|
Name |
Accession |
Description |
Interval |
E-value |
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-241 |
3.91e-115 |
|
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: 329.69 E-value: 3.91e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAG 80
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQLVKPFAGLSVLDNVTVGALHRAPNV---------------SAAKKHAAEIVERLGLGAKREQPASSLTLPDRKR 145
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreeREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 146 LEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEV 225
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
250
....*....|....*.
gi 1082692222 226 VRDPAVLGCYLGEETE 241
Cdd:COG0411 241 RADPRVIEAYLGEEAA 256
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-231 |
5.51e-104 |
|
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: 300.51 E-value: 5.51e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGIGRT 84
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVTVGALHRAPN----------VSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALAT 154
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082692222 155 RPELLLLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAV 231
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-239 |
4.44e-64 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 200.22 E-value: 4.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAA-LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAA 79
Cdd:PRK11300 1 MSQPlLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 GIGRTFQLVKPFAGLSVLDNVTVgALHRAPNV----------------SAAKKHAAEIVERLGLGAKREQPASSLTLPDR 143
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLV-AQHQQLKTglfsgllktpafrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 144 KRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPG 223
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 239
|
250
....*....|....*.
gi 1082692222 224 EVVRDPAVLGCYLGEE 239
Cdd:PRK11300 240 EIRNNPDVIKAYLGEA 255
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-238 |
7.63e-55 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 176.08 E-value: 7.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAG 80
Cdd:COG4674 7 HGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQlvKP--FAGLSVLDNVTVgALHRAPNV---------SAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVA 149
Cdd:COG4674 87 IGRKFQ--KPtvFEELTVFENLEL-ALKGDRGVfaslfarltAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 150 RALATRPELLLLDEVMAGLRPTECDQMVEAFREInrAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:COG4674 164 MLLAQDPKLLLLDEPVAGMTDAETERTAELLKSL--AGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQADP 241
|
....*....
gi 1082692222 230 AVLGCYLGE 238
Cdd:COG4674 242 RVIEVYLGR 250
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-227 |
3.25e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 171.40 E-value: 3.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGlRPDQVCAAgIGRT 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVT-VGALHRAPNvSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDE 163
Cdd:COG1131 79 PQEPALYPDLTVRENLRfFARLYGLPR-KEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082692222 164 VMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVR 227
Cdd:COG1131 158 PTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-237 |
4.09e-53 |
|
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: 171.32 E-value: 4.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 2 SAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGI 81
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 82 GrtfqLVkP-----FAGLSVLDNVTVGALHRapnvsAAKKHAAEIVERLG-----LGAKREQPASSLTLPDRKRLEVARA 151
Cdd:COG0410 81 G----YV-PegrriFPSLTVEENLLLGAYAR-----RDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 152 LATRPELLLLDEVMAGLRPTECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAV 231
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEV 229
|
....*.
gi 1082692222 232 LGCYLG 237
Cdd:COG0410 230 REAYLG 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-228 |
2.65e-52 |
|
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: 168.77 E-value: 2.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGIGRT 84
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVTVGALHRapnvsaAKKHAAEIVERL-----GLGAKREQPASSLTLPDRKRLEVARALATRPELL 159
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYAR------RRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082692222 160 LLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRD 228
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-237 |
1.57e-47 |
|
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: 156.93 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGIGRT 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVTVgALHRAPNVSAAKKHAAE-IVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDE 163
Cdd:cd03218 81 PQEASIFRKLTVEENILA-VLEIRGLSKKEREEKLEeLLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082692222 164 VMAGLRP---TECDQMVEAFREinraEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVLGCYLG 237
Cdd:cd03218 160 PFAGVDPiavQDIQKIIKILKD----RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-239 |
2.51e-46 |
|
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: 153.97 E-value: 2.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGIGRT 84
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVTVgALHRAPNVSAA--KKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLD 162
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMA-VLEIRKDLDRAerEERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 163 EVMAGLRP---TECDQMVEAFREinraEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVLGCYLGEE 239
Cdd:TIGR04406 161 EPFAGVDPiavGDIKKIIKHLKE----RGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLGEQ 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-239 |
3.45e-46 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 153.65 E-value: 3.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGIGRT 84
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEV 164
Cdd:COG1137 84 PQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082692222 165 MAGLRP---TECDQMVEAFREinraEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVLGCYLGEE 239
Cdd:COG1137 164 FAGVDPiavADIQKIIRHLKE----RGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLGED 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-225 |
5.56e-44 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 154.41 E-value: 5.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAG 80
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQ---LVKPFaglSVLDNVTVGALHRA---PNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALAT 154
Cdd:COG3845 82 IGMVHQhfmLVPNL---TVAENIVLGLEPTKggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 155 RPELLLLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEV 225
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-225 |
2.05e-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: 146.54 E-value: 2.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGrrIDGLRPDQVCAAGIGRT 84
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG--EDVRKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVT-VGALHRaPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDE 163
Cdd:COG4555 80 PDERGLYDRLTVRENIRyFAELYG-LFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082692222 164 VMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEV 225
Cdd:COG4555 159 PTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-232 |
2.28e-43 |
|
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: 145.94 E-value: 2.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFR-GLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAAGIGR 83
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL-RRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 84 TFQ-----LVKPfaglSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPEL 158
Cdd:COG1122 80 VFQnpddqLFAP----TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082692222 159 LLLDEVMAGLRPTECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVL 232
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-230 |
1.18e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 147.55 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcaaG 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR---N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQ---LvkpFAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLG--AKReqpassltLPD------RKRLEVA 149
Cdd:COG3842 79 VGMVFQdyaL---FPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEglADR--------YPHqlsggqQQRVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 150 RALATRPELLLLDEVMAGL----RptecDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEV 225
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALdaklR----EEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
....*
gi 1082692222 226 VRDPA 230
Cdd:COG3842 224 YERPA 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-228 |
7.69e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 148.63 E-value: 7.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAG 80
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQLVKPFAGLSVLDNVTVGALHRAP---NVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPE 157
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 158 LLLLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRD 228
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTED 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-229 |
1.14e-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: 148.51 E-value: 1.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSF-----RGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcaA 79
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSL--R 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 GIGRTFQLV--KPFAGL----SVLDNVTVGA-LHRAPNVSAAKKHAAEIVERLGLGAK-REQPASSLTLPDRKRLEVARA 151
Cdd:COG1123 339 ELRRRVQMVfqDPYSSLnprmTVGDIIAEPLrLHGLLSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082692222 152 LATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-231 |
1.39e-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: 139.34 E-value: 1.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCA-- 78
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 79 AGIGRTFQ---LvkpFAGLSVLDNVTVGaLHRAPNVSAAKKH--AAEIVERLGLGAKREQPASSLTLPDRKRLEVARALA 153
Cdd:COG1127 82 RRIGMLFQggaL---FDSLTVFENVAFP-LREHTDLSEAEIRelVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 154 TRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVR--DPAV 231
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAsdDPWV 237
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-224 |
6.41e-40 |
|
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: 137.12 E-value: 6.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGrrIDGLRPDQVCAAGIGRT 84
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVTV-GALHRAPNvSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDE 163
Cdd:cd03265 79 FQDLSVDDELTGWENLYIhARLYGVPG-AERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 164 VMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGE 224
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-220 |
7.15e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 139.09 E-value: 7.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 4 ALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDglrPDQVcaAGIG- 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDR--RRIGy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 83 ----RtfqlvkpfaGL----SVLDNVT-VGALHRAPnVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALA 153
Cdd:COG4152 76 lpeeR---------GLypkmKVGEQLVyLARLKGLS-KAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082692222 154 TRPELLLLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARG 220
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3-239 |
8.81e-40 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 137.33 E-value: 8.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 3 AALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGIG 82
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 83 RTFQLVKPFAGLSVLDNV-TVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLL 161
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 162 DEVMAGLRPT---ECDQMVEAFREinraEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVLGCYLGE 238
Cdd:PRK10895 162 DEPFAGVDPIsviDIKRIIEHLRD----SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGE 237
|
.
gi 1082692222 239 E 239
Cdd:PRK10895 238 D 238
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-216 |
1.41e-39 |
|
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: 134.45 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIdGLRPDQVCAAgIGRT 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEVKRR-IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVtvgalhrapnvsaakkhaaeiveRLGLGAKReqpassltlpdrkRLEVARALATRPELLLLDEV 164
Cdd:cd03230 79 PEEPSLYENLTVRENL-----------------------KLSGGMKQ-------------RLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1082692222 165 MAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEV 216
Cdd:cd03230 123 TSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-220 |
2.47e-39 |
|
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: 135.34 E-value: 2.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQvcaAGIGRT 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER---RNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEV 164
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 165 MAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARG 220
Cdd:cd03259 158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-231 |
2.44e-38 |
|
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: 133.40 E-value: 2.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRP--DQVCAAGIG 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 83 RTFQLVKPFAGLSVLDNVTVGAL-HRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLL 161
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082692222 162 DEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVR--DPAV 231
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAsdDPLV 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-220 |
2.51e-38 |
|
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: 132.34 E-value: 2.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPdqvCAAGIGRT 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE---ALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVTVGA-LHRAPnvsaaKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDE 163
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLArLLGIR-----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1082692222 164 VMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARG 220
Cdd:cd03268 153 PTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-218 |
5.59e-38 |
|
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: 130.24 E-value: 5.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGIGRT 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLvkpfaglsvldnvTVGalhrapnvsaakkhaaeiverlglgakreqpassltlpDRKRLEVARALATRPELLLLDEV 164
Cdd:cd03216 81 YQL-------------SVG--------------------------------------ERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1082692222 165 MAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIA 218
Cdd:cd03216 110 TAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-229 |
5.62e-38 |
|
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: 132.32 E-value: 5.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRG----LRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAA- 79
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 -GIGRTFQLVKPFAGLSVLDNVTVG-ALHRAPNVSAAKKhAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPE 157
Cdd:cd03258 82 rRIGMIFQHFNLLSSRTVFENVALPlEIAGVPKAEIEER-VLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082692222 158 LLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-225 |
5.83e-38 |
|
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: 132.69 E-value: 5.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSF-RGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAA--GI 81
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 82 GRTFQ---LVKPfagLSVLDNVTVGALHRAPNVS--------AAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVAR 150
Cdd:cd03256 81 GMIFQqfnLIER---LSVLENVLSGRLGRRSTWRslfglfpkEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 151 ALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEV 225
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-231 |
6.50e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 132.91 E-value: 6.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFR----GLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDqv 76
Cdd:COG1116 4 AAPALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 77 caagIGRTFQlvKP--FAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQpassltLPD------RKRLEV 148
Cdd:COG1116 82 ----RGVVFQ--EPalLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDA------YPHqlsggmRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 149 ARALATRPELLLLDEVMAGL----RptecDQMVEAFREINRAEGLTIMLIEH-VMRAVmALAQRIVVLHHGeviargaPG 223
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALdaltR----ERLQDELLRLWQETGKTVLFVTHdVDEAV-FLADRVVVLSAR-------PG 217
|
....*...
gi 1082692222 224 EVVRDPAV 231
Cdd:COG1116 218 RIVEEIDV 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-228 |
2.75e-37 |
|
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: 130.28 E-value: 2.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRG----LRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDqvcaag 80
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQlvKP--FAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPEL 158
Cdd:cd03293 75 RGYVFQ--QDalLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 159 LLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEH-VMRAVmALAQRIVVLHhgeviarGAPGEVVRD 228
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHdIDEAV-FLADRVVVLS-------ARPGRIVAE 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-220 |
7.40e-37 |
|
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: 128.94 E-value: 7.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDglrpdqvcaAGIGRT 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---------IAARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGL----SVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLL 160
Cdd:cd03269 72 IGYLPEERGLypkmKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 161 LDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARG 220
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-230 |
1.56e-36 |
|
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: 129.00 E-value: 1.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 4 ALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQvcaAGIGR 83
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---RNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 84 TFQLVKPFAGLSVLDNVTVG--ALHRAPNVSAA--KKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELL 159
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGlrVKPRSERPPEAeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 160 LLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPA 230
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-230 |
1.81e-36 |
|
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: 128.51 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQvcaAGIGRT 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK---RPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEV 164
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 165 MAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPA 230
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-234 |
1.89e-36 |
|
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: 134.26 E-value: 1.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRG--LRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADA---GEIVFRGRRIDGLrPDQ 75
Cdd:COG1123 1 MTPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLEL-SEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 76 VCAAGIGRTFQLV-KPFAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALAT 154
Cdd:COG1123 80 LRGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 155 RPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVLGC 234
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAA 239
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-215 |
2.78e-36 |
|
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: 127.20 E-value: 2.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 6 EVRGVSKSF-RGLRAV-HDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAAGIGR 83
Cdd:cd03225 1 ELKNLSFSYpDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL-RRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 84 TFQlvKP---FAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLL 160
Cdd:cd03225 80 VFQ--NPddqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 161 LDEVMAGLRPTECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHGE 215
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-216 |
2.99e-36 |
|
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: 127.61 E-value: 2.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRG----LRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRP---DQVC 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 78 AAGIGRTFQ---LVkPFagLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALAT 154
Cdd:cd03255 81 RRHIGFVFQsfnLL-PD--LTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082692222 155 RPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVmALAQRIVVLHHGEV 216
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-235 |
3.72e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.90 E-value: 3.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPD-----Q 75
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigyvpQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 76 vcAAGIGRTFqlvkPfagLSVLDNVTVGALHRAPNV----SAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARA 151
Cdd:COG1121 83 --RAEVDWDF----P---ITVRDVVLMGRYGRRGLFrrpsRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 152 LATRPELLLLDEVMAGLRPTECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHGeVIARGAPGEVVRDPAV 231
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENL 231
|
....
gi 1082692222 232 LGCY 235
Cdd:COG1121 232 SRAY 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-230 |
2.06e-35 |
|
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: 125.88 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLR-AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAAGIGR 83
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL-RRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 84 TFQLVKPFAGLSVLDNV-TVGALHRAPNvSAAKKHAAEIVERLGLGAK--REQPASSLTLPDRKRLEVARALATRPELLL 160
Cdd:cd03295 80 VIQQIGLFPHMTVEENIaLVPKLLKWPK-EKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 161 LDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPA 230
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPA 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-225 |
4.74e-35 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 124.60 E-value: 4.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVY-----AADAGEIVFRGRRIDGLRPDQVCA- 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVLELr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 79 AGIGRTFQLVKPFAGlSVLDNVTVGA-LHRapnvSAAKKHAAEIVE----RLGLG--AKREQPASSLTLPDRKRLEVARA 151
Cdd:cd03260 81 RRVGMVFQKPNPFPG-SIYDNVAYGLrLHG----IKLKEELDERVEealrKAALWdeVKDRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082692222 152 LATRPELLLLDEVMAGLRPTECDQMVEAFREINRAegLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEV 225
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-224 |
2.03e-34 |
|
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: 122.61 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLR--AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIdgLRPDQVCAAGIG 82
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 83 RTFQ---LvkpFAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELL 159
Cdd:cd03263 79 YCPQfdaL---FDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 160 LLDEVMAGLRPTECDQMVEAFREInrAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGE 224
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-230 |
2.12e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 126.03 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSaaLEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPdqVCAAG 80
Cdd:COG1118 1 MS--IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLP--PRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQ---LvkpFAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLG--AKReqpassltLPD------RKRLEVA 149
Cdd:COG1118 77 VGFVFQhyaL---FPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEglADR--------YPSqlsggqRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 150 RALATRPELLLLDEVMAGL----RPtecdQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEV 225
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALdakvRK----ELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
....*
gi 1082692222 226 VRDPA 230
Cdd:COG1118 222 YDRPA 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-226 |
6.89e-34 |
|
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: 122.46 E-value: 6.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 4 ALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAAGIGR 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL-ARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 84 TFQLVKPFAGLSVLDNVTVGalhRAP------NVSAA-KKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRP 156
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALG---RYPhlglfgRPSAEdREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 157 ELLLLDEVMAGLrptecD-----QMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVV 226
Cdd:COG1120 157 PLLLLDEPTSHL-----DlahqlEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-229 |
6.48e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 121.72 E-value: 6.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRG----LRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAA- 79
Cdd:COG1135 2 IELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 -GIGRTFQlvkPFAGLS---VLDNVtvgALhraP----NVSAA--KKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVA 149
Cdd:COG1135 82 rKIGMIFQ---HFNLLSsrtVAENV---AL---PleiaGVPKAeiRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 150 RALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANP 232
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-217 |
1.09e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 120.96 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 4 ALEVRGVSKSFR------GL---------------RAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIV 62
Cdd:COG4586 1 IIEVENLSKTYRvyekepGLkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 63 FRG-----RRIDGLRpdqvcaaGIG-----RTfQLvkpFAGLSVLDNVTV-GALHRAPNvSAAKKHAAEIVERLGLGAKR 131
Cdd:COG4586 81 VLGyvpfkRRKEFAR-------RIGvvfgqRS-QL---WWDLPAIDSFRLlKAIYRIPD-AEYKKRLDELVELLDLGELL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 132 EQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLrptecD----QMVEAF-REINRAEGLTIMLIEHVMRAVMALAQ 206
Cdd:COG4586 149 DTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGL-----DvvskEAIREFlKEYNRERGTTILLTSHDMDDIEALCD 223
|
250
....*....|.
