|
Name |
Accession |
Description |
Interval |
E-value |
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-228 |
6.35e-94 |
|
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: 274.94 E-value: 6.35e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLLLQPAELRAR 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRF--DG---EDITGLPPHRIAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGYVPQGRHIFSQMSVEDNLLIALMAAQD-DRSRAIPEMVFDLFPALYSLRHQRSGELPMEQQQHLALARALVLQPKL 159
Cdd:COG0410 78 LGIGYVPEGRRIFPSLTVEENLLLGAYARRDrAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495377997 160 VILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQLDD 228
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-236 |
3.51e-93 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 272.86 E-value: 3.51e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLLLQPAELRART 81
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRL--DG---EDITKLPPHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 GIGYVPQGRHIFSQMSVEDNLLIAlMAAQDDRSRAIPEMVFDLFPALYSLRHQRSGELPMEQQQHLALARALVLQPKLVI 161
Cdd:TIGR03410 76 GIAYVPQGREIFPRLTVEENLLTG-LAALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 162 LDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQLDDLTVNKWLT 236
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLA 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-228 |
8.36e-90 |
|
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: 263.91 E-value: 8.36e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLLLQPAELRART 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF--DG---RDITGLPPHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 GIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRSRAIPEMVFDLFPALYSLRHQRSGELPMEQQQHLALARALVLQPKLVI 161
Cdd:cd03224 76 GIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 162 LDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQLDD 228
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-225 |
2.81e-52 |
|
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: 169.83 E-value: 2.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLLLQPAELRAR 80
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILF--DG---RDITGLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGYVPQGRHIFSQMSVEDNLLIALMAAQD--------------DRSRAIPEMVFDL--FPALYSLRHQRSGELPMEQQ 144
Cdd:COG0411 79 LGIARTFQNPRLFPELTVLENVLVAAHARLGrgllaallrlprarREEREARERAEELleRVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 145 QHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVA 224
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
.
gi 495377997 225 Q 225
Cdd:COG0411 239 E 239
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-225 |
3.29e-49 |
|
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: 161.07 E-value: 3.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSmtWQEDGappEDLLLQPAELRART 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGS--VLFDG---EDITGLPPHEIARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 GIGYVPQGRHIFSQMSVEDNLLIALMAAQD---------DRSRAIPEMVFDL--FPALYSLRHQRSGELPMEQQQHLALA 150
Cdd:cd03219 76 GIGRTFQIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELleRVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 151 RALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQ 225
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-233 |
6.05e-46 |
|
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: 153.09 E-value: 6.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLllqpaELRAR 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI--DGEDVRKE-----PREAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGYVPQGRHIFSQMSVEDNL--LIALMAAQDDRSRAIPEMVFDLFpALYSLRHQRSGELPMEQQQHLALARALVLQPK 158
Cdd:COG4555 74 RQIGVLPDERGLYDRLTVRENIryFAELYGLFDEELKKRIEELIELL-GLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 159 LVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQLDDLTVNK 233
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-226 |
6.10e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 150.21 E-value: 6.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDlllQPAELRARt 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRV--LGEDVAR---DPAEVRRR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 gIGYVPQGRHIFSQMSVEDNLLI--ALMAAQDDRSRAIPEMVFDLFpALYSLRHQRSGELPMEQQQHLALARALVLQPKL 159
Cdd:COG1131 75 -IGYVPQEPALYPDLTVRENLRFfaRLYGLPRKEARERIDELLELF-GLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 160 VILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-228 |
5.88e-41 |
|
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: 139.94 E-value: 5.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMtwQEDGAPPEDLllQPAELRA-R 80
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEV--LIDGEDISGL--SEAELYRlR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGYVPQGRHIFSQMSVEDNllIALM-----AAQDDRSRAIPEMVFDLFpALYSLRHQRSGELPMEQQQHLALARALVL 155
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFEN--VAFPlrehtRLSEEEIREIVLEKLEAV-GLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495377997 156 QPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQLDD 228
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-218 |
4.19e-40 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 138.09 E-value: 4.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLLLQPAELRAR 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVF--DG---KDITDWQTAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRSRAIPEMVFDLFPALYSLRHQRSGELPMEQQQHLALARALVLQPKLV 160
Cdd:PRK11614 80 EAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 161 ILDEPTEGMSPWLEEEMGNLIRRLnREYGLTILLLEQHVSFVRRVADYFLLLHRGRNV 218
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-216 |
3.85e-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: 133.29 E-value: 3.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDlllQPAELRARt 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV--LGKDIKK---EPEEVKRR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 gIGYVPQGRHIFSQMSVEDNLlialmaaqddrsraipemvfdlfpaLYSLrhqrsGelpmeQQQHLALARALVLQPKLVI 161
Cdd:cd03230 75 -IGYLPEEPSLYENLTVRENL-------------------------KLSG-----G-----MKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 162 LDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-228 |
2.64e-38 |
|
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: 133.18 E-value: 2.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLL-LQPAELRA 79
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV--DG---QDITgLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 80 -RTGIGYVPQGRHIFSQMSVEDNLLIALM-------AAQDDRSRAIPEMV-----FDLFPAlyslrhqrsgELP--MeqQ 144
Cdd:COG1127 80 lRRRIGMLFQGGALFDSLTVFENVAFPLRehtdlseAEIRELVLEKLELVglpgaADKMPS----------ELSggM--R 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 145 QHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVA 224
Cdd:COG1127 148 KRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPE 227
|
....
gi 495377997 225 QLDD 228
Cdd:COG1127 228 ELLA 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-225 |
5.32e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.52 E-value: 5.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEdlllqpaelRAR 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRL--FGKPPR---------RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGYVPQgRHIFSQ---MSVED----------NLLIALMAAQDDRSRAIPEMVfdlfpALYSLRHQRSGELPMEQQQHL 147
Cdd:COG1121 75 RRIGYVPQ-RAEVDWdfpITVRDvvlmgrygrrGLFRRPSRADREAVDEALERV-----GLEDLADRPIGELSGGQQQRV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 148 ALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRnVAHGKVAQ 225
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGL-VAHGPPEE 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-221 |
3.43e-36 |
|
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: 126.88 E-value: 3.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 11 YGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEdlllqpaelRARTGIGYVPQgR 90
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV--FGKPLE---------KERKRIGYVPQ-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 91 HIFSQ---MSVEDNLLIALMAA--------QDDRSRAIP--EMVfdlfpALYSLRHQRSGELPMEQQQHLALARALVLQP 157
Cdd:cd03235 77 RSIDRdfpISVRDVVLMGLYGHkglfrrlsKADKAKVDEalERV-----GLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495377997 158 KLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRgRNVAHG 221
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNR-TVVASG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-221 |
1.16e-35 |
|
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: 126.08 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFY----GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQedgapPEDLLLQPAE 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD-----GKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 77 LRA--RTGIGYVPQgrHIFS----QMSVEDNLLIALMAAQDDRSRAI--------------PEMVFDLFPalyslrHQRS 136
Cdd:cd03257 76 LRKirRKEIQMVFQ--DPMSslnpRMTIGEQIAEPLRIHGKLSKKEArkeavllllvgvglPEEVLNRYP------HELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 137 GelpmEQQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:cd03257 148 G----GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
....*
gi 495377997 217 NVAHG 221
Cdd:cd03257 224 IVEEG 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-228 |
1.21e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 124.01 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVN-QFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPedLLLQPAELRA 79
Cdd:COG3638 2 MLELRNLSkRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILV--DGQDV--TALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 80 -RTGIGYVPQGRHIFSQMSVEDNLLIALMAAqddrsRAIPEMVFDLFP------ALYSLR--------HQRSGELPMEQQ 144
Cdd:COG3638 78 lRRRIGMIFQQFNLVPRLSVLTNVLAGRLGR-----TSTWRSLLGLFPpedrerALEALErvgladkaYQRADQLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 145 QHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVA 224
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPA 232
|
....
gi 495377997 225 QLDD 228
Cdd:COG3638 233 ELTD 236
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-226 |
1.31e-34 |
|
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: 123.46 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQN----HILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDL-LLQPA 75
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLV--DG---TDLtLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 76 ELR-ARTGIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRSRaIPEMVFDL--FPALYSLRHQRSGELPMEQQQHLALARA 152
Cdd:cd03258 76 ELRkARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAE-IEERVLELleLVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495377997 153 LVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-216 |
2.91e-34 |
|
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: 121.14 E-value: 2.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLLLQPAELRARt 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI--DGEDLTDLEDELPPLRRR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 gIGYVPQGRHIFSQMSVEDNLLIALmaaqddrsraipemvfdlfpalyslrhqrSGElpmeQQQHLALARALVLQPKLVI 161
Cdd:cd03229 78 -IGMVFQDFALFPHLTVLENIALGL-----------------------------SGG----QQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 162 LDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-221 |
5.27e-34 |
|
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: 121.47 E-value: 5.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLLLQPAELRart 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI--DG---RDVTGVPPERR--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 GIGYVPQGRHIFSQMSVEDNLLIAL------MAAQDDRSRAIPEMVfDLFPALYSLRHQRSGElpmeQQQHLALARALVL 155
Cdd:cd03259 73 NIGMVFQDYALFPHLTVAENIAFGLklrgvpKAEIRARVRELLELV-GLEGLLNRYPHELSGG----QQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 156 QPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-226 |
5.28e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 123.68 E-value: 5.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappedlllQPAELRAR 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW--DG--------EPLDPEDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGYVPQGRHIFSQMSVEDNL--LIAL--MAAQDDRSRAipEMVFDLFpALYSLRHQRSGELPMEQQQHLALARALVLQ 156
Cdd:COG4152 71 RRIGYLPEERGLYPKMKVGEQLvyLARLkgLSKAEAKRRA--DEWLERL-GLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 157 PKLVILDEPTEGMSP----WLEEEmgnlIRRLNREyGLTILL----LEQhvsfVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:COG4152 148 PELLILDEPFSGLDPvnveLLKDV----IRELAAK-GTTVIFsshqMEL----VEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-226 |
5.63e-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: 5.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLllqPAELRAR 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLL--DGRDLASL---SRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TgIGYVPQGRHIFSQMSVEDnlLIAL--------MAAQDDRSRAIPEMVFDLFpALYSLRHQRSGELPMEQQQHLALARA 152
Cdd:COG1120 76 R-IAYVPQEPPAPFGLTVRE--LVALgryphlglFGRPSAEDREAVEEALERT-GLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495377997 153 LVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-226 |
1.38e-33 |
|
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: 121.06 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQ----NHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPpedllLQPAE 76
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTF--DGRP-----VTRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 77 LRA-RTGIGYVPQgrHIFS----QMSVEDNLLIALMAA-QDDRSRAIPEMV--FDLFPALYSLR-HQRSGElpmeQQQHL 147
Cdd:COG1124 74 RKAfRRRVQMVFQ--DPYAslhpRHTVDRILAEPLRIHgLPDREERIAELLeqVGLPPSFLDRYpHQLSGG----QRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495377997 148 ALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-216 |
1.39e-33 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 120.26 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 3 SLRSVNQFY--GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLllQPAELRAR 80
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV--DGKDLTKL--SLKELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 tgIGYVPQG-RHIFSQMSVEDNLLIALMAAQDDRSRaIPEMVFDLFPA--LYSLRHQRSGELPMEQQQHLALARALVLQP 157
Cdd:cd03225 77 --VGLVFQNpDDQFFGPTVEEEVAFGLENLGLPEEE-IEERVEEALELvgLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495377997 158 KLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
2.19e-33 |
|
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: 125.79 E-value: 2.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQN-----HILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDllLQPA 75
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF--DGKDLTK--LSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 76 ELRA-RTGIGYVPQG--RHIFSQMSVEDNLLIALMAAQDDRSRAIPEMVFDLFPAL---YSLRHQRSGELPMEQQQHLAL 149
Cdd:COG1123 336 SLRElRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVglpPDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 150 ARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-226 |
2.25e-33 |
|
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: 119.98 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPIN-----SGSMTWqeDGAPPEDLLLQPAE 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLL--DGKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 77 LRARtgIGYVPQGRHIFSqMSVEDNLLIAL-------MAAQDDRSRAIPEMVfDLFPALysLRHQRSGELPMEQQQHLAL 149
Cdd:cd03260 79 LRRR--VGMVFQKPNPFP-GSIYDNVAYGLrlhgiklKEELDERVEEALRKA-ALWDEV--KDRLHALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 150 ARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYglTILL----LEQhvsfVRRVADYFLLLHRGRNVAHGKVAQ 225
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIvthnMQQ----AARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 495377997 226 L 226
Cdd:cd03260 227 I 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-226 |
1.25e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 118.56 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLLLQPAELRA- 79
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITV--DG---EDLTDSKKDINKl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 80 RTGIGYVPQGRHIFSQMSVEDNLLIALMAAQ-------DDRSRAIPEMV-----FDLFPAlyslrhQRSGElpmeQQQHL 147
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLAPIKVKkmskaeaEERAMELLERVgladkADAYPA------QLSGG----QQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495377997 148 ALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
15-228 |
2.05e-32 |
|
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: 118.05 E-value: 2.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 15 HILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEdgappEDLL-LQPAELRA-RTGIGYVPQGRHI 92
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDG-----TDINkLKGKALRQlRRQIGMIFQQFNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 93 FSQMSVEDNLLIALMAAqddRS--RAIpemvFDLFP------ALYSLR--------HQRSGELPMEQQQHLALARALVLQ 156
Cdd:cd03256 90 IERLSVLENVLSGRLGR---RStwRSL----FGLFPkeekqrALAALErvglldkaYQRADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495377997 157 PKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQLDD 228
Cdd:cd03256 163 PKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTD 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
1.07e-31 |
|
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: 121.16 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFY--GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPIN---SGSMTWQEdgappEDLLLQPA 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDG-----RDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 76 ELRARTgIGYVPQ-GRHIFSQMSVEDNLLIALMAAQDDRsRAIPEMVFDLFPA--LYSLRHQRSGELPMEQQQHLALARA 152
Cdd:COG1123 79 ALRGRR-IGMVFQdPMTQLNPVTVGDQIAEALENLGLSR-AEARARVLELLEAvgLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495377997 153 LVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-233 |
1.18e-31 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 116.24 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNH-ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTW--QEDGAppedllLQPAEL 77
Cdd:TIGR02315 1 MLEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLegTDITK------LRGKKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 78 R-ARTGIGYVPQGRHIFSQMSVEDNLLIALMAAQDdrsrAIPeMVFDLFP------ALYSLR--------HQRSGELPME 142
Cdd:TIGR02315 75 RkLRRRIGMIFQHYNLIERLTVLENVLHGRLGYKP----TWR-SLLGRFSeedkerALSALErvgladkaYQRADQLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 143 QQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGK 222
Cdd:TIGR02315 150 QQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGA 229
|
250
....*....|.
gi 495377997 223 VAQLDDLTVNK 233
Cdd:TIGR02315 230 PSELDDEVLRH 240
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-226 |
2.17e-31 |
|
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: 114.95 E-value: 2.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEdgappEDLLLQPAELRART 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG-----QDITKLPMHKRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 GIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRSRAIP--EMVFDLFpALYSLRHQRSGELPMEQQQHLALARALVLQPKL 159
Cdd:cd03218 76 GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEklEELLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 160 VILDEPTEGMSPWLEEEMGNLIRRLnREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-226 |
2.97e-31 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 114.74 E-value: 2.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFY-GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLllQPAELRAR 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLV--DGKDITKK--NLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 tgIGYVPQ--GRHIFSqMSVEDNLLIALM------AAQDDRSRAIPEMVfdlfpALYSLRHQRSGELPMEQQQHLALARA 152
Cdd:COG1122 77 --VGLVFQnpDDQLFA-PTVEEDVAFGPEnlglprEEIRERVEEALELV-----GLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495377997 153 LVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-216 |
9.49e-31 |
|
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: 111.18 E-value: 9.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 3 SLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLLLQpaelRARTG 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI--DGKDIAKLPLE----ELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 83 IGYVPQgrhiFSQmsvednllialmaaqddrsraipemvfdlfpalyslrhqrsGelpmeQQQHLALARALVLQPKLVIL 162
Cdd:cd00267 75 IGYVPQ----LSG-----------------------------------------G-----QRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495377997 163 DEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-216 |
9.17e-30 |
|
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: 109.01 E-value: 9.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYG--QNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLllQPAELRA 79
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI--DGVDLRDL--DLESLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 80 RtgIGYVPQGRHIFSqMSVEDNLLialmaaqddrsraipemvfdlfpalyslrhqrSGElpmeQQQHLALARALVLQPKL 159
Cdd:cd03228 77 N--IAYVPQDPFLFS-GTIRENIL--------------------------------SGG----QRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 160 VILDEPTEGMSPWLEEEMGNLIRRLNReyGLTILLLEQHVSFVRRvADYFLLLHRGR 216
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-220 |
1.11e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 108.67 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEdlLLQPAELRARt 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV--DGKEVS--FASPRDARRA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 GIGYVPQgrhifsqmsvednllialmaaqddrsraipemvfdlfpalyslrhqrsgeLPMEQQQHLALARALVLQPKLVI 161
Cdd:cd03216 76 GIAMVYQ--------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495377997 162 LDEPTEGMSPWLEEEMGNLIRRLnREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAH 220
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-216 |
1.98e-29 |
|
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: 109.54 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLLLQPAELRA-R 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII--DG---LKLTDDKKNINElR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGYVPQGRHIFSQMSVEDNLLIALM-------AAQDDRSRAIPEMVfdlfpALYSLRHQRSGELPMEQQQHLALARAL 153
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLAPIkvkgmskAEAEERALELLEKV-----GLADKADAYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495377997 154 VLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-216 |
2.43e-29 |
|
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: 109.50 E-value: 2.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQN----HILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQE---DGAPPEDLllqp 74
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdiSKLSEKEL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 75 AELRARTgIGYVPQGRHIFSQMSVEDNLLIALMAAQDdRSRAIPEMVFDLFPA--LYSLRHQRSGELPMEQQQHLALARA 152
Cdd:cd03255 77 AAFRRRH-IGFVFQSFNLLPDLTALENVELPLLLAGV-PKKERRERAEELLERvgLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 153 LVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLleqhVSFVRRVADYF---LLLHRGR 216
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVV----VTHDPELAEYAdriIELRDGK 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-194 |
3.89e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 108.98 E-value: 3.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQN----HILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAP----PEDLLl 72
Cdd:COG1136 4 LLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLI--DGQDisslSEREL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 73 qpAELRARTgIGYVPQGRHIFSQMSVEDNLLIALMAA----QDDRSRAipEMVFDLFpALYSLRHQRSGELPMEQQQHLA 148
Cdd:COG1136 81 --ARLRRRH-IGFVFQFFNLLPELTALENVALPLLLAgvsrKERRERA--RELLERV-GLGDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 149 LARALVLQPKLVILDEPTegmspwleeemGNL-----------IRRLNREYGLTILL 194
Cdd:COG1136 155 IARALVNRPKLILADEPT-----------GNLdsktgeevlelLRELNRELGTTIVM 200
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-237 |
5.33e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 108.69 E-value: 5.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNqfYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEdgappEDLLLQPAELRar 80
Cdd:COG3840 1 MLRLDDLT--YRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG-----QDLTALPPAER-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 tgigyvP-----QGRHIFSQMSVEDNLLIA------LMAAQDDRSRAIPEMVfdlfpALYSLRHQRSGELPMEQQQHLAL 149
Cdd:COG3840 72 ------PvsmlfQENNLFPHLTVAQNIGLGlrpglkLTAEQRAQVEQALERV-----GLAGLLDRLPGQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 150 ARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQLDDL 229
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDG 220
|
....*...
