|
Name |
Accession |
Description |
Interval |
E-value |
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-235 |
2.63e-111 |
|
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: 318.85 E-value: 2.63e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGI 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 81 GYVPEDRQVFPEHTVEENIELG---KKDNSNSfdDWPIDKIWETFPILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEIL 157
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGayaRRDRAEV--RADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 158 LLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDTKTRDKYLAI 235
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLGV 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-225 |
1.69e-108 |
|
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: 311.29 E-value: 1.69e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGIGYV 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENIELGKKDNSNSFDDWPIDKIWETFPILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPS 163
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 164 EGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKD 225
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-235 |
3.92e-84 |
|
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: 249.75 E-value: 3.92e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGIGYV 83
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENIELG---KKDNSNSFDDwpidKIWETFPILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLD 160
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGlaaLPRRSRKIPD----EIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347602354 161 EPSEGLAPIIVEDIVKILENLKKL-GVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDtKTRdKYLAI 235
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDED-KVR-RYLAV 230
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-233 |
2.84e-53 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 171.60 E-value: 2.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGI 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 81 GYVPEDRQVFPEHTVEENIELGKKDNSNSFDDWPIDKIWETFPILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLD 160
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347602354 161 EPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDTKTRDKYL 233
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYL 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-226 |
2.44e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 169.09 E-value: 2.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPtsKRALSGIGYV 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP--AEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENIEL--GKKDNSNSFDDWPIDKIWETFPiLVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDE 161
Cdd:COG1131 79 PQEPALYPDLTVRENLRFfaRLYGLPRKEARERIDELLELFG-LTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 162 PSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHfcmEVAK---EAIIIDKGKAVWTGSLDDLQKDT 226
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLE---EAERlcdRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-233 |
4.84e-52 |
|
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: 168.11 E-value: 4.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGIGYV 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENI----ELGKKDNSNSFDDwpIDKIWETFPILvKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLL 159
Cdd:cd03218 81 PQEASIFRKLTVEENIlavlEIRGLSKKEREEK--LEELLEEFHIT-HLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 160 DEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDTKTRDKYL 233
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYL 231
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
13-233 |
3.00e-51 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 166.30 E-value: 3.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGIGYVPEDRQVFPE 92
Cdd:TIGR04406 11 YKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYLPQEASIFRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 HTVEENIEL---GKKDNSNSFDDWPIDKIWETFPIlVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPI 169
Cdd:TIGR04406 91 LTVEENIMAvleIRKDLDRAEREERLEALLEEFQI-SHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 170 IVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDTKTRDKYL 233
Cdd:TIGR04406 170 AVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYL 233
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-233 |
1.35e-50 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 164.82 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGI 80
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 81 GYVPEDRQVFPEHTVEENI----ELGKKDNSNSFDDwpIDKIWETFPILvKLKNRLAGQLSGGEQQMLSIARTLVGNPEI 156
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNIlavlELRKLSKKEREER--LEELLEEFGIT-HLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347602354 157 LLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDTKTRDKYL 233
Cdd:COG1137 158 ILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYL 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-225 |
3.05e-48 |
|
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: 158.75 E-value: 3.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGIGYV 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENIELG-KKDNSNSFDDWPI----DKIWE-TFPIL--VKLK---NRLAGQLSGGEQQMLSIARTLVG 152
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAaQARTGSGLLLARArreeREARErAEELLerVGLAdlaDRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347602354 153 NPEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKD 225
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-222 |
1.74e-47 |
|
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: 156.94 E-value: 1.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPtsKRALSGIGY 82
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP--REARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 83 VPEDRQVFPEHTVEENIELGKKDNSNSFDDWP--IDKIWETFpILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLD 160
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAELYGLFDEELKkrIEELIELL-GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 161 EPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-233 |
1.46e-44 |
|
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: 149.80 E-value: 1.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGI 80
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 81 GyvpedR-----QVFPEHTVEENIELG-----KKDNSNSFDDWP---------IDKIWEtfpIL--VKL---KNRLAGQL 136
Cdd:COG0411 82 A-----RtfqnpRLFPELTVLENVLVAaharlGRGLLAALLRLPrarreereaRERAEE---LLerVGLadrADEPAGNL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 137 SGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKK-LGVTILLAEQNMHFCMEVAKEAIIIDKGKAVW 215
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIA 233
|
250
....*....|....*...
gi 1347602354 216 TGSLDDLQKDTKTRDKYL 233
Cdd:COG0411 234 EGTPAEVRADPRVIEAYL 251
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-212 |
6.00e-44 |
|
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: 145.62 E-value: 6.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALsgIGYV 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR--IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENIElgkkdnsnsfddwpidkiwetfpilvklknrlagqLSGGEQQMLSIARTLVGNPEILLLDEPS 163
Cdd:cd03230 79 PEEPSLYENLTVRENLK-----------------------------------LSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1347602354 164 EGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGK 212
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-233 |
2.24e-43 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 146.19 E-value: 2.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGI 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 81 GYVPEDRQVFPEHTVEENI----ELGKKDNSNSFDDwPIDKIWETFPIlVKLKNRLAGQLSGGEQQMLSIARTLVGNPEI 156
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLmavlQIRDDLSAEQRED-RANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347602354 157 LLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDTKTRDKYL 233
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYL 235
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-215 |
1.57e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 144.08 E-value: 1.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELikkptsKRALSGI 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP------RRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 81 GYVPEDRQV---FPEhTVEENIELGKKDNSNSF-----DDWpiDKIWEtfpILVK-----LKNRLAGQLSGGEQQMLSIA 147
Cdd:COG1121 78 GYVPQRAEVdwdFPI-TVRDVVLMGRYGRRGLFrrpsrADR--EAVDE---ALERvgledLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 148 RTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVW 215
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-215 |
3.07e-42 |
|
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: 142.29 E-value: 3.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPtskralSGIGYVPEDRQV--- 89
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER------KRIGYVPQRRSIdrd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 90 FPEhTVEENIELGKkDNSNSFDDWPIDKIWE------TFPILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPS 163
Cdd:cd03235 83 FPI-SVRDVVLMGL-YGHKGLFRRLSKADKAkvdealERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 164 EGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVW 215
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVAS 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-212 |
3.73e-42 |
|
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: 142.22 E-value: 3.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 14 GNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSgIGYV---PEDrQVF 90
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGLVfqnPDD-QFF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 pEHTVEENIELGKKdNSNSFDDWPIDKIWETFPI--LVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAP 168
Cdd:cd03225 90 -GPTVEEEVAFGLE-NLGLPEEEIEERVEEALELvgLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1347602354 169 IIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGK 212
Cdd:cd03225 168 AGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-229 |
4.33e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 144.48 E-value: 4.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELikkptSKRALSGIGYV 83
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-----DPEDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENIE-------LGKKDNSNSFDDWpidkiwetfpiLVKL-----KNRLAGQLSGGEQQMLSIARTLV 151
Cdd:COG4152 77 PEERGLYPKMKVGEQLVylarlkgLSKAEAKRRADEW-----------LERLglgdrANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 152 GNPEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDTKTR 229
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRN 223
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-222 |
2.61e-41 |
|
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: 140.55 E-value: 2.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 14 GNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKpTSKRALSGIGYV---PEDrQVF 90
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKK-NLRELRRKVGLVfqnPDD-QLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 pEHTVEENIELGKKdNSNsfddWPIDKIWEtfpiLVK----------LKNRLAGQLSGGEQQMLSIARTLVGNPEILLLD 160
Cdd:COG1122 90 -APTVEEDVAFGPE-NLG----LPREEIRE----RVEealelvglehLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 161 EPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-162 |
5.52e-41 |
|
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: 137.39 E-value: 5.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRALSGIGYVPEDRQVFPEHTVEEN 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD-LTDDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347602354 99 IELGK--KDNSNSFDDWPIDKIWETFPILVKLKNRL---AGQLSGGEQQMLSIARTLVGNPEILLLDEP 162
Cdd:pfam00005 80 LRLGLllKGLSKREKDARAEEALEKLGLGDLADRPVgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-217 |
5.64e-40 |
|
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: 136.58 E-value: 5.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKkptSKRALSGIGYV 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK---NIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENIE-----LGKKDNSnsfddwpIDKIWETfpilVKLKN---RLAGQLSGGEQQMLSIARTLVGNPE 155
Cdd:cd03268 78 IEAPGFYPNLTARENLRllarlLGIRKKR-------IDEVLDV----VGLKDsakKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 156 ILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTG 217
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-222 |
1.00e-37 |
|
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: 131.09 E-value: 1.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQ--VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPtsKRALSGIGYVPEDRQVF 90
Cdd:cd03263 10 YKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR--KAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 PEHTVEENIEL-----GKKDNSNSFDdwpIDKIWETFPiLVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEG 165
Cdd:cd03263 88 DELTVREHLRFyarlkGLPKSEIKEE---VELLLRVLG-LTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1347602354 166 LAPIIVEDIVKILENLKKlGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:cd03263 164 LDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
13-212 |
1.21e-37 |
|
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: 128.90 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRALSGIGYVPedrqvfpe 92
Cdd:cd00267 9 YGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD-IAKLPLEELRRRIGYVP-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 htveenielgkkdnsnsfddwpidkiwetfpilvklknrlagQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVE 172
Cdd:cd00267 80 ------------------------------------------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1347602354 173 DIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGK 212
Cdd:cd00267 118 RLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-212 |
3.79e-37 |
|
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: 128.46 E-value: 3.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEEL----IKKPTSKRAlsg 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdleDELPPLRRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 80 IGYVPEDRQVFPEHTVEENIELGkkdnsnsfddwpidkiwetfpilvklknrlagqLSGGEQQMLSIARTLVGNPEILLL 159
Cdd:cd03229 78 IGMVFQDFALFPHLTVLENIALG---------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 160 DEPSEGLAPIIVEDIVKILENLKK-LGVTILLAEQNMHFCMEVAKEAIIIDKGK 212
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-217 |
3.99e-37 |
|
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: 129.18 E-value: 3.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRalsGIGYVPEDRQVFPE 92
Cdd:cd03259 10 YGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---NIGMVFQDYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 HTVEENIELGKKDNSNSFDDWPIDKIWETFpiLVKLK---NRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPI 169
Cdd:cd03259 87 LTVAENIAFGLKLRGVPKAEIRARVRELLE--LVGLEgllNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1347602354 170 IVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTG 217
Cdd:cd03259 165 LREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-222 |
5.58e-37 |
|
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: 130.16 E-value: 5.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSgIGY 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 83 VPEDRQVFPEHTVEENIELGKKDNSNSFDDWP------IDKIWETFPILvKLKNRLAGQLSGGEQQMLSIARTLVGNPEI 156
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRYPHLGLFGRPSaedreaVEEALERTGLE-HLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347602354 157 LLLDEPSEGLapiiveDI---VKILENLKKL----GVTILLAeqnMH---FCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:COG1120 159 LLLDEPTSHL------DLahqLEVLELLRRLarerGRTVVMV---LHdlnLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-217 |
9.84e-37 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 128.17 E-value: 9.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGeelikKPTSKRALSGIGYV 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-----KPLDIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENI-------ELGKKDNSNSFDDWpidkiWETFPILVKLKNRLAgQLSGGEQQMLSIARTLVGNPEI 156
Cdd:cd03269 76 PEERGLYPKMKVIDQLvylaqlkGLKKEEARRRIDEW-----LERLELSEYANKRVE-ELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347602354 157 LLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTG 217
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-223 |
2.20e-36 |
|
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: 127.49 E-value: 2.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRAlsGIGYV 83
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRR--RIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENIELGKKDNSNSFDDWP--IDKIWETFPiLVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDE 161
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRerIDELLDFVG-LLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347602354 162 PSEGLAPIIVEDIVKILENLKK-LGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQ 223
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
13-226 |
1.13e-35 |
|
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: 126.08 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIK-KPTSKRAL-SGIGYVPEDRQVF 90
Cdd:cd03261 10 FGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlSEAELYRLrRRMGMLFQSGALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 PEHTVEENIELGKKDNSNsFDDWPIDKIwetfpILVKL--------KNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEP 162
Cdd:cd03261 90 DSLTVFENVAFPLREHTR-LSEEEIREI-----VLEKLeavglrgaEDLYPAELSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 163 SEGLAPIIVEDIVKILENLKK-LGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDT 226
Cdd:cd03261 164 TAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-214 |
1.24e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 125.55 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQ-VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRAL--SGIGYVPEDRQV 89
Cdd:COG2884 11 YPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrRRIGVVFQDFRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 90 FPEHTVEENIEL-----GKKDNSnsfddwpIDKiwETFPIL--VKLKNR---LAGQLSGGEQQMLSIARTLVGNPEILLL 159
Cdd:COG2884 91 LPDRTVYENVALplrvtGKSRKE-------IRR--RVREVLdlVGLSDKakaLPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 160 DEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAV 214
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-214 |
6.47e-35 |
|
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: 123.52 E-value: 6.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 12 FYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGeeliKKPTSKRALSGIGYVPED--RQV 89
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG----KPIKAKERRKSIGYVMQDvdYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 90 FPEhTVEENIELGKKDNSNSFDDwpIDKIWETFPILvKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPI 169
Cdd:cd03226 85 FTD-SVREELLLGLKELDAGNEQ--AETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1347602354 170 IVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAV 214
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-216 |
2.81e-34 |
|
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: 120.23 E-value: 2.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEEL-IKKPTSKRALsGIGY 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVsFASPRDARRA-GIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 83 VPedrqvfpehtveenielgkkdnsnsfddwpidkiwetfpilvklknrlagQLSGGEQQMLSIARTLVGNPEILLLDEP 162
Cdd:cd03216 80 VY--------------------------------------------------QLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 163 SEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWT 216
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-214 |
2.16e-33 |
|
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: 119.92 E-value: 2.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNS----QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALS 78
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 79 G--IGYVPED--RQVFPEHTVEENIELGKKDNSNSFDDWPIDKIWETFPILVKLK----NRLAGQLSGGEQQMLSIARTL 150
Cdd:cd03257 81 RkeIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPeevlNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 151 VGNPEILLLDEPSEGLAPIIVEDIVKILENLKK-LGVTILLAEQNMHFCMEVAKEAIIIDKGKAV 214
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-212 |
5.68e-33 |
|
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: 118.40 E-value: 5.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRAL-SGIGY 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELrQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 83 VPEDRQVFPEHTVEENIELG-----KKDNSNSfddwpiDKIWETFPILVKLKNR---LAGQLSGGEQQMLSIARTLVGNP 154
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLApikvkGMSKAEA------EERALELLEKVGLADKadaYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 155 EILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGK 212
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
11-212 |
8.32e-33 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 118.12 E-value: 8.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 11 AFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRAL--SGIGYVPEDRQ 88
Cdd:TIGR02673 10 AYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLlrRRIGVVFQDFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 89 VFPEHTVEENIEL-----GKKDNsnsfdDWPIdkiwETFPILVKL-----KNRLAGQLSGGEQQMLSIARTLVGNPEILL 158
Cdd:TIGR02673 90 LLPDRTVYENVALplevrGKKER-----EIQR----RVGAALRQVglehkADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 159 LDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGK 212
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-225 |
1.11e-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: 118.44 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNS-QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSK-RAL-SGIGYVPEDRQV 89
Cdd:cd03256 10 YPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlRQLrRQIGMIFQQFNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 90 FPEHTVEENIELGKKDNSNSFDDW-----PIDK-----IWETFPILVKLKNRlAGQLSGGEQQMLSIARTLVGNPEILLL 159
Cdd:cd03256 90 IERLSVLENVLSGRLGRRSTWRSLfglfpKEEKqralaALERVGLLDKAYQR-ADQLSGGQQQRVAIARALMQQPKLILA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347602354 160 DEPSEGLAPIIVEDIVKILENL-KKLGVTILLaeqNMHFcMEVAKE----AIIIDKGKAVWTGSLDDLQKD 225
Cdd:cd03256 169 DEPVASLDPASSRQVMDLLKRInREEGITVIV---SLHQ-VDLAREyadrIVGLKDGRIVFDGPPAELTDE 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-214 |
1.65e-32 |
|
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: 117.67 E-value: 1.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVK-----SGSIKLKGEELIKKPTSKRAL- 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDVLELr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 78 SGIGYVPEDRQVFPEhTVEENIELGKKDNSnSFDDWPIDKI----------WEtfpilvKLKNRL-AGQLSGGEQQMLSI 146
Cdd:cd03260 81 RRVGMVFQKPNPFPG-SIYDNVAYGLRLHG-IKLKEELDERveealrkaalWD------EVKDRLhALGLSGGQQQRLCL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 147 ARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKlGVTILLAEQNMHFCMEVAKEAIIIDKGKAV 214
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
13-224 |
2.68e-32 |
|
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: 117.39 E-value: 2.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRA--LSGIGYVpedrqvF 90
Cdd:COG1127 15 FGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelRRRIGML------F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 pEH-------TVEENIELGKKDNSNsFDDWPIDKIwetfpILVKLK--------NRLAGQLSGGEQQMLSIARTLVGNPE 155
Cdd:COG1127 89 -QGgalfdslTVFENVAFPLREHTD-LSEAEIREL-----VLEKLElvglpgaaDKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 156 ILLLDEPSEGLAPIIVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQK 224
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELrDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-189 |
3.53e-32 |
|
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: 117.05 E-value: 3.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQvLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRalsGIGYV 83
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---DISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENIELG--KKDNSNSFDDWPIDKIWETFPIlVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDE 161
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGlkKRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180
....*....|....*....|....*....
gi 1347602354 162 PSEGLAPIIVEDIVKILENL-KKLGVTIL 189
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIrKEFGVTVL 184
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-214 |
6.17e-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: 116.63 E-value: 6.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRAL-SGIG 81
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 82 YVPEDRQVFPEHTVEENIELGkkdnsnsfddwpidkiwetfPILVKLKNR---------------LA-------GQLSGG 139
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLA--------------------PIKVKKMSKaeaeeramellervgLAdkadaypAQLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 140 EQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAV 214
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIV 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-190 |
1.42e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 118.28 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRalsGI 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR---NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 81 GYVPEDRQVFPEHTVEENIELGKKdnsnsFDDWP-------IDKIWEtfpiLVKLK---NRLAGQLSGGEQQMLSIARTL 150
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVAFGLR-----MRGVPkaeirarVAELLE----LVGLEglaDRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1347602354 151 VGNPEILLLDEPSEGL-APIIVE---DIVKIlenLKKLGVTILL 190
Cdd:COG3842 151 APEPRVLLLDEPLSALdAKLREEmreELRRL---QRELGITFIY 191
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-214 |
1.45e-31 |
|
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: 114.07 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 5 ETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSgIGYVP 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 85 edrQVfpehtveeNIELGkkdnsnsfddwpidkiwetfpiLVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSE 164
Cdd:cd03214 80 ---QA--------LELLG----------------------LAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 165 GLapiiveDI---VKILENLKKL----GVTILLAeqnMH-------FCMEVakeaIIIDKGKAV 214
Cdd:cd03214 127 HL------DIahqIELLELLRRLarerGKTVVMV---LHdlnlaarYADRV----ILLKDGRIV 177
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-217 |
3.37e-31 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 114.00 E-value: 3.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 6 TKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPtsKRALSGIGYVPE 85
Cdd:cd03266 8 TKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP--AEARRRLGFVSD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 86 DRQVFPEHTVEENIEL-----G-KKDNSNSFDDWPIDKIWetfpiLVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLL 159
Cdd:cd03266 86 STGLYDRLTARENLEYfaglyGlKGDELTARLEELADRLG-----MEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 160 DEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTG 217
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-217 |
4.57e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 114.34 E-value: 4.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEE--LIKKPTSKRALS--- 78
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdFSQKPSEKAIRLlrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 79 GIGYVPEDRQVFPEHTVEEN-IE-------LGKKDnsnsfddwPIDKIWEtfpILVKLK-----NRLAGQLSGGEQQMLS 145
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlIEapckvlgLSKEQ--------AREKAMK---LLARLRltdkaDRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 146 IARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTG 217
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-195 |
1.28e-30 |
|
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: 112.39 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKN---NIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKG------EELIKKPTSKRalsGIGYVPEDRQV 89
Cdd:cd03297 10 LPDFTLKIDFDlneEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQR---KIGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 90 FPEHTVEENIELGKKDNSNSFDDWPIDKIWETFPiLVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPI 169
Cdd:cd03297 87 FPHLNVRENLAFGLKRKRNREDRISVDELLDLLG-LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180
....*....|....*....|....*..