gi 1082692222 207 RIVVLHHGEVI 217
Cdd:COG4586 224 RVIVIDHGRII 234
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-229 |
1.38e-32 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 118.75 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 4 ALEVRGVSKSF----RGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIdGLRPDQVCAA 79
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV-TRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 GIGRTFQlvKPFAGL----SVLDNV-TVGALHRAPNVSAAkkhAAEIVERLGLGAK-REQPASSLTLPDRKRLEVARALA 153
Cdd:COG1124 80 RVQMVFQ--DPYASLhprhTVDRILaEPLRIHGLPDREER---IAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 154 TRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-220 |
2.36e-32 |
|
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: 117.25 E-value: 2.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 6 EVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLR------PDQvcaA 79
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERkrigyvPQR---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 GIGRTFqlvkPfagLSVLDNVTVGALHRA---PNVSAAKKHAA-EIVERLGLGAKREQPASSLTLPDRKRLEVARALATR 155
Cdd:cd03235 78 SIDRDF----P---ISVRDVVLMGLYGHKglfRRLSKADKAKVdEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 156 PELLLLDEVMAGLRPTECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHgEVIARG 220
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLNR-TVVASG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-220 |
3.06e-32 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 117.22 E-value: 3.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRG----LRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQvcAAG 80
Cdd:cd03257 2 LEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRL--RKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQLV--KPFAGL----SVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASsltLPD------RKRLEV 148
Cdd:cd03257 80 RRKEIQMVfqDPMSSLnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNR---YPHelsggqRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082692222 149 ARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARG 220
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-220 |
7.06e-32 |
|
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: 116.66 E-value: 7.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFR------GL---------------RAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIvf 63
Cdd:cd03267 1 IEVSNLSKSYRvyskepGLigslkslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 64 rgrRIDGLRP---DQVCAAGIGRTF-QLVKPFAGLSVLDNVTVgaLHRAPNVSAA--KKHAAEIVERLGLGAKREQPASS 137
Cdd:cd03267 79 ---RVAGLVPwkrRKKFLRRIGVVFgQKTQLWWDLPVIDSFYL--LAAIYDLPPArfKKRLDELSELLDLEELLDTPVRQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 138 LTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVI 217
Cdd:cd03267 154 LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
...
gi 1082692222 218 ARG 220
Cdd:cd03267 234 YDG 236
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-217 |
1.14e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 116.72 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSF-RGL----RAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLrPDQVCAA 79
Cdd:COG1101 2 LELKNLSKTFnPGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 GIGRTFQlvKPFAG----LSVLDNVTVgALHR------APNVSAAKK-HAAEIVERLGLG-AKR-EQPASSLTLPDRKRL 146
Cdd:COG1101 81 YIGRVFQ--DPMMGtapsMTIEENLAL-AYRRgkrrglRRGLTKKRReLFRELLATLGLGlENRlDTKVGLLSGGQRQAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 147 EVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVI 217
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-215 |
2.88e-31 |
|
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: 113.44 E-value: 2.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPD-QVCAAGIGR 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 84 TFQLVKPFAGLSVLDNVTvgalhrapnvsaakkhaaeiverLGLGAKREQpassltlpdrkRLEVARALATRPELLLLDE 163
Cdd:cd03229 81 VFQDFALFPHLTVLENIA-----------------------LGLSGGQQQ-----------RVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1082692222 164 VMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGE 215
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-229 |
3.42e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 117.21 E-value: 3.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 6 EVRGVSKSF----RGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAA-- 79
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 GIGRTFQlvkPFAGLS---VLDNVtvgALH-RAPNVSAA--KKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALA 153
Cdd:PRK11153 83 QIGMIFQ---HFNLLSsrtVFDNV---ALPlELAGTPKAeiKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 154 TRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-163 |
4.32e-31 |
|
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: 111.97 E-value: 4.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 26 DVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAAGIGRTFQLVKPFAGLSVLDNVTVGAL 105
Cdd:pfam00005 7 TLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL-RKEIGYVFQDPQLFPRLTVRENLRLGLL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082692222 106 HRAPNVSAAKKHAAEIVERLGLGAKREQPA----SSLTLPDRKRLEVARALATRPELLLLDE 163
Cdd:pfam00005 86 LKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-220 |
4.60e-31 |
|
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: 114.00 E-value: 4.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLR----AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGrrIDGLRPDQVCAAG 80
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQLVKPFAGLSVLDNVT-VGALHrAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELL 159
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEyFAGLY-GLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 160 LLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARG 220
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-238 |
7.83e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 116.72 E-value: 7.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSaaLEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGL--RPDQVca 78
Cdd:PRK10851 1 MS--IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLhaRDRKV-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 79 agiGRTFQLVKPFAGLSVLDNV----TVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALAT 154
Cdd:PRK10851 77 ---GFVFQHYALFRHMTVFDNIafglTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 155 RPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPA---V 231
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPAtrfV 233
|
....*..
gi 1082692222 232 LGcYLGE 238
Cdd:PRK10851 234 LE-FMGE 239
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-227 |
3.17e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 112.48 E-value: 3.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFR-------GLR---------------AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADA 58
Cdd:COG1134 1 MSSMIEVENVSKSYRlyhepsrSLKelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 59 GEIVFRGRR---ID---GLRPDqvcaagigrtfqlvkpfagLSVLDNV-TVGALHRAPNvSAAKKHAAEIVERLGLGAKR 131
Cdd:COG1134 81 GRVEVNGRVsalLElgaGFHPE-------------------LTGRENIyLNGRLLGLSR-KEIDEKFDEIVEFAELGDFI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 132 EQPASSLTLPDRKRLEVARALATRPELLLLDEVMAglrptecdqmV--EAFRE-----IN--RAEGLTIMLIEHVMRAVM 202
Cdd:COG1134 141 DQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLA----------VgdAAFQKkclarIRelRESGRTVIFVSHSMGAVR 210
|
250 260
....*....|....*....|....*
gi 1082692222 203 ALAQRIVVLHHGEVIARGAPGEVVR 227
Cdd:COG1134 211 RLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-216 |
3.78e-30 |
|
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: 111.47 E-value: 3.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPD-QVCAAGIGR 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 84 TFQLVKPFAGLSVLDNVTVG---ALHRapNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLL 160
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLApikVKGM--SKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 161 LDEVMAGLRPTECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHGEV 216
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-230 |
9.53e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 113.63 E-value: 9.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 3 AALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQvcaAGIG 82
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---RNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 83 RTFQ---LvkpFAGLSVLDNVTVGaLhRAPNVSAA--KKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPE 157
Cdd:COG3839 79 MVFQsyaL---YPHMTVYENIAFP-L-KLRKVPKAeiDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082692222 158 LLLLDEVM----AGLRptecDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPA 230
Cdd:COG3839 154 VFLLDEPLsnldAKLR----VEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPA 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-229 |
1.59e-29 |
|
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: 110.50 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRaVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQvcaAGIGRT 84
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK---RDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEV 164
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 165 MAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-237 |
2.35e-29 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 109.97 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAG 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQLVKPFAGLSVLDNVTVGALHrapnvsAAKKHAAEIVERL-----GLGAKREQPASSLTLPDRKRLEVARALATR 155
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMGGFF------AERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 156 PELLLLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVLGCY 235
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
..
gi 1082692222 236 LG 237
Cdd:PRK11614 235 LG 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-224 |
9.44e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 108.22 E-value: 9.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFR-GLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAA--GI 81
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 82 GRTFQLVKPFAGLSVLDNVtvgAL----HRAPNvSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPE 157
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENV---ALplrvTGKSR-KEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082692222 158 LLLLDEVMAGLRPTECDQMVEAFREINRAeGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGE 224
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-220 |
1.70e-28 |
|
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: 107.28 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGaIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRriDGLRPDQVCAAGIGRT 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ--DVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNV-TVGALHRAPNvSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDE 163
Cdd:cd03264 78 PQEFGVYPNFTVREFLdYIAWLKGIPS-KEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1082692222 164 VMAGLRPTEcdqmVEAFREINR--AEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARG 220
Cdd:cd03264 157 PTAGLDPEE----RIRFRNLLSelGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-220 |
2.48e-28 |
|
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: 105.60 E-value: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 6 EVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcaagigrtf 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 86 qlvkpfaglsvldnvtvgALHRApnvsaakkHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVM 165
Cdd:cd03214 72 ------------------ARKIA--------YVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 166 AGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARG 220
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-221 |
2.52e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 108.18 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADA---------GEIVFR-GRRIDG 70
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQReGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 71 LRPDQVCAAGIGRTFQLVKPfagLSVLDNVTVGALHRAP--------NVSAAKKHAAEIVERLGLGAKREQPASSLTLPD 142
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNR---LSVLENVLIGALGSTPfwrtcfswFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082692222 143 RKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGA 221
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-215 |
9.93e-28 |
|
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: 103.48 E-value: 9.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 6 EVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAAGIGRTF 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL-RRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 86 QLVkpfAGLsvldnvtvgalhrapnvsaakkhaaeiverlglgakreqpassltlpdRKRLEVARALATRPELLLLDEVM 165
Cdd:cd00267 80 QLS---GGQ------------------------------------------------RQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1082692222 166 AGLRPTECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHGE 215
Cdd:cd00267 109 SGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-221 |
1.45e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 109.76 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAG 80
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQLVKPFAGLSVLDNVtvgaLHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLL 160
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENI----LFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082692222 161 LDEVMAGLRPTECDQMveaFREIN--RAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGA 221
Cdd:PRK15439 164 LDEPTASLTPAETERL---FSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
27-238 |
2.35e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.45 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 27 VPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQvcaagigR----TFQLVKPFAGLSVLDNVTV 102
Cdd:COG3840 22 IAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-------RpvsmLFQENNLFPHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 103 GaLHRAPNVSAA-KKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFR 181
Cdd:COG3840 95 G-LRPGLKLTAEqRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1082692222 182 EINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVV--RDPAVLGCYLGE 238
Cdd:COG3840 174 ELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLdgEPPPALAAYLGI 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-216 |
1.05e-26 |
|
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: 102.33 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQvcaAGIGRT 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVTVG-ALHRAPNVSAAKKhAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDE 163
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGlKLRKVPKDEIDER-VREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1082692222 164 VMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEV 216
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-239 |
1.10e-26 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 105.57 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 22 DAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGR-------RIDgLRPDQvcaAGIGRTFQLVKPFAGL 94
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsarGIF-LPPHR---RRIGYVFQEARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 95 SVLDNVTVGaLHRAPnVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECD 174
Cdd:COG4148 93 SVRGNLLYG-RKRAP-RAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 175 QMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVLGCYLGEE 239
Cdd:COG4148 171 EILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEE 235
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-230 |
1.92e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 105.30 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQvcaAGIGRT 84
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ---RPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVTVGalhrapnVSAAKKHAAEIVER----LGL-----GAKREqpASSLTLPDRKRLEVARALATR 155
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFG-------LKQDKLPKAEIASRvnemLGLvhmqeFAKRK--PHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 156 PELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPA 230
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPT 242
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-234 |
3.79e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 103.35 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAG 80
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQLVKPfaGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLL 160
Cdd:PRK13537 84 VVPQFDNLDP--DFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082692222 161 LDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRdpAVLGC 234
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE--SEIGC 232
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-232 |
5.16e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.08 E-value: 5.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSF-RGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQV-CAAGIG 82
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLeVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 83 RTFQ-----LVKPfaglSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPE 157
Cdd:PRK13639 82 IVFQnpddqLFAP----TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 158 LLLLDEVMAGLRPTECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVL 232
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-218 |
6.45e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 104.99 E-value: 6.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAG 80
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQLVKPFAGLSVLDNVTVGAL-HRAP--NVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPE 157
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGQLpHKGGivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082692222 158 LLLLDEVMAGLRPTECDQMveaFREIN--RAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIA 218
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQL---FRVIRelRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-220 |
8.04e-26 |
|
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: 100.06 E-value: 8.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 26 DVPQGaIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGR-------RIDgLRPDQvcaAGIGRTFQLVKPFAGLSVLD 98
Cdd:cd03297 20 DLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkKIN-LPPQQ---RKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 99 NVTVGALHRAPNVSaaKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVE 178
Cdd:cd03297 95 NLAFGLKRKRNRED--RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1082692222 179 AFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARG 220
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-234 |
8.66e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 102.99 E-value: 8.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 2 SAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIdglrPDQVCAA-- 79
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLAra 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 GIGRTFQLVKPFAGLSVLDNVTVgaLHRAPNVSAAKKHAA--EIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPE 157
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLV--FGRYFGMSTREIEAVipSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082692222 158 LLLLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPavLGC 234
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH--IGC 266
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-226 |
1.46e-25 |
|
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: 104.53 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 4 ALEVRGVSKSFRGLR--AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAAGI 81
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL-RRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 82 GRTFQLVKPFAGlSVLDNVTVGalhrAPNVS------AAKK-HAAEIVERLGLGAKREQPASSLTLPD--RKRLEVARAL 152
Cdd:COG2274 552 GVVLQDVFLFSG-TIRENITLG----DPDATdeeiieAARLaGLHDFIEALPMGYDTVVGEGGSNLSGgqRQRLAIARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 153 ATRPELLLLDEVMAGLRPTECDQMVEAFREINRaeGLTIMLIEHvmR-AVMALAQRIVVLHHGEVIARGAPGEVV 226
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAH--RlSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
16-232 |
1.49e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.08 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 16 GLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQV-CAAGIGRTFQlvKPFAGL 94
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMkLRESVGMVFQ--DPDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 95 ---SVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPT 171
Cdd:PRK13636 96 fsaSVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 172 ECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVL 232
Cdd:PRK13636 176 GVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEML 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-231 |
3.02e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 103.33 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGIGRT 84
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVTVGalhRAP-------NV---SAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALAT 154
Cdd:PRK09700 86 YQELSVIDELTVLENLYIG---RHLtkkvcgvNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082692222 155 RPELLLLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAV 231
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIV 238
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-218 |
3.25e-25 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 103.16 E-value: 3.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAG 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQLVKPFAGLSVLDNVTVGA--LHRAPNVSAAKKH--AAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRP 156
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGRefVNRFGRIDWKKMYaeADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082692222 157 ELLLLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIA 218
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIA 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-229 |
5.04e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 98.63 E-value: 5.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPD-QVCAAGIGR 83
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDeRLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 84 TFQLVKPFAGLSVLDNVTVGALH-RAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLD 162
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGPLRvRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082692222 163 EVMAGLRPTECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-216 |
1.35e-24 |
|
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: 97.09 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSF-RGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQV--CAAGI 81
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 82 GRTFQLVKPFAGLSVLDNVT-----VGALHRApnvsaAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRP 156
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAfalevTGVPPRE-----IRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 157 ELLLLDEVMAGLRPTECDQMVEAFREINRAeGLTIMLIEHVMRAVMALAQRIVVLHHGEV 216
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-229 |
2.69e-24 |
|
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: 100.53 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSF---RGL--------RAVHDAWIDVPQGAIVGLIGPNGAGKTT----IFNMVAGvyaadAGEIVFRGRRID 69
Cdd:COG4172 276 LEARDLKVWFpikRGLfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIPS-----EGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 70 GLRPDQVCAagIGRTFQLV--KPFAGLS----VLDNVTVG-ALHRaPNVSAA--KKHAAEIVERLGLgakreQPASSLTL 140
Cdd:COG4172 351 GLSRRALRP--LRRRMQVVfqDPFGSLSprmtVGQIIAEGlRVHG-PGLSAAerRARVAEALEEVGL-----DPAARHRY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 141 P------DRKRLEVARALATRPELLLLDEvmaglrPTEC-D-----QMVEAFREINRAEGLTIMLIEHVMRAVMALAQRI 208
Cdd:COG4172 423 PhefsggQRQRIAIARALILEPKLLVLDE------PTSAlDvsvqaQILDLLRDLQREHGLAYLFISHDLAVVRALAHRV 496
|
250 260
....*....|....*....|.
gi 1082692222 209 VVLHHGEVIARGAPGEVVRDP 229
Cdd:COG4172 497 MVMKDGKVVEQGPTEQVFDAP 517
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-220 |
8.94e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 94.87 E-value: 8.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 27 VPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPdqvCAAGIGRTFQLVKPFAGLSVLDNVtvgALH 106
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP---ADRPVSMLFQENNLFAHLTVEQNV---GLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 107 RAPNV---SAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREI 183
Cdd:cd03298 95 LSPGLkltAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1082692222 184 NRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARG 220
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-235 |
1.09e-23 |
|
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: 95.54 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 2 SAALEVRGVSKSFRGLRAVHDawID--VPQGAIVGLIGPNGAGKTTIFNMVAG-VYAADAGEIVFRGRRIDG-----LRP 73
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDD--ISwtVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGedvweLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 74 DqvcaagIGrtfqLVKPF------AGLSVLDNV------TVGaLHRAPNvSAAKKHAAEIVERLGLGAKREQPASSLTLP 141
Cdd:COG1119 79 R------IG----LVSPAlqlrfpRDETVLDVVlsgffdSIG-LYREPT-DEQRERARELLELLGLAHLADRPFGTLSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 142 DRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGA 221
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGP 226
|
250
....*....|....