gi 495377997 230 TVNKWLTA 237
Cdd:COG3840 221 EPPPALAA 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-221 |
6.74e-29 |
|
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: 108.14 E-value: 6.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPpedllLQPAelrART 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF--DGKP-----LDIA---ARN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 GIGYVPQGRHIFSQMSVEDNLL----IALMAAQDDRSRAipEMVFDLFpALYSLRHQRSGELPMEQQQHLALARALVLQP 157
Cdd:cd03269 71 RIGYLPEERGLYPKMKVIDQLVylaqLKGLKKEEARRRI--DEWLERL-ELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495377997 158 KLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-221 |
9.52e-29 |
|
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: 106.75 E-value: 9.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 3 SLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLllqPAELRARTg 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL--DGKDLASL---SPKELARK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 83 IGYVPQgrhifsqmsvednlLIALMAAQDdrsraipemvfdlfpalysLRHQRSGELPMEQQQHLALARALVLQPKLVIL 162
Cdd:cd03214 75 IAYVPQ--------------ALELLGLAH-------------------LADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495377997 163 DEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-212 |
2.22e-28 |
|
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: 106.57 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 9 QFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDGAPPEDlllqpaelRARTgIGYVPQ 88
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE--------RRKS-IGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 89 --GRHIFSQmSVEDNLLIALMAAQDDRSRAipEMVFDLFpALYSL--RHQRSgeLPMEQQQHLALARALVLQPKLVILDE 164
Cdd:cd03226 79 dvDYQLFTD-SVREELLLGLKELDAGNEQA--ETVLKDL-DLYALkeRHPLS--LSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495377997 165 PTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLL 212
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-166 |
3.17e-28 |
|
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: 104.65 E-value: 3.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPpedlLLQPAELRARTGIGYVPQGRHIFSQMSV 98
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILL--DGQD----LTDDERKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 99 EDNLLIAL-------MAAQDDRSRAIPEmvFDLFPALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPT 166
Cdd:pfam00005 77 RENLRLGLllkglskREKDARAEEALEK--LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-226 |
2.12e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 107.09 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQN----HILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCimgrlpIN------SGSMTWqeDGappEDL 70
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRC------INllerptSGSVLV--DG---VDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 71 L-LQPAELR-ARTGIGYVPQGRHIFSQMSVEDN----LLIALMAAQDDRSRAIP--EMVfDL------FPAlyslrhQRS 136
Cdd:COG1135 70 TaLSERELRaARRKIGMIFQHFNLLSSRTVAENvalpLEIAGVPKAEIRKRVAEllELV-GLsdkadaYPS------QLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 137 GelpmEQQQHLALARALVLQPKLVILDEPTEGMSP-----WLEeemgnLIRRLNREYGLTILLL--EQHVsfVRRVADYF 209
Cdd:COG1135 143 G----GQKQRVGIARALANNPKVLLCDEATSALDPettrsILD-----LLKDINRELGLTIVLIthEMDV--VRRICDRV 211
|
250
....*....|....*..
gi 495377997 210 LLLHRGRNVAHGKVAQL 226
Cdd:COG1135 212 AVLENGRIVEQGPVLDV 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-194 |
7.52e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 105.57 E-value: 7.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLLLQPAELRar 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL--DG---RDVTGLPPEKR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 tGIGYVPQGRHIFSQMSVEDNLLIALM------AAQDDRSRAIPEMVfdlfpALYSLRHQRSGELPMEQQQHLALARALV 154
Cdd:COG3842 78 -NVGMVFQDYALFPHLTVAENVAFGLRmrgvpkAEIRARVAELLELV-----GLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495377997 155 LQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILL 194
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIY 191
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-226 |
1.06e-26 |
|
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: 102.58 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYG--QNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTwqedgAPPEDLLLQPAElrA 79
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAY-----INGYSIRTDRKA--A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 80 RTGIGYVPQGRHIFSQMSVEDNLLIalMAaqddRSRAIP--------EMVFDLFpALYSLRHQRSGELPMEQQQHLALAR 151
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHLRF--YA----RLKGLPkseikeevELLLRVL-GLTDKANKRARTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 152 ALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNReyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-221 |
1.89e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 102.66 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 11 YGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEdgappEDLLLQPAELRARTGIGYVPQGR 90
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD-----EDISLLPLHARARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 91 HIFSQMSVEDNLLIALMAAQDDRSRAIPEMVFDLFPALY--SLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEG 168
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHieHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495377997 169 MSPWLEEEMGNLIRRLnREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:PRK10895 168 VDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHG 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-193 |
2.65e-26 |
|
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: 101.02 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEdgappEDLLLQPAELRAR 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG-----EPIRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 tgIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRSRAIPEMVFDLFpALYSLRHQRSGELPMEQQQHLALARALVLQPKLV 160
Cdd:COG4133 77 --LAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAV-GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|...
gi 495377997 161 ILDEPTEGMSPWLEEEMGNLIRRLNREYGLTIL 193
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-221 |
3.26e-26 |
|
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: 101.12 E-value: 3.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTcTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLLLQPAELRARt 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRI--DG---QDVLKQPQKLRRR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 gIGYVPQGRHIFSQMSVEDNL--LIALMAAQDDRSRAIPEMVFDLFpALYSLRHQRSGELPMEQQQHLALARALVLQPKL 159
Cdd:cd03264 74 -IGYLPQEFGVYPNFTVREFLdyIAWLKGIPSKEVKARVDEVLELV-NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 160 VILDEPTEGMSPwlEEEMG--NLIRRLNREyglTILLLEQH-VSFVRRVADYFLLLHRGRNVAHG 221
Cdd:cd03264 152 LIVDEPTAGLDP--EERIRfrNLLSELGED---RIVILSTHiVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-227 |
3.66e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.49 E-value: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEdlLLQPAELRAR 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL--DGEPVR--FRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 tGIGYVPQGRHIFSQMSVEDNLLIALM---------AAQDDRSRAIPEMV-FDLFPalyslrHQRSGELPMEQQQHLALA 150
Cdd:COG1129 80 -GIAIIHQELNLVPNLSVAENIFLGREprrgglidwRAMRRRARELLARLgLDIDP------DTPVGDLSVAQQQLVEIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 151 RALVLQPKLVILDEPTEGMSpwlEEEMGNL---IRRLnREYGLTILL----LEQhvsfVRRVADYFLLLHRGRNVAHGKV 223
Cdd:COG1129 153 RALSRDARVLILDEPTASLT---EREVERLfriIRRL-KAQGVAIIYishrLDE----VFEIADRVTVLRDGRLVGTGPV 224
|
....
gi 495377997 224 AQLD 227
Cdd:COG1129 225 AELT 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-221 |
4.42e-26 |
|
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: 100.75 E-value: 4.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMT-WQEDGAPPEDLLLQpaelrar 80
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfDGKSYQKNIEALRR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 tgIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRSRA--IPEMVfdlfpALYSLRHQRSGELPMEQQQHLALARALVLQPK 158
Cdd:cd03268 74 --IGALIEAPGFYPNLTARENLRLLARLLGIRKKRIdeVLDVV-----GLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495377997 159 LVILDEPTEGMSPWLEEEMGNLIRRLnREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-223 |
4.72e-26 |
|
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: 101.26 E-value: 4.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHiLWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLLLQPAELRart 81
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL--NG---KDITNLPPEKR--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 GIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRSRaIPEMVFDL--FPALYSLRHQRSGELPMEQQQHLALARALVLQPKL 159
Cdd:cd03299 72 DISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKE-IERKVLEIaeMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495377997 160 VILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKV 223
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKP 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-221 |
1.41e-25 |
|
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: 99.36 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQN----HILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAppeDLLLQPAE 76
Cdd:cd03266 1 MITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV--DGF---DVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 77 LRARtgIGYVPQGRHIFSQMSVEDNLLI--ALMAAQDDRSRAIPEMVFDLFpALYSLRHQRSGELPMEQQQHLALARALV 154
Cdd:cd03266 76 ARRR--LGFVSDSTGLYDRLTARENLEYfaGLYGLKGDELTARLEELADRL-GMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 155 LQPKLVILDEPTEGMSPWLEEEMGNLIRRLnREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-226 |
1.84e-25 |
|
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: 99.37 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 11 YGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTwqedgAPPEDLLLQPAELRARtgIGYVPQGR 90
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-----VAGHDVVREPREVRRR--IGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 91 HIFSQMSVEDNLLI--ALMAAQDDRSRAIPEMVFDLFpALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEG 168
Cdd:cd03265 83 SVDDELTGWENLYIhaRLYGVPGAERRERIDELLDFV-GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 169 MSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-226 |
2.39e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 99.33 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLLLQPAELRAR 80
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL--DG---EDITHLPMHKRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRS--RAIPEMVFDLFpALYSLRHQRSGELPMEQQQHLALARALVLQPK 158
Cdd:COG1137 78 LGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKerEERLEELLEEF-GITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495377997 159 LVILDEPTEGMSPWLEEEMGNLIRRLnREYGLTILLLEQHvsfVR---RVADYFLLLHRGRNVAHGKVAQL 226
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHN---VRetlGICDRAYIISEGKVLAEGTPEEI 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-226 |
3.55e-25 |
|
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: 102.91 E-value: 3.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNH-ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLllQPAELRAR 80
Cdd:COG4988 337 IELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI--NGVDLSDL--DPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 tgIGYVPQGRHIFsQMSVEDNLLIALMAAQDDRSRAIPEMVF--DLFPALYSLRHQRSGE----LPMEQQQHLALARALV 154
Cdd:COG4988 413 --IAWVPQNPYLF-AGTIRENLRLGRPDASDEELEAALEAAGldEFVAALPDGLDTPLGEggrgLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495377997 155 LQPKLVILDEPTEGMSPWLEEEMGNLIRRLNReyGLTILLLEQHVSFVRRvADYFLLLHRGRNVAHGKVAQL 226
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEEL 558
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-226 |
5.32e-25 |
|
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: 102.54 E-value: 5.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLllQPAELRARtgIGYVPQGRHIFSq 95
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL--GGVDLRDL--DEDDLRRR--IAVVPQRPHLFD- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 MSVEDNLLIALMAAQDDRSRAIPEMVfDLFPALYSLR---HQRSGE----LPMEQQQHLALARALVLQPKLVILDEPTEG 168
Cdd:COG4987 423 TTLRENLRLARPDATDEELWAALERV-GLGDWLAALPdglDTWLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEG 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 169 MSPWLEEEMGNLIRRLNReyGLTILLLEQHVSFVRRvADYFLLLHRGRNVAHGKVAQL 226
Cdd:COG4987 502 LDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEEL 556
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-226 |
8.45e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.52 E-value: 8.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 20 VDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLllqPAELRARTGIGYVPQGRHIFSQMSVE 99
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILL--RGQHIEGL---PGHQIARMGVVRTFQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 100 DNLLIA------------LMAAQDDR---SRAIPEMVFDL-FPALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILD 163
Cdd:PRK11300 99 ENLLVAqhqqlktglfsgLLKTPAFRraeSEALDRAATWLeRVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495377997 164 EPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-226 |
8.64e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.86 E-value: 8.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTwqEDGAPPEDLLLQPAELRAR 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLI--VDGLKVNDPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIgyVPQGRHIFSQMSVEDNLLI-------ALMAAQDDRSRAIPEMVfdlfpALYSLRHQRSGELPMEQQQHLALARAL 153
Cdd:PRK09493 79 AGM--VFQQFYLFPHLTALENVMFgplrvrgASKEEAEKQARELLAKV-----GLAERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495377997 154 VLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-216 |
2.34e-24 |
|
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: 96.54 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLllqPAELRart 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL--DGKDITNL---PPHKR--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 GIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRS---RAIPEMVfDLFpALYSLRHQRSGELPMEQQQHLALARALVLQPK 158
Cdd:cd03300 73 PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAeikERVAEAL-DLV-QLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 159 LVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-226 |
3.89e-24 |
|
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: 96.14 E-value: 3.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 5 RSVNQFY-GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLLLqpAELRARtgI 83
Cdd:cd03254 6 ENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILI--DGIDIRDISR--KSLRSM--I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 84 GYVPQGRHIFSQmSVEDNLLIALMAAQDDR-SRAIPEMVFDLF-----PALYSLRHQRSGELPMEQQQHLALARALVLQP 157
Cdd:cd03254 80 GVVLQDTFLFSG-TIMENIRLGRPNATDEEvIEAAKEAGAHDFimklpNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495377997 158 KLVILDEPTEGMSPWLEEEMGNLIRRLNReyGLTILLLEQHVSFVRRvADYFLLLHRGRNVAHGKVAQL 226
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-226 |
4.99e-24 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 96.21 E-value: 4.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCI--MGRLPIN---SGSMTWqeDGAPPEDLLLQPAE 76
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrMNDLVPGvriEGKVLF--DGQDIYDKKIDVVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 77 LRARtgIGYVPQGRHIFSqMSVEDNLLIALMAAQ-------DDRSR------AIPEMVFD-LFPALYSLrhqrSGElpme 142
Cdd:TIGR00972 80 LRRR--VGMVFQKPNPFP-MSIYDNIAYGPRLHGikdkkelDEIVEeslkkaALWDEVKDrLHDSALGL----SGG---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 143 QQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYglTILLLEQHVSFVRRVADYFLLLHRGRNVAHGK 222
Cdd:TIGR00972 149 QQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFYDGELVEYGP 226
|
....
gi 495377997 223 VAQL 226
Cdd:TIGR00972 227 TEQI 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-228 |
5.13e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 96.53 E-value: 5.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDGAPPEDLL-LQPAELR- 78
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYaLSEAERRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 79 -ARTGIGYVPQGRHIFSQMSVE--DNLLIALMAA-----QDDRSRA--------IPEMVFDLFPALYslrhqrSGELpme 142
Cdd:PRK11701 86 lLRTEWGFVHQHPRDGLRMQVSagGNIGERLMAVgarhyGDIRATAgdwlerveIDAARIDDLPTTF------SGGM--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 143 qQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGK 222
Cdd:PRK11701 157 -QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGL 235
|
....*..