gi 1347602354 170 IVEDIVKILENLKK-LGVTILLAEQNM 195
Cdd:cd03297 166 LRLQLLPELKQIKKnLNIPVIFVTHDL 192
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
13-225 |
1.53e-30 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 115.59 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVlfDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEEL------IKKPTSKRAlsgIGYVPED 86
Cdd:TIGR02142 9 LGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkgIFLPPEKRR---IGYVFQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 87 RQVFPEHTVEENIELGKKDNSNSFDDWPIDKIWETFPIlVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGL 166
Cdd:TIGR02142 84 ARLFPHLSVRGNLRYGMKRARPSERRISFERVIELLGI-GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 167 APIIVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKD 225
Cdd:TIGR02142 163 DDPRKYEILPYLERLhAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-221 |
1.57e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.82 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 6 TKSMNAFYGNSQVlfdmSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEEL-IKKPTSKRALsGIGYVP 84
Cdd:COG3845 12 TKRFGGVVANDDV----SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrIRSPRDAIAL-GIGMVH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 85 EDRQVFPEHTVEENIELGKKDNSNSFDDWP-----IDKIWETFPILVKLkNRLAGQLSGGEQQMLSIARTLVGNPEILLL 159
Cdd:COG3845 87 QHFMLVPNLTVAENIVLGLEPTKGGRLDRKaararIRELSERYGLDVDP-DAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347602354 160 DEPSEGLAPIIVEDIVKILENLKKLGVTIL-----LAEqnmhfCMEVAKEAIIIDKGKAVWTGSLDD 221
Cdd:COG3845 166 DEPTAVLTPQEADELFEILRRLAAEGKSIIfithkLRE-----VMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-212 |
2.09e-30 |
|
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: 112.20 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 6 TKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRAL---SGIGY 82
Cdd:cd03255 7 SKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfrrRHIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 83 VPEDRQVFPEHTVEENIEL-----GKKDNSNsfddwpIDKIWETFPI--LVKLKNRLAGQLSGGEQQMLSIARTLVGNPE 155
Cdd:cd03255 87 VFQSFNLLPDLTALENVELplllaGVPKKER------RERAEELLERvgLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347602354 156 ILLLDEPSEGLAPIIVEDIVKILENL-KKLGVTILLAEQNmhfcMEVAKEA---IIIDKGK 212
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD----PELAEYAdriIELRDGK 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
17-222 |
2.17e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 117.31 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 17 QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIK-KPTSKRALSG-IGYVPED--RQVFPE 92
Cdd:COG1123 279 RAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlSRRSLRELRRrVQMVFQDpySSLNPR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 HTVEENIELGKKDNSNSFDDWPIDKIWEtfpIL--VKL----KNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGL 166
Cdd:COG1123 359 MTVGDIIAEPLRLHGLLSRAERRERVAE---LLerVGLppdlADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSAL 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1347602354 167 APIIVEDIVKILENLKK-LGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:COG1123 436 DVSVQAQILNLLRDLQReLGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
23-233 |
2.43e-30 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 112.78 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 23 SLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGIGYVPEDRQVFPEHTVEENIELG 102
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVRLFREMTVIENLLVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 103 --KKDNSNSF------------DDWPIDK--IWETFPILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGL 166
Cdd:PRK11300 105 qhQQLKTGLFsgllktpafrraESEALDRaaTWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGL 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 167 APIIVEDIVKILENLKK-LGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDTKTRDKYL 233
Cdd:PRK11300 185 NPKETKELDELIAELRNeHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIKAYL 252
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
13-212 |
3.48e-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: 110.17 E-value: 3.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNS--QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIK-KPTSKRALsgIGYVPEDRQV 89
Cdd:cd03228 10 YPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKN--IAYVPQDPFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 90 FPEhTVEENIelgkkdnsnsfddwpidkiwetfpilvklknrlagqLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPI 169
Cdd:cd03228 88 FSG-TIRENI------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1347602354 170 IVEDIVKILENLKKlGVTILLAEQNMHfCMEVAKEAIIIDKGK 212
Cdd:cd03228 131 TEALILEALRALAK-GKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-212 |
9.75e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.91 E-value: 9.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIK-KPTSKRALsgIGY 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQ--VAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 83 VPEDRQVFPEhTVEENIELGKKDNSNSFDDWPIDKIWETFPILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEP 162
Cdd:COG4619 79 VPQEPALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1347602354 163 SEGLAP---IIVEDIvkILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGK 212
Cdd:COG4619 158 TSALDPentRRVEEL--LREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-217 |
1.09e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 110.87 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEE--LIKKPTSK--RAL-S 78
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDKaiRELrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 79 GIGYVPEDRQVFPEHTVEEN-IE-----LG-KKDNSNSfddwPIDKIWETFPiLVKLKNRLAGQLSGGEQQMLSIARTLV 151
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNlIEapcrvLGlSKDQALA----RAEKLLERLR-LKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347602354 152 GNPEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTG 217
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-217 |
1.77e-29 |
|
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: 109.59 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKkNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALsgIGYV 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR--IGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENIE----LGKKDNSNSfdDWPIDKIWEtfpiLVKL---KNRLAGQLSGGEQQMLSIARTLVGNPEI 156
Cdd:cd03264 78 PQEFGVYPNFTVREFLDyiawLKGIPSKEV--KARVDEVLE----LVNLgdrAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347602354 157 LLLDEPSEGLAPiivEDIVKILENLKKLG--VTILLAEQNMHFCMEVAKEAIIIDKGKAVWTG 217
Cdd:cd03264 152 LIVDEPTAGLDP---EERIRFRNLLSELGedRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-222 |
1.80e-29 |
|
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: 115.00 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 14 GNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVK---SGSIKLKGEELIKKPTSKRAlSGIGYVPED--RQ 88
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG-RRIGMVFQDpmTQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 89 VFPeHTVEENIELGKKDNSNSFDDWpIDKIWETFPiLVKLKNRLA---GQLSGGEQQMLSIARTLVGNPEILLLDEPSEG 165
Cdd:COG1123 96 LNP-VTVGDQIAEALENLGLSRAEA-RARVLELLE-AVGLERRLDrypHQLSGGQRQRVAIAMALALDPDLLIADEPTTA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 166 LAPIIVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:COG1123 173 LDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-228 |
1.82e-29 |
|
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: 110.28 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNS----QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELiKKPTSKRALS 78
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV-TRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 79 GIGYVPED--RQVFPEHTVEENIE-----LGKKDNSnsfddwpiDKIWEtfpILVK------LKNRLAGQLSGGEQQMLS 145
Cdd:COG1124 80 RVQMVFQDpyASLHPRHTVDRILAeplriHGLPDRE--------ERIAE---LLEQvglppsFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 146 IARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKK-LGVTILLAEQNM----HFCMEVAkeaiIIDKGKAVWTGSLD 220
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLavvaHLCDRVA----VMQNGRIVEELTVA 224
|
....*...
gi 1347602354 221 DLQKDTKT 228
Cdd:COG1124 225 DLLAGPKH 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
12-225 |
2.13e-29 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 110.15 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 12 FYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIK-KPTSKRAL-SGIGYVPEDRQV 89
Cdd:COG3638 12 YPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlRGRALRRLrRRIGMIFQQFNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 90 FPEHTVEENIELGkkdnsnSFDDWPIdkiWET----FP---------------ILVKLKNRlAGQLSGGEQQMLSIARTL 150
Cdd:COG3638 92 VPRLSVLTNVLAG------RLGRTST---WRSllglFPpedreralealervgLADKAYQR-ADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 151 VGNPEILLLDEPSEGLAPIIVEDIVKILENL-KKLGVTILLaeqNMHFcMEVAKE----AIIIDKGKAVWTGSLDDLQKD 225
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVV---NLHQ-VDLARRyadrIIGLRDGRVVFDGPPAELTDA 237
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
13-222 |
2.23e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 112.55 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEEL-IKKPTSKRalsGIGYVPEDRQVFP 91
Cdd:COG1118 12 FGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRER---RVGFVFQHYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 92 EHTVEENIELGKKDNSNSFDDwpIDKIWETFPILVKL---KNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLap 168
Cdd:COG1118 89 HMTVAENIAFGLRVRPPSKAE--IRARVEELLELVQLeglADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGAL-- 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347602354 169 iiveDI-VK------ILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:COG1118 165 ----DAkVRkelrrwLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-222 |
3.98e-29 |
|
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: 109.31 E-value: 3.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLF-DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSgIGY 82
Cdd:cd03295 1 IEFENVTKRYGGGKKAVnNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK-IGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 83 VPEDRQVFPEHTVEENIELGKKdnsnsFDDWPIDKIWETFPILVKL--------KNRLAGQLSGGEQQMLSIARTLVGNP 154
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPK-----LLKWPKEKIRERADELLALvgldpaefADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347602354 155 EILLLDEPSEGLAPIIVEDIVKILENLKK-LGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQeLGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-225 |
5.32e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.19 E-value: 5.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLE----TKSmnafYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRALS 78
Cdd:COG1129 4 LLEmrgiSKS----FGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEP-VRFRSPRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 79 -GIGYVPEDRQVFPEHTVEENIELGKKDNSNSFDDWPidKIW-ETFPILVKLK-----NRLAGQLSGGEQQMLSIARTLV 151
Cdd:COG1129 79 aGIAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWR--AMRrRARELLARLGldidpDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347602354 152 GNPEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTIL-----LAEqnmhfCMEVAKEAIIIDKGKAVWTGSLDDLQKD 225
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIyishrLDE-----VFEIADRVTVLRDGRLVGTGPVAELTED 230
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-190 |
7.18e-29 |
|
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: 107.13 E-value: 7.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGIGYVPEDRQ---VFPEHTVEE 97
Cdd:cd03215 18 DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPEDRKregLVLDLSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIELGKkdnsnsfddwpidkiwetfpilvklknrlagQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKI 177
Cdd:cd03215 98 NIALSS-------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRL 146
|
170
....*....|...
gi 1347602354 178 LENLKKLGVTILL 190
Cdd:cd03215 147 IRELADAGKAVLL 159
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
14-162 |
1.55e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 108.25 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 14 GNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRalsgiGYVPEDRQVFPEH 93
Cdd:COG1116 22 GGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-VTGPGPDR-----GVVFQEPALLPWL 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 94 TVEENIELG---KKDNSNSFDDWpIDKIWEtfpiLVKLK---NRLAGQLSGGEQQMLSIARTLVGNPEILLLDEP 162
Cdd:COG1116 96 TVLDNVALGlelRGVPKAERRER-ARELLE----LVGLAgfeDAYPHQLSGGMRQRVAIARALANDPEVLLMDEP 165
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-229 |
1.80e-28 |
|
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: 107.32 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRalsGIGYV 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---PVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENIELG---KKDNSNSFDdwpiDKIWETFPiLVKLK---NRLAGQLSGGEQQMLSIARTLVGNPEIL 157
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGlrlKKLPKAEIK----ERVAEALD-LVQLEgyaNRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347602354 158 LLDEPSEGLAPIIVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDTKTR 229
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANR 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-217 |
1.85e-28 |
|
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: 106.81 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 20 FDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSgigYVPEDRQVFPEHTVEENI 99
Cdd:cd03298 15 MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVS---MLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 100 ELGKKDNS--NSFDDWPIDKIWETFPILVKLKnRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKI 177
Cdd:cd03298 92 GLGLSPGLklTAEDRQAIEVALARVGLAGLEK-RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1347602354 178 LENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTG 217
Cdd:cd03298 171 VLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
14-222 |
4.91e-28 |
|
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: 106.13 E-value: 4.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 14 GNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKkpTSKRAL----SGIGYVPEDRQV 89
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTL--LSGKELrkarRRIGMIFQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 90 FPEHTVEENIELGKKdnsnsFDDWPIDKIWETFPILVKL------KNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPS 163
Cdd:cd03258 94 LSSRTVFENVALPLE-----IAGVPKAEIEERVLELLELvgledkADAYPAQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 164 EGLAPIIVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:cd03258 169 SALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
17-190 |
5.68e-28 |
|
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: 105.63 E-value: 5.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 17 QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELikkptsKRALSGIGYVPEDRQVFPEHTVE 96
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV------TGPGPDRGYVFQQDALLPWLTVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 97 ENIELGKKDNSNSFDDwpIDKIWETFPILVKLK---NRLAGQLSGGEQQMLSIARTLVGNPEILLLDEP----SEGLAPI 169
Cdd:cd03293 92 DNVALGLELQGVPKAE--ARERAEELLELVGLSgfeNAYPHQLSGGMRQRVALARALAVDPDVLLLDEPfsalDALTREQ 169
|
170 180
....*....|....*....|.
gi 1347602354 170 IVEDIVKILEnlkKLGVTILL 190
Cdd:cd03293 170 LQEELLDIWR---ETGKTVLL 187
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
5.73e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 107.20 E-value: 5.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFY-GNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSK-RALS 78
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 79 GIGYVPEDRQVFPEhTVEENIELGKKDNSnsFDDWPID-KIWETFPIL--VKLKNRLAGQLSGGEQQMLSIARTLVGNPE 155
Cdd:PRK13652 81 GLVFQNPDDQIFSP-TVEQDIAFGPINLG--LDEETVAhRVSSALHMLglEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347602354 156 ILLLDEPSEGLAPIIVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDD--LQKDTKTR 229
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEifLQPDLLAR 234
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
13-191 |
6.30e-28 |
|
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: 105.25 E-value: 6.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALsgIGYVPEDRQVFPE 92
Cdd:COG4133 12 RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR--LAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 HTVEENIELGKKDNSNSFDDWPIDKIWETFpILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVE 172
Cdd:COG4133 90 LTVRENLRFWAALYGLRADREAIDEALEAV-GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVA 168
|
170
....*....|....*....
gi 1347602354 173 DIVKILENLKKLGVTILLA 191
Cdd:COG4133 169 LLAELIAAHLARGGAVLLT 187
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-222 |
1.33e-27 |
|
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: 105.50 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRalsGIGYVPEDRQVFPE 92
Cdd:cd03296 12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGFVFQHYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 HTVEENIELGKKDNSNSfDDWPIDKIWETFPILVKL------KNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGL 166
Cdd:cd03296 89 MTVFDNVAFGLRVKPRS-ERPPEAEIRAKVHELLKLvqldwlADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1347602354 167 APIIVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:cd03296 168 DAKVRKELRRWLRRLhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-191 |
1.66e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 104.74 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MN-LLETKSMNAFYGNS----QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKR 75
Cdd:COG1136 1 MSpLLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 76 AL---SGIGYVPEDRQVFPEHTVEENIEL-------GKKDNSNSFDDWpIDKiwetfpilVKLKNRL---AGQLSGGEQQ 142
Cdd:COG1136 81 ARlrrRHIGFVFQFFNLLPELTALENVALplllagvSRKERRERAREL-LER--------VGLGDRLdhrPSQLSGGQQQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1347602354 143 MLSIARTLVGNPEILLLDEP-----SE-GlapiivEDIVKILENL-KKLGVTILLA 191
Cdd:COG1136 152 RVAIARALVNRPKLILADEPtgnldSKtG------EEVLELLRELnRELGTTIVMV 201
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-189 |
2.47e-27 |
|
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: 103.40 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 17 QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVK--SGSIKLKGeelikKPTSKRALSG-IGYVPEDRQVFPEH 93
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLING-----RPLDKRSFRKiIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 94 TVEENIElgkkdnsnsfddwpidkiwetfpILVKLKnrlagQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVED 173
Cdd:cd03213 98 TVRETLM-----------------------FAAKLR-----GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170
....*....|....*.
gi 1347602354 174 IVKILENLKKLGVTIL 189
Cdd:cd03213 150 VMSLLRRLADTGRTII 165
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-217 |
4.23e-27 |
|
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: 103.49 E-value: 4.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRalsGIGYV 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENIELGKKdnSNSFDDWPID-KIWETFPIL--VKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLD 160
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLK--LRKVPKDEIDeRVREVAELLqiEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 161 EPSEGL-APIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTG 217
Cdd:cd03301 156 EPLSNLdAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-217 |
8.62e-27 |
|
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: 102.73 E-value: 8.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 17 QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLI---KVKSGSIKLKGEELIKKPTSKRalsgIGYVPEDRQVFPEH 93
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKPDQFQKC----VAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 94 TVEE------NIELGKKdnsnsFDDWPIDKIWETFPI----LVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPS 163
Cdd:cd03234 97 TVREtltytaILRLPRK-----SSDAIRKKRVEDVLLrdlaLTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 164 EGLAPIIVEDIVKILENLKKLGVTILLA-EQNMHFCMEVAKEAIIIDKGKAVWTG 217
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTiHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-162 |
1.12e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 105.16 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRalsGI 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR---NI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 81 GYVPEDRQVFPEHTVEENIELG-------KKDnsnsfddwpIDKiwetfpiLVK----------LKNRLAGQLSGGEQQM 143
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPlklrkvpKAE---------IDR-------RVReaaellgledLLDRKPKQLSGGQRQR 141
|
170
....*....|....*....
gi 1347602354 144 LSIARTLVGNPEILLLDEP 162
Cdd:COG3839 142 VALGRALVREPKVFLLDEP 160
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-212 |
2.94e-26 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 101.33 E-value: 2.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQV-LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRAL--SGI 80
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 81 GYVPEDRQVFPEHTVEENIELGKKDNSNSFDDWPiDKIWETFPiLVKLKNR---LAGQLSGGEQQMLSIARTLVGNPEIL 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIR-KRVPAALE-LVGLSHKhraLPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 158 LLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGK 212
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-222 |
4.25e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 101.53 E-value: 4.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVK-----SGSIKLKGEELIKKPTS-- 73
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 74 KRALSGIGYVPEDrqvFPEHTVEENIELGKKDN--SNSFDD------WPIDK--IWEtfpilvKLKNRL---AGQLSGGE 140
Cdd:PRK14247 81 RRRVQMVFQIPNP---IPNLSIFENVALGLKLNrlVKSKKElqervrWALEKaqLWD------EVKDRLdapAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 141 QQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKlGVTILLAeqnMHFCMEVAKEA---IIIDKGKAVWTG 217
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLV---THFPQQAARISdyvAFLYKGQIVEWG 227
|
....*
gi 1347602354 218 SLDDL 222
Cdd:PRK14247 228 PTREV 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-196 |
4.74e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 101.65 E-value: 4.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSsTF-KAITGLI------KVkSGSIKLKGEELIKK---PTS 73
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKS-TLlRCLNRMNdlipgaRV-EGEILLDGEDIYDPdvdVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 74 KRALsgIGYVPEDRQVFPeHTVEENIELG-----KKDNSNsfddwpIDKI----------WEtfpilvKLKNRL---AGQ 135
Cdd:COG1117 90 LRRR--VGMVFQKPNPFP-KSIYDNVAYGlrlhgIKSKSE------LDEIveeslrkaalWD------EVKDRLkksALG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 136 LSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPI---IVEDIvkILEnLKKlGVTILLAEQNMH 196
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIstaKIEEL--ILE-LKK-DYTIVIVTHNMQ 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-229 |
4.94e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 103.76 E-value: 4.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRAlsgIGY 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP---INM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 83 VPEDRQVFPEHTVEENIELGKKDnsnsfDDWPIDKIW---ETFPILVKLK---NRLAGQLSGGEQQMLSIARTLVGNPEI 156
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGLKQ-----DKLPKAEIAsrvNEMLGLVHMQefaKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347602354 157 LLLDEPSEGLAPIIVE----DIVKILEnlkKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDTKTR 229
Cdd:PRK11607 171 LLLDEPMGALDKKLRDrmqlEVVDILE---RVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
19-223 |
6.71e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 100.60 E-value: 6.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSgigyvpedrQVFPEH----- 93
Cdd:COG3840 15 PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVS---------MLFQENnlfph 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 94 -TVEENIELGKKDNS--NSFDDWPIDKIWETFPiLVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPII 170
Cdd:COG3840 86 lTVAQNIGLGLRPGLklTAEQRAQVEQALERVG-LAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 171 VEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQ 223
Cdd:COG3840 165 RQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALL 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-225 |
7.02e-26 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 103.26 E-value: 7.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 20 FDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEEL------IKKPTSKRAlsgIGYVPEDRQVFPEH 93
Cdd:COG4148 16 LDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargIFLPPHRRR---IGYVFQEARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 94 TVEENIELGKKDNSNSFDDWPIDKIWETF---PILvklkNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPsegLAPII 170
Cdd:COG4148 93 SVRGNLLYGRKRAPRAERRISFDEVVELLgigHLL----DRRPATLSGGERQRVAIGRALLSSPRLLLMDEP---LAALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 171 V---EDIVKILENL-KKLGVTILLAEQNMHfcmEVAKEA---IIIDKGKAVWTGSLDDLQKD 225
Cdd:COG4148 166 LarkAEILPYLERLrDELDIPILYVSHSLD---EVARLAdhvVLLEQGRVVASGPLAEVLSR 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-223 |
9.70e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.04 E-value: 9.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 23 SLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSgigYVPEDRQVFPEHTVEENIELG 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVS---MLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 103 KKDNS--NSFDDWPIDKIWETFPILVKLkNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILEN 180
Cdd:PRK10771 96 LNPGLklNAAQREKLHAIARQMGIEDLL-ARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1347602354 181 L-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQ 223
Cdd:PRK10771 175 VcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-222 |
2.01e-25 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 103.76 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELikKPTSKRAL-SGIGYVPEDRQVFPEhTVE 96
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL--RQIDPASLrRQIGVVLQDVFLFSG-TIR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 97 ENIELGKKDnsnsFDDwpiDKIWEtfpILvklknRLAG---------------------QLSGGEQQMLSIARTLVGNPE 155
Cdd:COG2274 567 ENITLGDPD----ATD---EEIIE---AA-----RLAGlhdfiealpmgydtvvgeggsNLSGGQRQRLAIARALLRNPR 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347602354 156 ILLLDEPSEGLAPiIVEDIvkILENLKKL--GVTILLAEQNMHFcMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:COG2274 632 ILILDEATSALDA-ETEAI--ILENLRRLlkGRTVIIIAHRLST-IRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-222 |
3.05e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 99.01 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRAL-SGIG 81
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 82 YVPEDRQVFPEHTVEENIELG-------KKDNSNSFDDWPIDKIWetfpiLVKLKNRLAGQLSGGEQQMLSIARTLVGNP 154
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGplrvrgaSKEEAEKQARELLAKVG-----LAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 155 EILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-231 |
5.77e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.38 E-value: 5.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGN-SQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTS---KRALS 78
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSlleVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 79 GIGYVPEDRQVFPEhTVEENIELGKKDNSNSFDDwpIDKIWETFPILVKL---KNRLAGQLSGGEQQMLSIARTLVGNPE 155
Cdd:PRK13639 81 GIVFQNPDDQLFAP-TVEEDVAFGPLNLGLSKEE--VEKRVKEALKAVGMegfENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347602354 156 ILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDTKTRDK 231
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRK 233
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
18-225 |
6.63e-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: 102.15 E-value: 6.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELikkptskRALSG------IGYVPEDRQVFp 91
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL-------RDLDEddlrrrIAVVPQRPHLF- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 92 EHTVEENIELGKKDNSNsfddwpiDKIWEtfpIL--VKLKNRLAG--------------QLSGGEQQMLSIARTLVGNPE 155
Cdd:COG4987 422 DTTLRENLRLARPDATD-------EELWA---ALerVGLGDWLAAlpdgldtwlgeggrRLSGGERRRLALARALLRDAP 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347602354 156 ILLLDEPSEGLAPIIVEDIVK-ILENLKklGVTILLAeqnMHF--CMEVAKEAIIIDKGKAVWTGSLDDLQKD 225
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLAdLLEALA--GRTVLLI---THRlaGLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-222 |
8.06e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 99.49 E-value: 8.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKptSKRALSGIGYV 83
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR--ARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENIELGKKdnsnsFDDWPIDKIWETFPILV---KLKNRL---AGQLSGGEQQMLSIARTLVGNPEIL 157
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGR-----YFGLSAAAARALVPPLLefaKLENKAdakVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347602354 158 LLDEPSEGLAPIIVEDIVKILENLKKLGVTILLaeqNMHFcMEVAK----EAIIIDKGKAVWTGSLDDL 222
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILL---TTHF-MEEAErlcdRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-229 |
1.84e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.39 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRAlsgIGYV 83
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK---VGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENIELG-------KKDNSNSFDdwpiDKIWETFPI--LVKLKNRLAGQLSGGEQQMLSIARTLVGNP 154
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGltvlprrERPNAAAIK----AKVTQLLEMvqLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347602354 155 EILLLDEPSEGLAPIIVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDTKTR 229
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATR 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-224 |
1.12e-23 |
|
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: 98.68 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 14 GNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIK-KPTSKRALsgIGYVPEDRQVFPE 92
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQ--IAWVPQNPYLFAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 hTVEENIELGKKDNSNS----------FDDWpIDKI---WETfpilvklknRL---AGQLSGGEQQMLSIARTLVGNPEI 156
Cdd:COG4988 426 -TIRENLRLGRPDASDEeleaaleaagLDEF-VAALpdgLDT---------PLgegGRGLSGGQAQRLALARALLRDAPL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 157 LLLDEPSEGLAPIIVEDIVKILENLKKlGVTILLAEQNMHFcMEVAKEAIIIDKGKAVWTGSLDDLQK 224
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLAL-LAQADRILVLDDGRIVEQGTHEELLA 560
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
17-221 |
1.30e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.87 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 17 QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKG------EELIKKPTSKRalsGIGYVPEDRQVF 90
Cdd:PRK11144 12 DLCLTVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaEKGICLPPEKR---RIGYVFQDARLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 PEHTVEENIELGKKDNSNS-FDDwpidkiwetfpiLVK------LKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPs 163
Cdd:PRK11144 89 PHYKVRGNLRYGMAKSMVAqFDK------------IVAllgiepLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 164 egLAPIiveDI------VKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDD 221
Cdd:PRK11144 156 --LASL---DLprkrelLPYLERLaREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-190 |
2.32e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.52 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVK-----SGSIKLKGEELIKKPTSK- 74
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 75 RALSGIGYVPEDRQVFPEHTVEENIELGKKDNS-----NSFDD---WPIDK--IWEtfpilvKLKNRL---AGQLSGGEQ 141
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvkskKELDErveWALKKaaLWD------EVKDRLndyPSNLSGGQR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1347602354 142 QMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKlGVTILL 190
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVL 203
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-162 |
3.75e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.07 E-value: 3.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSgigy 82
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 83 vpedRQVFPEH-------TVEENIELGKKDNSNSFDdwpidkiwETFPI---------LVKLKNRLAGQLSGGEQQMLSI 146
Cdd:PRK13548 78 ----RAVLPQHsslsfpfTVEEVVAMGRAPHGLSRA--------EDDALvaaalaqvdLAHLAGRDYPQLSGGEQQRVQL 145
|
170 180
....*....|....*....|..