gi 1082692222 222 PGEVVRDPAVLGCY 235
Cdd:COG1119 227 KEEVLTSENLSEAF 240
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-220 |
1.26e-23 |
|
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: 94.52 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFR----------------------GLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIV 62
Cdd:cd03220 1 IELENVSKSYPtykggssslkklgilgrkgevgEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 63 FRGrridglRPDQVCAAGIGrtFQlvkpfAGLSVLDNVT-VGALHRAPNVSAAKKhAAEIVERLGLGAKREQPASSLTLP 141
Cdd:cd03220 81 VRG------RVSSLLGLGGG--FN-----PELTGRENIYlNGRLLGLSRKEIDEK-IDEIIEFSELGDFIDLPVKTYSSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082692222 142 DRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARG 220
Cdd:cd03220 147 MKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-230 |
1.89e-23 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 98.30 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 2 SAALEVRGVSKSFRGLR--AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAA 79
Cdd:COG4987 331 GPSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL-RR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 GIGRTFQLVKPFAGlSVLDNVTVGAlhraPNVSAAKKHAAeiVERLGLGAKREQpassltLPD----------------- 142
Cdd:COG4987 410 RIAVVPQRPHLFDT-TLRENLRLAR----PDATDEELWAA--LERVGLGDWLAA------LPDgldtwlgeggrrlsgge 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 143 RKRLEVARALATRPELLLLDEVMAGL-RPTEcDQMVEAFREinRAEGLTIMLIEHVMRAvMALAQRIVVLHHGEVIARGA 221
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLdAATE-QALLADLLE--ALAGRTVLLITHRLAG-LERMDRILVLEDGRIVEQGT 552
|
....*....
gi 1082692222 222 PGEVVRDPA 230
Cdd:COG4987 553 HEELLAQNG 561
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-192 |
3.21e-23 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 92.93 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 3 AALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPD---QVCAA 79
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyrrRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 GigrtfQLVKPFAGLSVLDNVTvgALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELL 159
Cdd:COG4133 81 G-----HADGLKPELTVRENLR--FWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|...
gi 1082692222 160 LLDEVMAGLRPTECDQMVEAFREINRAEGLTIM 192
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
3.83e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.42 E-value: 3.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFR-GLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGlRPDQVCAA 79
Cdd:PRK13647 1 MDNIIEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA-ENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 GIGRTFQlvKP----FAGlSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATR 155
Cdd:PRK13647 80 KVGLVFQ--DPddqvFSS-TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082692222 156 PELLLLDEVMAGLRPTECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPgEVVRDPAVLG 233
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDIVE 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-224 |
1.25e-22 |
|
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: 95.98 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 2 SAALEVRGVSKSF-RGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCA-- 78
Cdd:COG4988 334 PPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRqi 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 79 AGIGRTFQLvkpFAGlSVLDNVTVG-------ALHRApnvsAAKKHAAEIVERL--GLGAKREQPASSLTLPDRKRLEVA 149
Cdd:COG4988 414 AWVPQNPYL---FAG-TIRENLRLGrpdasdeELEAA----LEAAGLDEFVAALpdGLDTPLGEGGRGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082692222 150 RALATRPELLLLDEVMAGLRP-TEcDQMVEAFREInrAEGLTIMLIEHvmR-AVMALAQRIVVLHHGEVIARGAPGE 224
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAeTE-AEILQALRRL--AKGRTVILITH--RlALLAQADRILVLDDGRIVEQGTHEE 557
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-232 |
1.49e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 94.63 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQvcaAGIGRT 84
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN---RHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVTVG-ALHRAPNvsaakkhaAEIVERLgLGAKR----EQPAssltlpDRK----------RLEVA 149
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGlRMQKTPA--------AEITPRV-MEALRmvqlEEFA------QRKphqlsggqqqRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 150 RALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
...
gi 1082692222 230 AVL 232
Cdd:PRK09452 237 KNL 239
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-229 |
1.49e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 92.91 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSfRGLRAV-HDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAA--GI 81
Cdd:PRK11831 8 VDMRGVSFT-RGNRCIfDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVrkRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 82 GRTFQLVKPFAGLSVLDNVTVgALHRAPNVSAAKKHAAEI--VERLGL-GAKREQPaSSLTLPDRKRLEVARALATRPEL 158
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAY-PLREHTQLPAPLLHSTVMmkLEAVGLrGAAKLMP-SELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 159 LLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-218 |
1.70e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 95.38 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADA--GEIVFRGR--RIDGLRPDQv 76
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEelQASNIRDTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 77 cAAGIGRTFQ---LVKpfaGLSVLDNVTVGA-LHRAPNVSAAKKH--AAEIVERLGLGAKREQPASSLTLPDRKRLEVAR 150
Cdd:PRK13549 81 -RAGIAIIHQelaLVK---ELSVLENIFLGNeITPGGIMDYDAMYlrAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082692222 151 ALATRPELLLLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIA 218
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHIG 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-215 |
2.41e-22 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 89.75 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSF--RGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAgIG 82
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 83 RTFQLVKPFAGlSVLDNVTVGalhrapnvsaakkhaaeiverlGlgakreQpassltlpdRKRLEVARALATRPELLLLD 162
Cdd:cd03228 80 YVPQDPFLFSG-TIRENILSG----------------------G------Q---------RQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1082692222 163 EVMAGLRP-TEcDQMVEAFREInrAEGLTIMLIEHVMrAVMALAQRIVVLHHGE 215
Cdd:cd03228 122 EATSALDPeTE-ALILEALRAL--AKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-229 |
4.52e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 91.13 E-value: 4.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 3 AALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTI---FNMVAGVY--AADAGEIVFRGRRIDGLrPDQVC 77
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLlrvFNRLIELYpeARVSGEVYLDGQDIFKM-DVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 78 AAGIGRTFQLVKPFAGLSVLDNVTVGalhraPNVSAAKKHAAEIVERLGLGAKREQ-----------PASSLTLPDRKRL 146
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALG-----LKLNRLVKSKKELQERVRWALEKAQlwdevkdrldaPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 147 EVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAegLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVV 226
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
...
gi 1082692222 227 RDP 229
Cdd:PRK14247 234 TNP 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-218 |
5.40e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.93 E-value: 5.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 4 ALEVRGVSKSfrglRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGIGr 83
Cdd:COG1129 256 VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIA- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 84 tfqLVkP--------FAGLSVLDNVTVGALHRAP-----NVSAAKKHAAEIVERLGLGAK-REQPASSL-------TLpd 142
Cdd:COG1129 331 ---YV-PedrkgeglVLDLSIRENITLASLDRLSrggllDRRRERALAEEYIKRLRIKTPsPEQPVGNLsggnqqkVV-- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 143 rkrleVARALATRPELLLLDEvmaglrPTE-CDqmVEAFREINR------AEGLTIMLIEHVMRAVMALAQRIVVLHHGE 215
Cdd:COG1129 405 -----LAKWLATDPKVLILDE------PTRgID--VGAKAEIYRlirelaAEGKAVIVISSELPELLGLSDRILVMREGR 471
|
...
gi 1082692222 216 VIA 218
Cdd:COG1129 472 IVG 474
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-232 |
5.77e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 91.62 E-value: 5.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 18 RAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDG------LRPDQvcaAGIGRTFQLvkPF 91
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknkkLKPLR---KKVGIVFQF--PE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 92 AGL---SVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAK-REQPASSLTLPDRKRLEVARALATRPELLLLDEVMAG 167
Cdd:PRK13634 96 HQLfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 168 LRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVL 232
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEL 240
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-171 |
1.57e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 7 VRGVSKSFrGLRAV-HDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGR-RI------DGLRPDQ--- 75
Cdd:COG0488 1 LENLSKSF-GGRPLlDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlRIgylpqePPLDDDLtvl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 76 -VCAAGIGRTFQLVKPFAGLSVLDNVTVGALHRAPNVSAAKKH---------AAEIVERLGLG-AKREQPASSLTLPDRK 144
Cdd:COG0488 80 dTVLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEAlggweaearAEEILSGLGFPeEDLDRPVSELSGGWRR 159
|
170 180
....*....|....*....|....*..
gi 1082692222 145 RLEVARALATRPELLLLDEvmaglrPT 171
Cdd:COG0488 160 RVALARALLSEPDLLLLDE------PT 180
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-229 |
2.66e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 89.33 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTT---IFN----MVAGVYAadAGEIVFRG-----RRI 68
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNrmndLIPGARV--EGEILLDGediydPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 69 D--GLRpdqvcaAGIGRTFQLVKPFAgLSVLDNVTVGA-LHRAPNvsaaKKHAAEIVERLGLGA--------KREQPASS 137
Cdd:COG1117 86 DvvELR------RRVGMVFQKPNPFP-KSIYDNVAYGLrLHGIKS----KSELDEIVEESLRKAalwdevkdRLKKSALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 138 LTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREInrAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVI 217
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
250
....*....|..
gi 1082692222 218 ARGAPGEVVRDP 229
Cdd:COG1117 233 EFGPTEQIFTNP 244
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-214 |
5.32e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 87.91 E-value: 5.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 25 IDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCaagigrTFQLVKPFAGLSVLDNV--TV 102
Cdd:TIGR01184 6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV------VFQNYSLLPWLTVRENIalAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 103 GALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFRE 182
Cdd:TIGR01184 80 DRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170 180 190
....*....|....*....|....*....|..
gi 1082692222 183 INRAEGLTIMLIEHVMRAVMALAQRIVVLHHG 214
Cdd:TIGR01184 160 IWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-232 |
6.35e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.51 E-value: 6.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 2 SAALEVRGVSKSFRGLR--AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAA 79
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI-RK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 GIGRTFQlvKP---FAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRP 156
Cdd:PRK13632 84 KIGIIFQ--NPdnqFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 157 ELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMaLAQRIVVLHHGEVIARGAPGEVVRDPAVL 232
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEIL 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-225 |
9.05e-21 |
|
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: 87.28 E-value: 9.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 6 EVRGVSKSFRGLR-AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLrPDQVCAAGIGRT 84
Cdd:cd03254 4 EFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGlSVLDNVTVGALhRAP----NVSAAKKHAAEIVERL--GLGAKREQPASSLTLPDRKRLEVARALATRPEL 158
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGRP-NATdeevIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082692222 159 LLLDEVMAGLRPtECDQMV-EAFREINraEGLTIMLIEHVMRAVMAlAQRIVVLHHGEVIARGAPGEV 225
Cdd:cd03254 161 LILDEATSNIDT-ETEKLIqEALEKLM--KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-232 |
1.15e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 89.01 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVfrgrrIDGlrpDQVCAAGIGR- 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIF-----IDG---EDVTHRSIQQr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 84 ----TFQLVKPFAGLSVLDNVTVGAlhRAPNVSAA--KKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPE 157
Cdd:PRK11432 79 dicmVFQSYALFPHMSLGENVGYGL--KMLGVPKEerKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 158 LLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVL 232
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASR 231
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-235 |
1.90e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 86.71 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcaAGIgRT 84
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWEL--ARR-RA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 F-----QLVKPFaglSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALA------ 153
Cdd:COG4559 79 VlpqhsSLAFPF---TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 154 -TRPELLLLDEVMAGLRPTECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVL 232
Cdd:COG4559 156 dGGPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLE 234
|
...
gi 1082692222 233 GCY 235
Cdd:COG4559 235 RVY 237
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-217 |
2.09e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 89.46 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAAD--AGEIVFRG--RRIDGLRPDQvcAAG 80
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGevCRFKDIRDSE--ALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQ---LVkPFagLSVLDNVTVG---ALHRAPNVSAAKKHAAEIVERLGLgakREQPA---SSLTLPDRKRLEVARA 151
Cdd:NF040905 80 IVIIHQelaLI-PY--LSIAENIFLGnerAKRGVIDWNETNRRARELLAKVGL---DESPDtlvTDIGVGKQQLVEIAKA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 152 LATRPELLLLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVI 217
Cdd:NF040905 154 LSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-230 |
2.75e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 88.16 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 3 AALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQvcaAGIG 82
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE---RGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 83 RTFQLVKPFAGLSVLDNVTVG-ALHRAPNVSAAKK--HAAEIverLGLGAKREQPASSLTLPDRKRLEVARALATRPELL 159
Cdd:PRK11000 79 MVFQSYALYPHLSVAENMSFGlKLAGAKKEEINQRvnQVAEV---LQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 160 LLDEVM----AGLRPtecdQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPA 230
Cdd:PRK11000 156 LLDEPLsnldAALRV----QMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-229 |
3.24e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 86.25 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 20 VHDAWIDVPQGAIVGLIGPNGAGKTT---IFNMVAGVYAADA---GEIVFRGR---RIDGLRPDQvcaaGIGRTFQLVKP 90
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTllkVLNRLIEIYDSKIkvdGKVLYFGKdifQIDAIKLRK----EVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 91 FAGLSVLDNVTVG-ALHRAPNVSAAKKHAAEIVERLGLGA----KREQPASSLTLPDRKRLEVARALATRPELLLLDEVM 165
Cdd:PRK14246 102 FPHLSIYDNIAYPlKSHGIKEKREIKKIVEECLRKVGLWKevydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082692222 166 AGLRPTECDQMVEAFREINRAegLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-217 |
4.28e-20 |
|
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: 85.00 E-value: 4.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 6 EVRGVSKSF-RGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDglRPDQVCAAGI--- 81
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK--AKERRKSIGYvmq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 82 GRTFQLVkpfaGLSVLDNVTVGalhrAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLL 161
Cdd:cd03226 79 DVDYQLF----TDSVREELLLG----LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 162 DEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVI 217
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-225 |
4.87e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.21 E-value: 4.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 25 IDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRID-GLRPDQVCAAGIGRTFQLVKPFAGLSVLDNVTVG 103
Cdd:PRK13638 22 LDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDySKRGLLALRQQVATVFQDPEQQIFYTDIDSDIAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 104 ALHrapNVSAAKkhaAEIVERLG-----LGAK--REQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQM 176
Cdd:PRK13638 102 SLR---NLGVPE---AEITRRVDealtlVDAQhfRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1082692222 177 VEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEV 225
Cdd:PRK13638 176 IAIIRRI-VAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-229 |
5.44e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 85.57 E-value: 5.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 3 AALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGI- 81
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 82 ------GRTFQLVKPFAGLSVLDNVTVGAL--HRAPNVSAAKKhAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALA 153
Cdd:PRK11264 82 qlrqhvGFVFQNFNLFPHRTVLENIIEGPVivKGEPKEEATAR-ARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 154 TRPELLLLDEVMAGLRPTECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-228 |
8.97e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.56 E-value: 8.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 18 RAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEI------VFRGRRIDGLRPDQvcaAGIGRTFQLvkPF 91
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivVSSTSKQKEIKPVR---KKVGVVFQF--PE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 92 AGL---SVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAK-REQPASSLTLPDRKRLEVARALATRPELLLLDEVMAG 167
Cdd:PRK13643 95 SQLfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 168 LRPTECDQMVEAFREINRAeGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRD 228
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-226 |
9.54e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.14 E-value: 9.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 4 ALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGlrPdqvcAAGIGR 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG--P----GAERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 84 TFQLVKPFAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDE 163
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082692222 164 VMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGeviargaPGEVV 226
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG-------PGRVV 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-234 |
1.20e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.82 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 3 AALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCA--AG 80
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARrrAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQLVKPFaglSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALA------T 154
Cdd:PRK13548 81 LPQHSSLSFPF---TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 155 RPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP---AV 231
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPEtlrRV 237
|
...
gi 1082692222 232 LGC 234
Cdd:PRK13548 238 YGA 240
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-232 |
1.25e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.24 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLR-AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAAGIGR 83
Cdd:PRK13652 4 IETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV-RKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 84 TFQ-----LVKPfaglSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPEL 158
Cdd:PRK13652 83 VFQnpddqIFSP----TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082692222 159 LLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVL 232
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLL 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-227 |
1.37e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 87.14 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 4 ALEVRGVSKSFRGLRAV-HDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAAGIG 82
Cdd:COG1132 339 EIEFENVSFSYPGDRPVlKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL-RRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 83 RTFQLVKPFAGlSVLDNVTVGAlhraPNVS------AAKK-HAAEIVERL--GLGAKREQPASSLTLPDRKRLEVARALA 153
Cdd:COG1132 418 VVPQDTFLFSG-TIRENIRYGR----PDATdeeveeAAKAaQAHEFIEALpdGYDTVVGERGVNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 154 TRPELLLLDEVMAGLrPTECDQMV-EAFREInrAEGLTIMLIEHVMRAVMAlAQRIVVLHHGEVIARGAPGEVVR 227
Cdd:COG1132 493 KDPPILILDEATSAL-DTETEALIqEALERL--MKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELLA 563
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-232 |
1.61e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 84.36 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 6 EVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIvfrgrRIDGLRPDQVCAAGIGRTf 85
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEV-----LVDGLDVATTPSRELAKR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 86 qlvkpfagLSVL--DN-----VTVG---ALHRAP----NVSAA-KKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVAR 150
Cdd:COG4604 77 --------LAILrqENhinsrLTVRelvAFGRFPyskgRLTAEdREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 151 ALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRdPA 230
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIIT-PE 227
|
..