gi 495377997 223 VAQ-LDD 228
Cdd:PRK11701 236 TDQvLDD 242
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
19-226 |
1.70e-23 |
|
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: 96.71 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGS-----MTWQeDGAPPEDLllqPAELRArtgIGYVPQGRHIF 93
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRirlggEVLQ-DSARGIFL---PPHRRR---IGYVFQEARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 94 SQMSVEDNLLIALMAAQDDRSRAIPEMVFDLFpALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEGMSPWL 173
Cdd:COG4148 90 PHLSVRGNLLYGRKRAPRAERRISFDEVVELL-GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 174 EEEMGNLIRRLNREYGLTILLleqhVSF----VRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:COG4148 169 KAEILPYLERLRDELDIPILY----VSHsldeVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-216 |
1.71e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 93.96 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNH-ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDL-LLQPAELR 78
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLV--NG---QDLsRLKRREIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 79 A-RTGIGYVPQGRHIFSQMSVEDNLLIALMAA---QDDRSRAIPEmVFDLFpalySLRHqRSGELPME----QQQHLALA 150
Cdd:COG2884 76 YlRRRIGVVFQDFRLLPDRTVYENVALPLRVTgksRKEIRRRVRE-VLDLV----GLSD-KAKALPHElsggEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 151 RALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-226 |
4.59e-23 |
|
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: 97.21 E-value: 4.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDllLQPAELRARtgIGYVPQGRHIFSq 95
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI--DGIDLRQ--IDPASLRRQ--IGVVLQDVFLFS- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 MSVEDNLLIALMAAQDDRSRAIPEMVfDLFPALYSLRHQ-------RSGELPMEQQQHLALARALVLQPKLVILDEPTEG 168
Cdd:COG2274 563 GTIRENITLGDPDATDEEIIEAARLA-GLHDFIEALPMGydtvvgeGGSNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 169 MSPWLEEEMGNLIRRLNReyGLTILLLEQHVSFVRRvADYFLLLHRGRNVAHGKVAQL 226
Cdd:COG2274 642 LDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-194 |
7.87e-23 |
|
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: 92.15 E-value: 7.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQN----HILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEdlllqpael 77
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLV--DGEPVT--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 78 RARTGIGYVPQGRHIFSQMSVEDNLLIALMAA--QDDRSRAIPEMVFDLFPaLYSLRHQRSGELPMEQQQHLALARALVL 155
Cdd:cd03293 70 GPGPDRGYVFQQDALLPWLTVLDNVALGLELQgvPKAEARERAEELLELVG-LSGFENAYPHQLSGGMRQRVALARALAV 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 495377997 156 QPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILL 194
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLL 187
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-216 |
1.75e-22 |
|
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: 90.57 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEdlLLQPAELRARtGIGYVPQGRH---IFSQ 95
Cdd:cd03215 18 DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITL--DGKPVT--RRSPRDAIRA-GIAYVPEDRKregLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 MSVEDNLlialmaaqddrsraipemvfdlfpalySLRHQRSGelpmEQQQHLALARALVLQPKLVILDEPTEGMSPWLEE 175
Cdd:cd03215 93 LSVAENI---------------------------ALSSLLSG----GNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495377997 176 EMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:cd03215 142 EIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-194 |
1.80e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 92.07 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFY----GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEdlllqpae 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLV--DGKPVT-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 77 lRARTGIGYVPQGRHIFSQMSVEDNLLIAL------MAAQDDRSRAIPEMV----F-DLFPalyslrHQRSGElpmeQQQ 145
Cdd:COG1116 77 -GPGPDRGVVFQEPALLPWLTVLDNVALGLelrgvpKAERRERARELLELVglagFeDAYP------HQLSGG----MRQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 146 HLALARALVLQPKLVILDEP-------TegmspwlEEEMGNLIRRLNREYGLTILL 194
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPfgaldalT-------RERLQDELLRLWQETGKTVLF 194
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-221 |
2.44e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 91.61 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCI-------MGRLPINSGSMTWQEDGAPPEDLLLqp 74
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIAGHQFDFSQKPSEKAIRLL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 75 aelraRTGIGYVPQGRHIFSQMSVEDNLL-----IALMAAQDDRSRAIPemvfdlfpALYSLRHQ-RSGELPME----QQ 144
Cdd:COG4161 81 -----RQKVGMVFQQYNLWPHLTVMENLIeapckVLGLSKEQAREKAMK--------LLARLRLTdKADRFPLHlsggQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 145 QHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNrEYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:COG4161 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-228 |
5.79e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.20 E-value: 5.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQedGAPpedlllQPAELR-AR 80
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVL--GVP------VPARARlAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGYVPQGRHIFSQMSVEDNLLI----ALMAAQDDRSrAIPEMVfdLFPALYSLRHQRSGELPMEQQQHLALARALVLQ 156
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVfgryFGMSTREIEA-VIPSLL--EFARLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 157 PKLVILDEPTEGMSP------WleEEMGNLIRRlnreyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQLDD 228
Cdd:PRK13536 191 PQLLILDEPTTGLDPharhliW--ERLRSLLAR-----GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-224 |
6.15e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 92.17 E-value: 6.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQN----HILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCI-------MGRLPInsgsmtwqeDGappED 69
Cdd:PRK11153 1 MIELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCInllerptSGRVLV---------DG---QD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 70 LL-LQPAELR-ARTGIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRSrAIPEMVFDLFpALYSLRHQRS---GELPMEQQ 144
Cdd:PRK11153 69 LTaLSEKELRkARRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKA-EIKARVTELL-ELVGLSDKADrypAQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 145 QHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVA 224
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVS 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
12-216 |
7.71e-22 |
|
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: 88.43 E-value: 7.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 12 GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLLlqPAELRARtgIGYVPQGRH 91
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL--DGADISQWD--PNELGDH--VGYLPQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 92 IFSQmSVEDNLLialmaaqddrsraipemvfdlfpalyslrhqrSGelpmEQQQHLALARALVLQPKLVILDEPTEGMSP 171
Cdd:cd03246 87 LFSG-SIAENIL--------------------------------SG----GQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495377997 172 WLEEEMGNLIRRLnREYGLTILLLEQHVSFVRRvADYFLLLHRGR 216
Cdd:cd03246 130 EGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-221 |
1.04e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 89.69 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCI-------MGRLPINSGSMTWQEDGAPPEDLLLqp 74
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNHFDFSKTPSDKAIREL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 75 aelraRTGIGYVPQGRHIFSQMSVEDNLLIALM-----AAQDDRSRAIPemvfdlfpALYSLR-HQRSGELPME----QQ 144
Cdd:PRK11124 81 -----RRNVGMVFQQYNLWPHLTVQQNLIEAPCrvlglSKDQALARAEK--------LLERLRlKPYADRFPLHlsggQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 145 QHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLnREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-226 |
3.06e-21 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 90.11 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPIN---SGSMTWqeDGappEDLL-LQPAELRARTG--IGYVPQG--- 89
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILF--DG---EDLLkLSEKELRKIRGreIQMIFQDpmt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 90 ----RhifsqMSVEDNLLIALMA-----AQDDRSRAI----------PEMVFDLFPalyslrHQRSGElpmeQQQHLALA 150
Cdd:COG0444 98 slnpV-----MTVGDQIAEPLRIhgglsKAEARERAIellervglpdPERRLDRYP------HELSGG----MRQRVMIA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 151 RALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:COG0444 163 RALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-221 |
3.88e-21 |
|
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: 87.65 E-value: 3.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 13 QNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAppeDL-LLQPAELRARtgIGYVPQGRH 91
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLL--DGT---DIrQLDPADLRRN--IGYVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 92 IFSQmSVEDNLLIALMAAQDDRSRAIPEM--VFDLF---PALYSLRHQRSGE-LPMEQQQHLALARALVLQPKLVILDEP 165
Cdd:cd03245 89 LFYG-TLRDNITLGAPLADDERILRAAELagVTDFVnkhPNGLDLQIGERGRgLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 166 TEGMSPWLEEEmgnLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:cd03245 168 TSAMDMNSEER---LKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-193 |
3.96e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 90.13 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQE---DGAPPEDlllqpael 77
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvTDLPPKD-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 78 raRtGIGYVPQGRHIFSQMSVEDNLLIALM------AAQDDRSRAIPEMVfdlfpALYSLRHQRSGELPMEQQQHLALAR 151
Cdd:COG3839 75 --R-NIAMVFQSYALYPHMTVYENIAFPLKlrkvpkAEIDRRVREAAELL-----GLEDLLDRKPKQLSGGQRQRVALGR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495377997 152 ALVLQPKLVILDEPtegMS---PWLEEEMGNLIRRLNREYGLTIL 193
Cdd:COG3839 147 ALVREPKVFLLDEP---LSnldAKLRVEMRAEIKRLHRRLGTTTI 188
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-177 |
5.70e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 90.88 E-value: 5.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 12 GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLllQPAELRARtgIGYVPQGRH 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTL--DGVPVSSL--DQDEVRRR--VSVCAQDAH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 92 IFSQmSVEDNLLIALMAAQDDRSRAIPEMV--FDLFPALYSLRHQRSGE----LPMEQQQHLALARALVLQPKLVILDEP 165
Cdd:TIGR02868 420 LFDT-TVRENLRLARPDATDEELWAALERVglADWLRALPDGLDTVLGEggarLSGGERQRLALARALLADAPILLLDEP 498
|
170
....*....|..
gi 495377997 166 TEGMSPWLEEEM 177
Cdd:TIGR02868 499 TEHLDAETADEL 510
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-227 |
6.88e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.47 E-value: 6.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEdlLLQPAELRAR 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI--DGKPVR--IRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 tGIGYVPQgrH--IFSQMSVEDNLLIALMAAQD---DRSRAIpEMVFDLFpALYSLR---HQRSGELPMEQQQHLALARA 152
Cdd:COG3845 81 -GIGMVHQ--HfmLVPNLTVAENIVLGLEPTKGgrlDRKAAR-ARIRELS-ERYGLDvdpDAKVEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 153 LVLQPKLVILDEPTEGMSPwLE-EEMGNLIRRLNREyGLTILL----LEQhvsfVRRVADYFLLLHRGRNVAHGKVAQLD 227
Cdd:COG3845 156 LYRGARILILDEPTAVLTP-QEaDELFEILRRLAAE-GKSIIFithkLRE----VMAIADRVTVLRRGKVVGTVDTAETS 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-216 |
1.28e-20 |
|
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: 86.19 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTcTGVLGSPGMGKTTLVNCIMGRLPINSGSM-----TWQeDGAPPEDLllqPAELRartGIGYVPQGRHIF 93
Cdd:cd03297 16 KIDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtVLF-DSRKKINL---PPQQR---KIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 94 SQMSVEDNLLIALMAAQDDRSRAIPEMVFDLFpALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEGMSPWL 173
Cdd:cd03297 88 PHLNVRENLAFGLKRKRNREDRISVDELLDLL-GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495377997 174 EEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-226 |
1.35e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 87.06 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSG-SMTW--QEDGAppEDLllqpAEL 77
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgERRGG--EDV----WEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 78 RARtgIGYVPQGRH--IFSQMSVEDNLLIALMA----------AQDDRSRAIPEMVfdlfpALYSLRHQRSGELPMEQQQ 145
Cdd:COG1119 77 RKR--IGLVSPALQlrFPRDETVLDVVLSGFFDsiglyreptdEQRERARELLELL-----GLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 146 HLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILL----LEQHVSFVRRVadyfLLLHRGRNVAHG 221
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLvthhVEEIPPGITHV----LLLKDGRVVAAG 225
|
....*
gi 495377997 222 KVAQL 226
Cdd:COG1119 226 PKEEV 230
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-226 |
1.38e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.94 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDGAPPedlllqpAELRART 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-------RARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 GIGYVPQGRHIFSQMSVEDNLLI-----ALMAAQddrsraIPEMVFDL--FPALYSLRHQRSGELPMEQQQHLALARALV 154
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLLVfgryfGLSAAA------ARALVPPLleFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495377997 155 LQPKLVILDEPTEGMSPWLEEEMGNLIRRLnREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-218 |
1.52e-20 |
|
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: 86.56 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPinSGSMTWQE---DGAPPEdlllqPAELRARtgIGYVPQGRHI 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQilfNGQPRK-----PDQFQKC--VAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 93 FSQMSVEDNLL-IALMAAQDDRSRAIPEMVFDLFP----ALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTE 167
Cdd:cd03234 93 LPGLTVRETLTyTAILRLPRKSSDAIRKKRVEDVLlrdlALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495377997 168 GMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNV 218
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-226 |
1.91e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 88.28 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLLLQ-PAelRAR 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL--NG---RDLFTNlPP--RER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 tGIGYVPQG----RHifsqMSVEDNLLIALMAAQDDRsRAIPEMVFDL------------FPalyslrHQRSGElpmeQQ 144
Cdd:COG1118 76 -RVGFVFQHyalfPH----MTVAENIAFGLRVRPPSK-AEIRARVEELlelvqlegladrYP------SQLSGG----QR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 145 QHLALARALVLQPKLVILDEPtegmspwleeeMGNL-----------IRRLNREYGLTILlleqhvsFVR-------RVA 206
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEP-----------FGALdakvrkelrrwLRRLHDELGGTTV-------FVThdqeealELA 201
|
250 260
....*....|....*....|
gi 495377997 207 DYFLLLHRGRNVAHGKVAQL 226
Cdd:COG1118 202 DRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
19-221 |
2.56e-20 |
|
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: 85.62 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQE---DGAPPedlllqpaelrARTGIGYVPQGRHIFSQ 95
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvTAAPP-----------ADRPVSMLFQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 MSVEDNLLIA------LMAAQDDRSRAIPEMVfdlfpALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEGM 169
Cdd:cd03298 85 LTVEQNVGLGlspglkLTAEDRQAIEVALARV-----GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495377997 170 SPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:cd03298 160 DPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-216 |
3.13e-20 |
|
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: 85.85 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 5 RSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEdgappEDLLLQPAELRartGIG 84
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG-----EDATDVPVQER---NVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 85 YVPQGRHIFSQMSVEDNLLIALM---AAQDDRSRAIPEMVFDL--FPALYSLRHQRSGELPMEQQQHLALARALVLQPKL 159
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRvkpRSERPPEAEIRAKVHELlkLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 160 VILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-226 |
5.28e-20 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 85.47 E-value: 5.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCI--MGRL-PIN--SGSMTWqeDGappEDLL---LQ 73
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLiPGArvEGEILL--DG---EDIYdpdVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 74 PAELRARtgIGYVPQGRHIFSqMSVEDNLLIALMAAQDDRSRAIPEMVFDlfpalySLR------------HQRSGELPM 141
Cdd:COG1117 87 VVELRRR--VGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEE------SLRkaalwdevkdrlKKSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 142 EQQQHLALARALVLQPKLVILDEPTEGMSPW----LEEemgnLIRRLNREYglTILL----LEQhvsfVRRVADYFLLLH 213
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPIstakIEE----LILELKKDY--TIVIvthnMQQ----AARVSDYTAFFY 227
|
250
....*....|...
gi 495377997 214 RGRNVAHGKVAQL 226
Cdd:COG1117 228 LGELVEFGPTEQI 240
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-227 |
6.57e-20 |
|
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: 85.04 E-value: 6.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNH-ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCImGRLpINSGSMTWQEDGAPPEDLllQPAELRAR 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI-NRL-IEPTSGEIFIDGEDIREQ--DPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 tgIGYVPQGRHIFSQMSVEDNllIALM--------AAQDDRSRAIPEMVfDLFPAlySLRHQRSGELPMEQQQHLALARA 152
Cdd:cd03295 77 --IGYVIQQIGLFPHMTVEEN--IALVpkllkwpkEKIRERADELLALV-GLDPA--EFADRYPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 153 LVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHrgrnvaHGKVAQLD 227
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMK------NGEIVQVG 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-222 |
1.17e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 84.51 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 5 RSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPIN-----------SGSMTWQEDgappedllLQ 73
Cdd:PRK14267 8 VNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvegevrlFGRNIYSPD--------VD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 74 PAELRARtgIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRSRA-IPEMV------FDLFPALYSLRHQRSGELPMEQQQH 146
Cdd:PRK14267 80 PIEVRRE--VGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKeLDERVewalkkAALWDEVKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 147 LALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYglTILLLEQHVSFVRRVADYFLLLHRGRNVAHGK 222
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-226 |
1.77e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 86.76 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDllLQPAELRARtgIGYVPQGRHIFSqMSV 98
Cdd:COG1132 358 DISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI--DGVDIRD--LTLESLRRQ--IGVVPQDTFLFS-GTI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 99 EDNLLIALMAAQDDRSRAIPEMV-FDLFpaLYSLRH-------QRSGELPMEQQQHLALARALVLQPKLVILDEPTEGMS 170
Cdd:COG1132 431 RENIRYGRPDATDEEVEEAAKAAqAHEF--IEALPDgydtvvgERGVNLSGGQRQRIAIARALLKDPPILILDEATSALD 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 171 PWLEEEMGNLIRRLNReyGLTILLLEQHVSFVRRvADYFLLLHRGRNVAHGKVAQL 226
Cdd:COG1132 509 TETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEEL 561
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-212 |
3.67e-19 |
|
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: 85.80 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFY-GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMtwQEDGAPPEDLLlqPAELRAR 80
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI--AVNGVPLADAD--ADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 tgIGYVPQGRHIFSQmSVEDNLLIALMAAQDDRSR------AIPEMVFDLFPALYSLRHQRSGELPMEQQQHLALARALV 154
Cdd:TIGR02857 398 --IAWVPQHPFLFAG-TIAENIRLARPDASDAEIRealeraGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 155 LQPKLVILDEPTEGMSPWLEEEMGNLIRRLNReyGLTILLLeQHVSFVRRVADYFLLL 212
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLV-THRLALAALADRIVVL 529
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-228 |
3.81e-19 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 84.47 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 32 VLGSPGMGKTTLVNCIMGRLPINSGSMTWQEdgappEDLLLQPAELRartGIGYVPQGRHIFSQMSVEDNLLIALM---- 107
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDG-----EDVTNVPPHLR---HINMVFQSYALFPHMTVEENVAFGLKmrkv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 108 --AAQDDRSRAIPEMV-FDLFPALYSlrHQRSGElpmeQQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRL 184
Cdd:TIGR01187 73 prAEIKPRVLEALRLVqLEEFADRKP--HQLSGG----QQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495377997 185 NREYGLTILLLEQHVSFVRRVADYFLLLHRgrnvahGKVAQLDD 228
Cdd:TIGR01187 147 QEQLGITFVFVTHDQEEAMTMSDRIAIMRK------GKIAQIGT 184
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-226 |
7.05e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.49 E-value: 7.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 7 VNQFYGQNhILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQE---DGAPPedLLLQPAELRA-RTG 82
Cdd:PRK11264 10 VKKFHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitiDTARS--LSQQKGLIRQlRQH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 83 IGYVPQGRHIFSQMSVEDNL----LIALMAAQDD---RSRAIPEMVF-----DLFPalyslRHQRSGelpmeQQQHLALA 150
Cdd:PRK11264 87 VGFVFQNFNLFPHRTVLENIiegpVIVKGEPKEEataRARELLAKVGlagkeTSYP-----RRLSGG-----QQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 151 RALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-221 |
8.80e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 82.75 E-value: 8.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 17 LWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGrLPINSGSMTWQEDGAPPEDLLLQPAELRARTGIGYVPQ-GRHIFSQ 95
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNG-LIISETGQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQfPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 MSVEDNLL---IALMAAQDDRSRAIPEMVfDL--FPALYSLRhqRSGELPMEQQQHLALARALVLQPKLVILDEPTEGMS 170
Cdd:PRK13645 106 ETIEKDIAfgpVNLGENKQEAYKKVPELL-KLvqLPEDYVKR--SPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495377997 171 PWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-216 |
1.04e-18 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 82.16 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCI-------MGRLPINSGSMTWQEDGappeDLLLQ 73
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCInlletpdSGEIRVGGEEIRLKPDR----DGELV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 74 PAEL----RARTGIGYVPQGRHIFSQMSVEDNLLIALM-------AAQDDRSRAIPEMVfdlfpALYSLRHQRSGELPME 142
Cdd:COG4598 84 PADRrqlqRIRTRLGMVFQSFNLWSHMTVLENVIEAPVhvlgrpkAEAIERAEALLAKV-----GLADKRDAYPAHLSGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495377997 143 QQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:COG4598 159 QQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGR 231
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-226 |
1.29e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.94 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCI-------MGRLPINSGSMTWQEDgappEDLLLQP 74
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsEGSIVVNGQTINLVRD----KDGQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 75 A---ELRA-RTGIGYVPQGRHIFSQMSVEDNLLIAL-----MAAQDDRSRAIpemvfdLFPALYSLRHQRSGELPME--- 142
Cdd:PRK10619 82 AdknQLRLlRTRLTMVFQHFNLWSHMTVLENVMEAPiqvlgLSKQEARERAV------KYLAKVGIDERAQGKYPVHlsg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 143 -QQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:PRK10619 156 gQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
|
....*
gi 495377997 222 KVAQL 226
Cdd:PRK10619 235 APEQL 239
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-216 |
7.74e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 79.72 E-value: 7.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGsmtwqedgappeDLLLQPAEL-RAR 80
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG------------ELLAGTAPLaEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRSRAIPEMVfdlfpALYSlrhqRSGELPME----QQQHLALARALVLQ 156
Cdd:PRK11247 81 EDTRLMFQDARLLPWKKVIDNVGLGLKGQWRDAALQALAAV-----GLAD----RANEWPAAlsggQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 157 PKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-226 |
8.68e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 79.24 E-value: 8.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYgqNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQ-ED--GAPPedlllqpael 77
Cdd:PRK10771 1 MLKLTDITWLY--HHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgQDhtTTPP---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 78 rARTGIGYVPQGRHIFSQMSVEDNLLIA------LMAAQDDRSRAIPEMVFdLFPALYSLRHQRSGElpmeQQQHLALAR 151
Cdd:PRK10771 69 -SRRPVSMLFQENNLFSHLTVAQNIGLGlnpglkLNAAQREKLHAIARQMG-IEDLLARLPGQLSGG----QRQRVALAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 152 ALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK10771 143 CLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-227 |
1.56e-17 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 79.08 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILW---------DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEdgappEDLL 71
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFGakqrapvltNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRG-----QDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 72 -LQPAELRA-RTGIGYVPQGRH--IFSQMSVE-------DNLLIALMAAQDDRSRAIPEMVfdlfpalySLRHQRSGELP 140
Cdd:TIGR02769 77 qLDRKQRRAfRRDVQLVFQDSPsaVNPRMTVRqiigeplRHLTSLDESEQKARIAELLDMV--------GLRSEDADKLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 141 ME----QQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:TIGR02769 149 RQlsggQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
250
....*....|.