gi 1347602354 147 ARTLV------GNPEILLLDEP 162
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEP 167
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-190 |
4.27e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.63 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEEL-IKKPtsKRAL-SGIGYVPEDRQ---VFPEHTV 95
Cdd:COG1129 270 DVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrIRSP--RDAIrAGIAYVPEDRKgegLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 96 EENIELG--KKDNSNSFDDWP-----IDKIWETFPILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGlap 168
Cdd:COG1129 348 RENITLAslDRLSRGGLLDRRreralAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRG--- 424
|
170 180
....*....|....*....|....*
gi 1347602354 169 IIV---EDIVKILENLKKLGVTILL 190
Cdd:COG1129 425 IDVgakAEIYRLIRELAAEGKAVIV 449
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-195 |
5.64e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 93.69 E-value: 5.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSS---TFKAITGLIKV--KSGSIKLKGEELIKK---PTSK 74
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTilrCFNRLNDLIPGfrVEGKVTFHGKNLYAPdvdPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 75 RalSGIGYVPEDRQVFPEhTVEENIELGKKDNSNSFD-DWPIDK------IWETfpilVKLKNRLAGQ-LSGGEQQMLSI 146
Cdd:PRK14243 90 R--RRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGDmDELVERslrqaaLWDE----VKDKLKQSGLsLSGGQQQRLCI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1347602354 147 ARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKlGVTILLAEQNM 195
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHNM 210
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-222 |
1.32e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.99 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 2 NLLETKSMNAFYGN-SQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEEL---IKKPTSKRAL 77
Cdd:PRK13636 4 YILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 78 SGIGYVPEDRQVFPEHTVEE------NIELGKKDNSNSfddwpIDKIWETFPIlVKLKNRLAGQLSGGEQQMLSIARTLV 151
Cdd:PRK13636 84 VGMVFQDPDNQLFSASVYQDvsfgavNLKLPEDEVRKR-----VDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 152 GNPEILLLDEPSEGLAPIIVEDIVKIL-ENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLvEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
13-205 |
2.02e-22 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 90.75 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRALS----GIGYVPEDRQ 88
Cdd:TIGR03608 8 FGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQE-TPPLNSKKASKfrreKLGYLFQNFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 89 VFPEHTVEENIELG-------KKDNSNSfddwpIDKIWETFPILVKLKNRLAgQLSGGEQQMLSIARTLVGNPEILLLDE 161
Cdd:TIGR03608 87 LIENETVEENLDLGlkykklsKKEKREK-----KKEALEKVGLNLKLKQKIY-ELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1347602354 162 PSEGLAPIIVEDIVKILENLKKLGVTILLAEQNmhfcMEVAKEA 205
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHD----PEVAKQA 200
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-222 |
2.08e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.36 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRAlsGIGYVPEDRQVFPE 92
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARA--RIGVVPQFDNLDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 HTVEEN-IELGKKDNSNSfddwpiDKIWETFPILV-------KLKNRLAgQLSGGEQQMLSIARTLVGNPEILLLDEPSE 164
Cdd:PRK13536 129 FTVRENlLVFGRYFGMST------REIEAVIPSLLefarlesKADARVS-DLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 165 GLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-233 |
2.35e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 91.74 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLkGEELI--KKPTSK---- 74
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIdtARSLSQqkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 75 -RAL-SGIGYVPEDRQVFPEHTVEENIELGkkdnsnsfddwpidkiwetfPILVKLKNR---------------LAGQ-- 135
Cdd:PRK11264 80 iRQLrQHVGFVFQNFNLFPHRTVLENIIEG--------------------PVIVKGEPKeeatararellakvgLAGKet 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 136 -----LSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDK 210
Cdd:PRK11264 140 syprrLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQ 219
|
250 260
....*....|....*....|....*....
gi 1347602354 211 GKAVWTGSLDDL---QKDTKTR---DKYL 233
Cdd:PRK11264 220 GRIVEQGPAKALfadPQQPRTRqflEKFL 248
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-214 |
2.80e-22 |
|
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: 90.73 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQ--VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIK-KPTSKRAlsGI 80
Cdd:cd03245 3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRR--NI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 81 GYVPEDRQVFpEHTVEENIELGKKdnsnSFDDWPIDKIWETFPILVKLKNRLAG----------QLSGGEQQMLSIARTL 150
Cdd:cd03245 81 GYVPQDVTLF-YGTLRDNITLGAP----LADDERILRAAELAGVTDFVNKHPNGldlqigergrGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347602354 151 VGNPEILLLDEPSEGLapiiveDI---VKILENLKKL--GVTILLAEQNMHFcMEVAKEAIIIDKGKAV 214
Cdd:cd03245 156 LNDPPILLLDEPTSAM------DMnseERLKERLRQLlgDKTLIIITHRPSL-LDLVDRIIVMDSGRIV 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-190 |
2.83e-22 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 91.30 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLI-KVKSGSIKLKGEEL-------IKKPt 72
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERRggedvweLRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 73 skralsgIGYV-PEDRQVFPEH-TVEE--------NIELGKKdnsnsFDDWPIDKIWETFPIL--VKLKNRLAGQLSGGE 140
Cdd:COG1119 80 -------IGLVsPALQLRFPRDeTVLDvvlsgffdSIGLYRE-----PTDEQRERARELLELLglAHLADRPFGTLSQGE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1347602354 141 QQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKLG-VTILL 190
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVL 198
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-226 |
2.88e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 94.35 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIK-KPTSKRALsGIG 81
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTPAKAHQL-GIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 82 YVPEDRQVFPEHTVEENIELG---KKDNSNSFDDwpidkiwetfpILVKLKNRL-----AGQLSGGEQQMLSIARTLVGN 153
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGlpkRQASMQKMKQ-----------LLAALGCQLdldssAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347602354 154 PEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDT 226
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDD 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-225 |
2.93e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.47 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGIGY 82
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 83 VPEDRQVFPEHTVEENIELG----KKDNSNSFDDWPIDKIWETFPIL-VKLK---NRLAGQLSGGEQQMLSIARTLVGNP 154
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGrhltKKVCGVNIIDWREMRVRAAMMLLrVGLKvdlDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347602354 155 EILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKD 225
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-212 |
3.12e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.20 E-value: 3.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 16 SQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRALSGI----GYV---PEDrQ 88
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYH-ITPETGNKNLKKLrkkvSLVfqfPEA-Q 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 89 VFpEHTVEENIELGKKDNSNSFDDWPIDKI-W-ETFPILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGL 166
Cdd:PRK13641 98 LF-ENTVLKDVEFGPKNFGFSEDEAKEKALkWlKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1347602354 167 APIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGK 212
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGK 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-229 |
4.59e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.86 E-value: 4.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 2 NLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRalsGIG 81
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR---DIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 82 YVPEDRQVFPEHTVEENIELGKKDNSNSFDDWPiDKIWETFPI--LVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLL 159
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGLKMLGVPKEERK-QRVKEALELvdLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347602354 160 DEPSEGLAPIIVEDIV-KILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDTKTR 229
Cdd:PRK11432 161 DEPLSNLDANLRRSMReKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASR 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-162 |
5.03e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 94.08 E-value: 5.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 14 GNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIK--KPTSKRALsgIGYVPEDRQVFP 91
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD-IRdlTLESLRRQ--IGVVPQDTFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 92 EhTVEENIELGKKDNSNsfddwpiDKIWE--------TFpiLVKLKNRLA-------GQLSGGEQQMLSIARTLVGNPEI 156
Cdd:COG1132 428 G-TIRENIRYGRPDATD-------EEVEEaakaaqahEF--IEALPDGYDtvvgergVNLSGGQRQRIAIARALLKDPPI 497
|
....*.
gi 1347602354 157 LLLDEP 162
Cdd:COG1132 498 LILDEA 503
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
11-195 |
7.63e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 89.93 E-value: 7.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 11 AFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRAL--SGIGYVPEDRQ 88
Cdd:PRK10908 10 AYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFlrRQIGMIFQDHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 89 VFPEHTVEENIELGKKDNSNSFDD------WPIDKIwetfPILVKLKNrLAGQLSGGEQQMLSIARTLVGNPEILLLDEP 162
Cdd:PRK10908 90 LLMDRTVYDNVAIPLIIAGASGDDirrrvsAALDKV----GLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190
....*....|....*....|....*....|...
gi 1347602354 163 SEGLAPIIVEDIVKILENLKKLGVTILLAEQNM 195
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-222 |
7.82e-22 |
|
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: 89.98 E-value: 7.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 5 ETKSMNAFYGNS-QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRALSGIGYV 83
Cdd:cd03254 4 EFENVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGID-IRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEhTVEENIELGkkDNSNSFDDWPI-DKIWETFPILVKLKNRL-------AGQLSGGEQQMLSIARTLVGNPE 155
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLG--RPNATDEEVIEaAKEAGAHDFIMKLPNGYdtvlgenGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347602354 156 ILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAeqnmHFCMEV--AKEAIIIDKGKAVWTGSLDDL 222
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIA----HRLSTIknADKILVLDDGKIIEEGTHDEL 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-231 |
8.74e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 90.88 E-value: 8.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 16 SQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRAL-SGIGYV---PEdRQVFp 91
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrKKVGLVfqyPE-YQLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 92 EHTVEENIELGKKdNSNSFDDWPIDKIWETFPIL----VKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLA 167
Cdd:PRK13637 98 EETIEKDIAFGPI-NLGLSEEEIENRVKRAMNIVgldyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 168 PIIVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDTKTRDK 231
Cdd:PRK13637 177 PKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLES 241
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
11-191 |
1.41e-21 |
|
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: 92.73 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 11 AFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRaLSGIGYVPEDRQVF 90
Cdd:TIGR02857 330 AYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RDQIAWVPQHPFLF 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 PEhTVEENIELGKKDNSNSFDDWPIDK--IWETFPILVKLKNRLAGQ----LSGGEQQMLSIARTLVGNPEILLLDEPSE 164
Cdd:TIGR02857 409 AG-TIAENIRLARPDASDAEIREALERagLDEFVAALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
170 180
....*....|....*....|....*..
gi 1347602354 165 GLAPIIVEDIVKILENLKKlGVTILLA 191
Cdd:TIGR02857 488 HLDAETEAEVLEALRALAQ-GRTVLLV 513
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-222 |
1.62e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 90.91 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 14 GNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSK-RAL-SGIGYVPEDRQVFP 91
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElRAArRKIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 92 EHTVEENIEL-----GkkdnsnsfddWPIDKIWETFPILVKL------KNRLAGQLSGGEQQMLSIARTLVGNPEILLLD 160
Cdd:COG1135 96 SRTVAENVALpleiaG----------VPKAEIRKRVAELLELvglsdkADAYPSQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347602354 161 EPSEGLAPIIVEDIVKILENL-KKLGVTILLA--EqnmhfcMEVAKE----AIIIDKGKAVWTGSLDDL 222
Cdd:COG1135 166 EATSALDPETTRSILDLLKDInRELGLTIVLIthE------MDVVRRicdrVAVLENGRIVEQGPVLDV 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-228 |
3.68e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.87 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 2 NLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEE--LIK------KPTS 73
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinLVRdkdgqlKVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 74 KRAL----SGIGYVPEDRQVFPEHTVEENIE------LG-KKDNSNSFDDWPIDKIwetfPILVKLKNRLAGQLSGGEQQ 142
Cdd:PRK10619 84 KNQLrllrTRLTMVFQHFNLWSHMTVLENVMeapiqvLGlSKQEARERAVKYLAKV----GIDERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 143 MLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
....*.
gi 1347602354 223 QKDTKT 228
Cdd:PRK10619 240 FGNPQS 245
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-217 |
7.81e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 88.25 E-value: 7.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 2 NLLETKSMNAFYGN-SQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRALSGI 80
Cdd:PRK13647 3 NIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE-VNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 81 GYV---PEDrQVFPEhTVEE-------NIELGKKD-NSNSFDDWPIDKIWEtfpilvkLKNRLAGQLSGGEQQMLSIART 149
Cdd:PRK13647 82 GLVfqdPDD-QVFSS-TVWDdvafgpvNMGLDKDEvERRVEEALKAVRMWD-------FRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 150 LVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTG 217
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
13-190 |
8.36e-21 |
|
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: 85.73 E-value: 8.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQ--VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIK-KPTSKRALsgIGYVPEDRQV 89
Cdd:cd03246 10 YPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDH--VGYLPQDDEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 90 FPEhTVEENIelgkkdnsnsfddwpidkiwetfpilvklknrlagqLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPI 169
Cdd:cd03246 88 FSG-SIAENI------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180
....*....|....*....|.
gi 1347602354 170 IVEDIVKILENLKKLGVTILL 190
Cdd:cd03246 131 GERALNQAIAALKAAGATRIV 151
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-222 |
1.10e-20 |
|
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: 86.90 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 11 AFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRALSGIGYVPEDRQVF 90
Cdd:cd03253 9 AYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD-IREVTLDSLRRAIGVVPQDTVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 PEhTVEENIELGKKDNSnsfDDWPID--KIWETFPILVKLKNRLAGQ-------LSGGEQQMLSIARTLVGNPEILLLDE 161
Cdd:cd03253 88 ND-TIGYNIRYGRPDAT---DEEVIEaaKAAQIHDKIMRFPDGYDTIvgerglkLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347602354 162 PSEGLapiiveDIV---KILENLKKL--GVTILLAEQNMHFCMEvAKEAIIIDKGKAVWTGSLDDL 222
Cdd:cd03253 164 ATSAL------DTHterEIQAALRDVskGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-163 |
1.77e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.61 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRALSGIGYV 83
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKP-ISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEdRQVFPEH-TVEENIELGKK----------DNSNSFDDWPIDKIWetfpiLVKLKNRLAGQLSGGEQQMLSIARTLVG 152
Cdd:PRK11231 82 PQ-HHLTPEGiTVRELVAYGRSpwlslwgrlsAEDNARVNQAMEQTR-----INHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170
....*....|.
gi 1347602354 153 NPEILLLDEPS 163
Cdd:PRK11231 156 DTPVVLLDEPT 166
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
13-222 |
1.99e-20 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 89.41 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YG-NSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELikKPTSKRALSG-IGYVPEDRQVF 90
Cdd:TIGR01193 483 YGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL--KDIDRHTLRQfINYLPQEPYIF 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 pEHTVEENIELGKKDNSNSFDDW------PIDKIWETFPIlvKLKNRLA---GQLSGGEQQMLSIARTLVGNPEILLLDE 161
Cdd:TIGR01193 561 -SGSILENLLLGAKENVSQDEIWaaceiaEIKDDIENMPL--GYQTELSeegSSISGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 162 PSEGLAPIIVEDIVKILENLKKLGVtILLAEQnmhfcMEVAKEA---IIIDKGKAVWTGSLDDL 222
Cdd:TIGR01193 638 STSNLDTITEKKIVNNLLNLQDKTI-IFVAHR-----LSVAKQSdkiIVLDHGKIIEQGSHDEL 695
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-217 |
2.41e-20 |
|
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: 84.67 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 15 NSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALsgIGYVPEDRQVFpeht 94
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL--ISVLNQRPYLF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 95 veenielgkkDNSnsfddwpidkiwetfpilvkLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPI----I 170
Cdd:cd03247 88 ----------DTT--------------------LRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIterqL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1347602354 171 VEDIVKILENLKKLGVTILLAEqnmhfcMEVAKEAIIIDKGKAVWTG 217
Cdd:cd03247 138 LSLIFEVLKDKTLIWITHHLTG------IEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-222 |
2.52e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.10 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 16 SQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKgeELIKKPTSK-------RALSGIGYVPEDRQ 88
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIVVSSTSKqkeikpvRKKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 89 VFpEHTVEENIELGKKDNSNSFDDwpIDKI--------------WETFPIlvklknrlagQLSGGEQQMLSIARTLVGNP 154
Cdd:PRK13643 97 LF-EETVLKDVAFGPQNFGIPKEK--AEKIaaeklemvgladefWEKSPF----------ELSGGQMRRVAIAGILAMEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 155 EILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:PRK13643 164 EVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-187 |
5.04e-20 |
|
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: 88.19 E-value: 5.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFY-GNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSgIGY 82
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-VSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 83 VPEDRQVFpEHTVEENIELGKKDNSNsfddwpiDKIWETFPiLVKLKNRLAG--------------QLSGGEQQMLSIAR 148
Cdd:TIGR02868 414 CAQDAHLF-DTTVRENLRLARPDATD-------EELWAALE-RVGLADWLRAlpdgldtvlgeggaRLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1347602354 149 TLVGNPEILLLDEPSEGLAPI----IVEDIVKILENLKKLGVT 187
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAEtadeLLEDLLAALSGRTVVLIT 527
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-195 |
5.19e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 85.60 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVK-----SGSIKLKGEELIKKPTSKRAL 77
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 78 SG-IGYVPEDRQVFPeHTVEENIELGKKDNSNSfDDWPIDKIWET----FPILVKLKNRL---AGQLSGGEQQMLSIART 149
Cdd:PRK14239 85 RKeIGMVFQQPNPFP-MSIYENVVYGLRLKGIK-DKQVLDEAVEKslkgASIWDEVKDRLhdsALGLSGGQQQRVCIARV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1347602354 150 LVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKlGVTILLAEQNM 195
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKD-DYTMLLVTRSM 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-162 |
5.40e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.81 E-value: 5.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLkgeelikkPTSKRalsgIGYVPEDRQVFPE 92
Cdd:COG0488 8 FGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--------PKGLR----IGYLPQEPPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 HTVEENI---------------ELGKKDNSNSFDDWPIDKIWETFP-------------ILVKLK------NRLAGQLSG 138
Cdd:COG0488 76 LTVLDTVldgdaelraleaeleELEAKLAEPDEDLERLAELQEEFEalggweaearaeeILSGLGfpeedlDRPVSELSG 155
|
170 180
....*....|....*....|....