gi 1082692222 231 VL 232
Cdd:COG4604 228 VL 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-226 |
1.66e-19 |
|
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: 86.78 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGV--YAADAGEIVFR----------GRRIDGLR 72
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyvERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 73 PDQVC--------------------------AAGIGRTFQLvkpFAGLSVLDNVtVGALHRAP-NVSAAKKHAAEIVERL 125
Cdd:TIGR03269 81 PCPVCggtlepeevdfwnlsdklrrrirkriAIMLQRTFAL---YGDDTVLDNV-LEALEEIGyEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 126 GLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALA 205
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|.
gi 1082692222 206 QRIVVLHHGEVIARGAPGEVV 226
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVV 257
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-199 |
1.97e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.45 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTI---FN----MVAGVYAadAGEIVFRGRRIDGLRPDQV- 76
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTIlrcFNrlndLIPGFRV--EGKVTFHGKNLYAPDVDPVe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 77 CAAGIGRTFQLVKPFAGlSVLDNVTVGalhraPNVSAAKKHAAEIVER-LGLGA-------KREQPASSLTLPDRKRLEV 148
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPK-SIYDNIAYG-----ARINGYKGDMDELVERsLRQAAlwdevkdKLKQSGLSLSGGQQQRLCI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 149 ARALATRPELLLLDEVMAGLRPTECDQMVEAFREInrAEGLTIMLIEHVMR 199
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQ 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-218 |
2.72e-19 |
|
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: 86.03 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADA--GEIVFRGRRIDGLRPDQVCAAGIG 82
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 83 RTFQLVKPFAGLSVLDNVTVGALHRAP----NVSAAKKHAAEIVERLGLGAKRE-QPASSLTLPDRKRLEVARALATRPE 157
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLPggrmAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 158 LLLLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIA 218
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVA 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-220 |
3.10e-19 |
|
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: 83.05 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 19 AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAAGIGRTFQLVKPFAGlSVLD 98
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL-RRQIGLVSQDVFLFND-TVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 99 NVTVGALH--RAPNVSAAKK-HAAEIVERL--GLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLrPTEC 173
Cdd:cd03251 95 NIAYGRPGatREEVEEAARAaNAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSAL-DTES 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1082692222 174 DQMV-EAFREInrAEGLTIMLIEHVMRAVMAlAQRIVVLHHGEVIARG 220
Cdd:cd03251 174 ERLVqAALERL--MKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-227 |
4.88e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 83.53 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 19 AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIvfrgrRIDG--LRPDQV--CAAGIGRTFQlvKP---F 91
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI-----TVGGmvLSEETVwdVRRQVGMVFQ--NPdnqF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 92 AGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPT 171
Cdd:PRK13635 95 VGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 172 ECDQMVEAFREINRAEGLTIMLIEHVMRAVmALAQRIVVLHHGEVIARGAPGEVVR 227
Cdd:PRK13635 175 GRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-229 |
1.46e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 81.90 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRriDGLRPDQVCAAG 80
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR--DGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFqlvkpfaglsvLDNVTVGALHRAP------NVSAakkhAAEIVERL-GLGAK-----REQPASSLT--------- 139
Cdd:PRK11701 81 AERRR-----------LLRTEWGFVHQHPrdglrmQVSA----GGNIGERLmAVGARhygdiRATAGDWLErveidaari 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 140 --LPD------RKRLEVARALATRPELLLLDEVMAGLrptecDQMVEA-----FREINRAEGLTIMLIEHVMRAVMALAQ 206
Cdd:PRK11701 146 ddLPTtfsggmQQRLQIARNLVTHPRLVFMDEPTGGL-----DVSVQArlldlLRGLVRELGLAVVIVTHDLAVARLLAH 220
|
250 260
....*....|....*....|...
gi 1082692222 207 RIVVLHHGEVIARGAPGEVVRDP 229
Cdd:PRK11701 221 RLLVMKQGRVVESGLTDQVLDDP 243
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-211 |
2.07e-18 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 83.49 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 2 SAALEVRGVSKSFRGLR-AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAAG 80
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQLVKPFAGlSVLDNVtvgaLHRAPNVSAA-------KKHAAEIVERLGLGAKRE--QPASSLTLPDRKRLEVARA 151
Cdd:TIGR02857 398 IAWVPQHPFLFAG-TIAENI----RLARPDASDAeirealeRAGLDEFVAALPQGLDTPigEGGAGLSGGQAQRLALARA 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 152 LATRPELLLLDEVMAGLRPTECDQMVEAFREInrAEGLTIMLIEHvMRAVMALAQRIVVL 211
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTH-RLALAALADRIVVL 529
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-232 |
2.11e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.02 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 18 RAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVfrgrrIDGLRP--DQVCAAGI----GRTFQLvkPF 91
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKII-----IDGVDItdKKVKLSDIrkkvGLVFQY--PE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 92 AGL---SVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLP--DRKRLEVARALATRPELLLLDEVMA 166
Cdd:PRK13637 94 YQLfeeTIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFELSggQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 167 GLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVL 232
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETL 239
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-218 |
2.34e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 83.24 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 8 RGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGIGRTFQL 87
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 88 VKPFAGLSVLDNVTVGalhRAPN----VSAAK--KHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLL 161
Cdd:PRK10982 82 LNLVLQRSVMDNMWLG---RYPTkgmfVDQDKmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1082692222 162 DEVMAGLRPTECDQMveaFREIN--RAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIA 218
Cdd:PRK10982 159 DEPTSSLTEKEVNHL---FTIIRklKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-217 |
3.48e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVfRGRRI---------DGLRPDQ 75
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGETVkigyfdqhqEELDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 76 vcaagigrtfqlvkpfaglSVLDNVTvgalHRAPNVSaaKKHAAEIVERLGL-GAKREQPASSLTLPDRKRLEVARALAT 154
Cdd:COG0488 395 -------------------TVLDELR----DGAPGGT--EQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082692222 155 RPELLLLDEvmaglrPT-----EcdqMVEAFRE-INRAEGlTIMLIEHVMRAVMALAQRIVVLHHGEVI 217
Cdd:COG0488 450 PPNVLLLDE------PTnhldiE---TLEALEEaLDDFPG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
29-229 |
3.74e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 81.41 E-value: 3.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 29 QGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRID---GLRPDQVCAAGIGRTFQLvkPFAGL---SVLDNVTV 102
Cdd:PRK13641 32 EGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetGNKNLKKLRKKVSLVFQF--PEAQLfenTVLKDVEF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 103 GALHRAPNVSAAKKHAAEIVERLGLgakREQPAS----SLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVE 178
Cdd:PRK13641 110 GPKNFGFSEDEAKEKALKWLKKVGL---SEDLISkspfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 179 AFREINRAeGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:PRK13641 187 LFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-237 |
4.22e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.77 E-value: 4.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 4 ALEVRGVS-KSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGIG 82
Cdd:COG3845 257 VLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 83 R------TFQLVkpfAGLSVLDNVTVGALHRAP-------NVSAAKKHAAEIVERLGL-GAKREQPASSLTLPDRKRLEV 148
Cdd:COG3845 337 YipedrlGRGLV---PDMSVAENLILGRYRRPPfsrggflDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVIL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 149 ARALATRPELLLLDEVMAGLrptecD---------QMVEAfreinRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIAR 219
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGL-----DvgaiefihqRLLEL-----RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGE 483
|
250
....*....|....*...
gi 1082692222 220 GAPGEVvrDPAVLGCYLG 237
Cdd:COG3845 484 VPAAEA--TREEIGLLMA 499
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
27-196 |
4.50e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 79.82 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 27 VPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQ---VCAAGIGRTFQLVKPFAGLSVLDNVTVG 103
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKHVGFVFQSFMLIPTLNALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 104 ALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREI 183
Cdd:PRK10584 113 ALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSL 192
|
170
....*....|...
gi 1082692222 184 NRAEGLTIMLIEH 196
Cdd:PRK10584 193 NREHGTTLILVTH 205
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-232 |
5.14e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 80.61 E-value: 5.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 4 ALEVRGVSKSFRGLR--AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEivfRGR-RIDGLRPDQVCAAG 80
Cdd:PRK13640 5 IVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNP---NSKiTVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 I----GRTFQlvKP---FAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALA 153
Cdd:PRK13640 82 IrekvGIVFQ--NPdnqFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 154 TRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEH-VMRAVMalAQRIVVLHHGEVIARGAPGEVVRDPAVL 232
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHdIDEANM--ADQVLVLDDGKLLAQGSPVEIFSKVEML 237
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-216 |
5.32e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 82.36 E-value: 5.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSfrglrAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGIGRT 84
Cdd:PRK10762 258 LKVDNLSGP-----GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQ------LVkpfAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVE-----RLgLGAK---REQPASSLTLPDRKRLEVAR 150
Cdd:PRK10762 333 SEdrkrdgLV---LGMSVKENMSLTALRYFSRAGGSLKHADEQQAvsdfiRL-FNIKtpsMEQAIGLLSGGNQQKVAIAR 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082692222 151 ALATRPELLLLDEvmaglrPTE-CDqmVEAFRE----INR--AEGLTIMLIEHVMRAVMALAQRIVVLHHGEV 216
Cdd:PRK10762 409 GLMTRPKVLILDE------PTRgVD--VGAKKEiyqlINQfkAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
27-225 |
7.08e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 80.16 E-value: 7.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 27 VPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGrriDGLRPDQV--CAAGIGRTFQlvKP---FAGLSVLDNVT 101
Cdd:PRK13650 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVwdIRHKIGMVFQ--NPdnqFVGATVEDDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 102 VGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFR 181
Cdd:PRK13650 105 FGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1082692222 182 EINRAEGLTIMLIEHVMRAVmALAQRIVVLHHGEVIARGAPGEV 225
Cdd:PRK13650 185 GIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-230 |
1.46e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.85 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 19 AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRG---RRIDGLRPDQVCAAGIGRTFQLVKPFAGLS 95
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 96 VLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQ 175
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 176 MVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPA 230
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-232 |
2.92e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.97 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRG-----LRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVF---------RGRRIDG 70
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 71 LRPDQVCAAGIGRTFQLVKP----------FAGL-----SVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPA 135
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKEirrrvgvvfqFAEYqlfeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 136 S-SLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHG 214
Cdd:PRK13651 163 PfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
250
....*....|....*...
gi 1082692222 215 EVIARGAPGEVVRDPAVL 232
Cdd:PRK13651 242 KIIKDGDTYDILSDNKFL 259
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-238 |
3.20e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.89 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRpdqvcAAGIGRT 84
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS-----ARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSV-LDNVTVGALHRAPNVS-------AAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRP 156
Cdd:PRK09536 79 VASVPQDTSLSFeFDVRQVVEMGRTPHRSrfdtwteTDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 157 ELLLLDEVMAGLRPTECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVLGCYL 236
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVD-DGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFD 237
|
..
gi 1082692222 237 GE 238
Cdd:PRK09536 238 AR 239
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-225 |
3.60e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.13 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 18 RAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQvcaagIGRTF-----QLVKPfA 92
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-----LARRLallpqHHLTP-E 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 93 GLSVLDNVTVGalhRAPNVS-------AAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEvm 165
Cdd:PRK11231 90 GITVRELVAYG---RSPWLSlwgrlsaEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE-- 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 166 aglrPT---ECDQMVE---AFREINrAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEV 225
Cdd:PRK11231 165 ----PTtylDINHQVElmrLMRELN-TQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-217 |
3.69e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 78.19 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRG---------LRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQ 75
Cdd:PRK10419 4 LNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 76 vcAAGIGRTFQLVKPFAGLSVLDNVTVGALHRAP-----NVSAAKKHA--AEIVERLGLGA----KREQPASSLTLpdrK 144
Cdd:PRK10419 84 --RKAFRRDIQMVFQDSISAVNPRKTVREIIREPlrhllSLDKAERLAraSEMLRAVDLDDsvldKRPPQLSGGQL---Q 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082692222 145 RLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVI 217
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-220 |
6.34e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.98 E-value: 6.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 4 ALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRID---GLRPDQVCA-- 78
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKAIRElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 79 AGIGRTFQLVKPFAGLSVLDNvtvgaLHRAP------NVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARAL 152
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQN-----LIEAPcrvlglSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082692222 153 ATRPELLLLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARG 220
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-220 |
8.72e-17 |
|
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: 76.09 E-value: 8.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 4 ALEVRGVSKSFRGLR--AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPdQVCAAGI 81
Cdd:cd03245 2 RIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP-ADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 82 GRTFQLVKPFAGlSVLDNVTVGALHrapnvsAAKKHAAEIVERLGLGA-KREQPAS----------SLTLPDRKRLEVAR 150
Cdd:cd03245 81 GYVPQDVTLFYG-TLRDNITLGAPL------ADDERILRAAELAGVTDfVNKHPNGldlqigergrGLSGGQRQAVALAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 151 ALATRPELLLLDEVMAGLRPTECDQMVEAFREInrAEGLTIMLIEHVMrAVMALAQRIVVLHHGEVIARG 220
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-216 |
9.39e-17 |
|
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: 75.16 E-value: 9.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 3 AALEVRGVSksfrGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGIG 82
Cdd:cd03215 3 PVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 83 -----RTFQLVkpFAGLSVLDNVTVGALhrapnvsaakkhaaeiverlgLGAKREQpassltlpdrkRLEVARALATRPE 157
Cdd:cd03215 79 yvpedRKREGL--VLDLSVAENIALSSL---------------------LSGGNQQ-----------KVVLARWLARDPR 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 158 LLLLDEVMAGLrptecDqmVEAFREIN------RAEGLTIMLIEHVMRAVMALAQRIVVLHHGEV 216
Cdd:cd03215 125 VLILDEPTRGV-----D--VGAKAEIYrlirelADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-230 |
1.04e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 78.57 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRG----LRAVHDAWIDVPQGAIVGLIGPNGAGKT----TIFNMVAGVYAADAGEIVFRGRRIDGLRPDQV 76
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 77 CA---AGIGRTFQlvKPfagLSVLDNV-TVG-------ALHRAPNVSAAKKHAAEIVERLGLgakrEQPASSLT-LP--- 141
Cdd:COG4172 87 RRirgNRIAMIFQ--EP---MTSLNPLhTIGkqiaevlRLHRGLSGAAARARALELLERVGI----PDPERRLDaYPhql 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 142 ---DRKRLEVARALATRPELLLLDEvmaglrPTEC-D-----QMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLH 212
Cdd:COG4172 158 sggQRQRVMIAMALANEPDLLIADE------PTTAlDvtvqaQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMR 231
|
250
....*....|....*...