gi 495377997 217 NVAHGKVAQLD 227
Cdd:TIGR02769 229 IVEECDVAQLL 239
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-235 |
1.66e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 79.04 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDGAPPedlLLQPAELRAR 80
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPA---MSRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGYVPQGRHIFSQMSVEDNLLIALMaaqddRSRAIPEmvfdlfPALYS----------LR---HQRSGELPMEQQQHL 147
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNVAYPLR-----EHTQLPA------PLLHStvmmkleavgLRgaaKLMPSELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 148 ALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL- 226
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALq 232
|
250
....*....|.
gi 495377997 227 --DDLTVNKWL 235
Cdd:PRK11831 233 anPDPRVRQFL 243
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-221 |
1.71e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 79.75 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEdgappEDLL-LQPAELRA-RTGIgyvpqgRHIFS-- 94
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG-----KDLLgMKDDEWRAvRSDI------QMIFQdp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 95 ------QMSVEDnlLIA--------LMAAQD--DRSRAIPEMVfDLFPAL---YSlrHQRSGElpmeQQQHLALARALVL 155
Cdd:PRK15079 108 laslnpRMTIGE--IIAeplrtyhpKLSRQEvkDRVKAMMLKV-GLLPNLinrYP--HEFSGG----QCQRIGIARALIL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 156 QPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 244
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-221 |
1.74e-17 |
|
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: 77.59 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRL--PINSGSMTWqeDGAPpedllLQPAELRARtgIGYVPQGRHIF 93
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLI--NGRP-----LDKRSFRKI--IGYVPQDDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 94 SQMSVEDNLLIALmaaqddrsraipemvfdlfpALYSLrhqrSGElpmeQQQHLALARALVLQPKLVILDEPTEGMSPWL 173
Cdd:cd03213 95 PTLTVRETLMFAA--------------------KLRGL----SGG----ERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495377997 174 EEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:cd03213 147 ALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-221 |
2.05e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.55 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIM-------GRLPINSGSMTWQEDgappedlLLQPAELRARTGIGYVPQ 88
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFGKD-------IFQIDAIKLRKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 89 GRHIFSQMSVEDNLLIALMAAQDDRSRAIPEMVFD------LFPALYSLRHQRSGELPMEQQQHLALARALVLQPKLVIL 162
Cdd:PRK14246 98 QPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEEclrkvgLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495377997 163 DEPTEGMSPWLEEEMGNLIRRLNREygLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWG 234
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-216 |
2.34e-17 |
|
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: 77.68 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEdgappEDLLLQPAELRart 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG-----RDVTDLPPKDR--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 GIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRsRAIPEMVFDLFPALY--SLRHQRSGELPMEQQQHLALARALVLQPKL 159
Cdd:cd03301 73 DIAMVFQNYALYPHMTVYDNIAFGLKLRKVPK-DEIDERVREVAELLQieHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 160 VILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-191 |
3.48e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 79.22 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLLLQPAELRArt 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML--DG---QDITHVPAENRH-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 gIGYVPQGRHIFSQMSVEDNLLIAL-MaaQDDRSRAIPEMVFDlfpALYSLR---------HQRSGElpmeQQQHLALAR 151
Cdd:PRK09452 88 -VNTVFQSYALFPHMTVFENVAFGLrM--QKTPAAEITPRVME---ALRMVQleefaqrkpHQLSGG----QQQRVAIAR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495377997 152 ALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLT 191
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGIT 197
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-214 |
4.62e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.46 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLpinsgsmtwqedgAPPEDLLLQPAELRar 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLV-------------APDEGVIKRNGKLR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 tgIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRsraipemvfDLFPALYSLRHQRSGELPME-----QQQHLALARALVL 155
Cdd:PRK09544 69 --IGYVPQKLYLDTTLPLTVNRFLRLRPGTKKE---------DILPALKRVQAGHLIDAPMQklsggETQRVLLARALLN 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495377997 156 QPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHR 214
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-194 |
4.65e-17 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 77.09 E-value: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQN----HILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTW--QEDGAPPEDlllQP 74
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLagQDLFALDED---AR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 75 AELRARtGIGYVPQGRHIFSQMSVEDNLLIALMAAQD----DRSRAIPEMVfdlfpALYSLRHQRSGELPMEQQQHLALA 150
Cdd:COG4181 85 ARLRAR-HVGFVFQSFQLLPTLTALENVMLPLELAGRrdarARARALLERV-----GLGHRLDHYPAQLSGGEQQRVALA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495377997 151 RALVLQPKLVILDEPTEGmspwLEEEMG----NLIRRLNREYGLTILL 194
Cdd:COG4181 159 RAFATEPAILFADEPTGN----LDAATGeqiiDLLFELNRERGTTLVL 202
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-194 |
4.71e-17 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 78.93 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTwqEDGappEDLLLQPAELRart 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIY--QGG---RDITRLPPQKR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 GIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRSRA---IPEMVfDLFpALYSLRHQRSGELPMEQQQHLALARALVLQPK 158
Cdd:TIGR03265 77 DYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVaerVAELL-DLV-GLPGSERKYPGQLSGGQQQRVALARALATSPG 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 495377997 159 LVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILL 194
Cdd:TIGR03265 155 LLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIM 190
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
6.35e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.58 E-value: 6.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQ-NHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLLLQPAELRA 79
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILF--DGKPIDYSRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 80 RTGIGYVPQGRHIFSQMSVED------NLLIALMAAQDDRSRAIPEMvfdlfpALYSLRHQRSGELPMEQQQHLALARAL 153
Cdd:PRK13636 83 SVGMVFQDPDNQLFSASVYQDvsfgavNLKLPEDEVRKRVDNALKRT------GIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495377997 154 VLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-222 |
9.13e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.97 E-value: 9.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 11 YGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQedGAPPEDLLLQPAELRARTGIGYVPQGR 90
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQ--GKPLDYSKRGLLALRQQVATVFQDPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 91 HIFsQMSVEDNLLIALM---AAQDDRSRAIPEmVFDLFPALYsLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTE 167
Cdd:PRK13638 89 QIF-YTDIDSDIAFSLRnlgVPEAEITRRVDE-ALTLVDAQH-FRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 168 GMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGK 222
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-226 |
1.07e-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: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPiNSGSMTWqeDGAPPEDLllQPAELRartgigyvPQGRHI------ 92
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRF--DGQDLDGL--SRRALR--------PLRRRMqvvfqd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 93 -FS----QMSVEDnlLIA--------LMAAQDDRSRAI---------PEMvFDLFPalyslrHQRSGElpmeQQQHLALA 150
Cdd:COG4172 371 pFGslspRMTVGQ--IIAeglrvhgpGLSAAERRARVAealeevgldPAA-RHRYP------HEFSGG----QRQRIAIA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 151 RALVLQPKLVILDEPTEG--MSpwLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:COG4172 438 RALILEPKLLVLDEPTSAldVS--VQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-228 |
1.43e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.17 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDllLQPAELRAr 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEI--GGNPCAR--LTPAKAHQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRSRaipemVFDLFPAL-YSLR-HQRSGELPMEQQQHLALARALVLQPK 158
Cdd:PRK15439 86 LGIYLVPQEPLLFPNLSVKENILFGLPKRQASMQK-----MKQLLAALgCQLDlDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495377997 159 LVILDEPTEGMSPwleEEMGNLIRRLN--REYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQLDD 228
Cdd:PRK15439 161 ILILDEPTASLTP---AETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLST 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-216 |
1.87e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 77.07 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLLLQPAELRart 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI--DG---EDVTHRSIQQR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 GIGYVPQGRHIFSQMSVEDNL---LIALMAAQDDRSRAIPE---MVfDLfpALYSLRH--QRSGElpmeQQQHLALARAL 153
Cdd:PRK11432 79 DICMVFQSYALFPHMSLGENVgygLKMLGVPKEERKQRVKEaleLV-DL--AGFEDRYvdQISGG----QQQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495377997 154 VLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-221 |
2.27e-16 |
|
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: 77.48 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 12 GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAppeDLLLQPAELRARtGIGYVPQGRH 91
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL--DGA---DLSQWDREELGR-HIGYLPQDVE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 92 IFSQmSVEDNllIALMAAQDDRS------RA-IPEMVFDLfPALYSLRHQRSGE-LPMEQQQHLALARALVLQPKLVILD 163
Cdd:COG4618 417 LFDG-TIAEN--IARFGDADPEKvvaaakLAgVHEMILRL-PDGYDTRIGEGGArLSGGQRQRIGLARALYGDPRLVVLD 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495377997 164 EP-----TEGmspwlEEEMGNLIRRLnREYGLTILLLEQHVSFVrRVADYFLLLHRGRNVAHG 221
Cdd:COG4618 493 EPnsnldDEG-----EAALAAAIRAL-KARGATVVVITHRPSLL-AAVDKLLVLRDGRVQAFG 548
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-221 |
2.96e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.83 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 17 LWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDGAPPEDLLLQPAELRARTGIGYVPQGRHIFSQm 96
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQFPEHQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 97 SVEDNLLIALM---AAQDDRSRAIPEMVfDLFPALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEGMSPWL 173
Cdd:PRK13634 102 TVEKDICFGPMnfgVSEEDAKQKAREMI-ELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495377997 174 EEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-225 |
3.26e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.85 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLLLQPAELRARTGIGYVPQGRHIFSQMSV 98
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIII--DGVDITDKKVKLSDIRKKVGLVFQYPEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 99 EDnllIAL----MAAQDD----RSRAIPEMV-FDlfpalYSLRHQRSG-ELPMEQQQHLALARALVLQPKLVILDEPTEG 168
Cdd:PRK13637 103 KD---IAFgpinLGLSEEeienRVKRAMNIVgLD-----YEDYKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 169 MSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQ 225
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-219 |
3.49e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.98 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEdlLLQPAE-LRArtGIGYVPQGRH---IFS 94
Cdd:COG1129 270 DVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRL--DGKPVR--IRSPRDaIRA--GIAYVPEDRKgegLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 95 QMSVEDNLLIalmAAQDDRSRAIpemvfdlfpaLYSLRHQR---------------SGELPMEQ-----QQHLALARALV 154
Cdd:COG1129 344 DLSIRENITL---ASLDRLSRGG----------LLDRRRERalaeeyikrlriktpSPEQPVGNlsggnQQKVVLAKWLA 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495377997 155 LQPKLVILDEPTEGmspwleEEMGNLIRRLNREyGLTILL----LEQhvsfVRRVADYFLLLHRGRNVA 219
Cdd:COG1129 411 TDPKVLILDEPTRGidvgakAEIYRLIRELAAE-GKAVIVisseLPE----LLGLSDRILVMREGRIVG 474
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-215 |
4.50e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 75.89 E-value: 4.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 7 VNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEdgappEDLllqpAELRART-GIGY 85
Cdd:PRK10851 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG-----TDV----SRLHARDrKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 86 VPQGRHIFSQMSVEDNLLIAL----------MAAQDDRSRAIPEMV-----FDLFPAlyslrhQRSGelpmEQQQHLALA 150
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLtvlprrerpnAAAIKAKVTQLLEMVqlahlADRYPA------QLSG----GQKQRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 151 RALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRG 215
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-229 |
6.88e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.98 E-value: 6.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDGAPPEDlllqpAELRAR 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-----HKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGYVPQGRHIFSQMSVEDNLLIA-----------LMAAQDDRSRAipEMVFDLFPALYSLrHQRSGELPMEQQQHLAL 149
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLYIGrhltkkvcgvnIIDWREMRVRA--AMMLLRVGLKVDL-DEKVANLSISHKQMLEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 150 ARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL--D 227
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVsnD 235
|
..
gi 495377997 228 DL 229
Cdd:PRK09700 236 DI 237
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-216 |
9.09e-16 |
|
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: 73.21 E-value: 9.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 4 LRSVNQFYGQNHI-LWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGsmTWQEDGAPPEDLLLQPAELrARTG 82
Cdd:cd03292 3 FINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSG--TIRVNGQDVSDLRGRAIPY-LRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 83 IGYVPQGRHIFSQMSVEDNLLIALMAAQDDRsRAIPEMVFDLFpALYSLRHqRSGELPME----QQQHLALARALVLQPK 158
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGVPP-REIRKRVPAAL-ELVGLSH-KHRALPAElsggEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 159 LVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-221 |
1.85e-15 |
|
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: 71.58 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQN--HILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLllqpaELRA 79
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL--DGVPVSDL-----EKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 80 RTGIGYVPQGRHIFSQmSVEDNLLIALmaaqddrsraipemvfdlfpalyslrhqrSGElpmeQQQHLALARALVLQPKL 159
Cdd:cd03247 74 SSLISVLNQRPYLFDT-TLRNNLGRRF-----------------------------SGG----ERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495377997 160 VILDEPTEGMSPWLEEEMGNLIRRLNREYglTILLLEQHVSFVRRVaDYFLLLHRGRNVAHG 221
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-228 |
2.78e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.74 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGS--------MTWQEDGAPPEDLLl 72
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshiellgRTVQREGRLARDIR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 73 qpaelRARTGIGYVPQGRHIFSQMSVEDNLLIALMAA------------QDDRSRAIPEMVFdlfPALYSLRHQRSGELP 140
Cdd:PRK09984 83 -----KSRANTGYIFQQFNLVNRLSVLENVLIGALGStpfwrtcfswftREQKQRALQALTR---VGMVHFAHQRVSTLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 141 MEQQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAH 220
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
|
....*...
gi 495377997 221 GKVAQLDD 228
Cdd:PRK09984 235 GSSQQFDN 242
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-207 |
3.41e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 73.23 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLL-LQPAELRA-RTGIGYV---PQG---- 89
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILF--DG---QDITgLSGRELRPlRRRMQMVfqdPYAslnp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 90 RhifsqMSVEDNLLIALM-------AAQDDRSRAIPEMVfDLFPALYSlR--HQRSGElpmeQQQHLALARALVLQPKLV 160
Cdd:COG4608 111 R-----MTVGDIIAEPLRihglaskAERRERVAELLELV-GLRPEHAD-RypHEFSGG----QRQRIGIARALALNPKLI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495377997 161 ILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVAD 207
Cdd:COG4608 180 VCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISD 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-226 |
3.91e-15 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 71.88 E-value: 3.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLLLqpAELRARtgIGYVPQGRHIFSQ 95
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILI--DGHDVRDYTL--ASLRRQ--IGLVSQDVFLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 mSVEDNLLIALMAAQDDRSRAIPEMV-----FDLFPALYslrHQRSGE----LPMEQQQHLALARALVLQPKLVILDEPT 166
Cdd:cd03251 91 -TVAENIAYGRPGATREEVEEAARAAnahefIMELPEGY---DTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495377997 167 EGMSPWLEEEMGNLIRRL--NReyglTILLLEQHVSFVRRvADYFLLLHRGRNVAHGKVAQL 226
Cdd:cd03251 167 SALDTESERLVQAALERLmkNR----TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-230 |
5.65e-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: 73.30 E-value: 5.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 20 VDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMtWQEDGAPPEDLLLQPAELRARTG--IGYVPQGRHIFSQMS 97
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV-NVRVGDEWVDMTKPGPDGRGRAKryIGILHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 98 VEDNLLIALMAAQDD---RSRAIPEMVFDLFPALY--SLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEGMSPW 172
Cdd:TIGR03269 382 VLDNLTEAIGLELPDelaRMKAVITLKMVGFDEEKaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPI 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495377997 173 LEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQ-LDDLT 230
Cdd:TIGR03269 462 TKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEiVEELT 520
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-226 |
5.83e-15 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 71.36 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTwqEDGappEDL-LLQPAELRARtgIGYVPQGRHIFS 94
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVL--VDG---HDLaLADPAWLRRQ--VGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 95 QmSVEDNllIALMAAQDDRSRAIP--------EMVFDLFPALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPT 166
Cdd:cd03252 90 R-SIRDN--IALADPGMSMERVIEaaklagahDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495377997 167 EGMSpwlEEEMGNLIRRLNR-EYGLTILLLEQHVSFVRRvADYFLLLHRGRNVAHGKVAQL 226
Cdd:cd03252 167 SALD---YESEHAIMRNMHDiCAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-216 |
1.13e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 11 YGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDgappedlllqpaeLRartgIGYVPQGR 90
Cdd:COG0488 8 FGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-------------LR----IGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 91 HIFSQMSVEDNL------LIALMAAQDDRSRAIPEMVFDL---------FPAL--YSLRHQ------------RSGELPM 141
Cdd:COG0488 71 PLDDDLTVLDTVldgdaeLRALEAELEELEAKLAEPDEDLerlaelqeeFEALggWEAEARaeeilsglgfpeEDLDRPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 142 E-----QQQHLALARALVLQPKLVILDEPT-----EGMSpWLEEEMgnlirrlnREYGLTILLleqhVS----FVRRVAD 207
Cdd:COG0488 151 SelsggWRRRVALARALLSEPDLLLLDEPTnhldlESIE-WLEEFL--------KNYPGTVLV----VShdryFLDRVAT 217
|
....*....