gi 1347602354 139 GEQQMLSIARTLVGNPEILLLDEP 162
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEP 179
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-222 |
7.17e-20 |
|
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: 84.90 E-value: 7.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 17 QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRALSGIGYVPEDRQVFpEHTVE 96
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVD-IRDLNLRWLRSQIGLVSQEPVLF-DGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 97 ENIELGKKD-------------NSNSFddwpIDKIWETFPILVKLKnrlAGQLSGGEQQMLSIARTLVGNPEILLLDEPS 163
Cdd:cd03249 95 ENIRYGKPDatdeeveeaakkaNIHDF----IMSLPDGYDTLVGER---GSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 164 EGLaPIIVEDIV-KILENLKKLGVTILLAE-----QNmhfcmevAKEAIIIDKGKAVWTGSLDDL 222
Cdd:cd03249 168 SAL-DAESEKLVqEALDRAMKGRTTIVIAHrlstiRN-------ADLIAVLQNGQVVEQGTHDEL 224
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-162 |
1.83e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 84.01 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELikKPTSKRALSGIgy 82
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL--AAWSPWELARR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 83 vpedRQVFPEH-------TVEENIELGK--KDNSNSFDDWPIDKIWETFPILvKLKNRLAGQLSGGEQQMLSIARTLV-- 151
Cdd:COG4559 77 ----RAVLPQHsslafpfTVEEVVALGRapHGSSAAQDRQIVREALALVGLA-HLAGRSYQTLSGGEQQRVQLARVLAql 151
|
170
....*....|....*.
gi 1347602354 152 -----GNPEILLLDEP 162
Cdd:COG4559 152 wepvdGGPRWLFLDEP 167
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-190 |
2.14e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.23 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGIGYVPEDRQ---VFPEHTVEE 97
Cdd:COG3845 276 DVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAYIPEDRLgrgLVPDMSVAE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIELGKKDNSnSFDDWPI----------DKIWETFPILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGL- 166
Cdd:COG3845 356 NLILGRYRRP-PFSRGGFldrkairafaEELIEEFDVRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLd 434
|
170 180
....*....|....*....|....*.
gi 1347602354 167 --ApiiVEDIVKILENLKKLGVTILL 190
Cdd:COG3845 435 vgA---IEFIHQRLLELRDAGAAVLL 457
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-225 |
3.02e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 85.94 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKpTSKRAL-SGIGYVPEDRQVFPEHTVEE 97
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFK-SSKEALeNGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIELGKK-------DNSNSFDDwpIDKIWETFPILVKLKNRLAgQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPII 170
Cdd:PRK10982 93 NMWLGRYptkgmfvDQDKMYRD--TKAIFDELDIDIDPRAKVA-TLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 171 VEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKD 225
Cdd:PRK10982 170 VNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMD 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-191 |
3.15e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.90 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIklkgeelikkptSKRALSGIGYVPEDRQV--- 89
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGARVAYVPQRSEVpds 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 90 FPEhTVEENIELGKkdnsnsfddWP---------------IDKIWETFPILvKLKNRLAGQLSGGEQQMLSIARTLVGNP 154
Cdd:NF040873 70 LPL-TVRDLVAMGR---------WArrglwrrltrddraaVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 1347602354 155 EILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLA 191
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVV 175
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-215 |
3.92e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 83.21 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSgIGYVPEDRQV--FPEHTV 95
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY-IGRVFQDPMMgtAPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 96 EENIEL----GKKDNSNsfddWPIDKIW-ETFPILVK-----LKNRL---AGQLSGGEQQMLSIARTLVGNPEILLLDEP 162
Cdd:COG1101 100 EENLALayrrGKRRGLR----RGLTKKRrELFRELLAtlglgLENRLdtkVGLLSGGQRQALSLLMATLTKPKLLLLDEH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 163 SEGLAPIIVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVW 215
Cdd:COG1101 176 TAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIIL 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-214 |
5.51e-19 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 82.93 E-value: 5.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 6 TKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIK-KPTSKRALS-GIGYV 83
Cdd:TIGR02769 14 TGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQlDRKQRRAFRrDVQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PED--RQVFPEHTVEENI-----ELGKKDNSNSfddwpIDKIWETFPiLVKLK----NRLAGQLSGGEQQMLSIARTLVG 152
Cdd:TIGR02769 94 FQDspSAVNPRMTVRQIIgeplrHLTSLDESEQ-----KARIAELLD-MVGLRsedaDKLPRQLSGGQLQRINIARALAV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347602354 153 NPEILLLDEPSEGLAPIIVEDIVKILENLK-KLGVTILLAEQNMHFCMEVAKEAIIIDKGKAV 214
Cdd:TIGR02769 168 KPKLIVLDEAVSNLDMVLQAVILELLRKLQqAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-226 |
6.26e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.15 E-value: 6.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLkGEELI---KKPTSKRAL-SGIGYVPEdrqvFPEH- 93
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVItagKKNKKLKPLrKKVGIVFQ----FPEHq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 94 ----TVEENIELGKKDNSNSFDDwPIDKIWETFPiLVKLKNRLAGQ----LSGGEQQMLSIARTLVGNPEILLLDEPSEG 165
Cdd:PRK13634 98 lfeeTVEKDICFGPMNFGVSEED-AKQKAREMIE-LVGLPEELLARspfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 166 LAPIIVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDT 226
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
13-227 |
8.32e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 82.73 E-value: 8.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQ--VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSK-RALSGIGYVPEDRQv 89
Cdd:PRK13632 17 YPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEiRKKIGIIFQNPDNQ- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 90 FPEHTVEENIELGKKDNSNSFDDwpIDKIWETFPILVKLKNRLAGQ---LSGGEQQMLSIARTLVGNPEILLLDEPSEGL 166
Cdd:PRK13632 96 FIGATVEDDIAFGLENKKVPPKK--MKDIIDDLAKKVGMEDYLDKEpqnLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 167 APIIVEDIVKILENLKKLGV-TILLAEQNMHfcmEV--AKEAIIIDKGKAVWTGSLDDLQKDTK 227
Cdd:PRK13632 174 DPKGKREIKKIMVDLRKTRKkTLISITHDMD---EAilADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-190 |
9.66e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.33 E-value: 9.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGIGYVPEDRQV---FPEHTVEE 97
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSsglYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIeLGKKDNSNSFddWpID-----KIWETF--PILVKL--KNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAP 168
Cdd:PRK15439 361 NV-CALTHNRRGF--W-IKparenAVLERYrrALNIKFnhAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180
....*....|....*....|..
gi 1347602354 169 IIVEDIVKILENLKKLGVTILL 190
Cdd:PRK15439 437 SARNDIYQLIRSIAAQNVAVLF 458
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-217 |
9.70e-19 |
|
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: 81.61 E-value: 9.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLkgeelikkptskralsgIGYVPEDRQvfPEHTVEE 97
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV-----------------AGLVPWKRR--KKFLRRI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIELGKKdNSNSFDDWPIDkiweTFPIL--------VKLKNRLAG----------------QLSGGEQQMLSIARTLVGN 153
Cdd:cd03267 97 GVVFGQK-TQLWWDLPVID----SFYLLaaiydlppARFKKRLDElselldleelldtpvrQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 154 PEILLLDEPSEGLAPIIVEDIVKILENLKKL-GVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTG 217
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-199 |
9.95e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.08 E-value: 9.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSiklkgeelIKKPTSKRalsgI 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV--------IKRNGKLR----I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 81 GYVPEDRQVFPEH--TVEENIELgkKDNSNSFDdwpidkiwetfpILVKLKNRLAGQ--------LSGGEQQMLSIARTL 150
Cdd:PRK09544 70 GYVPQKLYLDTTLplTVNRFLRL--RPGTKKED------------ILPALKRVQAGHlidapmqkLSGGETQRVLLARAL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 151 VGNPEILLLDEPSEGL---APIIVEDIVKILENlkKLGVTILLAEQNMHFCM 199
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVdvnGQVALYDLIDQLRR--ELDCAVLMVSHDLHLVM 185
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-162 |
1.51e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.83 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNS----QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRa 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-VTGPGADR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 77 lsgiGYVPEDRQVFPEHTVEENIELGKKDNSNSFDDwpIDKIWETFPILVKLK---NRLAGQLSGGEQQMLSIARTLVGN 153
Cdd:COG4525 79 ----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAE--RRARAEELLALVGLAdfaRRRIWQLSGGMRQRVGIARALAAD 152
|
....*....
gi 1347602354 154 PEILLLDEP 162
Cdd:COG4525 153 PRFLLMDEP 161
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-202 |
1.69e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.35 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELikKPTSKRALSG- 79
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV--EALSARAASRr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 80 IGYVPEDRQVFPEHTVEENIELGKKDNSNSFDDW------PIDKIWETFPIlVKLKNRLAGQLSGGEQQMLSIARTLVGN 153
Cdd:PRK09536 79 VASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWtetdraAVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1347602354 154 PEILLLDEPSEGLapiiveDI---VKILENLKKL---GVTILLAEQNMH----FCMEVA 202
Cdd:PRK09536 158 TPVLLLDEPTASL------DInhqVRTLELVRRLvddGKTAVAAIHDLDlaarYCDELV 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-162 |
1.71e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.07 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPtskralsgi 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 81 gyvPEDRQV---------FPEHTVEENIELGKKDNSNSFDDwpIDKIWETFPILVKLK---NRLAGQLSGGEQQMLSIAR 148
Cdd:PRK09452 83 ---AENRHVntvfqsyalFPHMTVFENVAFGLRMQKTPAAE--ITPRVMEALRMVQLEefaQRKPHQLSGGQQQRVAIAR 157
|
170
....*....|....
gi 1347602354 149 TLVGNPEILLLDEP 162
Cdd:PRK09452 158 AVVNKPKVLLLDES 171
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-222 |
2.32e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.25 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 12 FYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEEL-----IKKPTSKRALSGIGYVPED 86
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 87 RQVFPEHTVEENIELGKKDNSNSfDDWPIDKIWETFPILVKL-------KNRLAGQLSGGEQQMLSIARTLVGNPEILLL 159
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPLKSHGIK-EKREIKKIVEECLRKVGLwkevydrLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347602354 160 DEPSEGLAPIIVEDIVKILENLKKlGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-218 |
2.60e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.82 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQ-----VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSI---------KLKGEELI 68
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 69 KKPTSK---------RALSGIGYVPEdRQVFPEhTVEENIELG------KKDNSNSFDDWPIDKIWETFPILvklkNRLA 133
Cdd:PRK13631 101 TNPYSKkiknfkelrRRVSMVFQFPE-YQLFKD-TIEKDIMFGpvalgvKKSEAKKLAKFYLNKMGLDDSYL----ERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 134 GQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKA 213
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
....*
gi 1347602354 214 VWTGS 218
Cdd:PRK13631 255 LKTGT 259
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-222 |
3.15e-18 |
|
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: 80.35 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRALSGIGYVPEDRQVFPEhTVEE 97
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD-VRDYTLASLRRQIGLVSQDVFLFND-TVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIELGKKD-------------NSNSFddwpIDKIWETFPILVKLKnrlAGQLSGGEQQMLSIARTLVGNPEILLLDEPSE 164
Cdd:cd03251 95 NIAYGRPGatreeveeaaraaNAHEF----IMELPEGYDTVIGER---GVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 165 GLAPIIVEDIVKILENLKKLGVTILLAeqnmH--FCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:cd03251 168 ALDTESERLVQAALERLMKNRTTFVIA----HrlSTIENADRIVVLEDGKIVERGTHEEL 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-162 |
3.17e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLkGEELIkkptskralsgIGY 82
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-----------IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 83 VPEDRQVF-PEHTVEENIELGKKDNSNSF------------DDWpidkiwetfpilvklkNRLAGQLSGGEQQMLSIART 149
Cdd:COG0488 383 FDQHQEELdPDKTVLDELRDGAPGGTEQEvrgylgrflfsgDDA----------------FKPVGVLSGGEKARLALAKL 446
|
170
....*....|...
gi 1347602354 150 LVGNPEILLLDEP 162
Cdd:COG0488 447 LLSPPNVLLLDEP 459
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-217 |
6.38e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.31 E-value: 6.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEelikkPTSKrAL--SGIGYVPEDRQV---FPEh 93
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ-----PTRQ-ALqkNLVAYVPQSEEVdwsFPV- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 94 TVEENIELGKKDN------SNSFDDWPIDKIWETFPILvKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLA 167
Cdd:PRK15056 96 LVEDVVMMGRYGHmgwlrrAKKRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1347602354 168 PIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIdKGKAVWTG 217
Cdd:PRK15056 175 VKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASG 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-226 |
6.40e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.97 E-value: 6.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELI-KKPTSKRAlSGIG 81
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQE-AGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 82 YVPEDRQVFPEHTVEENIELGKkDNSNSFD--DWpiDKIW-ETFPILVKLK-----NRLAGQLSGGEQQMLSIARTLVGN 153
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIFLGR-EFVNRFGriDW--KKMYaEADKLLARLNlrfssDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347602354 154 PEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDT 226
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDS 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-190 |
7.04e-18 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 79.43 E-value: 7.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRALsgigyVPEDRQVFPEHTVEEN 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQ-ITEPGPDRMV-----VFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 99 IELGKKDNSNSFDDWPIDKIWETFPILVKLK---NRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIV 175
Cdd:TIGR01184 75 IALAVDRVLPDLSKSERRAIVEEHIALVGLTeaaDKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170
....*....|....*.
gi 1347602354 176 -KILENLKKLGVTILL 190
Cdd:TIGR01184 155 eELMQIWEEHRVTVLM 170
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-190 |
1.00e-17 |
|
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: 79.61 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKkpTSKRALSG-----IGYVPEDRQVFPEH 93
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAA--MSRKELRElrrkkISMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 94 TVEENIELG-------KKDNsnsfddwpIDKIWETFPiLVKL---KNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPS 163
Cdd:cd03294 118 TVLENVAFGlevqgvpRAER--------EERAAEALE-LVGLegwEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180
....*....|....*....|....*...
gi 1347602354 164 EGLAPIIVEDIVKILENL-KKLGVTILL 190
Cdd:cd03294 189 SALDPLIRREMQDELLRLqAELQKTIVF 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-166 |
1.26e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.02 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 14 GNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELikKPTSKRAL-SGIGYVPEDRQVFpE 92
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI--ADYSEAALrQAISVVSQRVHLF-S 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 HTVEENIELGKKDNSnsfDDWPIDkiwetfpIL--VKLKNRLAG-------------QLSGGEQQMLSIARTLVGNPEIL 157
Cdd:PRK11160 428 ATLRDNLLLAAPNAS---DEALIE-------VLqqVGLEKLLEDdkglnawlgeggrQLSGGEQRRLGIARALLHDAPLL 497
|
....*....
gi 1347602354 158 LLDEPSEGL 166
Cdd:PRK11160 498 LLDEPTEGL 506
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-234 |
1.80e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 78.88 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEEL--IKKPTSKRALSGIGYVPEDRQvFPEHTVE 96
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVGIVFQNPETQ-FVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 97 ENIELGKKD------NSNSFDDWPIDKIWetfpiLVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPii 170
Cdd:PRK13644 97 EDLAFGPENlclppiEIRKRVDRALAEIG-----LEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP-- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347602354 171 vEDIVKILENLKKL---GVTILLAEQNMHFcMEVAKEAIIIDKGKAVWTGSLDDLQKDTKTRDKYLA 234
Cdd:PRK13644 170 -DSGIAVLERIKKLhekGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLT 234
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
13-212 |
1.82e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.07 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRalsGIGYVPEDRQVFPE 92
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER---GVGMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 HTVEENIELGKK--DNSNSFDDWPIDKIWETFPiLVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGL-API 169
Cdd:PRK11000 90 LSVAENMSFGLKlaGAKKEEINQRVNQVAEVLQ-LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLdAAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1347602354 170 IVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGK 212
Cdd:PRK11000 169 RVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-189 |
2.35e-17 |
|
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: 77.30 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 17 QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVK---SGSIKLKGEEliKKPTSKRALSGIGYVPEDRQVFPEH 93
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIP--YKEFAEKYPGEIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 94 TVEENIELGKKDNSNSFddwpidkiwetfpilvklknrLAGqLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVED 173
Cdd:cd03233 99 TVRETLDFALRCKGNEF---------------------VRG-ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALE 156
|
170
....*....|....*..
gi 1347602354 174 IVKILENL-KKLGVTIL 189
Cdd:cd03233 157 ILKCIRTMaDVLKTTTF 173
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-196 |
2.59e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.54 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKS-----GSIKLKGEELIKKPTS-KRAL 77
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 78 SGIGYVPEDRQVFPeHTVEENIELGKKdnsnsFDDW----PIDKIWETF----PILVKLKNRL---AGQLSGGEQQMLSI 146
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVK-----IVGWrpklEIDDIVESAlkdaDLWDEIKHKIhksALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1347602354 147 ARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLK-KLGVTILLAEQNMH 196
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLH 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-225 |
2.65e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.97 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKS--GSIKLKGEELIKKPTSKRALSGI 80
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 81 GYVPEDRQVFPEHTVEENIELGKKDNSNSFDDWpiDKIW-ETFPILVKLK-----NRLAGQLSGGEQQMLSIARTLVGNP 154
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGNEITPGGIMDY--DAMYlRAQKLLAQLKldinpATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347602354 155 EILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKD 225
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTED 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-222 |
3.31e-17 |
|
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: 77.53 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEEL-IKKPTSKRAlsGIGYVPEDRQVF------ 90
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRR--QVGVVLQENVLFnrsird 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 ------PEHTVEENIELGKKDNSNSFddwpIDKIWETFPILVKlkNRLAGqLSGGEQQMLSIARTLVGNPEILLLDEPSE 164
Cdd:cd03252 95 nialadPGMSMERVIEAAKLAGAHDF----ISELPEGYDTIVG--EQGAG-LSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 165 GLApiiVEDIVKILENLKKL--GVTILLAEQNMHFCMEvAKEAIIIDKGKAVWTGSLDDL 222
Cdd:cd03252 168 ALD---YESEHAIMRNMHDIcaGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
13-212 |
3.51e-17 |
|
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: 75.18 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKgeelikkPTSKralsgIGYVPedrqvfpe 92
Cdd:cd03221 10 YGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------STVK-----IGYFE-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 htveenielgkkdnsnsfddwpidkiwetfpilvklknrlagQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLapiive 172
Cdd:cd03221 70 ------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNHL------ 101
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1347602354 173 DI--VKILEN-LKKLGVTILLAEQNMHFCMEVAKEAIIIDKGK 212
Cdd:cd03221 102 DLesIEALEEaLKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-225 |
3.63e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 78.25 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSK-----RALSGIGYVPEDRQVFPEh 93
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqiRKKVGLVFQFPESQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 94 TVEENIELGKKDNSNSFDDwpIDKIWETFPILVKLKNRLAGQ----LSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPI 169
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEE--AEALAREKLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1347602354 170 IVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKD 225
Cdd:PRK13649 180 GRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-218 |
4.80e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 79.67 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 22 MSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRalSGIGYVPEDRQVFPEHTVEENIEL 101
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVR--QSLGMCPQHNILFHHLTVAEHILF 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 102 GKKDNSNSFDD--WPIDKIWETFPILVKlKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILE 179
Cdd:TIGR01257 1027 YAQLKGRSWEEaqLEMEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190
....*....|....*....|....*....|....*....