gi 1082692222 213 HGEVIARGAPGEVVRDPA 230
Cdd:COG4172 232 QGEIVEQGPTAELFAAPQ 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-229 |
1.45e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.36 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 15 RGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGIGRTFQLVKPFAGL 94
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 95 SvlDNVTVG-------ALHRAPNVSAAKKHAAEIVERLGLgakreQPASSLTLP------DRKRLEVARALATRPELLLL 161
Cdd:PRK10261 415 D--PRQTVGdsimeplRVHGLLPGKAAAARVAWLLERVGL-----LPEHAWRYPhefsggQRQRICIARALALNPKVIIA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082692222 162 DEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-232 |
1.99e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.59 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 17 LRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVF----------RGRRIDGLRPDqvcaagIGRTFQ 86
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipanlkKIKEVKRLRKE------IGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 87 LvkPFAGL---SVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLG---AKREqpASSLTLPDRKRLEVARALATRPELLL 160
Cdd:PRK13645 98 F--PEYQLfqeTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPedyVKRS--PFELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082692222 161 LDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVL 232
Cdd:PRK13645 174 LDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELL 245
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-226 |
2.61e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.79 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 21 HDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAAGIGRTFQLVKPFAGLSVLDNV 100
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV-ARRIGLLAQNATTPGDITVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 101 TVGALHRAPNVSAAKKHAAEIVER----LGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQM 176
Cdd:PRK10253 103 ARGRYPHQPLFTRWRKEDEEAVTKamqaTGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1082692222 177 VEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVV 226
Cdd:PRK10253 183 LELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-220 |
2.63e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.45 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAV-HDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRpDQVCAA 79
Cdd:PRK10790 337 QSGRIDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 GIGRTFQLVKPFAGlSVLDNVTVG----------ALHRAPNVSAAKKHAAEIVERLGlgakrEQpASSLTLPDRKRLEVA 149
Cdd:PRK10790 416 GVAMVQQDPVVLAD-TFLANVTLGrdiseeqvwqALETVQLAELARSLPDGLYTPLG-----EQ-GNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082692222 150 RALATRPELLLLDEVMAGLRP-TEcdQMVE-AFREINraEGLTIMLIEHVMRAVMAlAQRIVVLHHGEVIARG 220
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSgTE--QAIQqALAAVR--EHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQG 556
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-228 |
2.86e-16 |
|
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: 74.49 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGV--YAADAGEIVFRGRRIDGLRPDQVCAAGIG 82
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 83 RTFQLVKPFAGLSVLD---NVTVGalhrapnvsaakkhaaeiverlglgakreqpassLTLPDRKRLEVARALATRPELL 159
Cdd:cd03217 81 LAFQYPPEIPGVKNADflrYVNEG----------------------------------FSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082692222 160 LLDEVMAGLrptECDQMVEAFREIN--RAEGLTIMLIEHVMR-AVMALAQRIVVLHHGEVIARGaPGEVVRD 228
Cdd:cd03217 127 ILDEPDSGL---DIDALRLVAEVINklREEGKSVLIITHYQRlLDYIKPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-228 |
3.27e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.56 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 27 VPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDG-----LRPDqvcaagIGRTFQlvKP---FAGLSVLD 98
Cdd:PRK13648 32 IPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdnfekLRKH------IGIVFQ--NPdnqFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 99 NVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVE 178
Cdd:PRK13648 104 DVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1082692222 179 AFREINRAEGLTIMLIEHVMRAVMAlAQRIVVLHHGEVIARGAPGEVVRD 228
Cdd:PRK13648 184 LVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-225 |
3.60e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 76.31 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 4 ALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTiFNMVAGVYAADAGeivfrgRRidGLRPDQVCA--AGI 81
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAG------RR--PWRF*TWCAnrRAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 82 GRTFQLVKPF-----AGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRP 156
Cdd:NF000106 84 RRTIG*HRPVr*grrESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082692222 157 ELLLLDEVMAGLRPTECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEV 225
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-229 |
4.18e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.88 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTI---FNMVAGV--YAADAGEIVFRGRRIDGLRPDQ 75
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLlrtFNRLLELneEARVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 76 V-CAAGIGRTFQLVKPFAGLSVLDNVTVGAlhRAPNVSAAKKHAAEIVE-RLGLGAKREQP-------ASSLTLPDRKRL 146
Cdd:PRK14267 81 IeVRREVGMVFQYPNPFPHLTIYDNVAIGV--KLNGLVKSKKELDERVEwALKKAALWDEVkdrlndyPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 147 EVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINraEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVV 226
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELK--KEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
...
gi 1082692222 227 RDP 229
Cdd:PRK14267 237 ENP 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
27-225 |
6.66e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 74.74 E-value: 6.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 27 VPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRidgLRPDQV--CAAGIGRTFQlvKP---FAGLSVLDNVT 101
Cdd:PRK13642 30 ITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL---LTAENVwnLRRKIGMVFQ--NPdnqFVGATVEDDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 102 VGALHRA-PNVSAAKKHAAEIVERLGLGAKREQPASsLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAF 180
Cdd:PRK13642 105 FGMENQGiPREEMIKRVDEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVI 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1082692222 181 REINRAEGLTIMLIEHVMRAVmALAQRIVVLHHGEVIARGAPGEV 225
Cdd:PRK13642 184 HEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSEL 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-233 |
7.92e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 73.85 E-value: 7.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 26 DVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQvcaAGIGRTFQLVKPFAGLSVLDNVTVGaL 105
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR---RPVSMLFQENNLFSHLTVAQNIGLG-L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 106 HRAPNVSAAKKHA-AEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREIN 184
Cdd:PRK10771 97 NPGLKLNAAQREKlHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVC 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1082692222 185 RAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEV----VRDPAVLG 233
Cdd:PRK10771 177 QERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELlsgkASASALLG 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-227 |
8.77e-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: 74.06 E-value: 8.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 19 AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAAGIGRTFQLVKPFAGlSVLD 98
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL-RRQVGVVLQENVLFNR-SIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 99 NVTVG--ALHRAPNVSAAKKHAAE--IVE-RLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTEC 173
Cdd:cd03252 95 NIALAdpGMSMERVIEAAKLAGAHdfISElPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1082692222 174 DQMVEAFREInrAEGLTIMLIEHVMRAVMAlAQRIVVLHHGEVIARGAPGEVVR 227
Cdd:cd03252 175 HAIMRNMHDI--CAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-218 |
1.22e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.53 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRG----LRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQV 76
Cdd:PRK10535 1 MTALLELKDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 77 CA---AGIGRTFQLVKPFAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALA 153
Cdd:PRK10535 81 AQlrrEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 154 TRPELLLLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHvMRAVMALAQRIVVLHHGEVIA 218
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTH-DPQVAAQAERVIEIRDGEIVR 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-231 |
1.49e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 73.87 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 16 GLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGrrIDGLRPDQVCAAG--IGRTFQlvKP--- 90
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIRklVGIVFQ--NPetq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 91 FAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRP 170
Cdd:PRK13644 90 FVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 171 TECDQMVEAFREINRaEGLTIMLIEHVMRAVMAlAQRIVVLHHGEVIARGAPGEVVRDPAV 231
Cdd:PRK13644 170 DSGIAVLERIKKLHE-KGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSL 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-229 |
1.63e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.98 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 2 SAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIF-------NMVAGVYAAdaGEIVFRGRRIDGLRPD 74
Cdd:PRK14271 19 APAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmnDKVSGYRYS--GDVLLGGRSIFNYRDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 75 QVCAAGIGRTFQLVKPFAgLSVLDNVTVGAlhRAPNVSAAKKHAAEIVERL---GL-GAKREQPASS---LTLPDRKRLE 147
Cdd:PRK14271 97 LEFRRRVGMLFQRPNPFP-MSIMDNVLAGV--RAHKLVPRKEFRGVAQARLtevGLwDAVKDRLSDSpfrLSGGQQQLLC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 148 VARALATRPELLLLDEVMAGLRPTECDQMVEAFREInrAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVR 227
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
..
gi 1082692222 228 DP 229
Cdd:PRK14271 252 SP 253
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-230 |
2.25e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 72.89 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGV-----YAADAGEIVFRGRRIDGLRPDQ 75
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 76 V-CAAGIGRTFQLVKPFAgLSVLDNVTVGAlhRAPNVSAaKKHAAEIVERLGLGA------KREQPASSLTLP--DRKRL 146
Cdd:PRK14239 82 VdLRKEIGMVFQQPNPFP-MSIYENVVYGL--RLKGIKD-KQVLDEAVEKSLKGAsiwdevKDRLHDSALGLSggQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 147 EVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINraEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVV 226
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK--DDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
....
gi 1082692222 227 RDPA 230
Cdd:PRK14239 236 MNPK 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-228 |
2.75e-15 |
|
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: 74.45 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSF----RGL-RAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFR--GRRID--GLRPDQ 75
Cdd:TIGR03269 280 IKVRNVSKRYisvdRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgDEWVDmtKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 76 VCAAG--IGRTFQLVKPFAGLSVLDNVT-------------VGALHRAPNVSAAKKHAAEIVERLglgakreqpASSLTL 140
Cdd:TIGR03269 360 RGRAKryIGILHQEYDLYPHRTVLDNLTeaiglelpdelarMKAVITLKMVGFDEEKAEEILDKY---------PDELSE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 141 PDRKRLEVARALATRPELLLLDEVMAGLRP----TECDQMVEAFREINRaeglTIMLIEHVMRAVMALAQRIVVLHHGEV 216
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPitkvDVTHSILKAREEMEQ----TFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
250
....*....|..
gi 1082692222 217 IARGAPGEVVRD 228
Cdd:TIGR03269 507 VKIGDPEEIVEE 518
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-225 |
3.26e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.81 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 19 AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRG------------RRIDGL---RPDQVCAAGIgr 83
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenlwdiRNKAGMvfqNPDNQIVATI-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 84 tfqlvkpfaglsVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDE 163
Cdd:PRK13633 103 ------------VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082692222 164 VMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVmALAQRIVVLHHGEVIARGAPGEV 225
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-226 |
3.27e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 74.23 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 2 SAALEVRGVSKSFRGLR-AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIvfrgrRIDGLRPDQVCAAG 80
Cdd:PRK13657 332 KGAVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI-----LIDGTDIRTVTRAS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQLVKPFAGL---SVLDNVTVG-------ALHRApnvsAAKKHAAEIVER--LGLGAKREQPASSLTLPDRKRLEV 148
Cdd:PRK13657 407 LRRNIAVVFQDAGLfnrSIEDNIRVGrpdatdeEMRAA----AERAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAI 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 149 ARALATRPELLLLDEVMAGLRptecdqmVEAFREINRA-----EGLTIMLIEHVMRAVmALAQRIVVLHHGEVIARGAPG 223
Cdd:PRK13657 483 ARALLKDPPILILDEATSALD-------VETEAKVKAAldelmKGRTTFIIAHRLSTV-RNADRILVFDNGRVVESGSFD 554
|
...
gi 1082692222 224 EVV 226
Cdd:PRK13657 555 ELV 557
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-232 |
9.44e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 71.70 E-value: 9.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 14 FRGlRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRI--DGLRPD-QVCAAGIGRTFQLvkP 90
Cdd:PRK13649 18 FEG-RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItsTSKNKDiKQIRKKVGLVFQF--P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 91 FAGL---SVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAK-REQPASSLTLPDRKRLEVARALATRPELLLLDEVMA 166
Cdd:PRK13649 95 ESQLfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 167 GLRPTECDQMVEAFREINRAeGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAVL 232
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFL 239
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-208 |
9.46e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.00 E-value: 9.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 20 VHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAA---GIGRTFQLVKPFAGLSV 96
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 97 LDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQM 176
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180 190
....*....|....*....|....*....|..
gi 1082692222 177 VEAFREINRAEGLTIMLIEHVMRavmaLAQRI 208
Cdd:PRK11629 185 FQLLGELNRLQGTAFLVVTHDLQ----LAKRM 212
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-229 |
1.14e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 71.36 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFR---------GLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIV--------- 62
Cdd:PRK15112 1 VETLLEVRNLSKTFRyrtgwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhplhfg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 63 ---FRGRRI--------DGLRPDQvcaaGIGRTFQLvkPFAglsvldnvtvgaLHRAPNVSAAKKHAAEIVERLGLGAKR 131
Cdd:PRK15112 81 dysYRSQRIrmifqdpsTSLNPRQ----RISQILDF--PLR------------LNTDLEPEQREKQIIETLRQVGLLPDH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 132 EQPASSLTLPDRK-RLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVV 210
Cdd:PRK15112 143 ASYYPHMLAPGQKqRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLV 222
|
250
....*....|....*....
gi 1082692222 211 LHHGEVIARGAPGEVVRDP 229
Cdd:PRK15112 223 MHQGEVVERGSTADVLASP 241
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-220 |
1.33e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFR-GLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRID-GLRPDQVca 78
Cdd:PRK15056 3 QQAGIVVNDVTVTWRnGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqALQKNLV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 79 AGIGRTFQLVKPFAGLsVLDNVTVGALHRAPNVSAAKKHAAEIVE----RLGLGAKREQPASSLTLPDRKRLEVARALAT 154
Cdd:PRK15056 81 AYVPQSEEVDWSFPVL-VEDVVMMGRYGHMGWLRRAKKRDRQIVTaalaRVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 155 RPELLLLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRAVMALAQRIVVLhHGEVIARG 220
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASG 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-163 |
1.33e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 72.66 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVF----------RGRriDGLRPD 74
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklayvdQSR--DALDPN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 75 QvcaagigRTFQLVKpfAGLSVLD--NVTVGAlhRApnvsaakkhaaeIVERLGL-GAKREQPASSLTLPDRKRLEVARA 151
Cdd:TIGR03719 401 K-------TVWEEIS--GGLDIIKlgKREIPS--RA------------YVGRFNFkGSDQQKKVGQLSGGERNRVHLAKT 457
|
170
....*....|..
gi 1082692222 152 LATRPELLLLDE 163
Cdd:TIGR03719 458 LKSGGNVLLLDE 469
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-232 |
1.49e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.42 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 11 SKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEI----VFRGRRIDGLRPDQVCAAG------ 80
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNPYSKkiknfk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 -----IGRTFQLvkPFAGL---SVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAK-REQPASSLTLPDRKRLEVARA 151
Cdd:PRK13631 113 elrrrVSMVFQF--PEYQLfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 152 LATRPELLLLDEVMAGLRPTECDQMVEAFREiNRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPAV 231
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
.
gi 1082692222 232 L 232
Cdd:PRK13631 270 I 270
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
30-232 |
1.86e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.25 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 30 GAIVGLIGPNGAGKTTIFNMVAGVYAAdAGEIVFRGRRIDGLRP------------DQVCAAGIgRTFQLVkpfaglsvl 97
Cdd:COG4138 22 GELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAaelarhraylsqQQSPPFAM-PVFQYL--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 98 dnvtvgALHRAPNVSAAKKHA--AEIVERLGLGAKREQPASSLTLPDRKRLEVARAL-----ATRPE--LLLLDEVMAGL 168
Cdd:COG4138 91 ------ALHQPAGASSEAVEQllAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082692222 169 RPTE---CDQMVEAFREinraEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVrDPAVL 232
Cdd:COG4138 165 DVAQqaaLDRLLRELCQ----QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPENL 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
26-225 |
1.93e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.44 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 26 DVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGR-------RIDgLRPDQvcaAGIGRTFQLVKPFAGLSVLD 98
Cdd:PRK11144 20 TLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekGIC-LPPEK---RRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 99 NVTVGalhrapnvsAAKKHAAE---IVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGL---RPTE 172
Cdd:PRK11144 96 NLRYG---------MAKSMVAQfdkIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLdlpRKRE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1082692222 173 CDQMVEAF-REINraegLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEV 225
Cdd:PRK11144 167 LLPYLERLaREIN----IPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-62 |
3.39e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 71.30 E-value: 3.39e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIV 62
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK 382
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-230 |
4.07e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSF---RGL--------RAVHDAWIDVPQGAIVGLIGPNGAGKTTifnmvAGV----YAADAGEIVFRGRRID 69
Cdd:PRK15134 276 LDVEQLQVAFpirKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKST-----TGLallrLINSQGEIWFDGQPLH 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 70 GLRPDQVCAagIGRTFQLV--KPFAGL----SVLDNVTVGALHRAPNVSAAKKHAA--EIVERLGLGAK-REQPASSLTL 140
Cdd:PRK15134 351 NLNRRQLLP--VRHRIQVVfqDPNSSLnprlNVLQIIEEGLRVHQPTLSAAQREQQviAVMEEVGLDPEtRHRYPAEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 141 PDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARG 220
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
250
....*....|
gi 1082692222 221 APGEVVRDPA 230
Cdd:PRK15134 509 DCERVFAAPQ 518
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-227 |
5.19e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.92 E-value: 5.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 4 ALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDglrpdqvcaAG--- 80
Cdd:NF033858 266 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---------AGdia 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 ----IG---RTFQLvkpFAGLSVLDNVTvgaLH-RAPNVSAAKKHA--AEIVERLGLGAKREQPASSLTLPDRKRLEVAR 150
Cdd:NF033858 337 trrrVGymsQAFSL---YGELTVRQNLE---LHaRLFHLPAAEIAArvAEMLERFDLADVADALPDSLPLGIRQRLSLAV 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 151 ALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAvmalAQ---RIVVLHHGEVIARGAPGEVVR 227
Cdd:NF033858 411 AVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNE----AErcdRISLMHAGRVLASDTPAALVA 486
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-216 |
5.44e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.75 E-value: 5.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 10 VSKSFRGLR-AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQV--CAAGIGRTFQ 86
Cdd:PRK10908 7 VSKAYLGGRqALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 87 LVKPFAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMA 166
Cdd:PRK10908 87 DHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1082692222 167 GLRPTECDQMVEAFREINRAeGLTIMLIEHVMRAVMALAQRIVVLHHGEV 216
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-216 |
7.80e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.94 E-value: 7.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDqvcaagIGRT 84
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED------TRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 FQLVKPFAGLSVLDNVTVGAlhrapnVSAAKKHAAEIVERLGLgAKR--EQPAsSLTLPDRKRLEVARALATRPELLLLD 162
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGL-ADRanEWPA-ALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1082692222 163 EVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEV 216
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-230 |
9.12e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.49 E-value: 9.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 3 AALEVRGVSKSFRG-LRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQvcaAGI 81
Cdd:PRK11650 2 AGLKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD---RDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 82 GRTFQLVKPFAGLSVLDNVTVGALHRapNVSAAK-----KHAAEIVErlgLGAKREQPASSLTLPDRKRLEVARALATRP 156
Cdd:PRK11650 79 AMVFQNYALYPHMSVRENMAYGLKIR--GMPKAEieervAEAARILE---LEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082692222 157 ELLLLDEVM----AGLRPtecdQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPA 230
Cdd:PRK11650 154 AVFLFDEPLsnldAKLRV----QMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPA 227
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-226 |
1.82e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 69.15 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 19 AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRidglrpdQVCAAGIGRTFQlvkpfagLSVLD 98
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-------ALIAISSGLNGQ-------LTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 99 NVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPT---ECDQ 175
Cdd:PRK13545 105 NIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTftkKCLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 176 MVEAFREinraEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVV 226
Cdd:PRK13545 185 KMNEFKE----QGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVV 231
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-229 |
2.68e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.27 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 27 VPQGAIVGLIGPNGAGKTTIFNMVAGVYAAdAGEIVFRGRRIDGLRPdqvCAAGIGRTF--QLVKPFAGLSVLDNVtvgA 104
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSA---AELARHRAYlsQQQTPPFAMPVFQYL---T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 105 LHRAPNVSAAKKHAA--EIVERLGLGAKREQPASSLTLPDRKR-------LEVARALATRPELLLLDEVMAGLRPTE--- 172
Cdd:PRK03695 92 LHQPDKTRTEAVASAlnEVAEALGLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSLDVAQqaa 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1082692222 173 CDQMVEAFreinRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:PRK03695 172 LDRLLSEL----CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-226 |
3.75e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIvfrgRRIDGLRpdqvcaag 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----KRNGKLR-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQLVKPFAGLSvldnVTVGALHR-APNVSAAKKHAAeiVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELL 159
Cdd:PRK09544 69 IGYVPQKLYLDTTLP----LTVNRFLRlRPGTKKEDILPA--LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082692222 160 LLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHgEVIARGAPgEVV 226
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTP-EVV 207
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-216 |
4.51e-13 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 65.32 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRA--VHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAAGIG 82
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL-GDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 83 RTFQLVKPFAGlSVLDNVTVGAlhrapnvsaakkhaaeiverlglgakreqpassltlpDRKRLEVARALATRPELLLLD 162
Cdd:cd03246 80 YLPQDDELFSG-SIAENILSGG-------------------------------------QRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1082692222 163 EVMAGLRPtECDQMVEAFREINRAEGLTIMLIEHVMRaVMALAQRIVVLHHGEV 216
Cdd:cd03246 122 EPNSHLDV-EGERALNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-228 |
4.98e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 66.73 E-value: 4.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 19 AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQV---CAAGIGRTFQLvkPFAGL- 94
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYirpVRKRIGMVFQF--PESQLf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 95 --SVLDNVTVGALHRAPNVSAAKKHAAEIVerLGLGAKREQPASS---LTLPDRKRLEVARALATRPELLLLDEVMAGLR 169
Cdd:PRK13646 100 edTVEREIIFGPKNFKMNLDEVKNYAHRLL--MDLGFSRDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1082692222 170 PTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRD 228
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
30-235 |
5.04e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 67.83 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 30 GAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLR----PDQVCAAGigrtfQLVKPFAGlSVLDNVTVGaL 105
Cdd:TIGR00958 507 GEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhhylHRQVALVG-----QEPVLFSG-SVRENIAYG-L 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 106 HRAPN---VSAAKK-HAAEIVERLGLGAKRE--QPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLrPTECDQMVEA 179
Cdd:TIGR00958 580 TDTPDeeiMAAAKAaNAHDFIMEFPNGYDTEvgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL-DAECEQLLQE 658
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 180 FREinrAEGLTIMLIEHVMRAVMAlAQRIVVLHHGEVIARGAPGEVVRDPavlGCY 235
Cdd:TIGR00958 659 SRS---RASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ---GCY 707
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
30-216 |
5.52e-13 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 65.96 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 30 GAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLR----PDQVCAAGigrtfQLVKPFAGlSVLDNVTVGaL 105
Cdd:cd03248 40 GEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEhkylHSKVSLVG-----QEPVLFAR-SLQDNIAYG-L 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 106 HRAPNVS----AAKKHAAEIVERLGLGAKRE--QPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLrPTECDQMVE- 178
Cdd:cd03248 113 QSCSFECvkeaAQKAHAHSFISELASGYDTEvgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL-DAESEQQVQq 191
|
170 180 190
....*....|....*....|....*....|....*...