gi 495377997 208 YFLLLHRGR 216
Cdd:COG0488 218 RILELDRGK 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-216 |
1.20e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAP-----PEDLLlqpaelraRTGIGYVPQGRH-- 91
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTL--DGHEvvtrsPQDGL--------ANGIVYISEDRKrd 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 92 -IFSQMSVEDNL-LIAL-----MAAQDDRSRAipEMVFDLFPALYSL----RHQRSGELPMEQQQHLALARALVLQPKLV 160
Cdd:PRK10762 340 gLVLGMSVKENMsLTALryfsrAGGSLKHADE--QQAVSDFIRLFNIktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 161 ILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-208 |
1.59e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.58 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCI--MGRLpINS----GSMTWQedGAPPEDLLLQPA 75
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDL-IPGfrveGKVTFH--GKNLYAPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 76 ELRARtgIGYVPQGRHIFSQmSVEDNllIALMAAQDDRSRAIPEMVfdlfpaLYSLRH-----------QRSG-ELPMEQ 143
Cdd:PRK14243 88 EVRRR--IGMVFQKPNPFPK-SIYDN--IAYGARINGYKGDMDELV------ERSLRQaalwdevkdklKQSGlSLSGGQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 144 QQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYglTILLLEQHVSFVRRVADY 208
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDM 219
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
16-226 |
1.64e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.06 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMtwQEDGAPPEDLLLQPAelraRTGIGYVPQ------- 88
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI--RLDGRPLSSLSHSVL----RQGVAMVQQdpvvlad 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 89 --------GRHIfsqmsVEDNLLIALMAAQ-DDRSRAIPEmvfdlfpALYSLRHQRSGELPMEQQQHLALARALVLQPKL 159
Cdd:PRK10790 430 tflanvtlGRDI-----SEEQVWQALETVQlAELARSLPD-------GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 160 VILDEPTEGMSPWLEEEMGNLIRRLNREygLTILLLEQHVSFVRRvADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
9-226 |
1.68e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 70.99 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 9 QFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDGAPPEDLllqpAELRARTGIGYVPQ 88
Cdd:PRK13652 12 SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENI----REVRKFVGLVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 89 GRHIFSQmSVEDNLL---IALMAAQDDRSRAIPEMVFDLfpALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEP 165
Cdd:PRK13652 88 DDQIFSP-TVEQDIAfgpINLGLDEETVAHRVSSALHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495377997 166 TEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-193 |
2.18e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.21 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 3 SLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGsmtwqedgappeDLLLqpAELR---- 78
Cdd:PRK11000 5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSG------------DLFI--GEKRmndv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 79 --ARTGIGYVPQGRHIFSQMSVEDNLLIALMAAQ------DDRSRAIPEMVfdlfpALYSLRHQRSGELPMEQQQHLALA 150
Cdd:PRK11000 71 ppAERGVGMVFQSYALYPHLSVAENMSFGLKLAGakkeeiNQRVNQVAEVL-----QLAHLLDRKPKALSGGQRQRVAIG 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495377997 151 RALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTIL 193
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMI 188
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-226 |
2.47e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 71.64 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 12 GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPIN----SGSMTWQEdgappEDLL-LQPAELRARTG--IG 84
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDG-----QDLLgLSERELRRIRGnrIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 85 YvpqgrhIFsQ---------MSVEDNL-----LIALMAAQDDRSRAI----------PEMVFDLFPalyslrHQRSGElp 140
Cdd:COG4172 96 M------IF-QepmtslnplHTIGKQIaevlrLHRGLSGAAARARALellervgipdPERRLDAYP------HQLSGG-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 141 meQQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAH 220
Cdd:COG4172 161 --QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
....*.
gi 495377997 221 GKVAQL 226
Cdd:COG4172 239 GPTAEL 244
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-195 |
2.48e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.11 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDlllqPAELRar 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITL--DGKPVEG----PGAER-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 tgiGYVPQGRHIFSQMSVEDNLLIALMAA---QDDRSRAIPEMVFDLfpALYSLRHQRSGELPMEQQQHLALARALVLQP 157
Cdd:PRK11248 73 ---GVVFQNEGLLPWRNVQDNVAFGLQLAgveKMQRLEIAHQMLKKV--GLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 495377997 158 KLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLL 195
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLI 185
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-225 |
3.07e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.80 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDllLQPAELRAR 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRL--NGRPLAD--WSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIgyVPQ----------------GRHIFSQMSVEDNLLIALMAAQDD----RSRaipemvfdLFPALyslrhqrS-GEl 139
Cdd:PRK13548 78 RAV--LPQhsslsfpftveevvamGRAPHGLSRAEDDALVAAALAQVDlahlAGR--------DYPQL-------SgGE- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 140 pmeqQQHLALARALV------LQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLH 213
Cdd:PRK13548 140 ----QQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLH 215
|
250
....*....|..
gi 495377997 214 RGRNVAHGKVAQ 225
Cdd:PRK13548 216 QGRLVADGTPAE 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-192 |
4.91e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.92 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTwqedgappedLLLQPAE---LRARTGIGYVPQGRHIFSQ 95
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAW----------LFGQPVDagdIATRRRVGYMSQAFSLYGE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 MSVEDNLLiaLMA-----AQDDRSRAIPEMV--FDLFPALyslrHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEG 168
Cdd:NF033858 354 LTVRQNLE--LHArlfhlPAAEIAARVAEMLerFDLADVA----DALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSG 427
|
170 180 190
....*....|....*....|....*....|
gi 495377997 169 MSP------WleeemgNLIRRLNREYGLTI 192
Cdd:NF033858 428 VDPvardmfW------RLLIELSREDGVTI 451
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-221 |
7.51e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 69.38 E-value: 7.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQN-----HILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDGAPPEDLLLQPA 75
Cdd:PRK13643 1 MIKFEKVNYTYQPNspfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 76 ELRARTGIGYVPQGRHIFSQMSVEDnllIAL----MAAQDDRSRAIPEMVFDLFPALYSLRHQRSGELPMEQQQHLALAR 151
Cdd:PRK13643 81 PVRKKVGVVFQFPESQLFEETVLKD---VAFgpqnFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 152 ALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNrEYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-216 |
8.34e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 67.88 E-value: 8.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQedgappedlllqpaelrarTGIGYVPQGRHIFSq 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP-------------------GSIAYVSQEPWIQN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 MSVEDNLL-------------IALMAAQDDrsraipemvFDLFPAlyslrhqrsGELPM--E--------QQQHLALARA 152
Cdd:cd03250 80 GTIRENILfgkpfdeeryekvIKACALEPD---------LEILPD---------GDLTEigEkginlsggQKQRISLARA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495377997 153 LVLQPKLVILDEPtegMSP-------WLEEE--MGNLirRLNReyglTILLLEQHVSFVRRvADYFLLLHRGR 216
Cdd:cd03250 142 VYSDADIYLLDDP---LSAvdahvgrHIFENciLGLL--LNNK----TRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-194 |
9.11e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 68.74 E-value: 9.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYG----QNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPpedlLLQPAE 76
Cdd:COG4525 3 MLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITL--DGVP----VTGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 77 LRartgiGYVPQGRHIFSQMSVEDNLLIAL----MAAQDDRSRAipemvfDLFPALYSLRH---QRSGELPMEQQQHLAL 149
Cdd:COG4525 77 DR-----GVVFQKDALLPWLNVLDNVAFGLrlrgVPKAERRARA------EELLALVGLADfarRRIWQLSGGMRQRVGI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495377997 150 ARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILL 194
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFL 190
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-194 |
9.15e-14 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 68.82 E-value: 9.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLL-LQPAELRA--RTGIGYVPQGRHIFSQ 95
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI--DG---QDIAaMSRKELRElrRKKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 MSVEDN----LLIALMAAQDDRSRAIP--EMVfdlfpALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEGM 169
Cdd:cd03294 117 RTVLENvafgLEVQGVPRAEREERAAEalELV-----GLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180
....*....|....*....|....*
gi 495377997 170 SPWLEEEMGNLIRRLNREYGLTILL 194
Cdd:cd03294 192 DPLIRREMQDELLRLQAELQKTIVF 216
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-166 |
1.34e-13 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 67.44 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYG----QNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLLL-QPA 75
Cdd:NF038007 1 MLNMQNAEKCYItktiKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTL--AGKEVTNLSYsQKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 76 ELRaRTGIGYVPQGRHIFSQMSVEDNLLIALM---AAQDDRSRAIPEmVFDLFpALYSLRHQRSGELPMEQQQHLALARA 152
Cdd:NF038007 79 ILR-RELIGYIFQSFNLIPHLSIFDNVALPLKyrgVAKKERIERVNQ-VLNLF-GIDNRRNHKPMQLSGGQQQRVAIARA 155
|
170
....*....|....
gi 495377997 153 LVLQPKLVILDEPT 166
Cdd:NF038007 156 MVSNPALLLADEPT 169
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-216 |
1.42e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.32 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEdgappedlllqpaelraR 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE-----------------T 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGYVPQGRHIF-SQMSVEDNLLIALMAAQDDRSRAI-------PEMVFdlfpalyslrhQRSGELPMEQQQHLALARA 152
Cdd:COG0488 378 VKIGYFDQHQEELdPDKTVLDELRDGAPGGTEQEVRGYlgrflfsGDDAF-----------KPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 153 LVLQPKLVILDEPTegmspwleeemgN-L----IRRLN---REYGLTILLleqhVS----FVRRVADYFLLLHRGR 216
Cdd:COG0488 447 LLSPPNVLLLDEPT------------NhLdietLEALEealDDFPGTVLL----VShdryFLDRVATRILEFEDGG 506
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-227 |
1.61e-13 |
|
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: 69.08 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINS--GSMTWqeDGAPpedllLQPAELR 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYW--SGSP-----LKASNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 79 --ARTGIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRSRAIPEMVFDLFPALYSLRHQRS------GELPMEQQQHLALA 150
Cdd:TIGR02633 74 dtERAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADnvtrpvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 151 RALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNReYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQLD 227
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMS 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-216 |
1.73e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 65.55 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQedgappedlllqpaelrART 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-----------------STV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 82 GIGYvpqgrhiFSQMSvednllialmaaqddrsraipemvfdlfpalyslrhqrSGElpmeqQQHLALARALVLQPKLVI 161
Cdd:cd03221 64 KIGY-------FEQLS--------------------------------------GGE-----KMRLALAKLLLENPNLLL 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495377997 162 LDEPT-----EGMSpWLEEEMgnlirrlnREYGLTILLleqhVS----FVRRVADYFLLLHRGR 216
Cdd:cd03221 94 LDEPTnhldlESIE-ALEEAL--------KEYPGTVIL----VShdryFLDQVATKIIELEDGK 144
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-226 |
1.95e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 67.63 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNcIMGRL------PINSGSMTWqeDGappEDLLLQP- 74
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLR-VFNRLielypeARVSGEVYL--DG---QDIFKMDv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 75 AELRARtgIGYVPQGRHIFSQMSVEDNLLIALMAAQDDRSRA-IPEMV------FDLFPALYSLRHQRSGELPMEQQQHL 147
Cdd:PRK14247 78 IELRRR--VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKeLQERVrwalekAQLWDEVKDRLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495377997 148 ALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREygLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-216 |
2.00e-13 |
|
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: 69.08 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQeDGAPPEdlLLQPAElRARTGIGYVPQGRH---IFSQ 95
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFI-NGKPVD--IRNPAQ-AIRAGIAMVPEDRKrhgIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 MSVEDNLLIALMAAQDDRSRAIPEMVFDLFPALYSLRHQRS-------GELPMEQQQHLALARALVLQPKLVILDEPTEG 168
Cdd:TIGR02633 354 LGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTaspflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495377997 169 MSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-194 |
2.64e-13 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 67.81 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFY-GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTL---VNcimgRL-PINSGSMTWqeDGappEDLL-LQP 74
Cdd:COG1125 1 MIEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTlrmIN----RLiEPTSGRILI--DG---EDIRdLDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 75 AELRaRtGIGYVPQGRHIFSQMSVEDNllIALM--------AAQDDRSRAIPEMVfDLFPALYSLR--HQRSGElpmeQQ 144
Cdd:COG1125 72 VELR-R-RIGYVIQQIGLFPHMTVAEN--IATVprllgwdkERIRARVDELLELV-GLDPEEYRDRypHELSGG----QQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495377997 145 QHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILL 194
Cdd:COG1125 143 QRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVF 192
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-226 |
2.97e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.60 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPpedlLLQPAELRARTGIGYVPQGRHIFSQ 95
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL--DGVP----LVQYDHHYLHRQVALVGQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 mSVEDNLLIALMAAQDDRSRAIPEMVF--DLFPALYSLRHQRSGE----LPMEQQQHLALARALVLQPKLVILDEPTEGm 169
Cdd:TIGR00958 570 -SVRENIAYGLTDTPDEEIMAAAKAANahDFIMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSA- 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 170 spwLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRvADYFLLLHRGRNVAHGKVAQL 226
Cdd:TIGR00958 648 ---LDAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-226 |
3.32e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 67.68 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLvncimGRL-----PINSGSMTWqeDGappEDLLLQPAELRA--RTGIGYVPQG-- 89
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTL-----ARLltmieTPTGGELYY--QG---QDLLKADPEAQKllRQKIQIVFQNpy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 90 -----RHIFSQMsVEDNLLI--ALMAAQ-DDRSRAIPEMV------FDLFPalyslrHQRSGElpmeQQQHLALARALVL 155
Cdd:PRK11308 103 gslnpRKKVGQI-LEEPLLIntSLSAAErREKALAMMAKVglrpehYDRYP------HMFSGG----QRQRIAIARALML 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495377997 156 QPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK11308 172 DPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-226 |
4.10e-13 |
|
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: 66.41 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLLLQpaELRARtgIGYVPQGRHIFSq 95
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILL--DGVDIRDLNLR--WLRSQ--IGLVSQEPVLFD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 MSVEDNLLIALMAAQDD------RSRAIPEMVFDLFPALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEGM 169
Cdd:cd03249 91 GTIAENIRYGKPDATDEeveeaaKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 170 SPWLEEEMGNLIRRLNReyGLTILLLEQHVSFVRRvADYFLLLHRGRNVAHGKVAQL 226
Cdd:cd03249 171 DAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDEL 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-222 |
6.48e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.17 E-value: 6.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLLLQPAELRAr 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML--DG---VDLSHVPPYQRP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 tgIGYVPQGRHIFSQMSVEDNllIALMAAQDDRSRA-----IPEMVFDLFPALYSLR--HQRSGElpmeQQQHLALARAL 153
Cdd:PRK11607 93 --INMMFQSYALFPHMTVEQN--IAFGLKQDKLPKAeiasrVNEMLGLVHMQEFAKRkpHQLSGG----QRQRVALARSL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495377997 154 VLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLL----EQHVSFVRRVAdyflLLHRGRNVAHGK 222
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVthdqEEAMTMAGRIA----IMNRGKFVQIGE 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
13-205 |
7.75e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.61 E-value: 7.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 13 QNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQedGAPPEDL-LLQPAELRARTgIGYVPQGRH 91
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN--GQPMSKLsSAAKAELRNQK-LGFIYQFHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 92 IFSQMSVEDN----LLIALMAAQDDRSRAIpEMVFDLfpALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTE 167
Cdd:PRK11629 98 LLPDFTALENvampLLIGKKKPAEINSRAL-EMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 495377997 168 GMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRV 205
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM 212
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-183 |
8.71e-13 |
|
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: 65.21 E-value: 8.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNH--ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLLLQpaELRA 79
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI--DGVDISKIGLH--DLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 80 RTGIgyVPQGRHIFSQmSVEDNLLIALMAAQDDRSRAIP-----EMVFDLFPALYSlRHQRSGE-LPMEQQQHLALARAL 153
Cdd:cd03244 79 RISI--IPQDPVLFSG-TIRSNLDPFGEYSDEELWQALErvglkEFVESLPGGLDT-VVEEGGEnLSVGQRQLLCLARAL 154
|
170 180 190
....*....|....*....|....*....|
gi 495377997 154 VLQPKLVILDEPTEGMSPWLEEEMGNLIRR 183
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIRE 184
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-236 |
1.00e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.83 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 10 FYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCI--MGRLPIN---SGSMTWQEDGAPPEDLLLQpaelRARTGIG 84
Cdd:PRK14258 16 YYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEvrvEGRVEFFNQNIYERRVNLN----RLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 85 YVPQGRHIFSqMSVEDNLLIAL--------MAAQDDRSRAIPEMvfDLFPALYSLRHQRSGELPMEQQQHLALARALVLQ 156
Cdd:PRK14258 92 MVHPKPNLFP-MSVYDNVAYGVkivgwrpkLEIDDIVESALKDA--DLWDEIKHKIHKSALDLSGGQQQRLCIARALAVK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 157 PKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNvahgKVAQLDDL-TVNKWL 235
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNEN----RIGQLVEFgLTKKIF 244
|
.
gi 495377997 236 T 236
Cdd:PRK14258 245 N 245
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-221 |
2.50e-12 |
|
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: 64.28 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGrlpinsgsmtwqedgappedlLLQPAELRARTGiGYVPQGRH------- 91
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSG---------------------LLQPTSGEVRVA-GLVPWKRRkkflrri 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 92 --IFSQ-------MSVED--NLLIALMAAQDDRSRAIPEMVFDLFpALYSLRHQRSGELPMEQQQHLALARALVLQPKLV 160
Cdd:cd03267 97 gvVFGQktqlwwdLPVIDsfYLLAAIYDLPPARFKKRLDELSELL-DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495377997 161 ILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-216 |
4.14e-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: 65.42 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 30 TGVLGSPGMGKTTLVNCIMGRLPINSGS-MTWQEDGAPPEDLLlqpaelraRTGIGYVPQGRHIFSQMSVEDNLLIALM- 107
Cdd:TIGR01257 959 TAFLGHNGAGKTTTLSILTGLLPPTSGTvLVGGKDIETNLDAV--------RQSLGMCPQHNILFHHLTVAEHILFYAQl 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 108 --AAQDDRSRAIPEMVFDlfPALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIrrLN 185
Cdd:TIGR01257 1031 kgRSWEEAQLEMEAMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LK 1106
|
170 180 190
....*....|....*....|....*....|.