gi 1347602354 180 NLKKlGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGS 218
Cdd:TIGR01257 1106 KYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-222 |
6.10e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 79.23 E-value: 6.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 12 FYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTfkaITGLIKV---KSGSIKLKGEElIKKPTSKRALSGIGYVPEDRQ 88
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRVfdpQSGRILIDGTD-IRTVTRASLRRNIAVVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 89 VFpEHTVEENIELGKKDNSNS-------------FddwpIDKIWETFPILVKLKNRlagQLSGGEQQMLSIARTLVGNPE 155
Cdd:PRK13657 420 LF-NRSIEDNIRVGRPDATDEemraaaeraqahdF----IERKPDGYDTVVGERGR---QLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 156 ILLLDEPSEGLaPIIVEDIVK-ILENLKKLGVTILLAeqnmHFCMEV--AKEAIIIDKGKAVWTGSLDDL 222
Cdd:PRK13657 492 ILILDEATSAL-DVETEAKVKaALDELMKGRTTFIIA----HRLSTVrnADRILVFDNGRVVESGSFDEL 556
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-221 |
6.31e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 78.30 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIkkptskrALSGIGYVPEDRQV---FpEH-- 93
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLT-------ALSEKELRKARRQIgmiF-QHfn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 94 -----TVEENI----ELGKKDNSNsfddwpIDKIWETFPILVKL---KNRLAGQLSGGEQQMLSIARTLVGNPEILLLDE 161
Cdd:PRK11153 93 llssrTVFDNValplELAGTPKAE------IKARVTELLELVGLsdkADRYPAQLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347602354 162 PSEGLAPIIVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDD 221
Cdd:PRK11153 167 ATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-227 |
7.17e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.51 E-value: 7.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 17 QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSK-----RALSGIGYVPEDRQVFp 91
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirpvRKRIGMVFQFPESQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 92 EHTVEENIELGKKdNSNsfddWPIDKIWE-TFPILVKL---KNRLAG---QLSGGEQQMLSIARTLVGNPEILLLDEPSE 164
Cdd:PRK13646 100 EDTVEREIIFGPK-NFK----MNLDEVKNyAHRLLMDLgfsRDVMSQspfQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 165 GLAPIIVEDIVKILENLK-KLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDTK 227
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-191 |
7.89e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.80 E-value: 7.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 23 SLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEEL-IKKPtsKRAL-SGIGYVPEDRQ---VFPEHTVEE 97
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdIRSP--RDAIrAGIMLCPEDRKaegIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIELGKKDNSNSFdDWPIDKIWET-----FPILVKLKNRLAGQ----LSGGEQQMLSIARTLVGNPEILLLDEPSEGlap 168
Cdd:PRK11288 351 NINISARRHHLRA-GCLINNRWEAenadrFIRSLNIKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRG--- 426
|
170 180
....*....|....*....|....*.
gi 1347602354 169 IIV---EDIVKILENLKKLGVTILLA 191
Cdd:PRK11288 427 IDVgakHEIYNVIYELAAQGVAVLFV 452
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-218 |
8.74e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 77.36 E-value: 8.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 17 QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKL------KGEELIKKPTSKRALSGIGYVPEDRQVF 90
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKKIKEVKRLRKEIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 PEhTVEENIELGkkdnsnsfddwPI------DKIWETFPILVKL-------KNRLAGQLSGGEQQMLSIARTLVGNPEIL 157
Cdd:PRK13645 105 QE-TIEKDIAFG-----------PVnlgenkQEAYKKVPELLKLvqlpedyVKRSPFELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 158 LLDEPSEGLAPIIVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGS 218
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-212 |
1.05e-16 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 75.53 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 16 SQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRALSGIGYVPEDRQVFpEHTV 95
Cdd:cd03369 21 PPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGID-ISTIPLEDLRSSLTIIPQDPTLF-SGTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 96 EENIelgkkDNSNSFDDwpiDKIWETFPILVKLKNrlagqLSGGEQQMLSIARTLVGNPEILLLDEPSeglAPIIVEDIV 175
Cdd:cd03369 99 RSNL-----DPFDEYSD---EEIYGALRVSEGGLN-----LSQGQRQLLCLARALLKRPRVLVLDEAT---ASIDYATDA 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 1347602354 176 KILENLKKL--GVTILLAEQNMHFCMEVAKeAIIIDKGK 212
Cdd:cd03369 163 LIQKTIREEftNSTILTIAHRLRTIIDYDK-ILVMDAGE 200
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-190 |
1.37e-16 |
|
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: 77.02 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIK---VKSGSIKLKGEELIKKPTSK-RALSG--IGYVPEDrqvfPE-- 92
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElRKIRGreIQMIFQD----PMts 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 ----HTVEENIE--------LGKKDnsnsfddwPIDKIWETF-----PILVKLKNRLAGQLSGGEQQMLSIARTLVGNPE 155
Cdd:COG0444 99 lnpvMTVGDQIAeplrihggLSKAE--------ARERAIELLervglPDPERRLDRYPHELSGGMRQRVMIARALALEPK 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1347602354 156 ILLLDEPSEGLAPIIVEDIVKILENLKK-LGVTILL 190
Cdd:COG0444 171 LLIADEPTTALDVTIQAQILNLLKDLQReLGLAILF 206
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-229 |
1.71e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 76.34 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELikkPTSKR----- 75
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI---PAMSRsrlyt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 76 ALSGIGYVPEDRQVFPEHTVEENIELGKKDNSNsfddWPIDKIWETfpILVKLK--------NRLAGQLSGGEQQMLSIA 147
Cdd:PRK11831 82 VRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQ----LPAPLLHST--VMMKLEavglrgaaKLMPSELSGGMARRAALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 148 RTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKK-LGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDT 226
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSaLGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
...
gi 1347602354 227 KTR 229
Cdd:PRK11831 236 DPR 238
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-190 |
1.99e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 74.87 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGL--IKVKSGSIKLKGEELIKKPTSKRALSGIG 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 82 YVPEDRQVFPEhtveenielgkkdnsnsfddwpidkiwetfpilVKLKNRLAG---QLSGGEQQMLSIARTLVGNPEILL 158
Cdd:cd03217 81 LAFQYPPEIPG---------------------------------VKNADFLRYvneGFSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190
....*....|....*....|....*....|..
gi 1347602354 159 LDEPSEGLAPIIVEDIVKILENLKKLGVTILL 190
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLREEGKSVLI 159
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-190 |
2.21e-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: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELikKPTSKRALSG-IGYVPEDRQVFPEhTVE 96
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL--SQWDREELGRhIGYLPQDVELFDG-TIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 97 ENIELgkkdnsnsFDDWPIDKIWETfpilvklkNRLAG---------------------QLSGGEQQMLSIARTLVGNPE 155
Cdd:COG4618 424 ENIAR--------FGDADPEKVVAA--------AKLAGvhemilrlpdgydtrigeggaRLSGGQRQRIGLARALYGDPR 487
|
170 180 190
....*....|....*....|....*....|....*
gi 1347602354 156 ILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILL 190
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRALKARGATVVV 522
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-233 |
2.71e-16 |
|
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: 77.75 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 2 NLLETKSMNAFY-GNSQVLFD-MSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRalSG 79
Cdd:TIGR01257 1936 DILRLNELTKVYsGTSSPAVDrLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVH--QN 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 80 IGYVPEDRQVFPEHTVEENIELGKK------DNSNSFDDWPIDKIWetfpiLVKLKNRLAGQLSGGEQQMLSIARTLVGN 153
Cdd:TIGR01257 2014 MGYCPQFDAIDDLLTGREHLYLYARlrgvpaEEIEKVANWSIQSLG-----LSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 154 PEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQkdTKTRDKYL 233
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLK--SKFGDGYI 2166
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-217 |
4.16e-16 |
|
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: 76.76 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 22 MSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLK-GEELI----KKPTSK-RALSGIGYVPEDRQVFPEHTV 95
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVdmtkPGPDGRgRAKRYIGILHQEYDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 96 EENI----------ELGKKD-----NSNSFDDWPIDKIWETFPilvklknrlaGQLSGGEQQMLSIARTLVGNPEILLLD 160
Cdd:TIGR03269 383 LDNLteaiglelpdELARMKavitlKMVGFDEEKAEEILDKYP----------DELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 161 EPSEGLAPIIVEDIVK-ILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTG 217
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-225 |
4.53e-16 |
|
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: 76.40 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIK--VKSGSIKLKGEELIKKPTSKRALSGI 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 81 GYVPEDRQVFPEHTVEENIELGKKDNSNSFDDWPIDKIWETFPILVKLK------NRLAGQLSGGEQQMLSIARTLVGNP 154
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQldadnvTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347602354 155 EILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKD 225
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSED 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-221 |
1.28e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.19 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGE-----ELikkptskralsGIGYVpedrqvfPE 92
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallEL-----------GAGFH-------PE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 HTVEENIELG-------KKDNSNSFDDwpidkIWE-----TFpILVKLKN-------RLAgqlsggeqqmLSIARTLvgN 153
Cdd:COG1134 103 LTGRENIYLNgrllglsRKEIDEKFDE-----IVEfaelgDF-IDQPVKTyssgmraRLA----------FAVATAV--D 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 154 PEILLLDepsEGLApiiVEDIV------KILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDD 221
Cdd:COG1134 165 PDILLVD---EVLA---VGDAAfqkkclARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-224 |
2.10e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.97 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElikkPTSKRA--LSGIGYVPEDR-QVFPEHTVEE 97
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV----PFKRRKefARRIGVVFGQRsQLWWDLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIELGK----------KDNSNSFDD-WPIDKIWETfPIlvklknRlagQLSGGEQQMLSIARTLVGNPEILLLDEPSEGL 166
Cdd:COG4586 116 SFRLLKaiyripdaeyKKRLDELVElLDLGELLDT-PV------R---QLSLGQRMRCELAAALLHRPKILFLDEPTIGL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 167 apiiveDIV---KILENLKKL----GVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQK 224
Cdd:COG4586 186 ------DVVskeAIREFLKEYnrerGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-218 |
2.58e-15 |
|
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: 72.14 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSK-RalSGIGYVPEDRQVFpEHTVE 96
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlR--SRISIIPQDPVLF-SGTIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 97 ENIelgkkDNSNSFDDwpiDKIWETFPiLVKLKNRLAGQ--------------LSGGEQQMLSIARTLVGNPEILLLDEP 162
Cdd:cd03244 96 SNL-----DPFGEYSD---EELWQALE-RVGLKEFVESLpggldtvveeggenLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1347602354 163 SEGLAPIIVEDIVKIL-ENLKklGVTILLAEQNMHFCMEVAKEaIIIDKGKAVWTGS 218
Cdd:cd03244 167 TASVDPETDALIQKTIrEAFK--DCTVLTIAHRLDTIIDSDRI-LVLDKGRVVEFDS 220
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
13-162 |
2.77e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.42 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRA---------------- 76
Cdd:COG4604 11 YGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAkrlailrqenhinsrl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 77 ----LSGIGYVP--------EDRQVfpehtVEENIELgkkdnsnsFDdwpidkiwetfpiLVKLKNRLAGQLSGGEQQML 144
Cdd:COG4604 91 tvreLVAFGRFPyskgrltaEDREI-----IDEAIAY--------LD-------------LEDLADRYLDELSGGQRQRA 144
|
170
....*....|....*...
gi 1347602354 145 SIARTLVGNPEILLLDEP 162
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEP 162
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-212 |
3.34e-15 |
|
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: 71.35 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGeelikkptskralsGIGYVPEDRQVFPEhTVEE 97
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEPWIQNG-TIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIELGKkdnsnsfddwPIDKIW-----------ETFPILVKLKNRLAGQ----LSGGEQQMLSIARTLVGNPEILLLDEP 162
Cdd:cd03250 85 NILFGK----------PFDEERyekvikacalePDLEILPDGDLTEIGEkginLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 163 SEGLAPIIVEDIVK--ILENLKKlGVTILLAEQNMHFCMEVAKeAIIIDKGK 212
Cdd:cd03250 155 LSAVDAHVGRHIFEncILGLLLN-NKTRILVTHQLQLLPHADQ-IVVLDNGR 204
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-195 |
3.42e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.88 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGIGYVPEDRQ---VFPEHTVEE 97
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKrdgLVLGMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 N-------------IELGKKDNSNSFDDWpIDkiweTFPILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSE 164
Cdd:PRK10762 350 NmsltalryfsragGSLKHADEQQAVSDF-IR----LFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190
....*....|....*....|....*....|.
gi 1347602354 165 GLAPIIVEDIVKILENLKKLGVTILLAEQNM 195
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAEGLSIILVSSEM 455
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-216 |
3.50e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.41 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNS---------QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIK-K 70
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 71 PTSKRALSG-IGYVPEDR--QVFPEHTVEENI--------ELGKKDNSNSfddwpIDKIWETFPILVKLKNRLAGQLSGG 139
Cdd:PRK10419 81 RAQRKAFRRdIQMVFQDSisAVNPRKTVREIIreplrhllSLDKAERLAR-----ASEMLRAVDLDDSVLDKRPPQLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 140 EQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLK-KLGVTILLAEQNM----HFCMEVakeaIIIDKGKAV 214
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQqQFGTACLFITHDLrlveRFCQRV----MVMDNGQIV 231
|
..
gi 1347602354 215 WT 216
Cdd:PRK10419 232 ET 233
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-162 |
3.54e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.42 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRalsgiGY 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP-VEGPGAER-----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 83 VPEDRQVFPEHTVEENIELG------KKDNSNSFDDWPIDKIWetfpiLVKLKNRLAGQLSGGEQQMLSIARTLVGNPEI 156
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGlqlagvEKMQRLEIAHQMLKKVG-----LEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
....*.
gi 1347602354 157 LLLDEP 162
Cdd:PRK11248 150 LLLDEP 155
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-189 |
3.64e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.79 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 17 QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGIGYVPEDRQVFPEHTVE 96
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIYQELHLVPEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 97 ENIELGKKDNSNSFddwpIDK---IWETFPILVKLKNRL-----AGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAP 168
Cdd:PRK11288 98 ENLYLGQLPHKGGI----VNRrllNYEAREQLEHLGVDIdpdtpLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180
....*....|....*....|.
gi 1347602354 169 IIVEDIVKILENLKKLGVTIL 189
Cdd:PRK11288 174 REIEQLFRVIRELRAEGRVIL 194
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-212 |
4.05e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGIGYVPEDRQ---VFPEHTVEE 97
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIEL-------GKKDNSNSFDDWPIDKIWETFPILVKLK----NRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGL 166
Cdd:PRK09700 361 NMAIsrslkdgGYKGAMGLFHEVDEQRTAENQRELLALKchsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGI 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1347602354 167 APIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGK 212
Cdd:PRK09700 441 DVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
15-162 |
4.58e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 71.36 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 15 NSQVLF-DMSLKIKKNNIIALLGRNGAGKSSTFKAITG-LIKV--KSGSIKLKGEELIKKPTSKRalsGIGYVPEDRQVF 90
Cdd:COG4136 12 GGRPLLaPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQR---RIGILFQDDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 PEHTVEENIELGkkdnsnsfddwpidkiwetFPILVKLKNR------------LAG-------QLSGGEQQMLSIARTLV 151
Cdd:COG4136 89 PHLSVGENLAFA-------------------LPPTIGRAQRrarveqaleeagLAGfadrdpaTLSGGQRARVALLRALL 149
|
170
....*....|.
gi 1347602354 152 GNPEILLLDEP 162
Cdd:COG4136 150 AEPRALLLDEP 160
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
2-166 |
7.44e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.67 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 2 NLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElikkPTSKRALSGIG 81
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD----IDDPDVAEACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 82 YVPEDRQVFPEHTVEENIELGKKDNSNsfDDWPIDKIWETFPiLVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDE 161
Cdd:PRK13539 77 YLGHRNAMKPALTVAENLEFWAAFLGG--EELDIAAALEAVG-LAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
....*
gi 1347602354 162 PSEGL 166
Cdd:PRK13539 154 PTAAL 158
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
18-166 |
7.49e-15 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 70.93 E-value: 7.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRAL---SGIGYVPEDRQVFPEHT 94
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARlraRHVGFVFQSFQLLPTLT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 95 VEENI----EL-GKKDNSNSFDDWpIDKiwetfpilVKLKNRLA---GQLSGGEQQMLSIARTLVGNPEILLLDEPSEGL 166
Cdd:COG4181 107 ALENVmlplELaGRRDARARARAL-LER--------VGLGHRLDhypAQLSGGEQQRVALARAFATEPAILFADEPTGNL 177
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-190 |
1.18e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.58 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 2 NLLETKSMNAFYGNSQ----VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRAL 77
Cdd:PRK10584 5 NIVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 78 ---SGIGYVPEDRQVFPEHTVEENIELG---KKDNSNSFDDWPIDkIWETFPILVKLKNrLAGQLSGGEQQMLSIARTLV 151
Cdd:PRK10584 85 lraKHVGFVFQSFMLIPTLNALENVELPallRGESSRQSRNGAKA-LLEQLGLGKRLDH-LPAQLSGGEQQRVALARAFN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1347602354 152 GNPEILLLDEPSEGLAPIIVEDIVKILENL-KKLGVTILL 190
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLIL 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-166 |
1.43e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 72.28 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLkGEelikkpTSKralsgIGYV 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GE------TVK-----LAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVF-PEHTVEENI-------ELGKKD-NSNSFDDWpidkiwetFPILVKLKNRLAGQLSGGEQQMLSIARTLVGNP 154
Cdd:TIGR03719 391 DQSRDALdPNKTVWEEIsggldiiKLGKREiPSRAYVGR--------FNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGG 462
|
170
....*....|..
gi 1347602354 155 EILLLDEPSEGL 166
Cdd:TIGR03719 463 NVLLLDEPTNDL 474
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-227 |
1.45e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.27 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 17 QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSI-----------------KLKGEELIKKPTSK----- 74
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekeKVLEKLVIQKTRFKkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 75 ---RALSGIGYVPEDRQVFpEHTVEENIELGKKdnSNSFDDWPIDKIWETFPILVKLK----NRLAGQLSGGEQQMLSIA 147
Cdd:PRK13651 101 keiRRRVGVVFQFAEYQLF-EQTIEKDIIFGPV--SMGVSKEEAKKRAAKYIELVGLDesylQRSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 148 RTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDTK 227
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNK 257
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
116-235 |
3.36e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 70.53 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 116 DKIWETFPiLVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNM 195
Cdd:NF000106 126 DELLERFS-LTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYM 204
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1347602354 196 HFCMEVAKEAIIIDKGKAVWTGSLDDLQkdTKTRDKYLAI 235
Cdd:NF000106 205 EEAEQLAHELTVIDRGRVIADGKVDELK--TKVGGRTLQI 242
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-183 |
3.52e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 69.76 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQ---VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPT-SKRA 76
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 77 LSGIGYVPEDRQvFPEHTVEENIELGKKDNSNSFDDWpIDKIWETFPI--LVKLKNRLAGQLSGGEQQMLSIARTLVGNP 154
Cdd:PRK13650 82 KIGMVFQNPDNQ-FVGATVEDDVAFGLENKGIPHEEM-KERVNEALELvgMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180
....*....|....*....|....*....
gi 1347602354 155 EILLLDEPSEGLAPIIVEDIVKILENLKK 183
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRD 188
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-212 |
4.83e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 69.66 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 2 NLLETKSMNAFYGN--SQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPT-SKRALS 78
Cdd:PRK13635 4 EIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 79 GIGYVPEDRQvFPEHTVEENIELGKKDNSNSFD------DWPIDKI-WETFpilvklKNRLAGQLSGGEQQMLSIARTLV 151
Cdd:PRK13635 84 GMVFQNPDNQ-FVGATVQDDVAFGLENIGVPREemvervDQALRQVgMEDF------LNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 152 GNPEILLLDEPSEGLAPIIVEDIVKILENLK-KLGVTILlaeQNMHFCMEVAK--EAIIIDKGK 212
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKeQKGITVL---SITHDLDEAAQadRVIVMNKGE 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-217 |
6.50e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 68.33 E-value: 6.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 10 NAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGeelikKPTSKRALsGIGYVpedrqv 89
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-----RVSSLLGL-GGGFN------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 90 fPEHTVEENIELGK--KDNSNSFDDWPIDKIWEtFP-----ILVKLKNRLAGQLSggeQQMLSIARTLvgNPEILLLDep 162
Cdd:cd03220 97 -PELTGRENIYLNGrlLGLSRKEIDEKIDEIIE-FSelgdfIDLPVKTYSSGMKA---RLAFAIATAL--EPDILLID-- 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347602354 163 sEGLApiiVEDI------VKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTG 217
Cdd:cd03220 168 -EVLA---VGDAafqekcQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-166 |
6.62e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.26 E-value: 6.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 23 SLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKsGSIKLKGEEL--IKKPTSKRALSGIGYVPEdrqvFPEHTVEENIE 100
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELreLDPESWRKHLSWVGQNPQ----LPHGTLRDNVL 444
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 101 LGKKDNSNSFDDWPIDK--IWEtfpILVKLKNRL-------AGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGL 166
Cdd:PRK11174 445 LGNPDASDEQLQQALENawVSE---FLPLLPQGLdtpigdqAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-190 |
6.64e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 6.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIK-VKSGSIKLKGEELIKKPTSKRALSGIGYVPEDRQ---VFPEHTVE 96
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKrdgIVPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 97 ENIELGKKDNSNSFDdwPIDKIWETFPI---LVKLKNRLA------GQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLA 167
Cdd:PRK13549 360 KNITLAALDRFTGGS--RIDDAAELKTIlesIQRLKVKTAspelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180
....*....|....*....|...