gi 1082692222 179 AFREINRAEglTIMLIEHVMRAVMAlAQRIVVLHHGEV 216
Cdd:cd03248 192 ALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
30-229 |
5.72e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.53 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 30 GAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPD------------QVCAAGIGRTFQLVKPFAGLSVL 97
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlRLLRTRLTMVFQHFNLWSHMTVL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 98 DNVTvgalhRAP------NVSAAKKHAAEIVERLGL-GAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRP 170
Cdd:PRK10619 111 ENVM-----EAPiqvlglSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1082692222 171 TECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:PRK10619 186 ELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
7-229 |
6.72e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.35 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 7 VRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRpDQVCAAGIGRTFQ 86
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS-SKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 87 LVKPFAGLSVLDNVTV------GALHRAPnvSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLL 160
Cdd:PRK10575 93 QLPAAEGMTVRELVAIgrypwhGALGRFG--AADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082692222 161 LDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-224 |
7.66e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 67.35 E-value: 7.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRG--LRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGR-----RIDGLRpDQVC 77
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdyTLASLR-NQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 78 AAGigrtfQLVKPFAGlSVLDNVTVGA---LHRAPNVSAAK-KHAAEIVERL--GLGAKREQPASSLTLPDRKRLEVARA 151
Cdd:PRK11176 421 LVS-----QNVHLFND-TIANNIAYARteqYSREQIEEAARmAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 152 LATRPELLLLDEVMAGLrPTECDQMVE-AFREI--NRaeglTIMLIEHVMRAVMAlAQRIVVLHHGEVIARGAPGE 224
Cdd:PRK11176 495 LLRDSPILILDEATSAL-DTESERAIQaALDELqkNR----TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAE 564
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-220 |
1.01e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.77 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 2 SAALEVRGVSKSF--RGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAA 79
Cdd:PRK11160 336 QVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 gIGRTFQLVKPFAGlSVLDNVTVGalhrAPNVSAAKkhAAEIVERLGLGAKREQPAS----------SLTLPDRKRLEVA 149
Cdd:PRK11160 416 -ISVVSQRVHLFSA-TLRDNLLLA----APNASDEA--LIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082692222 150 RALATRPELLLLDEVMAGL-RPTEcDQMVEAFREInrAEGLTIMLIEHVMRAvMALAQRIVVLHHGEVIARG 220
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLdAETE-RQILELLAEH--AQNKTVLMITHRLTG-LEQFDRICVMDNGQIIEQG 555
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
30-220 |
2.92e-12 |
|
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: 63.34 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 30 GAIVGLIGPNGAGKTTIFNMVAG--VYAADAGEIVFRGRRIDglrpDQVCAAGIGRTFQlvkpfaglsvlDNVTVGALhr 107
Cdd:cd03213 35 GELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLD----KRSFRKIIGYVPQ-----------DDILHPTL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 108 apNVSAAKKHAAEIverlglgakreqpaSSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREInRAE 187
Cdd:cd03213 98 --TVRETLMFAAKL--------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADT 160
|
170 180 190
....*....|....*....|....*....|....
gi 1082692222 188 GLTIMLIEHVMRAVM-ALAQRIVVLHHGEVIARG 220
Cdd:cd03213 161 GRTIICSIHQPSSEIfELFDKLLLLSQGRVIYFG 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-226 |
3.07e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.45 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 30 GAIVGLIGPNGAGKTTIFNMVAGVYAAD---AGEIVFRGRRIDGLRPDQVCAagigrTFQLVKPFAG-LSVLDNVTVGAL 105
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISA-----YVQQDDLFIPtLTVREHLMFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 106 HRAP-NVSAAKKHAA--EIVERLGLGAKR------EQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQM 176
Cdd:TIGR00955 126 LRMPrRVTKKEKRERvdEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1082692222 177 VEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVV 226
Cdd:TIGR00955 206 VQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-229 |
4.25e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.44 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRG----LRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVyAADAGEIV---FRGRRIDGLR--PDQ 75
Cdd:PRK15093 4 LDIRNLTIEFKTsdgwVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTadrMRFDDIDLLRlsPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 76 ---VCAAGIGRTFQlvKPFAGLSVLDNVTVGALHRAPN----------VSAAKKHAAEIVERLGLGAKREQPAS---SLT 139
Cdd:PRK15093 83 rrkLVGHNVSMIFQ--EPQSCLDPSERVGRQLMQNIPGwtykgrwwqrFGWRKRRAIELLHRVGIKDHKDAMRSfpyELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 140 LPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIAR 219
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250
....*....|
gi 1082692222 220 GAPGEVVRDP 229
Cdd:PRK15093 241 APSKELVTTP 250
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-224 |
4.50e-12 |
|
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: 63.71 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 25 IDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAAGIGRTFQLVKPFAGlSVLDNVTVGA 104
Cdd:cd03249 24 LTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL-RSQIGLVSQEPVLFDG-TIAENIRYGK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 105 --LHRAPNVSAAKKHAA-EIVERLG------LGAKreqpASSLTLPDRKRLEVARALATRPELLLLDEVMAGLrPTECDQ 175
Cdd:cd03249 102 pdATDEEVEEAAKKANIhDFIMSLPdgydtlVGER----GSQLSGGQKQRIAIARALLRNPKILLLDEATSAL-DAESEK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1082692222 176 MVEAfrEINRA-EGLTIMLIEHVMRAVMAlAQRIVVLHHGEVIARGAPGE 224
Cdd:cd03249 177 LVQE--ALDRAmKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
18-229 |
6.01e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.99 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 18 RAVHDAWIDVPQGAIVGLIGPNGAGKT----TIFNMVAGVYAADAGEIVFRGRRIDGLRPD---QVCAAGIGRTFQlvKP 90
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKerrNLVGAEVAMIFQ--DP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 91 FAGLSvlDNVTVG-----AL--HRAPNVSAAKKHAAEIVERLGLGAkreqPASSLTL-PDR------KRLEVARALATRP 156
Cdd:PRK11022 99 MTSLN--PCYTVGfqimeAIkvHQGGNKKTRRQRAIDLLNQVGIPD----PASRLDVyPHQlsggmsQRVMIAMAIACRP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082692222 157 ELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-217 |
6.77e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.34 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 2 SAALEVRGVSKSFRG----LRAVHDAWIDVPQGAIVGLIGPNGAGKT-TIFNMV------AGVYAAdaGEIVFRG----- 65
Cdd:PRK15134 3 QPLLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpspPVVYPS--GDIRFHGesllh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 66 ---RRIDGLRPDQvcaagIGRTFQlvKPFAGLSVLDNVT-----VGALHRAPNVSAAKKHAAEIVERLGLgakrEQPASS 137
Cdd:PRK15134 81 aseQTLRGVRGNK-----IAMIFQ--EPMVSLNPLHTLEkqlyeVLSLHRGMRREAARGEILNCLDRVGI----RQAAKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 138 LT-LP------DRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVV 210
Cdd:PRK15134 150 LTdYPhqlsggERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAV 229
|
....*..
gi 1082692222 211 LHHGEVI 217
Cdd:PRK15134 230 MQNGRCV 236
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-214 |
7.42e-12 |
|
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: 64.65 E-value: 7.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 19 AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIdglrpdqvcAAGIGRTFQLVKPFAGLSVLD 98
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI---------LTNISDVHQNMGYCPQFDAID 2024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 99 NVTVGALH-------RAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPT 171
Cdd:TIGR01257 2025 DLLTGREHlylyarlRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 2104
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1082692222 172 ECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHG 214
Cdd:TIGR01257 2105 ARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-215 |
9.47e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.13 E-value: 9.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 4 ALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADA-----GEIVFRGRRIDGLRpdqVCA 78
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERR---VNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 79 AGIGRTFQLVKPFAGL---SVLDNVTVGA--LHRAPNV-------SAAKkhAAEIVERLGlgAKREQPASSLTLPDRKRL 146
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLfpmSVYDNVAYGVkiVGWRPKLeiddiveSALK--DADLWDEIK--HKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082692222 147 EVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGE 215
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-192 |
1.31e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 61.61 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLR--PDQVCA---- 78
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRdePHENILylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 79 -AGIgrtfqlvKPfaGLSVLDNVTV-GALHRapnvsAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRP 156
Cdd:TIGR01189 81 lPGL-------KP--ELSALENLHFwAAIHG-----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRR 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 1082692222 157 ELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIM 192
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLL 182
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-208 |
1.42e-11 |
|
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: 61.74 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSfRGLRAVHDAW-IDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPdqVCAAGIGR 83
Cdd:cd03231 1 LEADELTCE-RDGRALFSGLsFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD--SIARGLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 84 TFQLVKPFAGLSVLDNVT-VGALHRAPNVSAAkkhaaeiVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLD 162
Cdd:cd03231 78 LGHAPGIKTTLSVLENLRfWHADHSDEQVEEA-------LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1082692222 163 EVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRI 208
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-217 |
1.55e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.90 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 6 EVRGVSKSF-RGLRAVH-----DAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRgrrIDGLRPDQVCaa 79
Cdd:COG2401 26 RVAIVLEAFgVELRVVEryvlrDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD---VPDNQFGREA-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 gigrtfqlvkpfaglSVLDNVTvgalhRAPNVSAAKkhaaEIVERLGLGakreQPASSLTLPD------RKRLEVARALA 153
Cdd:COG2401 101 ---------------SLIDAIG-----RKGDFKDAV----ELLNAVGLS----DAVLWLRRFKelstgqKFRFRLALLLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082692222 154 TRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALA-QRIVVLHHGEVI 217
Cdd:COG2401 153 ERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVP 217
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-196 |
2.04e-11 |
|
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: 63.15 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAW-IDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcAAGIGR 83
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVsLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV-RRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 84 TFQLVKPFAGlSVLDNVTVGalhrAPNVSAAKKHAA-------EIVERL--GLGAKREQPASSLTLPDRKRLEVARALAT 154
Cdd:TIGR02868 414 CAQDAHLFDT-TVRENLRLA----RPDATDEELWAAlervglaDWLRALpdGLDTVLGEGGARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1082692222 155 RPELLLLDEVMAGLRPTECDQMVEAFREINraEGLTIMLIEH 196
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAAL--SGRTVVLITH 528
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
27-196 |
2.04e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.12 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 27 VPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLR---PDQVCAAGiGRTFqlVKPFagLSVLDNVTVG 103
Cdd:PRK13540 24 LPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLctyQKQLCFVG-HRSG--INPY--LTLRENCLYD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 104 aLHrapnVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREi 183
Cdd:PRK13540 99 -IH----FSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE- 172
|
170
....*....|...