gi 495377997 186 REYGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:TIGR01257 1107 YRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-226 |
4.21e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 64.76 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTlvncimGRLPinsGSMTWQEDGAPPEDLLLQPAELRA-R 80
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALP---AHV*GPDAGRRPWRF*TWCANRRAlR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGY---VPQGRHifSQMSVEDNLLIA----LMAAQDDRSRAiPEMV--FDLFPALYSLRHQRSGELpmeqQQHLALAR 151
Cdd:NF000106 85 RTIG*hrpVR*GRR--ESFSGRENLYMIgr*lDLSRKDARARA-DELLerFSLTEAAGRAAAKYSGGM----RRRLDLAA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 152 ALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:NF000106 158 SMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-182 |
4.41e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.85 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFY--GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLllqpAELRA 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL--NGQPIADY----SEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 80 RTGIGYVPQGRHIFSQmSVEDNLLIALMAAQDDRSRAIPEMVfdlfpALYSLRHQRSG----------ELPMEQQQHLAL 149
Cdd:PRK11160 413 RQAISVVSQRVHLFSA-TLRDNLLLAAPNASDEALIEVLQQV-----GLEKLLEDDKGlnawlgeggrQLSGGEQRRLGI 486
|
170 180 190
....*....|....*....|....*....|...
gi 495377997 150 ARALVLQPKLVILDEPTEGMSPWLEEEMGNLIR 182
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLA 519
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-195 |
4.78e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.26 E-value: 4.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 5 RSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGrlpinsgsmtwQEDGAPPEDLLL----------QP 74
Cdd:PRK10584 14 KSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAG-----------LDDGSSGEVSLVgqplhqmdeeAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 75 AELRARTgIGYVPQGRHIFSQMSVEDNL-LIALMAAQDD---RSRAIPEMV-FDLFPALYSLRHQRSGElpmeQQQHLAL 149
Cdd:PRK10584 83 AKLRAKH-VGFVFQSFMLIPTLNALENVeLPALLRGESSrqsRNGAKALLEqLGLGKRLDHLPAQLSGG----EQQRVAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495377997 150 ARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLL 195
Cdd:PRK10584 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILV 203
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-230 |
5.70e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.55 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQedGAPPEDLllQPAELRA-RTGIGYVPQG----- 89
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR--GEPLAKL--NRAQRKAfRRDIQMVFQDsisav 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 90 --RHIFSQMSVED--NLLIALMAAQDDRSRAIPEMVfDLFPALYSlrhQRSGELPMEQQQHLALARALVLQPKLVILDEP 165
Cdd:PRK10419 103 npRKTVREIIREPlrHLLSLDKAERLARASEMLRAV-DLDDSVLD---KRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 166 TEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQLDDLT 230
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFS 243
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-216 |
5.86e-12 |
|
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: 62.87 E-value: 5.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPpedlLLQPAELRARTGIGYVPQGRHIFSQ 95
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL--DGKP----ISQYEHKYLHSKVSLVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 mSVEDNLLIALMAAQDDRSRA----------IPEMVfdlfPALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEP 165
Cdd:cd03248 103 -SLQDNIAYGLQSCSFECVKEaaqkahahsfISELA----SGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495377997 166 TEGMSPWLEEEMGNLIRRLNREYglTILLLEQHVSFVRRvADYFLLLHRGR 216
Cdd:cd03248 178 TSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-215 |
7.97e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 63.23 E-value: 7.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 17 LWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDGAPPEDLllqpAELRARTGIGYV-PQGRHIFSq 95
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNF----EKLRKHIGIVFQnPDNQFVGS- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 mSVEDNLLIAL---MAAQDDRSRAIPEMVFDLfpALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEGMSPW 172
Cdd:PRK13648 100 -IVKYDVAFGLenhAVPYDEMHRRVSEALKQV--DMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495377997 173 LEEEMGNLIRRLNREYGLTILLLEQHVSFVRRvADYFLLLHRG 215
Cdd:PRK13648 177 ARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKG 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-221 |
1.09e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.98 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 17 LWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTwqedgappedLLLQPAELRARTG-IGYVPQGRHI--- 92
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIS----------ILGQPTRQALQKNlVAYVPQSEEVdws 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 93 FSQMsVEDNLLIA------LMAAQDDRSRAIPEMVFDLFPALySLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPT 166
Cdd:PRK15056 93 FPVL-VEDVVMMGryghmgWLRRAKKRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 167 EGMSPWLEEEMGNLIRRLnREYGLTILLLEQHVSFVRRVADYFLLLhRGRNVAHG 221
Cdd:PRK15056 171 TGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASG 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
11-221 |
1.18e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.72 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 11 YGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDL---------------LLQPA 75
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFL--GDKPISMLssrqlarrlallpqhHLTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 76 ELRARTGIGYvpqGR----HIFSQMSVEDNLLIAlmaaqddrsRAIPEMVFDlfpalySLRHQRSGELPMEQQQHLALAR 151
Cdd:PRK11231 90 GITVRELVAY---GRspwlSLWGRLSAEDNARVN---------QAMEQTRIN------HLADRRLTDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 152 ALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-210 |
1.29e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.49 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCI--MGRLPIN---SGSMTWQEDG--APPEDLLlq 73
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNiySPRTDTV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 74 paELRARtgIGYVPQGRHIFSqMSVEDNLLIAL-MAAQDDRSR------------AIPEMVFDLFpalyslrHQRSGELP 140
Cdd:PRK14239 83 --DLRKE--IGMVFQQPNPFP-MSIYENVVYGLrLKGIKDKQVldeavekslkgaSIWDEVKDRL-------HDSALGLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495377997 141 MEQQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYglTILLLEQHVSFVRRVAD---YFL 210
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDrtgFFL 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-216 |
1.38e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.41 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPinsgsmtwqedGAPPEDLLL--QPAELRA-----RTGIGYVPQGRH 91
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP-----------GRWEGEIFIdgKPVKIRNpqqaiAQGIAMVPEDRK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 92 ---IFSQMSVEDNllIALMAAQDDRSRAIPEMVFDLFPALYSLRHQR----SGELPMEQ-----QQHLALARALVLQPKL 159
Cdd:PRK13549 349 rdgIVPVMGVGKN--ITLAALDRFTGGSRIDDAAELKTILESIQRLKvktaSPELAIARlsggnQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 160 VILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-225 |
2.08e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.58 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCI-------MGRLPINSGSMTWQEDGA--PPEdlllqpaelraRTGIGYVPQG 89
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAIsgltrpqKGRIVLNGRVLFDAEKGIclPPE-----------KRRIGYVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 90 RHIFSQMSVEDNLLIAL---MAAQDDRSRAI--PEMVFDLFPALYSlrhqrSGElpmeqQQHLALARALVLQPKLVILDE 164
Cdd:PRK11144 85 ARLFPHYKVRGNLRYGMaksMVAQFDKIVALlgIEPLLDRYPGSLS-----GGE-----KQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 165 P---------TEGMsPWLEeemgnlirRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQ 225
Cdd:PRK11144 155 PlasldlprkRELL-PYLE--------RLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-226 |
3.73e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.27 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNcIMGRLpiNSGSMTWQEDGappeDLLL---------QPAELRARTGIGYv 86
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLR-TLNRM--NDKVSGYRYSG----DVLLggrsifnyrDVLEFRRRVGMLF- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 87 pQGRHIFSqMSVEDNLLIALMAaqddrSRAIPEMVFDLFP-------ALYSLRHQRSGELPME----QQQHLALARALVL 155
Cdd:PRK14271 108 -QRPNPFP-MSIMDNVLAGVRA-----HKLVPRKEFRGVAqarltevGLWDAVKDRLSDSPFRlsggQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495377997 156 QPKLVILDEPTEGMSPWLEEEMGNLIRRLNREygLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
14-228 |
4.72e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 60.90 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 14 NHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDGAPPEDLllqpAELRARTGIGYVPQGRHIF 93
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENE----KWVRSKVGLVFQDPDDQVF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 94 SqMSVEDNLLIALMAAQDDRSRaIPEMVFDLFPA--LYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEGMSP 171
Cdd:PRK13647 94 S-STVWDDVAFGPVNMGLDKDE-VERRVEEALKAvrMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 172 WLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQLDD 228
Cdd:PRK13647 172 RGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
12-226 |
5.32e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.99 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 12 GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINS-GSMTWQEDGAPpedllLQPAELRARTgiGYVPQGR 90
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkGSGSVLLNGMP-----IDAKEMRAIS--AYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 91 HIFSQMSVEDNLLIALM------AAQDDRSRAIPEMVFDLfpALYSLRHQRSGE------LPMEQQQHLALARALVLQPK 158
Cdd:TIGR00955 109 LFIPTLTVREHLMFQAHlrmprrVTKKEKRERVDEVLQAL--GLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 159 LVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
32-221 |
6.17e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.02 E-value: 6.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 32 VLGSPGMGKTTLVNCIMGRLPINSGSMtWQED--GAPPEDLLLQPA-----------ELRARTGIGYVPQGRHIFSQmSV 98
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTI-QVGDiyIGDKKNNHELITnpyskkiknfkELRRRVSMVFQFPEYQLFKD-TI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 99 EDNLLIALMAAQDDRSRAIPEMVFDL--FPALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEGMSPWLEEE 176
Cdd:PRK13631 135 EKDIMFGPVALGVKKSEAKKLAKFYLnkMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHE 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495377997 177 MGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:PRK13631 215 MMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-226 |
6.22e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.64 E-value: 6.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 12 GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMgRLPINSGSMTWqeDGAPPEDL-LLQPAELRARTGIGYVPQGR 90
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALL-RLINSQGEIWF--DGQPLHNLnRRQLLPVRHRIQVVFQDPNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 91 HIFSQMSVEDnlLIA---------LMAAQ-DDRSRAIPEMVfDLFPALyslRHQRSGELPMEQQQHLALARALVLQPKLV 160
Cdd:PRK15134 374 SLNPRLNVLQ--IIEeglrvhqptLSAAQrEQQVIAVMEEV-GLDPET---RHRYPAEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 161 ILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-216 |
9.90e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.50 E-value: 9.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFY-GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqedgAPPEDLLLQPAELR- 78
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWF----SGHDITRLKNREVPf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 79 ARTGIGYVPQGRHIFSQMSVEDNLLIALM---AAQDDRSRAIPEMV--FDLFPALYSLRHQRSGElpmeQQQHLALARAL 153
Cdd:PRK10908 77 LRRQIGMIFQDHHLLMDRTVYDNVAIPLIiagASGDDIRRRVSAALdkVGLLDKAKNFPIQLSGG----EQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495377997 154 VLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNReYGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-171 |
1.16e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.91 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 3 SLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTwqedgAPPEDLllqpAELRARTG 82
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVE-----VLGGDM----ADARHRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 83 ----IGYVPQ--GRHIFSQMSVEDNL-----LIALMAAQddRSRAIPEmvfdLFPA--LYSLRHQRSGELP--MEQQqhL 147
Cdd:NF033858 74 vcprIAYMPQglGKNLYPTLSVFENLdffgrLFGQDAAE--RRRRIDE----LLRAtgLAPFADRPAGKLSggMKQK--L 145
|
170 180
....*....|....*....|....
gi 495377997 148 ALARALVLQPKLVILDEPTEGMSP 171
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVDP 169
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-226 |
1.17e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.63 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 20 VDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINsGSmtwqedgappedLLLQPAELRA------RTGIGYVPQGRHIF 93
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GS------------LKINGIELREldpeswRKHLSWVGQNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 94 SQmSVEDNLLIALMAAQDDRSRA------IPEMVFDLFPALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTE 167
Cdd:PRK11174 436 HG-TLRDNVLLGNPDASDEQLQQalenawVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495377997 168 GMSPWLEEEMGNLIRRLNReyGLTILLLEQHVSFVRRVaDYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK11174 515 SLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAEL 570
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-221 |
1.26e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 60.03 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 17 LWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTwqedgapPEDLLLQPA---ELRARtgIGYVPQG-RHI 92
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTIT-------VGGMVLSEEtvwDVRRQ--VGMVFQNpDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 93 FSQMSVEDNLLIALmaaqddRSRAIP--EMVFDLFPALYSLR-----HQRSGELPMEQQQHLALARALVLQPKLVILDEP 165
Cdd:PRK13635 94 FVGATVQDDVAFGL------ENIGVPreEMVERVDQALRQVGmedflNREPHRLSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 166 TEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRvADYFLLLHRGRNVAHG 221
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
143-230 |
1.71e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.42 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 143 QQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGK 222
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
90
....*....|...
gi 495377997 223 VAQ-----LDDLT 230
Cdd:PRK15112 234 TADvlaspLHELT 246
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-226 |
5.88e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.83 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 17 LWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDGAPPEDLLLQPAELRARTGIGYVPQGRHIFSQM 96
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 97 SVEDnllIAL----MAAQDDRSRAIPEMVFDLFPALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEGMSPW 172
Cdd:PRK13649 103 VLKD---VAFgpqnFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495377997 173 LEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK13649 180 GRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-222 |
5.95e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.89 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRL--------PINSGSMTWQEDGAppedlllqpAELRARTGIGYV- 86
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpddnpnsKITVDGITLTAKTV---------WDIREKVGIVFQn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 87 PQGRhiFSQMSVEDNLLIALMAAQDDRSRAIpEMVFDLFPALYSLRHQRS--GELPMEQQQHLALARALVLQPKLVILDE 164
Cdd:PRK13640 93 PDNQ--FVGATVGDDVAFGLENRAVPRPEMI-KIVRDVLADVGMLDYIDSepANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 165 PTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVrRVADYFLLLHRGRNVAHGK 222
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGS 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-227 |
6.98e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.50 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 17 LWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDllLQPAELRARtGIGYVPQGRH---IF 93
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL--DGEDITG--LSPRERRRL-GVAYIPEDRLgrgLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 94 SQMSVEDNLliaLMAAQDD---------RSRAIPEMVFDLFPAlYSLRHqRSGELPMEQ-----QQHLALARALVLQPKL 159
Cdd:COG3845 349 PDMSVAENL---ILGRYRRppfsrggflDRKAIRAFAEELIEE-FDVRT-PGPDTPARSlsggnQQKVILARELSRDPKL 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 160 VILDEPTEGmspwLE----EEMGNLIRRLnREYGLTILLleqhVSF----VRRVADYFLLLHRGRNVAHGKVAQLD 227
Cdd:COG3845 424 LIAAQPTRG----LDvgaiEFIHQRLLEL-RDAGAAVLL----ISEdldeILALSDRIAVMYEGRIVGEVPAAEAT 490
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-226 |
8.66e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.81 E-value: 8.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPIN---SGSMTWQEDgappEDLLLQPAEL---RARtgigyvpQGRHI 92
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGR----EILNLPEKELnklRAE-------QISMI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 93 FSQ--------MSVEDNLLIALMAAQD-DRSRAIPEMVFDLFPALYSLRHQRSGELPME----QQQHLALARALVLQPKL 159
Cdd:PRK09473 103 FQDpmtslnpyMRVGEQLMEVLMLHKGmSKAEAFEESVRMLDAVKMPEARKRMKMYPHEfsggMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 160 VILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-216 |
9.07e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.26 E-value: 9.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDGAPPEdlllqpAELRA-RTGIGYVPQGRH---IFS 94
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPR------SPLDAvKKGMAYITESRRdngFFP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 95 QMSVEDNLLIA----------LMAAQDDRS-RAIPEMVFDLFPALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILD 163
Cdd:PRK09700 355 NFSIAQNMAISrslkdggykgAMGLFHEVDeQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495377997 164 EPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-195 |
1.62e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 56.63 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSM------------TW----------------------QEDG 64
Cdd:PRK13633 28 DVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtsdeenLWdirnkagmvfqnpdnqivativEEDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 65 A-PPEDLLLQPAELRARtgigyvpqgrhifsqmsVEDNLLIALMAaqdDRSRAIPemvfdlfpalyslrHQRSGElpmeQ 143
Cdd:PRK13633 108 AfGPENLGIPPEEIRER-----------------VDESLKKVGMY---EYRRHAP--------------HLLSGG----Q 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495377997 144 QQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLL 195
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILI 201
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-227 |
1.94e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINS--GSMTWqeDGAPpedllLQPAELR--ARTGIGYVPQGRHIFS 94
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIF--EGEE-----LQASNIRdtERAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 95 QMSVEDNL----------LIALMAAQDDRSRAIPEMVFDLFPALyslrhqRSGELPMEQQQHLALARALVLQPKLVILDE 164
Cdd:PRK13549 96 ELSVLENIflgneitpggIMDYDAMYLRAQKLLAQLKLDINPAT------PVGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 165 PTEGMSpwlEEEMG---NLIRRLnREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQLD 227
Cdd:PRK13549 170 PTASLT---ESETAvllDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMT 231
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-215 |
2.93e-09 |
|
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: 54.94 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRlpINSGSMTwqedGappeDLLL--QPAELRARTGIGYVPQGRHIF 93
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGR--KTAGVIT----G----EILIngRPLDKNFQRSTGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 94 SQMSVEDNLlialmaaqddrsraipemvfdLFPALysLRhqrsgELPMEQQQHLALARALVLQPKLVILDEPTEGMSPWL 173
Cdd:cd03232 92 PNLTVREAL---------------------RFSAL--LR-----GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495377997 174 EEEMGNLIRRLNREyGLTIL---------LLEQhvsFvrrvaDYFLLLHRG 215
Cdd:cd03232 144 AYNIVRFLKKLADS-GQAILctihqpsasIFEK---F-----DRLLLLKRG 185
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-221 |
6.67e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 55.42 E-value: 6.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNcIMGRL--PINSGSMTWQEDGAPPEDlllqpAELRA--RTGIGYVPQGRHIFS 94
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVR-LLNRLiePTRGQVLIDGVDIAKISD-----AELREvrRKKIAMVFQSFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 95 QMSVEDN----LLIALMAAQDDRSRAIPEMvfdLFPALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEGMS 170
Cdd:PRK10070 120 HMTVLDNtafgMELAGINAEERREKALDAL---RQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495377997 171 PWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-194 |
9.28e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 54.71 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTW-----------QEDGAPPEDLLLQPA---------ELR 78
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktKEKEKVLEKLVIQKTrfkkikkikEIR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 79 ARTGIGYVPQGRHIFSQMSVEDNLLIAL---MAAQDDRSRA--IPEMVfDLfPALYSlrhQRSG-ELPMEQQQHLALARA 152
Cdd:PRK13651 105 RRVGVVFQFAEYQLFEQTIEKDIIFGPVsmgVSKEEAKKRAakYIELV-GL-DESYL---QRSPfELSGGQKRRVALAGI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495377997 153 LVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILL 194
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIIL 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
133-226 |
1.10e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.71 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 133 HQRSGElpmeQQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLL 212
Cdd:PRK15134 155 HQLSGG----ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM 230
|
90
....*....|....