gi 1347602354 168 PIIVEDIVKILENLKKLGVTILL 190
Cdd:PRK13549 438 VGAKYEIYKLINQLVQQGVAIIV 460
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-161 |
1.42e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 69.36 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 11 AFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELikKPTSKRAL-SGIGYVPEDRQV 89
Cdd:PRK10790 349 AYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL--SSLSHSVLrQGVAMVQQDPVV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 90 FPEhTVEENIELGKkdnsnsfdDWPIDKIWETFPI-----LVK-----LKNRLAGQ---LSGGEQQMLSIARTLVGNPEI 156
Cdd:PRK10790 427 LAD-TFLANVTLGR--------DISEEQVWQALETvqlaeLARslpdgLYTPLGEQgnnLSVGQKQLLALARVLVQTPQI 497
|
....*
gi 1347602354 157 LLLDE 161
Cdd:PRK10790 498 LILDE 502
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-222 |
1.49e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.31 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 16 SQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIK---VKSGSIKLKGEELIKKPTSKRAlsgiGYVPEDRQVFPE 92
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDAKEMRAIS----AYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 HTVEENIELG-----KKDNSNSFDDWPIDKIWETFPiLVKLKNRLAGQ------LSGGEQQMLSIARTLVGNPEILLLDE 161
Cdd:TIGR00955 114 LTVREHLMFQahlrmPRRVTKKEKRERVDEVLQALG-LRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 162 PSEGLAPIIVEDIVKILENLKKLGVTILLA-EQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-218 |
1.59e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.09 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRALSGIGYVPEDRQVFPE 92
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEH-IQHYASKEVARRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 HTVEENIELGKKDNSNSFDDW------PIDKIWETFPIlVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGL 166
Cdd:PRK10253 96 ITVQELVARGRYPHQPLFTRWrkedeeAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1347602354 167 APIIVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGS 218
Cdd:PRK10253 175 DISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-212 |
1.70e-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: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVK-SGSIKLKGEELIKKPTSKRALSGIGYVPEDRQ---VFPEHTVE 96
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 97 ENIELGKKDNSNSFDDwpIDKIWETFPILV---KLKNRLA------GQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLA 167
Cdd:TIGR02633 358 KNITLSVLKSFCFKMR--IDAAAELQIIGSaiqRLKVKTAspflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1347602354 168 PIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGK 212
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-189 |
1.72e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.20 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 22 MSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPT-SKRALSGIGYVPEDRQvFPEHTVEENIE 100
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVFQNPDNQ-FVGATVEDDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 101 LGKKDNSNSFDDWpIDKIWETFPI--LVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKIL 178
Cdd:PRK13642 105 FGMENQGIPREEM-IKRVDEALLAvnMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVI 183
|
170
....*....|..
gi 1347602354 179 ENLK-KLGVTIL 189
Cdd:PRK13642 184 HEIKeKYQLTVL 195
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-189 |
2.04e-13 |
|
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: 65.64 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKlkgeelikKPTSKRALsgigYVPEdRQVFPEHTVEE 97
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG--------MPEGEDLL----FLPQ-RPYLPLGTLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIELgkkdnsnsfddwPIDKIwetfpilvklknrlagqLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPiIVEDivKI 177
Cdd:cd03223 83 QLIY------------PWDDV-----------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE-ESED--RL 130
|
170
....*....|..
gi 1347602354 178 LENLKKLGVTIL 189
Cdd:cd03223 131 YQLLKELGITVI 142
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-190 |
2.05e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.15 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 16 SQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRAL---SGIGYVPEDRQVFPE 92
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 HTVEENIEL----GKKDNSNSfddwpIDKIWETFPI--LVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGL 166
Cdd:PRK11629 102 FTALENVAMplliGKKKPAEI-----NSRALEMLAAvgLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180
....*....|....*....|....
gi 1347602354 167 APIIVEDIVKILENLKKLGVTILL 190
Cdd:PRK11629 177 DARNADSIFQLLGELNRLQGTAFL 200
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-166 |
2.18e-13 |
|
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: 66.36 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEEL-IKKPTSKRALSGIGY 82
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 83 VPEDRQVFpehTVEENIELGKKDNSNsfddwpiDKIWETFPI--LVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLD 160
Cdd:cd03231 81 APGIKTTL---SVLENLRFWHADHSD-------EQVEEALARvgLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
....*.
gi 1347602354 161 EPSEGL 166
Cdd:cd03231 151 EPTTAL 156
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-163 |
2.23e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.61 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNsQVLFD-MSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLkGEelikkpTSKralsgIGYVPEDRQVF- 90
Cdd:PRK11819 334 FGD-RLLIDdLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE------TVK-----LAYVDQSRDALd 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 PEHTVEENI-------ELGKKD-NSNSF---------DdwpidkiwetfpilvklKNRLAGQLSGGEQQMLSIARTLV-- 151
Cdd:PRK11819 401 PNKTVWEEIsggldiiKVGNREiPSRAYvgrfnfkggD-----------------QQKKVGVLSGGERNRLHLAKTLKqg 463
|
170
....*....|..
gi 1347602354 152 GNpeILLLDEPS 163
Cdd:PRK11819 464 GN--VLLLDEPT 473
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-218 |
2.45e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 67.42 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKG--EELIKKPTSKRALSGIGYVPEDRQVFPEhTV 95
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldTSDEENLWDIRNKAGMVFQNPDNQIVAT-IV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 96 EENIELG------KKDNSNSFDDWPIDKI--WEtfpilvkLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLA 167
Cdd:PRK13633 104 EEDVAFGpenlgiPPEEIRERVDESLKKVgmYE-------YRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 168 PIIVEDIVKILENL-KKLGVTILLAeqnMHFcMEVAKEA---IIIDKGKAVWTGS 218
Cdd:PRK13633 177 PSGRREVVNTIKELnKKYGITIILI---THY-MEEAVEAdriIVMDSGKVVMEGT 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-226 |
3.96e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.21 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 15 NSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELiKKPTSKRALSGIGYVPEDRQVFpEHT 94
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL-VQYDHHYLHRQVALVGQEPVLF-SGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 95 VEENIELGKKDNSN---------SFDDWPIDKIWETFPILVKLKnrlAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEG 165
Cdd:TIGR00958 571 VRENIAYGLTDTPDeeimaaakaANAHDFIMEFPNGYDTEVGEK---GSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347602354 166 LaPIIVEDIVKILENLKklGVTILLAEQNMHFCmEVAKEAIIIDKGKAVWTGSLDDLQKDT 226
Cdd:TIGR00958 648 L-DAECEQLLQESRSRA--SRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-212 |
4.68e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.62 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIkLKGeeliKKPTSKrALSGIGYVPEDRQVFPE 92
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPLAE-AREDTRLMFQDARLLPW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 HTVEENIELGKKDN--------------SNSFDDWPidkiwetfpilvklknrlaGQLSGGEQQMLSIARTLVGNPEILL 158
Cdd:PRK11247 96 KKVIDNVGLGLKGQwrdaalqalaavglADRANEWP-------------------AALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 159 LDEPSEGLAPIIVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGK 212
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-222 |
6.10e-13 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 67.43 E-value: 6.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELikKPTSKRAL-SGIGYVPEDRQVFpEHTVE 96
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL--ADYTLASLrRQVALVSQDVVLF-NDTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 97 ENIELGKKD--------------NSNSFddwpIDKIWE--TFPILVKlknrlAGQLSGGEQQMLSIARTLVGNPEILLLD 160
Cdd:TIGR02203 424 NNIAYGRTEqadraeieralaaaYAQDF----VDKLPLglDTPIGEN-----GVLLSGGQRQRLAIARALLKDAPILILD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 161 EPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMhfCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:TIGR02203 495 EATSALDNESERLVQAALERLMQGRTTLVIAHRLS--TIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-196 |
8.48e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.21 E-value: 8.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 31 IIALLGRNGAGKSSTFKAITGLIKVKSgsikLKGEELI--KKPTsKRALSGIGYVPEDRQVFPEHTVEENI------ELG 102
Cdd:PLN03211 96 ILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILAnnRKPT-KQILKRTGFVTQDDILYPHLTVRETLvfcsllRLP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 103 K---KDNSNSFDDWPIDKIWetfpiLVKLKNRLAGQ-----LSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDI 174
Cdd:PLN03211 171 KsltKQEKILVAESVISELG-----LTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180
....*....|....*....|..
gi 1347602354 175 VKILENLKKLGVTILlaeQNMH 196
Cdd:PLN03211 246 VLTLGSLAQKGKTIV---TSMH 264
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-189 |
1.24e-12 |
|
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: 64.30 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIK-KPTSKRALSGIGY 82
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEqRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 83 VPedrQVFPEHTVEENIE-----LGKKDNSnsfddwpidkIWETFPI--LVKLKNRLAGQLSGGEQQMLSIARTLVGNPE 155
Cdd:TIGR01189 81 LP---GLKPELSALENLHfwaaiHGGAQRT----------IEDALAAvgLTGFEDLPAAQLSAGQQRRLALARLWLSRRP 147
|
170 180 190
....*....|....*....|....*....|....*
gi 1347602354 156 ILLLDEPSEGLAPIIVEDIVKILE-NLKKLGVTIL 189
Cdd:TIGR01189 148 LWILDEPTTALDKAGVALLAGLLRaHLARGGIVLL 182
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
14-161 |
1.88e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 66.00 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 14 GNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIK-KPTSKRAlsGIGYVPEDRQVFPE 92
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASLRA--AIGIVPQDTVLFND 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 hTVEENIELGKKDNSN----------SFDDWpIDKI---WETfpiLVK---LKnrlagqLSGGEQQMLSIARTLVGNPEI 156
Cdd:COG5265 447 -TIAYNIAYGRPDASEeeveaaaraaQIHDF-IESLpdgYDT---RVGergLK------LSGGEKQRVAIARTLLKNPPI 515
|
....*
gi 1347602354 157 LLLDE 161
Cdd:COG5265 516 LIFDE 520
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-169 |
1.91e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.30 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKP--TSKRalsgIGYVpedRQVFP---EHTV 95
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDiaTRRR----VGYM---SQAFSlygELTV 356
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347602354 96 EENIELGKKDNSNSFDDWP--IDKIWETFPiLVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPI 169
Cdd:NF033858 357 RQNLELHARLFHLPAAEIAarVAEMLERFD-LADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-222 |
2.11e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.12 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGL-IKVK----SGSIKLKGEELIKKPTSKRALSGIGYVPEDR 87
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSgyrySGDVLLGGRSIFNYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 88 QVFPeHTVEENIELGKKDNS----NSFDDWPIDKIWETfPILVKLKNRLAG---QLSGGEQQMLSIARTLVGNPEILLLD 160
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRAHKlvprKEFRGVAQARLTEV-GLWDAVKDRLSDspfRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 161 EPSEGLAPIIVEDIVKILENLKKLgVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-218 |
2.21e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.64 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELikkPTSKRALSGIG- 81
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL---DYSKRGLLALRq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 82 -----YVPEDRQVFpeHT-VEENIELGKKdNSNSFDDWPIDKIWETFPIL--VKLKNRLAGQLSGGEQQMLSIARTLVGN 153
Cdd:PRK13638 78 qvatvFQDPEQQIF--YTdIDSDIAFSLR-NLGVPEAEITRRVDEALTLVdaQHFRHQPIQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 154 PEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGS 218
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-224 |
2.75e-12 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 64.49 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFY--GNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKsGSIKLKGEELIKKPTSKRAlSGIG 81
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWR-KAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 82 YVPEDRQVFpEHTVEENIElgkkdnsnSFDDWPIDKIW------------ETFPILVKLKNRLAGQ-LSGGEQQMLSIAR 148
Cdd:cd03289 81 VIPQKVFIF-SGTFRKNLD--------PYGKWSDEEIWkvaeevglksviEQFPGQLDFVLVDGGCvLSHGHKQLMCLAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347602354 149 TLVGNPEILLLDEPSEGLAPIIVEDIVKILENlKKLGVTILLAEQNMHFCMEvAKEAIIIDKGKaVWTgsLDDLQK 224
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENK-VRQ--YDSIQK 222
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-195 |
3.09e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIK-KPTSKRALSGIG 81
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 82 YvpeDRQVFPEHTVEENIELGKKDNSNSFDdwpIDKIWETFPiLVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDE 161
Cdd:PRK13540 81 H---RSGINPYLTLRENCLYDIHFSPGAVG---ITELCRLFS-LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|....*
gi 1347602354 162 PSEGLAPIIVEDIV-KILENLKKLGVTILLAEQNM 195
Cdd:PRK13540 154 PLVALDELSLLTIItKIQEHRAKGGAVLLTSHQDL 188
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-166 |
3.87e-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: 63.64 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 15 NSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGeelikKPTS----KRALSGIGYVPEDRQVF 90
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG-----KPISqyehKYLHSKVSLVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 pEHTVEENI-------------ELGKKDNSNSFddwpIDKIWETFPILVKLKnrlAGQLSGGEQQMLSIARTLVGNPEIL 157
Cdd:cd03248 101 -ARSLQDNIayglqscsfecvkEAAQKAHAHSF----ISELASGYDTEVGEK---GSQLSGGQKQRVAIARALIRNPQVL 172
|
....*....
gi 1347602354 158 LLDEPSEGL 166
Cdd:cd03248 173 ILDEATSAL 181
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-218 |
1.50e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 62.34 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLI---KVKSGSIKLKGEELIKKPTSKRAL-- 77
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGRLARDIrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 78 --SGIGYVPEDRQVFPEHTVEENIELGKKDNSnsfddwpidKIWET-FPILVKLKNRLAGQ-----------------LS 137
Cdd:PRK09984 84 srANTGYIFQQFNLVNRLSVLENVLIGALGST---------PFWRTcFSWFTREQKQRALQaltrvgmvhfahqrvstLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 138 GGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKL-GVTILLAEQNMHFCMEVAKEAIIIDKGKAVWT 216
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
|
..
gi 1347602354 217 GS 218
Cdd:PRK09984 235 GS 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-222 |
2.30e-11 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 62.78 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNS----QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGL----IKVKSGSIKLKGEELIKKPT 72
Cdd:COG4172 4 MPLLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 73 SK-RALSG--IGYvpedrqVFPE--------HTVEENI-E-------LGKKDNSnsfddwpiDKIWETFpILVKLKN--- 130
Cdd:COG4172 84 RElRRIRGnrIAM------IFQEpmtslnplHTIGKQIaEvlrlhrgLSGAAAR--------ARALELL-ERVGIPDper 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 131 RLAG---QLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKK-LGVTILLAEQNMHFCMEVAKEAI 206
Cdd:COG4172 149 RLDAyphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQReLGMALLLITHDLGVVRRFADRVA 228
|
250
....*....|....*.
gi 1347602354 207 IIDKGKAVWTGSLDDL 222
Cdd:COG4172 229 VMRQGEIVEQGPTAEL 244
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-227 |
2.99e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 61.69 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIkLKGEELIKKPTSKRALSGIGYV---PEDRqvFPEHTV 95
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAITDDNFEKLRKHIGIVfqnPDNQ--FVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 96 EENIELGKKDNSnsfddWPIDKIWETFPILVKLKNRLA------GQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPI 169
Cdd:PRK13648 102 KYDVAFGLENHA-----VPYDEMHRRVSEALKQVDMLEradyepNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1347602354 170 IVEDIVKILENLK-KLGVTILLAEQNMHFCMEvAKEAIIIDKGKAVWTGSLDDLQKDTK 227
Cdd:PRK13648 177 ARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-217 |
4.47e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.87 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 8 SMN----AFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGsiklkgeELIKKPTSKralsgIGYV 83
Cdd:TIGR03719 6 TMNrvskVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-------EARPQPGIK-----VGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENIELG---KKDNSNSFDDW------PIDKIWETFPILVKLKNRLAGQ------------------- 135
Cdd:TIGR03719 74 PQEPQLDPTKTVRENVEEGvaeIKDALDRFNEIsakyaePDADFDKLAAEQAELQEIIDAAdawdldsqleiamdalrcp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 136 --------LSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPiiveDIVKILEN-LKKLGVTILLAEQNMHFCMEVAKEAI 206
Cdd:TIGR03719 154 pwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVAWLERhLQEYPGTVVAVTHDRYFLDNVAGWIL 229
|
250
....*....|..
gi 1347602354 207 IIDKGKAV-WTG 217
Cdd:TIGR03719 230 ELDRGRGIpWEG 241
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-189 |
5.90e-11 |
|
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: 59.56 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 14 GNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTF-----KAITGLIKvksGSIKLKGEELikKPTSKRalsGIGYVPEDRQ 88
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLdvlagRKTAGVIT---GEILINGRPL--DKNFQR---STGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 89 VFPEHTVEENIELGKKdnsnsfddwpidkiwetfpilvklknrLAGqLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAP 168
Cdd:cd03232 90 HSPNLTVREALRFSAL---------------------------LRG-LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180
....*....|....*....|.
gi 1347602354 169 IIVEDIVKILENLKKLGVTIL 189
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQAIL 162
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-168 |
6.93e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.68 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRALSG-IGYVPED--RQV 89
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGD-MADARHRRAVCPrIAYMPQGlgKNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 90 FPEHTVEENIE-------LGKKDNsnsfdDWPIDKIWET-----FPilvklkNRLAGQLSGGEQQMLSIARTLVGNPEIL 157
Cdd:NF033858 90 YPTLSVFENLDffgrlfgQDAAER-----RRRIDELLRAtglapFA------DRPAGKLSGGMKQKLGLCCALIHDPDLL 158
|
170
....*....|.
gi 1347602354 158 LLDEPSEGLAP 168
Cdd:NF033858 159 ILDEPTTGVDP 169
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-222 |
8.27e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 61.19 E-value: 8.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIK-KPTSKRalSGIGYVPEDRQVFPEhTVEE 97
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLR--NQVALVSQNVHLFND-TIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIELGKKDNSNSFDDWPIDKIWETFPILVKLKNRL---AGQ----LSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPII 170
Cdd:PRK11176 436 NIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLdtvIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 171 VEDIVKILENLKKLGVTILLAeqnmH--FCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:PRK11176 516 ERAIQAALDELQKNRTSLVIA----HrlSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-222 |
8.54e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 60.82 E-value: 8.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSK-RAL--SGIGYVPEDRQVFPEHTVEE 97
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElREVrrKKIAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIELGKK---DNSNSFDDWPIDKIWEtfpilVKLKNRLAG---QLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIV 171
Cdd:PRK10070 126 NTAFGMElagINAEERREKALDALRQ-----VGLENYAHSypdELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 172 EDIVKILENLK-KLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:PRK10070 201 TEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-189 |
1.01e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 60.52 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSK-RALsgigyvpedRQ----VF----- 90
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElRPL---------RRrmqmVFqdpya 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 ---PEHTVEENIELGKKDNSNSFDDWPIDKIWETFPiLVKLK----NRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPS 163
Cdd:COG4608 107 slnPRMTVGDIIAEPLRIHGLASKAERRERVAELLE-LVGLRpehaDRYPHEFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
170 180 190
....*....|....*....|....*....|...