gi 1082692222 184 NRAEGLTIMLIEH 196
Cdd:PRK13540 173 HRAKGGAVLLTSH 185
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-218 |
2.07e-11 |
|
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: 62.92 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 20 VHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVY-AADAGEIVFRGRRIDGLRPDQVCAAGIG-----RTFQLVKPFAG 93
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKPVDIRNPAQAIRAGIAmvpedRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 94 lsVLDNVTVGALHRAP-----NVSAAKKHAAEIVERLGL-GAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAG 167
Cdd:TIGR02633 356 --VGKNITLSVLKSFCfkmriDAAAELQIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1082692222 168 LrptECDQMVEAFREINR--AEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIA 218
Cdd:TIGR02633 434 V---DVGAKYEIYKLINQlaQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-240 |
3.84e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVS---KSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVY-AADAGEIVFRGRRIDGLRPDQVCAAG 80
Cdd:PRK13549 260 LEVRNLTawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYpGRWEGEIFIDGKPVKIRNPQQAIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IG-----RTFQLVKPfaGLSVLDNVTVGALHRAPNVS-----AAKKHAAEIVERLGL-GAKREQPASSLTLPDRKRLEVA 149
Cdd:PRK13549 340 IAmvpedRKRDGIVP--VMGVGKNITLAALDRFTGGSriddaAELKTILESIQRLKVkTASPELAIARLSGGNQQKAVLA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 150 RALATRPELLLLDEvmaglrPT---ECDQMVEAFREINR--AEGLTIMLIEHVMRAVMALAQRIVVLHHGEViargaPGE 224
Cdd:PRK13549 418 KCLLLNPKILILDE------PTrgiDVGAKYEIYKLINQlvQQGVAIIVISSELPEVLGLSDRVLVMHEGKL-----KGD 486
|
250 260
....*....|....*....|
gi 1082692222 225 VVRDPA----VLGCYLGEET 240
Cdd:PRK13549 487 LINHNLtqeqVMEAALRSEH 506
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
22-224 |
4.55e-11 |
|
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: 60.71 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 22 DAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAgIGRTFQLVkpfaglsVLDNVT 101
Cdd:cd03253 19 DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA-IGVVPQDT-------VLFNDT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 102 VGALHRAPNVSAAKkhaAEIVErlglGAKREQPASS-LTLPD-----------------RKRLEVARALATRPELLLLDE 163
Cdd:cd03253 91 IGYNIRYGRPDATD---EEVIE----AAKAAQIHDKiMRFPDgydtivgerglklsggeKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 164 VMAGLRPTECDQMVEAFREInrAEGLTIMLIEHVMRAVMAlAQRIVVLHHGEVIARGAPGE 224
Cdd:cd03253 164 ATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-225 |
4.95e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.06 E-value: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 4 ALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEI-VFRGRRIDGLRPDQVCAA--- 79
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGDMADARHRRAVCPRiay 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 ---GIGRTFqlvkpFAGLSVLDNVTVGAlhRAPNVSAAKKHA--AEIVERLGLGAKREQPASSLTLPDRKRLEVARALAT 154
Cdd:NF033858 81 mpqGLGKNL-----YPTLSVFENLDFFG--RLFGQDAAERRRriDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIH 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 155 RPELLLLDEVMAGLRPTECDQMVEAFREInRAE--GLTIMliehVMRAVMALAQR---IVVLHHGEVIARGAPGEV 225
Cdd:NF033858 154 DPDLLILDEPTTGVDPLSRRQFWELIDRI-RAErpGMSVL----VATAYMEEAERfdwLVAMDAGRVLATGTPAEL 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-235 |
6.25e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.61 E-value: 6.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 15 RGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADA--------GEIVFRGR---RIDGLRPDQVCAAgigr 83
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEplaAIDAPRLARLRAV---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 84 TFQLVKPFAGLSVLDNVTVGALHRAPNVSAAKKHAAEI----VERLGLGAKREQPASSLTLPDRKRLEVARALA------ 153
Cdd:PRK13547 88 LPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIawqaLALAGATALVGRDVTTLSGGELARVQFARVLAqlwpph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 154 ---TRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPA 230
Cdd:PRK13547 168 daaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAH 247
|
....*
gi 1082692222 231 VLGCY 235
Cdd:PRK13547 248 IARCY 252
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-222 |
6.44e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.95 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 7 VRGVSKSFR--GLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRI----DGLRpdqvcaAG 80
Cdd:TIGR01257 931 VKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetnlDAVR------QS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 81 IGRTFQLVKPFAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLL 160
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082692222 161 LDEVMAGLRPTECDQMVEAFreINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAP 222
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-220 |
7.20e-11 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 59.25 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRG--LRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGrridglrpdqvcaagig 82
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 83 rtfqlvKPFAGLSVLDNVTVGALHRAPNVsaakkHAAEIVERLGLgakreqpasSLTLPDRKRLEVARALATRPELLLLD 162
Cdd:cd03247 64 ------VPVSDLEKALSSLISVLNQRPYL-----FDTTLRNNLGR---------RFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082692222 163 EVMAGLRPTECDQMVEAFREInrAEGLTIMLIEHVMRAvMALAQRIVVLHHGEVIARG 220
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEV--LKDKTLIWITHHLTG-IEHMDKILFLENGKIIMQG 178
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-215 |
7.61e-11 |
|
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: 58.23 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIvfrgrridglrpdqvcaagigrt 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 85 fqlvkpfaglSVLDNVTVGalhrapnvsaakkhaaeIVERLGLGAKReqpassltlpdrkRLEVARALATRPELLLLDEv 164
Cdd:cd03221 58 ----------TWGSTVKIG-----------------YFEQLSGGEKM-------------RLALAKLLLENPNLLLLDE- 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 165 maglrPTE------CDQMVEAFREINRaeglTIMLIEH---VMRAVmalAQRIVVLHHGE 215
Cdd:cd03221 97 -----PTNhldlesIEALEEALKEYPG----TVILVSHdryFLDQV---ATKIIELEDGK 144
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-229 |
2.01e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 59.72 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 17 LRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAA--GIGRTFQlvKPFAGL 94
Cdd:PRK15079 34 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsDIQMIFQ--DPLASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 95 SvlDNVTVGALHRAP-NVSAAKKHAAEIVERLglgakREQPASSLTLPDR-------------KRLEVARALATRPELLL 160
Cdd:PRK15079 112 N--PRMTIGEIIAEPlRTYHPKLSRQEVKDRV-----KAMMLKVGLLPNLinryphefsggqcQRIGIARALILEPKLII 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082692222 161 LDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-220 |
2.47e-10 |
|
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: 58.44 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 17 LRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADA---GEIVFRGRRidgLRPDQV--CAAGIGRTFQLVKpf 91
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQP---RKPDQFqkCVAYVRQDDILLP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 92 aGLSVLDNVTVGALHRAPNVS--AAKKHAAEIV--ERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAG 167
Cdd:cd03234 95 -GLTVRETLTYTAILRLPRKSsdAIRKKRVEDVllRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1082692222 168 LRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARG 220
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-210 |
3.05e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.41 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 29 QGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIvfrgrrIDGLR----PdqvcaagigrtfQLVKPFAglsvldNVTVGA 104
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------DEDLKisykP------------QYISPDY------DGTVEE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 105 LHRAPNVSA--AKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLrptECDQMVEAFRE 182
Cdd:COG1245 421 FLRSANTDDfgSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL---DVEQRLAVAKA 497
|
170 180 190
....*....|....*....|....*....|.
gi 1082692222 183 INR-AE--GLTIMLIEHVMRAVMALAQRIVV 210
Cdd:COG1245 498 IRRfAEnrGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
26-227 |
5.03e-10 |
|
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: 58.99 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 26 DVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQvcaagIGRTF----QLVKPFAGlSVLDNVT 101
Cdd:COG4618 354 SLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE-----LGRHIgylpQDVELFDG-TIAENIA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 102 vgalhRAPNVSAAKKHAA-------EIVERLGLGAKREQPASSLTLPD--RKRLEVARALATRPELLLLDEVMAGLrPTE 172
Cdd:COG4618 428 -----RFGDADPEKVVAAaklagvhEMILRLPDGYDTRIGEGGARLSGgqRQRIGLARALYGDPRLVVLDEPNSNL-DDE 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 173 CDQM-VEAFREInRAEGLTIMLIEHVMrAVMALAQRIVVLHHGEVIARGAPGEVVR 227
Cdd:COG4618 502 GEAAlAAAIRAL-KARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-210 |
6.51e-10 |
|
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: 57.42 E-value: 6.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 26 DVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIdGLRPDQVCAAGIGRTFQLVKpfaglSVLDNVTVGAL 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKADYEGTVRDLLS-----SITKDFYTHPY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 106 HRapnvsaakkhaAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLrptECDQMVEAFREINR 185
Cdd:cd03237 95 FK-----------TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL---DVEQRLMASKVIRR 160
|
170 180
....*....|....*....|....*...
gi 1082692222 186 ---AEGLTIMLIEHVMRAVMALAQRIVV 210
Cdd:cd03237 161 faeNNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
29-192 |
1.05e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.42 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 29 QGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAgIG-RTFqlVKPFagLSVLDNVTVGALHR 107
Cdd:PRK13539 27 AGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY-LGhRNA--MKPA--LTVAENLEFWAAFL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 108 ApnvsAAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAE 187
Cdd:PRK13539 102 G----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQG 177
|
....*
gi 1082692222 188 GLTIM 192
Cdd:PRK13539 178 GIVIA 182
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-226 |
1.07e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 33 VGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRG-----------RRIDGLRPDQ-VCAAGIGRtFQLvKPFAGLSvlDNV 100
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltdlRRVLSIIPQSpVLFSGTVR-FNI-DPFSEHN--DAD 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 101 TVGALHRApnvsaakkHAAEIVER--LGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLrPTECDQMVE 178
Cdd:PLN03232 1341 LWEALERA--------HIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV-DVRTDSLIQ 1411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1082692222 179 -AFREINRAegLTIMLIEHVMRAVMAlAQRIVVLHHGEVIARGAPGEVV 226
Cdd:PLN03232 1412 rTIREEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-229 |
1.96e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.16 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 27 VPQGAIVGLIGPNGAGKTTIFNMVAGvYAADAGEIVFRGRRIDGLRPDQ--VCAAGIGRTFQLvkpFAGlSVLDNVTVGA 104
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESwrKHLSWVGQNPQL---PHG-TLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 105 lhraPNVSAA-------KKHAAEIVERLGLG---AKREQpASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECD 174
Cdd:PRK11174 448 ----PDASDEqlqqaleNAWVSEFLPLLPQGldtPIGDQ-AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1082692222 175 QMVEAFREInrAEGLTIMLIEHVMRavmALAQ--RIVVLHHGEVIARGAPGEVVRDP 229
Cdd:PRK11174 523 LVMQALNAA--SRRQTTLMVTHQLE---DLAQwdQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
30-163 |
2.51e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 30 GAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPD---QVC----AAGIgrtfqlvKPFagLSVLDNVTV 102
Cdd:PRK13538 27 GELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhqDLLylghQPGI-------KTE--LTALENLRF 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082692222 103 -GALHRAPNVSAakkhAAEIVERLGLgAKREQ-PASSLTLPDRKRLEVARALATRPELLLLDE 163
Cdd:PRK13538 98 yQRLHGPGDDEA----LWEALAQVGL-AGFEDvPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-210 |
3.88e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 29 QGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGR------RIdglRPDQvcaagigrtfqlvkpfaglsvldNVTV 102
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykpqYI---KPDY-----------------------DGTV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 103 GALHRapnvSAAKK-----HAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLrptECDQMV 177
Cdd:PRK13409 418 EDLLR----SITDDlgssyYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL---DVEQRL 490
|
170 180 190
....*....|....*....|....*....|....*.
gi 1082692222 178 EAFREINR-AE--GLTIMLIEHVMRAVMALAQRIVV 210
Cdd:PRK13409 491 AVAKAIRRiAEerEATALVVDHDIYMIDYISDRLMV 526
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-230 |
7.07e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKsfRGLRavHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGI--- 81
Cdd:PRK11288 258 LRLDGLKG--PGLR--EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGImlc 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 82 --GRTFQLVKPFAglSVLDNVTVGAL-HRAP-----NVSAAKKHAAEIVERLGL-GAKREQPASSLTLPDRKRLEVARAL 152
Cdd:PRK11288 334 peDRKAEGIIPVH--SVADNINISARrHHLRagcliNNRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWL 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 153 ATRPELLLLDEVMAGLRptecdqmVEAFREINR------AEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIargapGEVV 226
Cdd:PRK11288 412 SEDMKVILLDEPTRGID-------VGAKHEIYNviyelaAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA-----GELA 479
|
....
gi 1082692222 227 RDPA 230
Cdd:PRK11288 480 REQA 483
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-228 |
1.23e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.05 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 1 MSAALEVRGVSKSFRGLR--------------------AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGE 60
Cdd:PRK13546 1 MNVSVNIKNVTKEYRIYRtnkermkdalipkhknktffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 61 IVFRGRRidglrpdQVCAAGIGRTFQlvkpfagLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLGAKREQPASSLTL 140
Cdd:PRK13546 81 VDRNGEV-------SVIAISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 141 PDRKRLEVARALATRPELLLLDEVMAGLRPT---ECDQMVEAFREINRaeglTIMLIEHVMRAVMALAQRIVVLHHGEVI 217
Cdd:PRK13546 147 GMRAKLGFSINITVNPDILVIDEALSVGDQTfaqKCLDKIYEFKEQNK----TIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
250
....*....|.
gi 1082692222 218 ARGAPGEVVRD 228
Cdd:PRK13546 223 DYGELDDVLPK 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-216 |
1.29e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 26 DVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGigrtfqLV-----KPFAGLsVLD-- 98
Cdd:PRK15439 285 EVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARG------LVylpedRQSSGL-YLDap 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 99 ---NVTVGALHRAPNVSAAKKHAAeIVERL--GLGAK---REQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRP 170
Cdd:PRK15439 358 lawNVCALTHNRRGFWIKPARENA-VLERYrrALNIKfnhAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1082692222 171 TECDQMVEAFREINrAEGLTIMLIEHVMRAVMALAQRIVVLHHGEV 216
Cdd:PRK15439 437 SARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-220 |
3.16e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.56 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 19 AVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCA--AGIGRTfqlvkPFA-GLS 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSrlAVVSQT-----PFLfSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 96 VLDNVTVGAlhraPNVSAAK-KHAAEI------VERLGLGAKREQPASSLTLP--DRKRLEVARALATRPELLLLDEVMA 166
Cdd:PRK10789 405 VANNIALGR----PDATQQEiEHVARLasvhddILRLPQGYDTEVGERGVMLSggQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1082692222 167 GLRPTECDQMVEAFREInrAEGLTIMLIEHVMRAvMALAQRIVVLHHGEVIARG 220
Cdd:PRK10789 481 AVDGRTEHQILHNLRQW--GEGRTVIISAHRLSA-LTEASEILVMQHGHIAQRG 531
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
13-220 |
9.57e-08 |
|
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: 50.40 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 13 SFRGL--RAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNmvAGVYAADAgeivfrgRRIDGLRPdqvcaagigrtfqlvKP 90
Cdd:cd03238 2 TVSGAnvHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGK-------ARLISFLP---------------KF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 91 FAGLSVLdnvtVGALHRAPNVsaakkhaaeiverlGLG-AKREQPASSLTLPDRKRLEVARALATRPE--LLLLDEVMAG 167
Cdd:cd03238 58 SRNKLIF----IDQLQFLIDV--------------GLGyLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1082692222 168 LRPTECDQMVEAFREInRAEGLTIMLIEHvMRAVMALAQRIVVLHH------GEVIARG 220
Cdd:cd03238 120 LHQQDINQLLEVIKGL-IDLGNTVILIEH-NLDVLSSADWIIDFGPgsgksgGKVVFSG 176
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
25-220 |
9.67e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.33 E-value: 9.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 25 IDVPQGAIVGLIGPNGAGKTTIFNMVAGV--YAADAGEIVFRGRRIDGLRPDQVCAAGIGRTFQLVKPFAGLSvldnvtv 102
Cdd:PRK09580 22 LEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYPVEIPGVS------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 103 GALHRAPNVSAAKKH-AAEIVERLGLGAKREQPASSLTLPD---------------RKRLEVARALATRPELLLLDEVMA 166
Cdd:PRK09580 95 NQFFLQTALNAVRSYrGQEPLDRFDFQDLMEEKIALLKMPEdlltrsvnvgfsggeKKRNDILQMAVLEPELCILDESDS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 167 GLrptECDQM------VEAFREINRAegltIMLIEHVMRAVMALAQRIV-VLHHGEVIARG 220
Cdd:PRK09580 175 GL---DIDALkivadgVNSLRDGKRS----FIIVTHYQRILDYIKPDYVhVLYQGRIVKSG 228
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
35-215 |
2.21e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 35 LIGPNGAGKTTIFNMVAG----VYAADageIVFRGRRidglrpdqvcaAGIGRTFQLVKPFAG-------------LSVL 97
Cdd:PRK10938 291 IVGPNGAGKSTLLSLITGdhpqGYSND---LTLFGRR-----------RGSGETIWDIKKHIGyvssslhldyrvsTSVR 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 98 DNVTVG-----ALHRApnVS-AAKKHAAEIVERLGLGAK-REQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRP 170
Cdd:PRK10938 357 NVILSGffdsiGIYQA--VSdRQQKLAQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1082692222 171 TEcDQMVEAFREINRAEGLTimliehvmravmalaQRIVVLHHGE 215
Cdd:PRK10938 435 LN-RQLVRRFVDVLISEGET---------------QLLFVSHHAE 463
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-168 |
2.27e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 50.10 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 2 SAALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPD----QV- 76
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyrqQVs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 77 -CaagigrtFQLVKPFaGLSVLDNVTVGALHRapNVSAAKKHAAEIVERLGLGAKR-EQPASSLTLPDRKRLEVARALAT 154
Cdd:PRK10247 85 yC-------AQTPTLF-GDTVYDNLIFPWQIR--NQQPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQF 154
|
170
....*....|....
gi 1082692222 155 RPELLLLDEVMAGL 168
Cdd:PRK10247 155 MPKVLLLDEITSAL 168
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-61 |
2.93e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 2.93e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082692222 4 ALEVRGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEI 61
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-230 |
7.84e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.95 E-value: 7.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 19 AVHDAWIDVPQGAIVGLIGPNGAGKT-TIFNMVaGVYAAD---AGEIVFRGRRIDGLRPDQ---VCAAGIGRTFQlvKPF 91
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSqTAFALM-GLLAANgriGGSATFNGREILNLPEKElnkLRAEQISMIFQ--DPM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 92 AGLS----VLDNVT-VGALHRAPNvsaaKKHAAEIVERLGLGAKREQPASSLTL-PD------RKRLEVARALATRPELL 159
Cdd:PRK09473 108 TSLNpymrVGEQLMeVLMLHKGMS----KAEAFEESVRMLDAVKMPEARKRMKMyPHefsggmRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082692222 160 LLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDPA 230
Cdd:PRK09473 184 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
143-230 |
1.74e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 143 RKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAP 222
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSV 253
|
....*...