gi 495377997 213 HRGRNVAHGKVAQL 226
Cdd:PRK15134 231 QNGRCVEQNRAATL 244
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-227 |
1.34e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQedGAPPEdllLQPAELRARTGIGYVPQGRHIFSQMSV 98
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQ--GKEID---FKSSKEALENGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 99 EDNL------LIALMAAQD---DRSRAI-PEMVFDLFPalyslrHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEG 168
Cdd:PRK10982 91 MDNMwlgrypTKGMFVDQDkmyRDTKAIfDELDIDIDP------RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495377997 169 MSpwlEEEMGNL---IRRLnREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQLD 227
Cdd:PRK10982 165 LT---EKEVNHLftiIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLT 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-234 |
1.43e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.02 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDG--APPEDLLLQPaeLRARTGIGYVPQGRHIFSQm 96
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITitHKTKDKYIRP--VRKRIGMVFQFPESQLFED- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 97 SVEDNLLIAL----MAAQDDRSRAIpEMVFDL-FP--ALYSLRHQRSGElpmeQQQHLALARALVLQPKLVILDEPTEGM 169
Cdd:PRK13646 102 TVEREIIFGPknfkMNLDEVKNYAH-RLLMDLgFSrdVMSQSPFQMSGG----QMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 170 SPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL--DDLTVNKW 234
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELfkDKKKLADW 243
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-187 |
2.21e-08 |
|
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: 54.25 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 26 PGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTwqedgAPPEDLLLQPAELRarTGIGYVPQGRHIFSQMSVEDNLLIA 105
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDAT-----VAGKSILTNISDVH--QNMGYCPQFDAIDDLLTGREHLYLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 106 LmaaqddRSRAIP----EMVFD-----LFPALYSLRhqRSGELPMEQQQHLALARALVLQPKLVILDEPTEGMSPWLEEE 176
Cdd:TIGR01257 2037 A------RLRGVPaeeiEKVANwsiqsLGLSLYADR--LAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170
....*....|.
gi 495377997 177 MGNLIRRLNRE 187
Cdd:TIGR01257 2109 LWNTIVSIIRE 2119
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-226 |
2.84e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 52.87 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNcIMGR-LPINSGSMTWqeDGAPPEDLllqPAELRARTgIGYVPQGRHIFS 94
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRhQPPSEGEILL--DAQPLESW---SSKAFARK-VAYLPQQLPAAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 95 QMSVEDNLLI-------AL-MAAQDDRSRAipEMVFDLFpALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPT 166
Cdd:PRK10575 99 GMTVRELVAIgrypwhgALgRFGAADREKV--EEAISLV-GLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 167 EGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-165 |
2.97e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 13 QNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPinsgsmtwqedgaPPEDlllqpAELRARTGIGYVPQGRHI 92
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS-------------HAET-----SSVVIRGSVAYVPQVSWI 690
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495377997 93 FSQmSVEDNLLIALMAAQDDRSRAIPEMVF----DLFPAlYSLRH--QRSGELPMEQQQHLALARALVLQPKLVILDEP 165
Cdd:PLN03232 691 FNA-TVRENILFGSDFESERYWRAIDVTALqhdlDLLPG-RDLTEigERGVNISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-215 |
3.31e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 12 GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGsmtwqedgappedlllqpAELRARTGIGYVPQGRH 91
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD------------------ASVVIRGTVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 92 IFSQmSVEDNLLIALMAAQDDRSRAIpemvfdlfpALYSLRH--------------QRSGELPMEQQQHLALARALVLQP 157
Cdd:PLN03130 690 IFNA-TVRDNILFGSPFDPERYERAI---------DVTALQHdldllpggdlteigERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495377997 158 KLVILDEPTEGMSPWLEEEMGNliRRLNREY-GLTILLLEQHVSFVRRVaDYFLLLHRG 215
Cdd:PLN03130 760 DVYIFDDPLSALDAHVGRQVFD--KCIKDELrGKTRVLVTNQLHFLSQV-DRIILVHEG 815
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-232 |
4.19e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLpiNSGSMTWQED--GAPPEDLLLQpaelraRTgIGYVPQGR-HI 92
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGDRlvNGRPLDSSFQ------RS-IGYVQQQDlHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 93 fSQMSVEDNLliaLMAAQDDRSRAIP--------EMVFDLFP------ALYSLrhqrSGE-LPMEQQQHLALARALVLQP 157
Cdd:TIGR00956 849 -PTSTVRESL---RFSAYLRQPKSVSksekmeyvEEVIKLLEmesyadAVVGV----PGEgLNVEQRKRLTIGVELVAKP 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 158 KLVI-LDEPTEGM---SPWleeEMGNLIRRLNrEYGLTIL---------LLEQHvsfvrrvaDYFLLLHRGrnvahGKVA 224
Cdd:TIGR00956 921 KLLLfLDEPTSGLdsqTAW---SICKLMRKLA-DHGQAILctihqpsaiLFEEF--------DRLLLLQKG-----GQTV 983
|
....*...
gi 495377997 225 QLDDLTVN 232
Cdd:TIGR00956 984 YFGDLGEN 991
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
138-226 |
4.82e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 52.60 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 138 ELPMEQQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRN 217
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQT 237
|
....*....
gi 495377997 218 VAHGKVAQL 226
Cdd:COG4170 238 VESGPTEQI 246
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
19-183 |
7.94e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.12 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTwqedgAPPEDLLL----QPaelrartgigYVPQGrhifs 94
Cdd:COG4178 381 DLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA-----RPAGARVLflpqRP----------YLPLG----- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 95 qmSVEDNLLIALMAAQ--DDRSRAIPEMVF--DLFPALYSLRHqRSGELPMEQQQHLALARALVLQPKLVILDEPTEGMS 170
Cdd:COG4178 441 --TLREALLYPATAEAfsDAELREALEAVGlgHLAERLDEEAD-WDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
170
....*....|...
gi 495377997 171 PWLEEEMGNLIRR 183
Cdd:COG4178 518 EENEAALYQLLRE 530
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
12-229 |
7.95e-08 |
|
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: 50.99 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 12 GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRlP---INSGSMTWQEdgappEDLLLQPAELRARTGIGyvpq 88
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PkyeVTEGEILFKG-----EDITDLPPEERARLGIF---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 89 grhifsqmsvednllialMAAQddRSRAIPEMVFDLFpaLYSLRHQRSGelpmEQQQHLALARALVLQPKLVILDEPTEG 168
Cdd:cd03217 81 ------------------LAFQ--YPPEIPGVKNADF--LRYVNEGFSG----GEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 169 MSPWLEEEMGNLIRRLnREYGLTILLLEQHvsfvRRVADYF-----LLLHRGRNVAHGKVAQLDDL 229
Cdd:cd03217 135 LDIDALRLVAEVINKL-REEGKSVLIITHY----QRLLDYIkpdrvHVLYDGRIVKSGDKELALEI 195
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-215 |
8.06e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 51.18 E-value: 8.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 17 LWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLLLQPAELRARTGIGYVPQGRHIFSQm 96
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW--SNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 97 SVEDNLLIAlMAAQDDRSRAIPEMVfDLFPALYSLRH-------QRSGELPMEQQQHLALARALVLQPKLVILDEPTEGM 169
Cdd:cd03290 94 TVEENITFG-SPFNKQRYKAVTDAC-SLQPDIDLLPFgdqteigERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495377997 170 SPWLEEE-MGNLIRRLNREYGLTILLLEQHVSFVRRvADYFLLLHRG 215
Cdd:cd03290 172 DIHLSDHlMQEGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-226 |
8.29e-08 |
|
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: 51.46 E-value: 8.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLLLQpaELRARtgIGYVPQGRHIFSQ 95
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI--DGQDIREVTLD--SLRRA--IGVVPQDTVLFND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 mSVEDNLLIALMAAQDD--RSRAIPEMVFDL---FPALYSLR-HQRSGELPMEQQQHLALARALVLQPKLVILDEPTEGM 169
Cdd:cd03253 90 -TIGYNIRYGRPDATDEevIEAAKAAQIHDKimrFPDGYDTIvGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 170 SPWLEEEMGNLIRRLNReyGLTILLLEQHVSFVRRvADYFLLLHRGRNVAHGKVAQL 226
Cdd:cd03253 169 DTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-224 |
1.28e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.98 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPIN--------SGSMTWqeDGAPPEDL-L 71
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTL--NGEPLAAIdA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 72 LQPAELRArtgigYVPQGRHIFSQMSVEDNLLIALM------AAQDDRSRAIPEMVFDLFPALYSLRHQ----RSGELPM 141
Cdd:PRK13547 79 PRLARLRA-----VLPQAAQPAFAFSAREIVLLGRYpharraGALTHRDGEIAWQALALAGATALVGRDvttlSGGELAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 142 EQqqhlaLARAL---------VLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLL 212
Cdd:PRK13547 154 VQ-----FARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAML 228
|
250
....*....|..
gi 495377997 213 HRGRNVAHGKVA 224
Cdd:PRK13547 229 ADGAIVAHGAPA 240
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
138-231 |
1.48e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.96 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 138 ELPMEQQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRN 217
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
90
....*....|....
gi 495377997 218 VahgKVAQLDDLTV 231
Cdd:PRK15093 238 V---ETAPSKELVT 248
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-221 |
1.74e-07 |
|
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: 50.10 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappEDLLLQPAElRARTGIGYVPQGRHIFSQ 95
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI--DG---IDISTIPLE-DLRSSLTIIPQDPTLFSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 mSVEDNLLIALMaaQDDRsraipemvfDLFPALyslRHQRSGE-LPMEQQQHLALARALVLQPKLVILDEPTEGmspwLE 174
Cdd:cd03369 97 -TIRSNLDPFDE--YSDE---------EIYGAL---RVSEGGLnLSQGQRQLLCLARALLKRPRVLVLDEATAS----ID 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495377997 175 EEMGNLIRRLNRE--YGLTILLLEQHvsfVRRVADY--FLLLHRGRNVAHG 221
Cdd:cd03369 158 YATDALIQKTIREefTNSTILTIAHR---LRTIIDYdkILVMDAGEVKEYD 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-221 |
1.87e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 4 LRS--VNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQE---DGAPPEDLllQP---- 74
Cdd:PRK10261 325 LRSglLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqriDTLSPGKL--QAlrrd 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 75 ---------AELRARTGIGYvpqgrHIFSQMSVEdNLLIALMAAQddRSRAIPEMVFDLFPALYSLRHQRSGElpmeQQQ 145
Cdd:PRK10261 403 iqfifqdpyASLDPRQTVGD-----SIMEPLRVH-GLLPGKAAAA--RVAWLLERVGLLPEHAWRYPHEFSGG----QRQ 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 146 HLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-166 |
1.93e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 51.00 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLLLQPAELRAR 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLV--AGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TgigyVPQGRHIFSQMSVEDNLLI---------ALMAAQDDRS--RAIPEMVFDLFPAlyslrhQRSGELPMEQQQHLAL 149
Cdd:PRK09536 81 S----VPQDTSLSFEFDVRQVVEMgrtphrsrfDTWTETDRAAveRAMERTGVAQFAD------RPVTSLSGGERQRVLL 150
|
170
....*....|....*..
gi 495377997 150 ARALVLQPKLVILDEPT 166
Cdd:PRK09536 151 ARALAQATPVLLLDEPT 167
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
143-193 |
3.11e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 48.69 E-value: 3.11e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 495377997 143 QQQHLALARALVLQPKLVILDEPTEGmspwLEEEMGNLIRRLNREYGLTIL 193
Cdd:cd03223 96 EQQRLAFARLLLHKPKFVFLDEATSA----LDEESEDRLYQLLKELGITVI 142
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
13-193 |
3.54e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 49.73 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 13 QNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGappeDLLLQPAELRARTGIGYVPQG-RH 91
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII--DG----DLLTEENVWDIRHKIGMVFQNpDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 92 IFSQMSVEDNLLIALmaaqDDRSRAIPEMVFDLFPAL-----YSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPT 166
Cdd:PRK13650 93 QFVGATVEDDVAFGL----ENKGIPHEEMKERVNEALelvgmQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180
....*....|....*....|....*..
gi 495377997 167 EGMSPWLEEEMGNLIRRLNREYGLTIL 193
Cdd:PRK13650 169 SMLDPEGRLELIKTIKGIRDDYQMTVI 195
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-219 |
3.61e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.49 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFY----GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNcIMGRLPINSgSMTWQEDGAPPEDLLL-QPA 75
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKPT-SGTYRVAGQDVATLDAdALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 76 ELRaRTGIGYVPQGRHIFSQMSVEDNLLI----ALMAAQDDRSRAIpEMVFDLfpALYSLRHQRSGELPMEQQQHLALAR 151
Cdd:PRK10535 82 QLR-REHFGFIFQRYHLLSHLTAAQNVEVpavyAGLERKQRLLRAQ-ELLQRL--GLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 152 ALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLnREYGLTILLLeQHVSFVRRVADYFLLLHRGRNVA 219
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIV-THDPQVAAQAERVIEIRDGEIVR 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-216 |
4.07e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.05 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEdgappEDLLLQPAELRARTGIGYVPQGRH---IFSQ 95
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNG-----KEINALSTAQRLARGLVYLPEDRQssgLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 MSVEDN---LLIALMA--AQDDRSRAIPEMVFDLFPALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEGMS 170
Cdd:PRK15439 356 APLAWNvcaLTHNRRGfwIKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495377997 171 PWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-169 |
4.29e-07 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 49.03 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 20 VDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQedgaPPEDLLLQPAELRARTGIGYVPQgrhIFSQMSVE 99
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLN----GGPLDFQRDSIARGLLYLGHAPG---IKTTLSVL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495377997 100 DNL-LIALMAAQDDRSRAIPEMvfdlfpALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEGM 169
Cdd:cd03231 92 ENLrFWHADHSDEQVEEALARV------GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-222 |
4.43e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.44 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 17 LWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDGAPPEDLLLQPAELRARTGIGYVPQGRHIFSQM 96
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 97 SVEDNLLIAL-MAAQDDRSR----------AIPEMVFDLFPAlyslrhqrsgELPMEQQQHLALARALVLQPKLVILDEP 165
Cdd:PRK13641 103 VLKDVEFGPKnFGFSEDEAKekalkwlkkvGLSEDLISKSPF----------ELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495377997 166 TEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGK 222
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHAS 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
133-221 |
4.56e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 49.31 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 133 HQRSGElpmeQQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLL 212
Cdd:PRK13639 136 HHLSGG----QKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVM 210
|
....*....
gi 495377997 213 HRGRNVAHG 221
Cdd:PRK13639 211 SDGKIIKEG 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-222 |
7.32e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 48.83 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNH-ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQE-DGAPPEDLllqpAELR 78
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGiDTGDFSKL----QGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 79 ARTGIGYV-PQ----GRHIFSQMSV-EDNLLIALMAAQDDRSRAIPEMvfdlfpALYSLRHQRSGELPMEQQQHLALARA 152
Cdd:PRK13644 77 KLVGIVFQnPEtqfvGRTVEEDLAFgPENLCLPPIEIRKRVDRALAEI------GLEKYRHRSPKTLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 153 LVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVrRVADYFLLLHRGRNVAHGK 222
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGE 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-193 |
8.29e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 48.03 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPIN---SGSMTWqeDGAPPedlllQPAELRARTGIGYVPQGRHI 92
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHY--NGIPY-----KEFAEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 93 FSQMSVEDNLLIALMAAQDDRSRAIpemvfdlfpalyslrhqrSGelpmEQQQHLALARALVLQPKLVILDEPTEGMSPW 172
Cdd:cd03233 95 FPTLTVRETLDFALRCKGNEFVRGI------------------SG----GERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180
....*....|....*....|.
gi 495377997 173 LEEEMGNLIRRLNREYGLTIL 193
Cdd:cd03233 153 TALEILKCIRTMADVLKTTTF 173
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-183 |
8.52e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 47.95 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDGAPPEDLllqpaelraRTGIGYVPQGRHIFSQ 95
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---------AEACHYLGHRNAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 MSVEDNLliALMAAQDDRSRAIPEMVFDLFpALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPTEGMSPWLEE 175
Cdd:PRK13539 88 LTVAENL--EFWAAFLGGEELDIAAALEAV-GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
....*...
gi 495377997 176 EMGNLIRR 183
Cdd:PRK13539 165 LFAELIRA 172
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-193 |
1.30e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 47.79 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEdgappEDLLLQPAElRAR 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEG-----EDISTLKPE-IYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGYVPQGRHIFSQmSVEDNLLIALM---------AAQDDRSR-AIPEMVFDlfpalyslrhQRSGELPMEQQQHLALA 150
Cdd:PRK10247 81 QQVSYCAQTPTLFGD-TVYDNLIFPWQirnqqpdpaIFLDDLERfALPDTILT----------KNIAELSGGEKQRISLI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495377997 151 RALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTIL 193
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVL 192
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
133-226 |
1.88e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 133 HQRSGELpmeqQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLL 212
Cdd:PRK10261 167 HQLSGGM----RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
90
....*....|....
gi 495377997 213 HRGRNVAHGKVAQL 226
Cdd:PRK10261 243 YQGEAVETGSVEQI 256
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-166 |
2.04e-06 |
|
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: 46.97 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 20 VDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLLLQPAElrartGIGYVPQGRHIFSQMSVE 99
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRW--NGTPLAEQRDEPHE-----NILYLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495377997 100 DNL--LIALMAAQDdrsraipEMVFDLFPA--LYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPT 166
Cdd:TIGR01189 92 ENLhfWAAIHGGAQ-------RTIEDALAAvgLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
15-223 |
2.20e-06 |
|
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: 46.55 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 15 HILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIM---GRLPINSGSMTwqedgaPPEDLLLQPAELRA--RTGIGYVPQG 89
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLyasGKARLISFLPK------FSRNKLIFIDQLQFliDVGLGYLTLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 90 RhIFSQMSVednllialmaaqddrsraipemvfdlfpalyslrhqrsGELpmeQQQHLALARALVLQPKLVILDEPTEGM 169
Cdd:cd03238 83 Q-KLSTLSG--------------------------------------GEL---QRVKLASELFSEPPGTLFILDEPSTGL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495377997 170 SPWLEEEMGNLIRRLnREYGLTILLLEQHVSFVRRvADYFLLLHRGRNVAHGKV 223
Cdd:cd03238 121 HQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSS-ADWIIDFGPGSGKSGGKV 172
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-198 |
2.74e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.88 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 13 QNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQ-EDGAPPEDLLLQPAELRARTgigyVPQGRH 91
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDvPDNQFGREASLIDAIGRKGD----FKDAVE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 92 IFSQMSVEDNLLIalmaaqddrsraipemvfdlfpalysLRhqRSGELPMEQQQHLALARALVLQPKLVILDEPTEGMSP 171
Cdd:COG2401 118 LLNAVGLSDAVLW--------------------------LR--RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180
....*....|....*....|....*..