gi 1347602354 164 EGLapiiveD------IVKILENLKK-LGVTIL 189
Cdd:COG4608 186 SAL------DvsiqaqVLNLLEDLQDeLGLTYL 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-226 |
1.10e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.20 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 2 NLLETKSMNAFYGNSQ--VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLI---KVKSGSIKLKGEELIKKPT-SKR 75
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVwDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 76 ALSGIGYVPEDRQvFPEHTVEENIELGKKDNSNSFDDWP--IDKIWETFPILVKLKNRLAgQLSGGEQQMLSIARTLVGN 153
Cdd:PRK13640 84 EKVGIVFQNPDNQ-FVGATVGDDVAFGLENRAVPRPEMIkiVRDVLADVGMLDYIDSEPA-NLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347602354 154 PEILLLDEPSEGLAPIIVEDIVKILENLKK------LGVTILLAEQNMhfcmevAKEAIIIDKGKAVWTGSLDDLQKDT 226
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKknnltvISITHDIDEANM------ADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-214 |
1.27e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.49 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 17 QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVK-----SGSIKLKGEELIKKPTSK-RALSG--IGYVPEDRQ 88
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTlRGVRGnkIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 89 VF--PEHTVEENI------------ELGKKDNSNSFDDWPIDKIwetfpilvklKNRLAG---QLSGGEQQMLSIARTLV 151
Cdd:PRK15134 103 VSlnPLHTLEKQLyevlslhrgmrrEAARGEILNCLDRVGIRQA----------AKRLTDyphQLSGGERQRVMIAMALL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 152 GNPEILLLDEPSEGLAPIIVEDIVKILENLKK-LGVTILLAEQNMHFCMEVAKEAIIIDKGKAV 214
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQeLNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-222 |
1.37e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 60.59 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSStfkaitgLIKVKSGsikLKGEElikkPTSKRALSGIGYV 83
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSV-------LMHVLRG---MDQYE----PTSGRIIYHVALC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 PEDRQVFPEHTVEENIEL-GKKDNSNSFDDWPIDK-------------IWETFPI------------------------- 124
Cdd:TIGR03269 67 EKCGYVERPSKVGEPCPVcGGTLEPEEVDFWNLSDklrrrirkriaimLQRTFALygddtvldnvlealeeigyegkeav 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 125 --------LVKLKNR---LAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVK-ILENLKKLGVTILLAE 192
Cdd:TIGR03269 147 gravdlieMVQLSHRithIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTS 226
|
250 260 270
....*....|....*....|....*....|
gi 1347602354 193 QNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:TIGR03269 227 HWPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-191 |
4.89e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 57.93 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKvKSGSIKLKGEELikKPTSKRALSGI-GYVPEDRQ------VF- 90
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPL--SDWSAAELARHrAYLSQQQSppfampVFq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 ------PEHTVEENIELgkkdnsnsfddwPIDKIWETFPILVKLkNRLAGQLSGGEQQMLSIARTLV-----GNPE--IL 157
Cdd:COG4138 89 ylalhqPAGASSEAVEQ------------LLAQLAEALGLEDKL-SRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1347602354 158 LLDEPSEGLapiiveDIV------KILENLKKLGVTILLA 191
Cdd:COG4138 156 LLDEPMNSL------DVAqqaaldRLLRELCQQGITVVMS 189
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-200 |
5.12e-10 |
|
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: 59.15 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 14 GNSqVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKsGSIKLKGEELiKKPTSKRALSGIGYVPEDRQVFpEH 93
Cdd:TIGR01271 1231 GRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSW-NSVTLQTWRKAFGVIPQKVFIF-SG 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 94 TVEENIElgkkdnsnSFDDWPIDKIW------------ETFPilVKLKNRLAGQ---LSGGEQQMLSIARTLVGNPEILL 158
Cdd:TIGR01271 1307 TFRKNLD--------PYEQWSDEEIWkvaeevglksviEQFP--DKLDFVLVDGgyvLSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1347602354 159 LDEPSEGLAPIIVEDIVKILENLKKlGVTILLAEQNMHFCME 200
Cdd:TIGR01271 1377 LDEPSAHLDPVTLQIIRKTLKQSFS-NCTVILSEHRVEALLE 1417
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-163 |
5.42e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 57.80 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 26 IKKNNIIALLGRNGAGKSsTFkaitglIKVKSGSIKLKGEELIKkptskrALSGIGYVPEDRQVFPEHTVEEniELGKKD 105
Cdd:cd03237 22 ISESEVIGILGPNGIGKT-TF------IKMLAGVLKPDEGDIEI------ELDTVSYKPQYIKADYEGTVRD--LLSSIT 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 106 nsnsfDDWPIDKIWETFPI----LVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPS 163
Cdd:cd03237 87 -----KDFYTHPYFKTEIAkplqIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-225 |
9.21e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 9.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITG-LIKVKSGSIKLKGEelikkptskralsgIGYVPEDRQVFpEHTVEE 97
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS--------------VAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIELGKKDNSNSF----DDWPIDKIWETFP--ILVKLKNRlAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIV 171
Cdd:PLN03232 698 NILFGSDFESERYwraiDVTALQHDLDLLPgrDLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVA 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1347602354 172 EDIVK--ILENLKklGVTILLAEQNMHFCMEVAKeAIIIDKGKAVWTGSLDDLQKD 225
Cdd:PLN03232 777 HQVFDscMKDELK--GKTRVLVTNQLHFLPLMDR-IILVSEGMIKEEGTFAELSKS 829
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-222 |
1.23e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 57.22 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLE----TKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIK----VKSGSIKLKGEELIK-KP 71
Cdd:COG4170 1 MPLLDirnlTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKlSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 72 TSKRALSG--IGYVPEDRQVF--PEHTVEENIE--LGKKDNSNSFDDWPIDKIWETFPIL--VKLK------NRLAGQLS 137
Cdd:COG4170 81 RERRKIIGreIAMIFQEPSSCldPSAKIGDQLIeaIPSWTFKGKWWQRFKWRKKRAIELLhrVGIKdhkdimNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 138 GGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKL-GVTILLAEQNMHFCMEVAKEAIIIDKGKAVWT 216
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLqGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
....*.
gi 1347602354 217 GSLDDL 222
Cdd:COG4170 241 GPTEQI 246
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-190 |
1.28e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.81 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFY----GNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKkpTSKRALS 78
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAT--LDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 79 GI-----GYVPEDRQVFPEHTVEENIE-------LGKKdnsnsfddwpidkiwETFPILVKLKNRLA---------GQLS 137
Cdd:PRK10535 82 QLrrehfGFIFQRYHLLSHLTAAQNVEvpavyagLERK---------------QRLLRAQELLQRLGledrveyqpSQLS 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1347602354 138 GGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILL 190
Cdd:PRK10535 147 GGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII 199
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-162 |
1.66e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.58 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFD-MSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTS-KRALSGIGYVPedrQVFPEHTV 95
Cdd:PRK13538 15 ILFSgLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyHQDLLYLGHQP---GIKTELTA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 96 EENIELGKKDnSNSFDDwpiDKIWEtfpIL--VKLKNR---LAGQLSGGEQQMLSIARTLVGNPEILLLDEP 162
Cdd:PRK13538 92 LENLRFYQRL-HGPGDD---EALWE---ALaqVGLAGFedvPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-222 |
3.02e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.90 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 1 MNLLETKSMNAFYGNSQVLFD----MSLKIKKNNIIALLGRNGAGKSSTFKAITGLI----KVKSGSIKLKGEELIK-KP 71
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRavdrISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRiSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 72 TSKRALSG--IGYVPED--RQVFPEHTVE----ENIELGKKDNSNSFDDWPIDkiwetfpiLVKL------KNRL---AG 134
Cdd:PRK11022 81 KERRNLVGaeVAMIFQDpmTSLNPCYTVGfqimEAIKVHQGGNKKTRRQRAID--------LLNQvgipdpASRLdvyPH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 135 QLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKA 213
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
....*....
gi 1347602354 214 VWTGSLDDL 222
Cdd:PRK11022 233 VETGKAHDI 241
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-166 |
3.60e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.28 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFygNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGIGY 82
Cdd:PRK10982 250 ILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 83 VPEDRQ---VFPEHTVEEN----------IELGKKDNSNSFDD--WPIDKIWETFPIlvklKNRLAGQLSGGEQQMLSIA 147
Cdd:PRK10982 328 VTEERRstgIYAYLDIGFNslisnirnykNKVGLLDNSRMKSDtqWVIDSMRVKTPG----HRTQIGSLSGGNQQKVIIG 403
|
170
....*....|....*....
gi 1347602354 148 RTLVGNPEILLLDEPSEGL 166
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGI 422
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-189 |
4.25e-09 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 54.75 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 17 QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLK-GEELIKKPT-SKRAL-----SGIGYVPEDRQV 89
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhDGGWVDLAQaSPREIlalrrRTIGYVSQFLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 90 FP-----EHTVEENIELGKkDNSNSFD---DW------PiDKIWETFPilvklknrlaGQLSGGEQQMLSIARTLVGNPE 155
Cdd:COG4778 105 IPrvsalDVVAEPLLERGV-DREEARArarELlarlnlP-ERLWDLPP----------ATFSGGEQQRVNIARGFIADPP 172
|
170 180 190
....*....|....*....|....*....|....
gi 1347602354 156 ILLLDEPSEGLAPIIVEDIVKILENLKKLGVTIL 189
Cdd:COG4778 173 LLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-220 |
5.09e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 2 NLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITG--LIKVKSGSIKLKGEELIKKPTSKRALSG 79
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 80 I----GYVPEdrqvFPEHTVEENIELGKKDNSNSFDDWPIDKIwETFPI------LVKLKNRLAGQ-----LSGGEQQML 144
Cdd:CHL00131 86 IflafQYPIE----IPGVSNADFLRLAYNSKRKFQGLPELDPL-EFLEIineklkLVGMDPSFLSRnvnegFSGGEKKRN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347602354 145 SIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAI-IIDKGKAVWTGSLD 220
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVhVMQNGKIIKTGDAE 237
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-223 |
5.88e-09 |
|
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: 56.07 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEelikkptskralsgIGYVPEDRQVFPeHTVEE 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMP-GTIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIELGKkdnsnSFDDWPID------KIWETFPILVKLKNRLAGQ----LSGGEQQMLSIARTLVGNPEILLLDEPSEGLA 167
Cdd:TIGR01271 506 NIIFGL-----SYDEYRYTsvikacQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347602354 168 PIIVEDI-----VKILENLKKLGVTILLAEqnmhfcMEVAKEAIIIDKGKAVWTGSLDDLQ 223
Cdd:TIGR01271 581 VVTEKEIfesclCKLMSNKTRILVTSKLEH------LKKADKILLLHEGVCYFYGTFSELQ 635
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-231 |
6.35e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSStfkaitgLIKVKS---------GSIKLKGEELIKKPTS 73
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKST-------LMKVLSgvyphgsyeGEILFDGEVCRFKDIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 74 KRALSGIGYVPEDRQVFPEHTVEENIELGKKDNSNSFDDWPidkiwETFPILVKLKNR---------LAGQLSGGEQQML 144
Cdd:NF040905 74 DSEALGIVIIHQELALIPYLSIAENIFLGNERAKRGVIDWN-----ETNRRARELLAKvgldespdtLVTDIGVGKQQLV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 145 SIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTgslDDLQK 224
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIET---LDCRA 225
|
....*..
gi 1347602354 225 DTKTRDK 231
Cdd:NF040905 226 DEVTEDR 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-163 |
7.36e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.18 E-value: 7.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 25 KIKKNNIIALLGRNGAGKSsTF-KAITGLIKVKSGSIKLKgeelIK---KPTskralsgigYVPEDRqvfpEHTVEENIE 100
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKT-TFaKILAGVLKPDEGEVDED----LKisyKPQ---------YISPDY----DGTVEEFLR 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347602354 101 lgkKDNSNSFDDwpidKIWET---FPI-LVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPS 163
Cdd:COG1245 424 ---SANTDDFGS----SYYKTeiiKPLgLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
32-217 |
7.61e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.25 E-value: 7.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 32 IALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSK-RALS-GIGYVPED--RQVFPEHTVEENI-------E 100
Cdd:PRK10261 353 LSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlQALRrDIQFIFQDpyASLDPRQTVGDSImeplrvhG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 101 LGKKDNSNSFDDWPIDKIwetfPILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILEN 180
Cdd:PRK10261 433 LLPGKAAAARVAWLLERV----GLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLD 508
|
170 180 190
....*....|....*....|....*....|....*...
gi 1347602354 181 LKK-LGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTG 217
Cdd:PRK10261 509 LQRdFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-163 |
8.70e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 8.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 26 IKKNNIIALLGRNGAGKSsTF-KAITGLIKVKSGSIKLKgeelIKkptskralsgIGYVPEDRQVFPEHTVEENIELGKK 104
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKT-TFaKLLAGVLKPDEGEVDPE----LK----------ISYKPQYIKPDYDGTVEDLLRSITD 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347602354 105 DNSNSFddwpidkiWET---FPI-LVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPS 163
Cdd:PRK13409 427 DLGSSY--------YKSeiiKPLqLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-162 |
9.68e-09 |
|
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: 55.08 E-value: 9.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKvKSGSIKLKGEELIKKPTSK-RALsgigyvpedRQ----VF----- 90
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlRPL---------RRrmqvVFqdpfg 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 ---PEHTVEE---------NIELGKKDNSnsfddwpiDKIWEtfpIL--VKLK----NRLAGQLSGGEQQMLSIARTLVG 152
Cdd:COG4172 374 slsPRMTVGQiiaeglrvhGPGLSAAERR--------ARVAE---ALeeVGLDpaarHRYPHEFSGGQRQRIAIARALIL 442
|
170
....*....|
gi 1347602354 153 NPEILLLDEP 162
Cdd:COG4172 443 EPKLLVLDEP 452
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-227 |
1.09e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 54.33 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKR--ALSGIGYVPED--RQVFPEHTVE 96
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWraVRSDIQMIFQDplASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 97 ENI---------ELGKKDNSnsfddwpiDKIWETFP---ILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSE 164
Cdd:PRK15079 119 EIIaeplrtyhpKLSRQEVK--------DRVKAMMLkvgLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 165 GLAPIIVEDIVKILENLKK-LGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDLQKDTK 227
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQReMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-162 |
1.29e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 8 SMN----AFYGNSQVLFDMSL------KIkknniiALLGRNGAGKSSTFKAITGLIKVKSGsiklkgeELIKKPTSKral 77
Cdd:PRK11819 8 TMNrvskVVPPKKQILKDISLsffpgaKI------GVLGLNGAGKSTLLRIMAGVDKEFEG-------EARPAPGIK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 78 sgIGYVPEDRQVFPEHTVEENIELG---KKDNSNSFDD------WPIDKIWETFPILVKLKNRLA--------------- 133
Cdd:PRK11819 72 --VGYLPQEPQLDPEKTVRENVEEGvaeVKAALDRFNEiyaayaEPDADFDALAAEQGELQEIIDaadawdldsqleiam 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1347602354 134 ------------GQLSGGEQQMLSIARTLVGNPEILLLDEP 162
Cdd:PRK11819 150 dalrcppwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-220 |
1.32e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGE----ELIKKPTSKRALSGIGYVPEDRQ 88
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivaRLQQDPPRNVEGTVYDFVAEGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 89 VFPEH--------------TVEENI-ELGKK----DNSNSfddWPID-KIWETfpiLVKLK---NRLAGQLSGGEQQMLS 145
Cdd:PRK11147 93 EQAEYlkryhdishlvetdPSEKNLnELAKLqeqlDHHNL---WQLEnRINEV---LAQLGldpDAALSSLSGGWLRKAA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347602354 146 IARTLVGNPEILLLDEPSEGLapiiveDIVKI--LEN-LKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAV-WTGSLD 220
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHL------DIETIewLEGfLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVsYPGNYD 239
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-221 |
1.96e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.01 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 23 SLKIKKNNIIALLGRNGAGKSSTFKAITGLIkVKSGSIKLKGEELIKKPTSKRALSGIGYVPEDRQVFPEHtVEENIELG 102
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMP-VFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 103 KKDNSNSFDDWP-IDKIWETFPILVKLkNRLAGQLSGGEQQ-------MLSIARTLvgNPE--ILLLDEPSEGLapiive 172
Cdd:PRK03695 94 QPDKTRTEAVASaLNEVAEALGLDDKL-GRSVNQLSGGEWQrvrlaavVLQVWPDI--NPAgqLLLLDEPMNSL------ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 173 DIV------KILENLKKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDD 221
Cdd:PRK03695 165 DVAqqaaldRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-195 |
2.11e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.25 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELiKKPTSKRALSGIGYVPEDRQVFPEHTVEE 97
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL-ESWSSKAFARKVAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIELGKKDNSNSFDDWPI---DKIWETFPiLVKLK---NRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGL---AP 168
Cdd:PRK10575 105 LVAIGRYPWHGALGRFGAadrEKVEEAIS-LVGLKplaHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALdiaHQ 183
|
170 180
....*....|....*....|....*..
gi 1347602354 169 IIVEDIVKILENLKKLGVTILLAEQNM 195
Cdd:PRK10575 184 VDVLALVHRLSQERGLTVIAVLHDINM 210
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-162 |
2.85e-08 |
|
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: 53.80 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEelikkptskralsgIGYVPEDRQVfPEHTVEEN 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQQAWI-QNDSLREN 718
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 99 IELGKKDNSNSFDdwpidKIWETFPILVKLKNRLAG----------QLSGGEQQMLSIARTLVGNPEILLLDEP 162
Cdd:TIGR00957 719 ILFGKALNEKYYQ-----QVLEACALLPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-166 |
3.50e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.52 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVK--------SGSIKLKGEELIKKPTSKRALSGIGYVPEDRQV 89
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 90 FPeHTVEENIELG-----KKDNSNSFDDWPIdkIWETFPI--LVKLKNRLAGQLSGGEQQMLSIARTL---------VGN 153
Cdd:PRK13547 96 FA-FSAREIVLLGryphaRRAGALTHRDGEI--AWQALALagATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172
|
170
....*....|...
gi 1347602354 154 PEILLLDEPSEGL 166
Cdd:PRK13547 173 PRYLLLDEPTAAL 185
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
130-212 |
3.54e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.55 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 130 NRLAGQLSGGEQQMLSIARTLVGNPE--ILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMHFcMEVAKEaiI 207
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDV-LSSADW--I 158
|
....*
gi 1347602354 208 IDKGK 212
Cdd:cd03238 159 IDFGP 163
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
36-166 |
4.05e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 53.27 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 36 GRNGAGKSSTFKAITGLIKVKSGSIKL-KGEELI---KKP-----TSKRALSgigYvPEDRQVFPEHTVEENIE---LGK 103
Cdd:COG4178 396 GPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLflpQRPylplgTLREALL---Y-PATAEAFSDAELREALEavgLGH 471
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 104 -KDNSNSFDDWpiDKIwetfpilvklknrlagqLSGGEQQMLSIARTLVGNPEILLLDEPSEGL 166
Cdd:COG4178 472 lAERLDEEADW--DQV-----------------LSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-197 |
9.81e-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: 50.79 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSI----KLKGEELIKKPTSKRALSgIGYVPEDRQVFpEHT 94
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYS-VAYAAQKPWLL-NAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 95 VEENIELGKKDNSNSF----DDWPIDKIWETFPILVKLKNRLAG-QLSGGEQQMLSIARTLVGNPEILLLDEPSEGL--- 166
Cdd:cd03290 95 VEENITFGSPFNKQRYkavtDACSLQPDIDLLPFGDQTEIGERGiNLSGGQRQRICVARALYQNTNIVFLDDPFSALdih 174
|
170 180 190
....*....|....*....|....*....|...
gi 1347602354 167 --APIIVEDIVKILENLKKlgvTILLAEQNMHF 197
Cdd:cd03290 175 lsDHLMQEGILKFLQDDKR---TLVLVTHKLQY 204
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
10-223 |
9.83e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 51.40 E-value: 9.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 10 NAFYGN-----SQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEelikkptskralsgIGYVP 84
Cdd:cd03291 39 NLFFSNlclvgAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 85 EDRQVFPeHTVEENIELGKkdnsnSFDDWPID------KIWETFPILVKLKNRLAGQ----LSGGEQQMLSIARTLVGNP 154
Cdd:cd03291 105 QFSWIMP-GTIKENIIFGV-----SYDEYRYKsvvkacQLEEDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 155 EILLLDEPSEGLAPIIVEDI-----VKILENLKKLGVTILLAEqnmhfcMEVAKEAIIIDKGKAVWTGSLDDLQ 223
Cdd:cd03291 179 DLYLLDSPFGYLDVFTEKEIfescvCKLMANKTRILVTSKMEH------LKKADKILILHEGSSYFYGTFSELQ 246
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-218 |
1.02e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.01 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 14 GNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKvKSGSIKLKGEELikKPTSKRALsgigyVPEDRQ---VF 90
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPL--HNLNRRQL-----LPVRHRiqvVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 --------PEHTVEENIELG----KKDNSNSFDDWPIDKIWETFPILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILL 158
Cdd:PRK15134 369 qdpnsslnPRLNVLQIIEEGlrvhQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347602354 159 LDEPSEGLAPIIVEDIVKILENLK-KLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGS 218
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQqKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-166 |
1.28e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKL-KGeelIKkptskralsgIG 81
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKG---IK----------LG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 82 YvpedrqvFPEHtveeNIELGKKDNSnsfddwPIDKIWETFPILV--KLKNRLAG-------------QLSGGEQQMLSI 146
Cdd:PRK10636 379 Y-------FAQH----QLEFLRADES------PLQHLARLAPQELeqKLRDYLGGfgfqgdkvteetrRFSGGEKARLVL 441
|
170 180
....*....|....*....|
gi 1347602354 147 ARTLVGNPEILLLDEPSEGL 166
Cdd:PRK10636 442 ALIVWQRPNLLLLDEPTNHL 461
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-165 |
1.35e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 17 QVLFDMSLKIKKNNIIALLGRNGAGKS----STFKAITGliKVKSGSIKLKGEElIKKPTSKRAL-SGIGYVPEDRQVFP 91
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTelamSVFGRSYG--RNISGTVFKDGKE-VDVSTVSDAIdAGLAYVTEDRKGYG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 92 ---EHTVEENIELG--KKDNSNSFddwpIDKIWETfPILVKLKNRL----------AGQLSGGEQQMLSIARTLVGNPEI 156
Cdd:NF040905 351 lnlIDDIKRNITLAnlGKVSRRGV----IDENEEI-KVAEEYRKKMniktpsvfqkVGNLSGGNQQKVVLSKWLFTDPDV 425
|
....*....