gi 1082692222 223 GEVVRDPA 230
Cdd:PRK10261 254 EQIFHAPQ 261
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-168 |
2.24e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 22 DAWidVPQGAIVGLIGPNGAGKTTIFNMVAGvyAADAGeIVFRGRRIDGLRP-DQVCAAGIGRTFQLVKPFAGLSVLDNV 100
Cdd:TIGR00956 783 DGW--VKPGTLTALMGASGAGKTTLLNVLAE--RVTTG-VITGGDRLVNGRPlDSSFQRSIGYVQQQDLHLPTSTVRESL 857
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 101 TVGALHRAPN-VSAAKK--HAAEIVERLGLGAKREQ----PASSLTLPDRKRLEVARALATRPELLL-LDEVMAGL 168
Cdd:TIGR00956 858 RFSAYLRQPKsVSKSEKmeYVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGL 933
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-177 |
3.81e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.18 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 30 GAIVGLIGPNGAGKTTIFNMVAGVYAAD--AGEIVFRGRridglRPDQVCAAGIGRTFQLVKPFAGLSVLDNVTVGALHR 107
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNR-----KPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLR 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082692222 108 APN--VSAAKKHAAE-IVERLGLgAKREQPA------SSLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMV 177
Cdd:PLN03211 169 LPKslTKQEKILVAEsVISELGL-TKCENTIignsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-163 |
4.47e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 47.24 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 9 GVSKSFRGLRAV-HDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRgrriDGLRpdqvcaagIGRTFQL 87
Cdd:TIGR03719 9 RVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ----PGIK--------VGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 88 VKPFAGLSVLDNV------TVGALHRAPNVSA------------AKKHAA--EIVERLG---LGAKREQPASSLTLPD-- 142
Cdd:TIGR03719 77 PQLDPTKTVRENVeegvaeIKDALDRFNEISAkyaepdadfdklAAEQAElqEIIDAADawdLDSQLEIAMDALRCPPwd 156
|
170 180 190
....*....|....*....|....*....|.
gi 1082692222 143 ----------RKRLEVARALATRPELLLLDE 163
Cdd:TIGR03719 157 advtklsggeRRRVALCRLLLSKPDMLLLDE 187
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
30-191 |
4.59e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 45.70 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 30 GAIVGLIGPNGAGKTTIFNMVAGvyAADAGEIvfRG-RRIDGLRPDQVCAAGIGRTFQLVKPFAGLSVLDNVTVGALHRA 108
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAG--RKTAGVI--TGeILINGRPLDKNFQRSTGYVEQQDVHSPNLTVREALRFSALLRG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 109 pnvsaakkhaaeiverlglgakreqpassLTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEAFREINRAeG 188
Cdd:cd03232 109 -----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS-G 158
|
...
gi 1082692222 189 LTI 191
Cdd:cd03232 159 QAI 161
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
15-163 |
6.02e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 15 RGLRAVHD-AWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGR--------------------RIDGLRP 73
Cdd:PRK10636 11 RGVRVLLDnATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqetpalpqpaleyVIDGDRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 74 DQvcaagigrtfQLVKPFAGLSVL-DNVTVGALHRAPNVSAA---KKHAAEIVERLGLGAKR-EQPASSLTLPDRKRLEV 148
Cdd:PRK10636 91 YR----------QLEAQLHDANERnDGHAIATIHGKLDAIDAwtiRSRAASLLHGLGFSNEQlERPVSDFSGGWRMRLNL 160
|
170
....*....|....*
gi 1082692222 149 ARALATRPELLLLDE 163
Cdd:PRK10636 161 AQALICRSDLLLLDE 175
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-226 |
7.59e-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: 46.48 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 2 SAALEVRGVSKSFR-GLRAV-HDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIvfrgrRIDGLRpdqvcAA 79
Cdd:TIGR00957 1282 RGRVEFRNYCLRYReDLDLVlRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI-----IIDGLN-----IA 1351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 80 GIGR---TFQL-VKP-----FAGlSVLDNVTVGALHRAPNVSAAKK--HAAEIVERL--GLGAKREQPASSLTLPDRKRL 146
Cdd:TIGR00957 1352 KIGLhdlRFKItIIPqdpvlFSG-SLRMNLDPFSQYSDEEVWWALElaHLKTFVSALpdKLDHECAEGGENLSVGQRQLV 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 147 EVARALATRPELLLLDEVMAGLrPTECDQMVEAFREiNRAEGLTIMLIEHVMRAVMALAqRIVVLHHGEVIARGAPGEVV 226
Cdd:TIGR00957 1431 CLARALLRKTKILVLDEATAAV-DLETDNLIQSTIR-TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLL 1507
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-222 |
1.11e-05 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 44.79 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 5 LEVRGVSKSFR-GLRAV-HDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVcaagig 82
Cdd:cd03244 3 IEFKNVSLRYRpNLPPVlKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 83 RTFQLVKP-----FAG-----LSVLDNVTVGALHRApnvsAAKKHAAEIVERL--GLGAKREQPASSLTLPDRKRLEVAR 150
Cdd:cd03244 77 RSRISIIPqdpvlFSGtirsnLDPFGEYSDEELWQA----LERVGLKEFVESLpgGLDTVVEEGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082692222 151 ALATRPELLLLDEVMAGLRPtECDQMV-----EAFREInraeglTIMLIEHVMRAVMAlAQRIVVLHHGEVIARGAP 222
Cdd:cd03244 153 ALLRKSKILVLDEATASVDP-ETDALIqktirEAFKDC------TVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-226 |
1.28e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 33 VGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRG-----------RRIDGLRPDQ-VCAAGIGRtFQLvKPFAGLSVLDnv 100
Cdd:PLN03130 1268 VGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmdlRKVLGIIPQApVLFSGTVR-FNL-DPFNEHNDAD-- 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 101 TVGALHRApnvsaakkHAAEIVER--LGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLrPTECDQMVE 178
Cdd:PLN03130 1344 LWESLERA--------HLKDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAV-DVRTDALIQ 1414
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1082692222 179 -AFREINRAegLTIMLIEHVMRAVMAlAQRIVVLHHGEVIARGAPGEVV 226
Cdd:PLN03130 1415 kTIREEFKS--CTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLL 1460
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-216 |
1.38e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.55 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 6 EVRGVSKSFRGlrAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQVCAAGIG--- 82
Cdd:PRK09700 267 EVRNVTSRDRK--KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAyit 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 83 ---------RTFQLVKPFAGLSVLDNVTVGALHRAPNVSAAKKHAAEIVERLGLG-AKREQPASSLTLPDRKRLEVARAL 152
Cdd:PRK09700 345 esrrdngffPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082692222 153 ATRPELLLLDEVMAGLRPTECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLHHGEV 216
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
30-86 |
1.42e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.02 E-value: 1.42e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1082692222 30 GAIVGLIGPNGAGKTTIFNMVAG--VYAADAGEIVFRGRRIDGLRPDQVCAAGIGRTFQ 86
Cdd:CHL00131 33 GEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGIFLAFQ 91
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-214 |
3.37e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 44.41 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 20 VHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVfrgrridglRPDQvcaagiGRTF---QlvKPFaglsv 96
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA---------RPAG------ARVLflpQ--RPY----- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 97 ldnVTVGALHRA---PNVSAAKKHAA--EIVERLGLG--AKR---EQP-ASSLTLPDRKRLEVARALATRPELLLLDEVM 165
Cdd:COG4178 437 ---LPLGTLREAllyPATAEAFSDAElrEALEAVGLGhlAERldeEADwDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1082692222 166 AGLRPTECDQMVEAFREinRAEGLTIMLIEHvmRA-VMALAQRIVVLHHG 214
Cdd:COG4178 514 SALDEENEAALYQLLRE--ELPGTTVISVGH--RStLAAFHDRVLELTGD 559
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-215 |
5.60e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 43.62 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 27 VPQ-GAIVGLIGPNGAGKTTIFNMVAGV-------YAADAG--EIV--FRGRRI----DGLRPDQVCAAgigrtfqlVKP 90
Cdd:COG1245 95 VPKkGKVTGILGPNGIGKSTALKILSGElkpnlgdYDEEPSwdEVLkrFRGTELqdyfKKLANGEIKVA--------HKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 91 ---------FAGlsvldnvTVGALHRAPNvsaAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLL 161
Cdd:COG1245 167 qyvdlipkvFKG-------TVRELLEKVD---ERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1082692222 162 DEVMAGLRPTECDQMVEAFREINRaEGLTIMLIEHVMRAVMALAQRIVVLhHGE 215
Cdd:COG1245 237 DEPSSYLDIYQRLNVARLIRELAE-EGKYVLVVEHDLAILDYLADYVHIL-YGE 288
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
30-196 |
1.17e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 42.65 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 30 GAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDGLRPDQvcaagIGRTFQLVkpFAGLSVLDNVTVGAlhrap 109
Cdd:PRK10522 349 GELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED-----YRKLFSAV--FTDFHLFDQLLGPE----- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 110 NVSAAKKHAAEIVERLGLGAKREQPASSLTLPD-----RKRLEVARALATRPELLLLDEVMAGLRPTecdqmveaFREIN 184
Cdd:PRK10522 417 GKPANPALVEKWLERLKMAHKLELEDGRISNLKlskgqKKRLALLLALAEERDILLLDEWAADQDPH--------FRREF 488
|
170 180
....*....|....*....|
gi 1082692222 185 --------RAEGLTIMLIEH 196
Cdd:PRK10522 489 yqvllpllQEMGKTIFAISH 508
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
37-170 |
1.44e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 41.76 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 37 GPNGAGKTTIFNMVAGVYAADAGEIvfrgrRIDG---LRPDQvcAAGIGRTFQLVKPFAGLSVLDNVT-VGALHRapnvS 112
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQI-----QIDGktaTRGDR--SRFMAYLGHLPGLKADLSTLENLHfLCGLHG----R 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082692222 113 AAKKHAAEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEVMAGLRP 170
Cdd:PRK13543 113 RAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-222 |
1.81e-04 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 41.24 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 18 RAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRIDG-----LR-------PDQVCAAGIGRTf 85
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTipledLRssltiipQDPTLFSGTIRS- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 86 qlvkpfaGLSVLDNVTVGALHRAPNVSAAkkhaaeiverlglgakreqpASSLTLPDRKRLEVARALATRPELLLLDEVM 165
Cdd:cd03369 101 -------NLDPFDEYSDEEIYGALRVSEG--------------------GLNLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 166 AGLrptecDQMVEA-FREINRAE--GLTIMLIEHVMRAVMALAqRIVVLHHGEVIARGAP 222
Cdd:cd03369 154 ASI-----DYATDAlIQKTIREEftNSTILTIAHRLRTIIDYD-KILVMDAGEVKEYDHP 207
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
215-239 |
1.99e-04 |
|
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: 37.62 E-value: 1.99e-04
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-196 |
2.33e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.72 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 29 QGAIVGLIGPNGAGKTTIFNMVAGV-------YAADAG--EIV--FRGRRI----DGLRPDQVCAAgigrtfqlVKP--- 90
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGElipnlgdYEEEPSwdEVLkrFRGTELqnyfKKLYNGEIKVV--------HKPqyv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 91 ------FAGlsvldnvTVGALHRAPNVSAAKKhaaEIVERLGLGAKREQPASSLTLPDRKRLEVARALATRPELLLLDEV 164
Cdd:PRK13409 170 dlipkvFKG-------KVRELLKKVDERGKLD---EVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|..
gi 1082692222 165 MAGLRPTECDQMVEAFREInrAEGLTIMLIEH 196
Cdd:PRK13409 240 TSYLDIRQRLNVARLIREL--AEGKYVLVVEH 269
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
8-229 |
3.13e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 41.10 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 8 RGVSKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGrrIDGLRPDQVCAAGIGRTFQL 87
Cdd:PRK11308 19 RGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG--QDLLKADPEAQKLLRQKIQI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 88 V--KPFAGLSvlDNVTVGALHRAP-----NVSAA--KKHAAEIVERLGLgakreQPASSLTLP------DRKRLEVARAL 152
Cdd:PRK11308 97 VfqNPYGSLN--PRKKVGQILEEPllintSLSAAerREKALAMMAKVGL-----RPEHYDRYPhmfsggQRQRIAIARAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082692222 153 ATRPELLLLDEVMAGLRPTECDQMVEAFREINRAEGLTIMLIEHVMRAVMALAQRIVVLHHGEVIARGAPGEVVRDP 229
Cdd:PRK11308 170 MLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
120-240 |
4.20e-04 |
|
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: 41.15 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 120 EIVERL------GLG-AKREQPASSLTLPDRKRLEVARALATRPE--LLLLDEVMAGLRPTECDQMVEAFREInRAEGLT 190
Cdd:TIGR00630 464 EIRERLgflidvGLDyLSLSRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNT 542
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082692222 191 IMLIEHVMRAvMALAQRIVVL------HHGEVIARGAPGEVVRDPAVL-GCYL-GEET 240
Cdd:TIGR00630 543 LIVVEHDEDT-IRAADYVIDIgpgageHGGEVVASGTPEEILANPDSLtGQYLsGRKK 599
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
125-225 |
4.20e-04 |
|
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: 41.15 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 125 LGLG-AKREQPASSLTLPDRKRLEVARAL---ATRPELLLLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMRa 200
Cdd:TIGR00630 816 VGLGyIRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNLD- 893
|
90 100 110
....*....|....*....|....*....|.
gi 1082692222 201 VMALAQRIVVL------HHGEVIARGAPGEV 225
Cdd:TIGR00630 894 VIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
25-196 |
5.44e-04 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 39.44 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 25 IDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVfrgrridglRPDQvcaagiGRTFQLV-KPFaglsvldnvtvg 103
Cdd:cd03223 22 FEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG---------MPEG------EDLLFLPqRPY------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 104 alhrapnvsaakkhaaeiverLGLGAKREQ---PASS-LTLPDRKRLEVARALATRPELLLLDEVMAGLRPTECDQMVEA 179
Cdd:cd03223 75 ---------------------LPLGTLREQliyPWDDvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170
....*....|....*..
gi 1082692222 180 FREinraEGLTIMLIEH 196
Cdd:cd03223 134 LKE----LGITVISVGH 146
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-68 |
6.31e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.48 E-value: 6.31e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1082692222 26 DVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGRRI 68
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP 63
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
30-163 |
1.30e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.33 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 30 GAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRgrriDGLRpdqvcaagIGRTFQLVKPFAGLSVLDNV------TVG 103
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA----PGIK--------VGYLPQEPQLDPEKTVRENVeegvaeVKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 104 ALHRAPNVSA------------AKKHAA--EIVERLG---LGAKREQPASSLTLPD------------RKRLEVARALAT 154
Cdd:PRK11819 101 ALDRFNEIYAayaepdadfdalAAEQGElqEIIDAADawdLDSQLEIAMDALRCPPwdakvtklsggeRRRVALCRLLLE 180
|
....*....
gi 1082692222 155 RPELLLLDE 163
Cdd:PRK11819 181 KPDMLLLDE 189
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-163 |
1.32e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.77 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 27 VPqGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEI---------VFRGRRIDGLRPDQvcaagigrtfqlvKPFAGLSVL 97
Cdd:PRK10636 336 VP-GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEFLRADE-------------SPLQHLARL 401
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 98 dnvtvgalhrAPNVSAAKkhaaeIVERLG----LGAKREQPASSLTLPDRKRLEVARALATRPELLLLDE 163
Cdd:PRK10636 402 ----------APQELEQK-----LRDYLGgfgfQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDE 456
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
11-66 |
1.89e-03 |
|
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: 38.22 E-value: 1.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1082692222 11 SKSFRGLRAVHDAWIDVPQGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVFRGR 66
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS 67
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
12-48 |
4.11e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.09 E-value: 4.11e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1082692222 12 KSFRGLRAVHdawIDVPQGaIVGLIGPNGAGKTTIFN 48
Cdd:pfam13476 4 ENFRSFRDQT---IDFSKG-LTLITGPNGSGKTTILD 36
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
125-224 |
4.29e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082692222 125 LGLG-AKREQPASSLTLPDRKRLEVARALATrpELL----LLDEVMAGLRPTECDQMVEAFREInRAEGLTIMLIEHVMR 199
Cdd:PRK00635 463 LGLPyLTPERALATLSGGEQERTALAKHLGA--ELIgityILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQ 539
|
90 100 110
....*....|....*....|....*....|.
gi 1082692222 200 aVMALAQRIV------VLHHGEVIARGAPGE 224
Cdd:PRK00635 540 -MISLADRIIdigpgaGIFGGEVLFNGSPRE 569
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
14-48 |
9.09e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.14 E-value: 9.09e-03
10 20 30
....*....|....*....|....*....|....*
gi 1082692222 14 FRGLRAVHDawIDVPQGaIVGLIGPNGAGKTTIFN 48
Cdd:COG0419 10 FRSYRDTET--IDFDDG-LNLIVGPNGAGKSTILE 41
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-63 |
9.38e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 35.81 E-value: 9.38e-03
10 20 30
....*....|....*....|....*....|....*
gi 1082692222 29 QGAIVGLIGPNGAGKTTIFNMVAGVYAADAGEIVF 63
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY 35
|
|
| |