gi 495377997 172 WLEEEMGNLIRRLNREYGLTILLLEQH 198
Cdd:COG2401 170 QTAKRVARNLQKLARRAGITLVVATHH 196
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-171 |
2.83e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.98 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 12 GQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMgRLPINSGSMtwQEDGAPPEDLLLQpaelRARTGIGYVPQGRH 91
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEI--QIDGVSWNSVTLQ----TWRKAFGVIPQKVF 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 92 IFSQmSVEDNLLIALMAAQDDRSRAIPEM----VFDLFPALYSLRHQRSGE-LPMEQQQHLALARALVLQPKLVILDEPT 166
Cdd:TIGR01271 1303 IFSG-TFRKNLDPYEQWSDEEIWKVAEEVglksVIEQFPDKLDFVLVDGGYvLSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
....*
gi 495377997 167 EGMSP 171
Cdd:TIGR01271 1382 AHLDP 1386
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-88 |
3.70e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.19 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDGAppedlllqpaelrart 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENAN---------------- 383
|
....*..
gi 495377997 82 gIGYVPQ 88
Cdd:PRK15064 384 -IGYYAQ 389
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-185 |
4.11e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 47.05 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDGAppedlllqpaelrartgIGYVPQgRHIFSQMSV 98
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGK-----------------LFYVPQ-RPYMTLGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 99 EDNLlIALMAAQDDRSRAIPEMVFDLFPALYSLRH--QRSG----------ELPMEQQQHLALARALVLQPKLVILDEPT 166
Cdd:TIGR00954 532 RDQI-IYPDSSEDMKRRGLSDKDLEQILDNVQLTHilEREGgwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170
....*....|....*....
gi 495377997 167 EGMSPWLEEEMGNLIRRLN 185
Cdd:TIGR00954 611 SAVSVDVEGYMYRLCREFG 629
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-221 |
4.14e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 46.52 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 11 YGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNcIMGRLPINSGSMTW---------------------QEDGAPPED 69
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLR-TLSRLMTPAHGHVWldgehiqhyaskevarrigllAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 70 LLLQpaELRARtgiGYVPQgRHIFSQMSVEDnllialmaaQDDRSRAIPEMvfdlfpALYSLRHQRSGELPMEQQQHLAL 149
Cdd:PRK10253 96 ITVQ--ELVAR---GRYPH-QPLFTRWRKED---------EEAVTKAMQAT------GITHLADQSVDTLSGGQRQRAWI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495377997 150 ARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHG 221
Cdd:PRK10253 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-216 |
4.79e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMtWqedgappedlllqpaelrARTGIGYVPQGRHIFSQ 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-W------------------AERSIAYVPQQAWIMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 mSVEDNLLIALMAAQDDRSRAIpeMVFDLFPALYSLrhqrSGELPME-----------QQQHLALARALVLQPKLVILDE 164
Cdd:PTZ00243 736 -TVRGNILFFDEEDAARLADAV--RVSQLEADLAQL----GGGLETEigekgvnlsggQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 165 PTEGmspwLEEEMGNLIRR---LNREYGLTILLLEQHVSFVRRvADYFLLLHRGR 216
Cdd:PTZ00243 809 PLSA----LDAHVGERVVEecfLGALAGKTRVLATHQVHVVPR-ADYVVALGDGR 858
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
7-193 |
6.96e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 45.85 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 7 VNQFYGqnhilwdVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDGAPPEDLLlqpaELRARTGIGYV 86
Cdd:PRK13642 20 VNQLNG-------VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVW----NLRRKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 87 -PQGRhiFSQMSVEDNLLIALmaaqddRSRAIP--EMVFDLFPALYSL-----RHQRSGELPMEQQQHLALARALVLQPK 158
Cdd:PRK13642 89 nPDNQ--FVGATVEDDVAFGM------ENQGIPreEMIKRVDEALLAVnmldfKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190
....*....|....*....|....*....|....*
gi 495377997 159 LVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTIL 193
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVL 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-228 |
7.11e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.54 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 22 LDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQedGAP-----PEDLllQPAelrartGIGYVPQGRHIFSQM 96
Cdd:PRK10762 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYL--GKEvtfngPKSS--QEA------GIGIIHQELNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 97 SVEDNLLIAL-------------MAAQDDRsraipemvfdLFPALySLRH---QRSGELPMEQQQHLALARALVLQPKLV 160
Cdd:PRK10762 95 TIAENIFLGRefvnrfgridwkkMYAEADK----------LLARL-NLRFssdKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 161 ILDEPTEGMSPWLEEEMGNLIRRLnREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQLDD 228
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTE 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
149-226 |
1.02e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.46 E-value: 1.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 149 LARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:COG4586 165 LAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEEL 242
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
6-226 |
4.22e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 43.93 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 6 SVNQF-YGQNH--ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQedGAPPEDLLLQpaELRARTG 82
Cdd:PRK10789 317 NIRQFtYPQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFH--DIPLTKLQLD--SWRSRLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 83 IgyVPQGRHIFSQmSVEDNllIAL---MAAQDDRSRA-----IPEMVFDLfPALYSLR-HQRSGELPMEQQQHLALARAL 153
Cdd:PRK10789 393 V--VSQTPFLFSD-TVANN--IALgrpDATQQEIEHVarlasVHDDILRL-PQGYDTEvGERGVMLSGGQKQRISIARAL 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495377997 154 VLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNReyGLTILLLEQHVSFVRRvADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQL 536
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-227 |
4.45e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 43.75 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 17 LWDVDLDLPPGTCTGVLGSPGMGKTTLvncimgrLPINSGSmtWQEDGAppeDLLLQPAELRART-------GIGYVPQG 89
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTL-------LKILSGN--YQPDAG---SILIDGQEMRFASttaalaaGVAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 90 RHIFSQMSVEDNLLIALMAAQD---DRSRAIPE-------MVFDLFPalyslrHQRSGELPMEQQQHLALARALVLQPKL 159
Cdd:PRK11288 88 LHLVPEMTVAENLYLGQLPHKGgivNRRLLNYEareqlehLGVDIDP------DTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495377997 160 VILDEPTEGMSPWLEEEMGNLIRRLnREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVA-HGKVAQLD 227
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYVAtFDDMAQVD 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
4.68e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 43.44 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYG--QNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMtwQEDGappedLLLQPAELR 78
Cdd:PRK13632 7 MIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEI--KIDG-----ITISKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 79 -ARTGIGYVPQG-RHIFSQMSVEDNLLIALMAAQDDRSRaIPEMVFDlfpalYSLRHQRSGELPME-------QQQHLAL 149
Cdd:PRK13632 80 eIRKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKK-MKDIIDD-----LAKKVGMEDYLDKEpqnlsggQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495377997 150 ARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRvADYFLLLHRGRNVAHGK 222
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGK 225
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
113-226 |
6.17e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.19 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 113 RSRAI----------PEMVFDLFPalyslrHQRSGELpmeqQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIR 182
Cdd:PRK11022 128 RQRAIdllnqvgipdPASRLDVYP------HQLSGGM----SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLL 197
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 495377997 183 RLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK11022 198 ELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-221 |
6.43e-05 |
|
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: 43.64 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 2 LSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMG--RLPINSGSMTWQ--------------EDGA 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 66 P---------PEDL----LLQPAELRARTGIGYVPQGRH-IFSQMSVEDNLLIALMAAQDDRSRAIpEMVFDLFpALYSL 131
Cdd:TIGR03269 81 PcpvcggtlePEEVdfwnLSDKLRRRIRKRIAIMLQRTFaLYGDDTVLDNVLEALEEIGYEGKEAV-GRAVDLI-EMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 132 RHQR---SGELPMEQQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADY 208
Cdd:TIGR03269 159 SHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250
....*....|...
gi 495377997 209 FLLLHRGRNVAHG 221
Cdd:TIGR03269 239 AIWLENGEIKEEG 251
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-169 |
9.84e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 9.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLP----INSGSMTWqeDGAPPEDLllqpaELRARTGIGYVPQGRH 91
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITY--DGITPEEI-----KKHYRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 92 IFSQMSVEDNL-LIALMAAQDDRSRAIPEMVF-----DLFPALYSLRHQRSGELPME--------QQQHLALARALVLQP 157
Cdd:TIGR00956 149 HFPHLTVGETLdFAARCKTPQNRPDGVSREEYakhiaDVYMATYGLSHTRNTKVGNDfvrgvsggERKRVSIAEASLGGA 228
|
170
....*....|..
gi 495377997 158 KLVILDEPTEGM 169
Cdd:TIGR00956 229 KIQCWDNATRGL 240
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-226 |
1.95e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.61 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLP--INSGSMTWQEDGAPpedllLQPAELRARTgIGYVPQ-------- 88
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagVRQTAGRVLLDGKP-----VAPCALRGRK-IATIMQnprsafnp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 89 -------GRHIFSQMSVEDNlLIALMAAQDDRSRAIPEMVFDLFPalyslrHQRSGElpMEQQQHLALarALVLQPKLVI 161
Cdd:PRK10418 95 lhtmhthARETCLALGKPAD-DATLTAALEAVGLENAARVLKLYP------FEMSGG--MLQRMMIAL--ALLCEAPFII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495377997 162 LDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRRVADYFLLLHRGRNVAHGKVAQL 226
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-207 |
2.31e-04 |
|
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: 41.69 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 31 GVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDgappedlllqpaelrartgIGYVPQGRHIFSQMSVEDnLLIALMAAQ 110
Cdd:COG1245 370 GIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-------------------ISYKPQYISPDYDGTVEE-FLRSANTDD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 111 DDRSRAIPEMVFDLfpALYSLRHQR-----SGELpmeqqQHLALARALVLQPKLVILDEPtegmSPWL--EE--EMGNLI 181
Cdd:COG1245 430 FGSSYYKTEIIKPL--GLEKLLDKNvkdlsGGEL-----QRVAIAACLSRDADLYLLDEP----SAHLdvEQrlAVAKAI 498
|
170 180
....*....|....*....|....*.
gi 495377997 182 RRLNREYGLTILLLEQHVSFVRRVAD 207
Cdd:COG1245 499 RRFAENRGKTAMVVDHDIYLIDYISD 524
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
143-207 |
2.62e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 2.62e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 143 QQQHLALARAL--VLQPKLVILDEPTEGMSPWLEEEMGNLIRRLnREYGLTILLLE---QHVSFVRRVAD 207
Cdd:PRK00635 481 EQERTALAKHLgaELIGITYILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEhdeQMISLADRIID 549
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-198 |
3.18e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.63 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVnQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEdgappedllLQPAELrAR 80
Cdd:PRK13541 1 MLSLHQL-QFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKN---------CNINNI-AK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 81 TGIGYVPQGRHIFSQMSVEDNLliALMAAQDDRSRAIPEMVFdlFPALYSLRHQRSGELPMEQQQHLALARALVLQPKLV 160
Cdd:PRK13541 70 PYCTYIGHNLGLKLEMTVFENL--KFWSEIYNSAETLYAAIH--YFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLW 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 495377997 161 ILDEPTEGMSPWLEEEMGNLIRRLNREYGltILLLEQH 198
Cdd:PRK13541 146 LLDEVETNLSKENRDLLNNLIVMKANSGG--IVLLSSH 181
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-202 |
3.88e-04 |
|
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: 39.66 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 26 PGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSmtwqedgappedlllqpaelrartgigyvpqgrhifsqmsvednllIA 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG----------------------------------------------VI 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 106 LMAAQDDRSRAIPEMVFDLFPALYSLRHQrsgelpmEQQQHLALARALVLQPKLVILDEPTEgmspWLEEEMGNLIRRLN 185
Cdd:smart00382 35 YIDGEDILEEVLDQLLLIIVGGKKASGSG-------ELRLRLALALARKLKPDVLILDEITS----LLDAEQEALLLLLE 103
|
170
....*....|....*..
gi 495377997 186 REYGLTILLLEQHVSFV 202
Cdd:smart00382 104 ELRLLLLLKSEKNLTVI 120
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
144-171 |
4.10e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 4.10e-04
10 20
....*....|....*....|....*....
gi 495377997 144 QQHLAL-ARALVLQPKLVILDEPTEGMSP 171
Cdd:PRK10938 406 QQRLALiVRALVKHPTLLILDEPLQGLDP 434
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
144-215 |
4.13e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.09 E-value: 4.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 144 QQHLALARALVLQPKLVILDEPTEGMS----PWLEEEMgnlirrlnREYGLTILLLEQHVSFVRRVADYFLLLHRG 215
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDietiEWLEGFL--------KTFQGSIIFISHDRSFIRNMATRIVDLDRG 229
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-59 |
4.21e-04 |
|
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: 41.07 E-value: 4.21e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 495377997 11 YGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMT 59
Cdd:TIGR03719 332 FGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE 380
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-216 |
7.54e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.10 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTwqedgappedllLQPAELRART-------GIGYVPQGRH 91
Cdd:PRK10982 266 DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTIT------------LHGKKINNHNaneainhGFALVTEERR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 92 ---IFSQMSVEDNLLIALMAA--------QDDRSRAIPEMVFDLFPALYSLRHQRSGELPMEQQQHLALARALVLQPKLV 160
Cdd:PRK10982 334 stgIYAYLDIGFNSLISNIRNyknkvgllDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEIL 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 161 ILDEPTEGMSPWLEEEMGNLIRRLNREyGLTILLLEQHVSFVRRVADYFLLLHRGR 216
Cdd:PRK10982 414 MLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-56 |
1.08e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.77 E-value: 1.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSG 56
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG 367
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-83 |
1.43e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.00 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 1 MLSLRSVNQFYGQNHILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGR--LPINSGSMTWQEdgappEDLLLQPAELR 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKG-----KDLLELSPEDR 75
|
....*
gi 495377997 79 ARTGI 83
Cdd:PRK09580 76 AGEGI 80
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-182 |
2.23e-03 |
|
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: 39.16 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 16 ILWDVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMTWqeDGAPPEDLLLQpaELRARTGIgyVPQGRHIFS- 94
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII--DGLNIAKIGLH--DLRFKITI--IPQDPVLFSg 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 95 ----------QMSVEDNLLIALMAAQDDRSRAIPEmvfdlfpalySLRHQRS--GE-LPMEQQQHLALARALVLQPKLVI 161
Cdd:TIGR00957 1375 slrmnldpfsQYSDEEVWWALELAHLKTFVSALPD----------KLDHECAegGEnLSVGQRQLVCLARALLRKTKILV 1444
|
170 180
....*....|....*....|.
gi 495377997 162 LDEPTEGmspwLEEEMGNLIR 182
Cdd:TIGR00957 1445 LDEATAA----VDLETDNLIQ 1461
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
143-216 |
2.58e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.86 E-value: 2.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 143 QQQHLALARALVLQPKLVILDEPTEGM---SPWL-EEEMGNLIRRLNReygLTILLLEQhVSFVRRVADYFLLLHRGR 216
Cdd:PTZ00265 584 QKQRISIARAIIRNPKILILDEATSSLdnkSEYLvQKTINNLKGNENR---ITIIIAHR-LSTIRYANTIFVLSNRER 657
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-59 |
2.82e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.56 E-value: 2.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 495377997 19 DVDLDLPPGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMT 59
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK 382
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
143-204 |
2.93e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.47 E-value: 2.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495377997 143 QQQHLALARALVLQPKLVILDEPTEGMSPWLEEEMGNLIRRLNREYGLTILLLEQHVSFVRR 204
Cdd:PTZ00265 1363 QKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR 1424
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-207 |
3.87e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 37.87 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 31 GVLGSPGMGKTTLVNCIMGRLPINSGSMTWQEDgappedlllqpaelrartgIGYVPQGRHIFSQMSVEDNLliALMAAQ 110
Cdd:PRK13409 369 GIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-------------------ISYKPQYIKPDYDGTVEDLL--RSITDD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 111 DDRSRAIPEMVFDLfpALYSLRHQRSGELPMEQQQHLALARALVLQPKLVILDEPtegmSPWL--EEEM--GNLIRRLNR 186
Cdd:PRK13409 428 LGSSYYKSEIIKPL--QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP----SAHLdvEQRLavAKAIRRIAE 501
|
170 180
....*....|....*....|.
gi 495377997 187 EYGLTILLLEQHVSFVRRVAD 207
Cdd:PRK13409 502 EREATALVVDHDIYMIDYISD 522
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-210 |
6.93e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.46 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 26 PGTCTGVLGSPGMGKTTLVNCIMGRLPINSGSMT----W------QEDGAppedlLLQPAelrartgIGYVPQGRHIFSQ 95
Cdd:PRK10636 26 PGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgnWqlawvnQETPA-----LPQPA-------LEYVIDGDREYRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495377997 96 MSVE--------DNLLIALMAAQDD-------RSRAIpemvfdlfpalySLRH-----QRSGELPMEQ-----QQHLALA 150
Cdd:PRK10636 94 LEAQlhdanernDGHAIATIHGKLDaidawtiRSRAA------------SLLHglgfsNEQLERPVSDfsggwRMRLNLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495377997 151 RALVLQPKLVILDEPTEGMS----PWLEEEMGNlirrlnreYGLTILLLEQHVSFVRRVADYFL 210
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLDldavIWLEKWLKS--------YQGTLILISHDRDFLDPIVDKII 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
143-218 |
7.43e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.08 E-value: 7.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495377997 143 QQQHLALARALVLQPKLVILDEPTEGMSpwlEEEMGNLIRRLN--REYGLTILLLEQHVSFVRRVADYFLLLHRGRNV 218
Cdd:NF040905 144 KQQLVEIAKALSKDVKLLILDEPTAALN---EEDSAALLDLLLelKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| |
