITyalyGKLPRRSEVIRSLNSLYAAPSEAAFAELEFSLGTKIYR 89
|
....*..
gi 552559136 98 VFEDLTV 104
Cdd:TIGR00618 90 VHRTLRC 96
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
147-234 |
1.78e-03 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.39 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552559136 147 LDQPASLLSHGQKQWL----EIGMLLIQKpdLLMLDEPVAGMSVAERKKTAELLRRItKDH--TVLVIEHDMQFVgDIAD 220
Cdd:cd03270 131 LSRSAPTLSGGEAQRIrlatQIGSGLTGV--LYVLDEPSIGLHPRDNDRLIETLKRL-RDLgnTVLVVEHDEDTI-RAAD 206
|
90 100
....*....|....*....|
gi 552559136 221 RVTVM------HQGKVLSEG 234
Cdd:cd03270 207 HVIDIgpgagvHGGEIVAQG 226
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
42-112 |
1.98e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.91 E-value: 1.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552559136 42 VIIGPNGAGKTTVLDLICGKTKATSGSIRFDGKELTRLKEHQIVHSGVGRKFQTPSVFEDLTVFENlEVSY 112
Cdd:pfam13304 3 VLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLED-GVRY 72
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
29-58 |
2.26e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.65 E-value: 2.26e-03
10 20 30
....*....|....*....|....*....|
gi 552559136 29 DDLSFYLDPKEIRVIIGPNGAGKTTVLDLI 58
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAI 42
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
22-72 |
2.62e-03 |
|
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: 38.02 E-value: 2.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 552559136 22 FDGFKAVDDLSFY-LDPKEIRVIIGPNGAGKTTVLDLIC----GKTKATSGSIRFD 72
Cdd:cd03279 11 FGPFREEQVIDFTgLDNNGLFLICGPTGAGKSTILDAITyalyGKTPRYGRQENLR 66
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
19-58 |
3.55e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 38.03 E-value: 3.55e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 552559136 19 TVSFDGFKAVDDLSFYLDPkeIRVIIGPNGAGKTTVLDLI 58
Cdd:COG4938 3 SISIKNFGPFKEAELELKP--LTLLIGPNGSGKSTLIQAL 40
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
19-58 |
4.35e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 37.96 E-value: 4.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 552559136 19 TVSFDGFKAVDDLSFYLDpKEIRVIIGPNGAGKTTVLDLI 58
Cdd:pfam13175 5 SIIIKNFRCLKDTEIDLD-EDLTVLIGKNNSGKSSILEAL 43
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
147-214 |
7.25e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 7.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552559136 147 LDQPASLLSHGQKQWLEIGMLLI---QKPDLLMLDEPVAGMSVAERKKTAELLRR-ITKDHTVLVIEHDMQF 214
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPAL 1764
|
|
| |