gi 1347602354 157 LLLDEPSEG 165
Cdd:NF040905 426 LILDEPTRG 434
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-222 |
1.77e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.47 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGL----IKVKSGSIKLKGEELIKKPTSKRALSGIGYVPedRQVF-PEHT- 94
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVAPCALRGRKIATIMQNP--RSAFnPLHTm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 95 ----VEENIELGKKDNSNS---------FDDwpIDKIWETFPIlvklknrlagQLSGGEQQMLSIARTLVGNPEILLLDE 161
Cdd:PRK10418 99 hthaRETCLALGKPADDATltaaleavgLEN--AARVLKLYPF----------EMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347602354 162 PSEGLAPIIVEDIVKILENL-KKLGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-222 |
2.24e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.01 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSI-------KLKGEELIKKPTSKRA---------LSGIGYVP 84
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllRRRSRQVIELSEQSAAqmrhvrgadMAMIFQEP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 85 ED--RQVFP-EHTVEENIELGK---KDNSNSFDDWPID--KIWETFPILvklkNRLAGQLSGGEQQMLSIARTLVGNPEI 156
Cdd:PRK10261 114 MTslNPVFTvGEQIAESIRLHQgasREEAMVEAKRMLDqvRIPEAQTIL----SRYPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347602354 157 LLLDEPSEGLAPIIVEDIVKILENLKK-LGVTILLAEQNMHFCMEVAKEAIIIDKGKAVWTGSLDDL 222
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKeMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-169 |
3.25e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITG-----------LIKVKSGSiklkGEEL--IKKptskralsG 79
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRGS----GETIwdIKK--------H 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 80 IGYVPE----DRQVfpeHTVEENIELgkkdnSNSFDDWPI-----DKI------WETfpiLVKLKNRLAGQ----LSGGE 140
Cdd:PRK10938 338 IGYVSSslhlDYRV---STSVRNVIL-----SGFFDSIGIyqavsDRQqklaqqWLD---ILGIDKRTADApfhsLSWGQ 406
|
170 180
....*....|....*....|....*....
gi 1347602354 141 QQMLSIARTLVGNPEILLLDEPSEGLAPI 169
Cdd:PRK10938 407 QRLALIVRALVKHPTLLILDEPLQGLDPL 435
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-189 |
5.45e-07 |
|
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: 49.75 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 15 NSQVLF-DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGsiklkgeeLIKKPTSKRalsgIGYVPE-------- 85
Cdd:TIGR00954 463 NGDVLIeSLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG--------RLTKPAKGK----LFYVPQrpymtlgt 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 86 --DRQVFPEhTVEENIELGkkdnsnsFDDWPIDKIWEtfpiLVKLKNRLAGQ------------LSGGEQQMLSIARTLV 151
Cdd:TIGR00954 531 lrDQIIYPD-SSEDMKRRG-------LSDKDLEQILD----NVQLTHILEREggwsavqdwmdvLSGGEKQRIAMARLFY 598
|
170 180 190
....*....|....*....|....*....|....*...
gi 1347602354 152 GNPEILLLDEPSEGLAPiIVEDivKILENLKKLGVTIL 189
Cdd:TIGR00954 599 HKPQFAILDECTSAVSV-DVEG--YMYRLCREFGITLF 633
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-190 |
7.18e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 23 SLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGS--------IKLKGEELIK--KPTSKRALSGIGYVPEDRQvfpE 92
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKlvSDEWQRNNTDMLSPGEDDT---G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 93 HTVEENIELGKKDNSNSfddwpiDKIWETFPIlVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVE 172
Cdd:PRK10938 100 RTTAEIIQDEVKDPARC------EQLAQQFGI-TALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQ 172
|
170
....*....|....*...
gi 1347602354 173 DIVKILENLKKLGVTILL 190
Cdd:PRK10938 173 QLAELLASLHQSGITLVL 190
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
13-163 |
7.60e-07 |
|
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: 49.40 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YG-NSQVLFdmSLKI-KKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSI-----------KLKGEEL---IKKPTSK-- 74
Cdd:COG1245 83 YGeNGFRLY--GLPVpKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGTELqdyFKKLANGei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 75 RALSGIGYVPEDRQVFpEHTVEENIElgKKDNSNSFDDW----PIDKIWetfpilvklkNRLAGQLSGGEQQMLSIARTL 150
Cdd:COG1245 161 KVAHKPQYVDLIPKVF-KGTVRELLE--KVDERGKLDELaeklGLENIL----------DRDISELSGGELQRVAIAAAL 227
|
170
....*....|...
gi 1347602354 151 VGNPEILLLDEPS 163
Cdd:COG1245 228 LRDADFYFFDEPS 240
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
13-163 |
8.11e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YG-NSQVLFdmSLKI-KKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSI-----------KLKGEEL---IKKPTSK-- 74
Cdd:PRK13409 83 YGvNGFKLY--GLPIpKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkRFRGTELqnyFKKLYNGei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 75 RALSGIGYVPEDRQVFpEHTVEEniELGKKDNSNSFDD----WPIDKIWetfpilvklkNRLAGQLSGGEQQMLSIARTL 150
Cdd:PRK13409 161 KVVHKPQYVDLIPKVF-KGKVRE--LLKKVDERGKLDEvverLGLENIL----------DRDISELSGGELQRVAIAAAL 227
|
170
....*....|...
gi 1347602354 151 VGNPEILLLDEPS 163
Cdd:PRK13409 228 LRDADFYFFDEPT 240
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-163 |
9.33e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.20 E-value: 9.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTS--KRALSGIGYVPedrqVFPEHTV 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTdlRRVLSIIPQSP----VLFSGTV 1326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 96 EENIElgKKDNSNSFDDWP------IDKIWETFPILVKLKNRLAGQ-LSGGEQQMLSIARTLVGNPEILLLDEPS 163
Cdd:PLN03232 1327 RFNID--PFSEHNDADLWEalerahIKDVIDRNPFGLDAEVSEGGEnFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
130-192 |
1.43e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.64 E-value: 1.43e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347602354 130 NRLAGQLSGGEQQMLSIART----LVGnpEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAE 192
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQigsgLTG--VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVE 196
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
12-161 |
1.80e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 12 FYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEEL--IKKPTskralsgIGYVPEDRQV 89
Cdd:PRK13541 9 FNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInnIAKPY-------CTYIGHNLGL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347602354 90 FPEHTVEENIELGKK-DNSNSFDDWPIdkiweTFPILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDE 161
Cdd:PRK13541 82 KLEMTVFENLKFWSEiYNSAETLYAAI-----HYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-196 |
1.92e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 1.92e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 136 LSGGEQQMLSIARTL---VGNPEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNMH 196
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMH 873
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-232 |
1.94e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.17 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEEL--IKKPTSKRALSGIGYVPedrQVFPEhTV 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtkLQLDSWRSRLAVVSQTP---FLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 96 EENIELGKKDNS-----------NSFDDwpIDKIWETFPILVKLKNRLagqLSGGEQQMLSIARTLVGNPEILLLDepsE 164
Cdd:PRK10789 406 ANNIALGRPDATqqeiehvarlaSVHDD--ILRLPQGYDTEVGERGVM---LSGGQKQRISIARALLLNAEILILD---D 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347602354 165 GLAPIIVEDIVKILENLKKLGV--TILLAEQNMHFCMEvAKEAIIIDKGKAVWTGSLDDL-QKDTKTRDKY 232
Cdd:PRK10789 478 ALSAVDGRTEHQILHNLRQWGEgrTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLaQQSGWYRDMY 547
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-211 |
3.60e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.32 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 136 LSGGEQQMLSIARTL---VGNPEILLLDEPSEGLApiiVEDIVKILENLKKL---GVTILLAEQNMHfcmeVAKEA-III 208
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLH---FDDIKKLLEVLQRLvdkGNTVVVIEHNLD----VIKTAdYII 902
|
...
gi 1347602354 209 DKG 211
Cdd:TIGR00630 903 DLG 905
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-166 |
3.61e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 5 ETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLkGEELikkptskralsGIGYVP 84
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKL-----------EVAYFD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 85 EDRQVF-PEHTVEENIELGKKDnsnsfddwpidkiwetfpILVKLKNRLA------------------GQLSGGEQQMLS 145
Cdd:PRK11147 389 QHRAELdPEKTVMDNLAEGKQE------------------VMVNGRPRHVlgylqdflfhpkramtpvKALSGGERNRLL 450
|
170 180
....*....|....*....|.
gi 1347602354 146 IARTLVGNPEILLLDEPSEGL 166
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDL 471
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-193 |
6.46e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSGIGYVPEDRQVFpEHTVEENIE 100
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLF-SNSIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 101 -----------LGKKDNSNSFDDWP------------------------------IDKIWETF----------PILV--- 126
Cdd:PTZ00265 482 yslyslkdleaLSNYYNEDGNDSQEnknkrnscrakcagdlndmsnttdsnelieMRKNYQTIkdsevvdvskKVLIhdf 561
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 127 ---------KLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPIIVEDIVKILENLK--KLGVTILLAEQ 193
Cdd:PTZ00265 562 vsalpdkyeTLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHR 639
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-166 |
8.29e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 45.69 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGE-----ELIKKPTSKRAL 77
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 78 ---SGIGYV---PED---RQVFPEHTVEENI-ELGKKDNSNSFD---DW------PIDKIwetfpilvklkNRLAGQLSG 138
Cdd:PRK11701 86 llrTEWGFVhqhPRDglrMQVSAGGNIGERLmAVGARHYGDIRAtagDWlerveiDAARI-----------DDLPTTFSG 154
|
170 180
....*....|....*....|....*...
gi 1347602354 139 GEQQMLSIARTLVGNPEILLLDEPSEGL 166
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGL 182
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
130-228 |
1.16e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.77 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 130 NRLAGQLSGGEQQMLSIART----LVGnpEILLLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQNmhfcmevaKEA 205
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQigsgLTG--VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD--------EDT 552
|
90 100 110
....*....|....*....|....*....|....*.
gi 1347602354 206 I-----IID--------KGKAVWTGSLDDLQKDTKT 228
Cdd:TIGR00630 553 IraadyVIDigpgagehGGEVVASGTPEEILANPDS 588
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
136-211 |
1.47e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.91 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 136 LSGGEQQMLSIARTL---VGNPEILLLDEPSEGLAPiivEDIVKILENLKKL---GVTILLAEQNMHfcmeVAKEA-III 208
Cdd:cd03271 170 LSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHF---HDVKKLLEVLQRLvdkGNTVVVIEHNLD----VIKCAdWII 242
|
...
gi 1347602354 209 DKG 211
Cdd:cd03271 243 DLG 245
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-166 |
1.59e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.96 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 17 QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTSKRALSgigyvpedRQ----VF-- 90
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLL--------RQkiqiVFqn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 91 ------PEHTV----EE----NIELGKKDNSnsfddwpiDKIWETFPiLVKLK----NRLAGQLSGGEQQMLSIARTLVG 152
Cdd:PRK11308 101 pygslnPRKKVgqilEEplliNTSLSAAERR--------EKALAMMA-KVGLRpehyDRYPHMFSGGQRQRIAIARALML 171
|
170
....*....|....
gi 1347602354 153 NPEILLLDEPSEGL 166
Cdd:PRK11308 172 DPDVVVADEPVSAL 185
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-163 |
1.63e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 44.66 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YG-NSQVLFDMSLkIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSI-----------------------KLKGEEL- 67
Cdd:cd03236 10 YGpNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildefrgselqnyftKLLEGDVk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 68 -IKKPTskralsgigYVPEDRQVFpEHTVEENIElgKKDNSNSFDDwpIDKIWETFPILvklkNRLAGQLSGGEQQMLSI 146
Cdd:cd03236 89 vIVKPQ---------YVDLIPKAV-KGKVGELLK--KKDERGKLDE--LVDQLELRHVL----DRNIDQLSGGELQRVAI 150
|
170
....*....|....*..
gi 1347602354 147 ARTLVGNPEILLLDEPS 163
Cdd:cd03236 151 AAALARDADFYFFDEPS 167
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-224 |
1.66e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLF-DMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIklkgeelIKKPTSKRAlsgigyvpedrqVFP 91
Cdd:PLN03073 518 YPGGPLLFkNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-------FRSAKVRMA------------VFS 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 92 EHTVEenielGKKDNSNsfddwPIDKIWETFPILVKLKNR-----------LAGQ----LSGGEQQMLSIARTLVGNPEI 156
Cdd:PLN03073 579 QHHVD-----GLDLSSN-----PLLYMMRCFPGVPEQKLRahlgsfgvtgnLALQpmytLSGGQKSRVAFAKITFKKPHI 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347602354 157 LLLDEPSEGLAPIIVEDIVKILEnLKKLGVtiLLAEQNMHFCMEVAKEAIIIDKGKAV-WTGSLDDLQK 224
Cdd:PLN03073 649 LLLDEPSNHLDLDAVEALIQGLV-LFQGGV--LMVSHDEHLISGSVDELWVVSEGKVTpFHGTFHDYKK 714
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-161 |
1.80e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIK-KPTSKRALSGIgyVPEDRQVFpEHTVE 96
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGI--IPQAPVLF-SGTVR 1330
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347602354 97 ENIelgkkDNSNSFDDwpiDKIWETFPIL----VKLKNRL--------AGQ-LSGGEQQMLSIARTLVGNPEILLLDE 161
Cdd:PLN03130 1331 FNL-----DPFNEHND---ADLWESLERAhlkdVIRRNSLgldaevseAGEnFSVGQRQLLSLARALLRRSKILVLDE 1400
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-191 |
1.98e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.18 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKvksgsiklkgeelikkptsKRALSGIGYVPEDrQVFPEHTVEE 97
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK-------------------GTPVAGCVDVPDN-QFGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIelgkkdnsnsfddWPIDKIWETFPIL--VKLKN-----RLAGQLSGGEQQMLSIARTLVGNPEILLLDEPSEGLAPII 170
Cdd:COG2401 105 AI-------------GRKGDFKDAVELLnaVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|..
gi 1347602354 171 VEDIVKILENL-KKLGVTILLA 191
Cdd:COG2401 172 AKRVARNLQKLaRRAGITLVVA 193
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-183 |
2.00e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.40 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 3 LLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGL--IKVKSGSIKLKGEELIKKPTSKRALSGI 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 81 ----GYVPE----DRQVFPEHTVEENIELGKKDNSNSFD--DWPIDKIwetfpILVKLKNRLAGQ-----LSGGEQQMLS 145
Cdd:PRK09580 81 fmafQYPVEipgvSNQFFLQTALNAVRSYRGQEPLDRFDfqDLMEEKI-----ALLKMPEDLLTRsvnvgFSGGEKKRND 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1347602354 146 IARTLVGNPEILLLDEPSEGL---APIIVEDIVKILENLKK 183
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLdidALKIVADGVNSLRDGKR 196
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-222 |
2.41e-05 |
|
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: 44.94 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEElIKKPTSKRALSGIGYVPEDRQVFpEHTVEE 97
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN-IAKIGLHDLRFKITIIPQDPVLF-SGSLRM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIElgkkdnsnSFDDWPIDKIWETFPiLVKLKNRLAGQ--------------LSGGEQQMLSIARTLVGNPEILLLDEPS 163
Cdd:TIGR00957 1379 NLD--------PFSQYSDEEVWWALE-LAHLKTFVSALpdkldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1347602354 164 EGLaPIIVEDIVKILENLKKLGVTILLAEQNMHFCMEVAKeAIIIDKGKAVWTGSLDDL 222
Cdd:TIGR00957 1450 AAV-DLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTR-VIVLDKGEVAEFGAPSNL 1506
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-188 |
2.46e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 21 DMSLKIKKNNIIALLGRNGAGKSST-FKaitglikvKSGSIKLKGEELIKkpTSKRALSGIGYVPEDRQVFPEHTVEENI 99
Cdd:PTZ00265 1247 EQNVGMKNVNEFSLTKEGGSGEDSTvFK--------NSGKILLDGVDICD--YNLKDLRNLFSIVSQEPMLFNMSIYENI 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 100 ELGKKDNS-----NSFDDWPIDKIWETFPILVKLKNRLAGQ-LSGGEQQMLSIARTLVGNPEILLLDEPSEGL----API 169
Cdd:PTZ00265 1317 KFGKEDATredvkRACKFAAIDEFIESLPNKYDTNVGPYGKsLSGGQKQRIAIARALLREPKILLLDEATSSLdsnsEKL 1396
|
170
....*....|....*....
gi 1347602354 170 IVEDIVKILENLKKLGVTI 188
Cdd:PTZ00265 1397 IEKTIVDIKDKADKTIITI 1415
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-194 |
2.96e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 2.96e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347602354 130 NRLAGQLSGGEQQMLSIARTLVGnpEIL----LLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEQN 194
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGA--ELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD 537
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-227 |
3.01e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 19 LFDMSLKIKKNNIIALLGRNGAGKSSTFKAITG-LIKVKSGSIKLKGEelikkptskralsgIGYVPEDRQVFpEHTVEE 97
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT--------------VAYVPQVSWIF-NATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 98 NIELGkkdnsNSFDDwpiDKIWETFPI--LVKLKNRLAG-----------QLSGGEQQMLSIARTLVGNPEILLLDEPSE 164
Cdd:PLN03130 698 NILFG-----SPFDP---ERYERAIDVtaLQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347602354 165 GLAPIIVEDIVK--ILENLKklGVTILLAEQNMHFCMEVAKeAIIIDKGKAVWTGSLDDLQKDTK 227
Cdd:PLN03130 770 ALDAHVGRQVFDkcIKDELR--GKTRVLVTNQLHFLSQVDR-IILVHEGMIKEEGTYEELSNNGP 831
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-166 |
3.74e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.45 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 17 QVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLikvKSGSIkLKGEELIKK-PTSKRALSGI-GYVPEDRQVFPEHT 94
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR---KTGGY-IEGDIRISGfPKKQETFARIsGYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 95 VEENI----------ELGKKDNSNSfddwpIDKIWETFPiLVKLKNRLAG-----QLSGGEQQMLSIARTLVGNPEILLL 159
Cdd:PLN03140 970 VRESLiysaflrlpkEVSKEEKMMF-----VDEVMELVE-LDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFM 1043
|
....*..
gi 1347602354 160 DEPSEGL 166
Cdd:PLN03140 1044 DEPTSGL 1050
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-162 |
4.28e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 2 NLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLkgeelikkptSKRAlsGIG 81
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW----------SENA--NIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 82 YVPEDrqvfPEHTVEENIEL--------GKKDNSN-----------SFDDwpIDKiwetfpilvKLKNrlagqLSGGEQQ 142
Cdd:PRK15064 386 YYAQD----HAYDFENDLTLfdwmsqwrQEGDDEQavrgtlgrllfSQDD--IKK---------SVKV-----LSGGEKG 445
|
170 180
....*....|....*....|
gi 1347602354 143 MLSIARTLVGNPEILLLDEP 162
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEP 465
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-186 |
4.45e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 43.16 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 2 NLLETKSMNAFYGNSQVLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIK-KPTSKRalSGI 80
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYR--QQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 81 GYVPEDRQVFPEhTVEENIELGKKDNSNSFDDWPIDKIWETFPILVKLKNRLAGQLSGGEQQMLSIARTLVGNPEILLLD 160
Cdd:PRK10247 84 SYCAQTPTLFGD-TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180
....*....|....*....|....*....
gi 1347602354 161 EPSEGL---APIIVEDIVKILENLKKLGV 186
Cdd:PRK10247 163 EITSALdesNKHNVNEIIHRYVREQNIAV 191
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-189 |
8.76e-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: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 26 IKKNNIIALLGRNGAGKSSTFKAITGliKVKSGSIKlKGEELIKKPTSKRALS-GIGYVPEDRQVFPEHTVEENIELG-- 102
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVIT-GGDRLVNGRPLDSSFQrSIGYVQQQDLHLPTSTVRESLRFSay 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 103 -------KKDNSNSFDDWPIDkIWEtfpiLVKLKNRLAGQLSGG---EQ-QMLSIARTLVGNPEILL-LDEPSEGLAPII 170
Cdd:TIGR00956 863 lrqpksvSKSEKMEYVEEVIK-LLE----MESYADAVVGVPGEGlnvEQrKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
170
....*....|....*....
gi 1347602354 171 VEDIVKILENLKKLGVTIL 189
Cdd:TIGR00956 938 AWSICKLMRKLADHGQAIL 956
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-161 |
4.15e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.11 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 23 SLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEEL-IKKPTSKRALsgIGYVPEDRQVFpEHTVEENiel 101
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPEDYRKL--FSAVFTDFHLF-DQLLGPE--- 416
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 102 GKKDNSNSFDDWpidkiWETFPILVKLK---NRLAG-QLSGGEQQMLSIARTLVGNPEILLLDE 161
Cdd:PRK10522 417 GKPANPALVEKW-----LERLKMAHKLEledGRISNlKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-161 |
8.45e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. 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: 213255 [Multi-domain] Cd Length: 257 Bit Score: 39.51 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 18 VLFDMSLKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKP--TSKRALSGIGYVPedrqVFPEHTV 95
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlhTLRSRLSIILQDP----ILFSGSI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 96 EENIELGKKDNSnsfddwpiDKIWETFPIlVKLKN---RLAGQL-----------SGGEQQMLSIARTLVGNPEILLLDE 161
Cdd:cd03288 112 RFNLDPECKCTD--------DRLWEALEI-AQLKNmvkSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDE 182
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
130-228 |
1.17e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 130 NRLAGQLSGGEQQ--ML--SIARTLVGnpeIL-LLDEPSEGLAPIIVEDIVKILENLKKLGVTILLAEqnmHfcmevAKE 204
Cdd:COG0178 480 DRSAGTLSGGEAQriRLatQIGSGLVG---VLyVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVE---H-----DED 548
|
90 100 110
....*....|....*....|....*....|....*..
gi 1347602354 205 AI-----IID--------KGKAVWTGSLDDLQKDTKT 228
Cdd:COG0178 549 TIraadyIIDigpgagehGGEVVAQGTPEEILKNPDS 585
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-186 |
2.29e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 37.97 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 4 LETKSMNAFYGNSQVLFDMSLkikknNIIAllGRNGAGKSSTFKAItglikvksgSIKLKGEelikKPTSKRALSGigyv 83
Cdd:cd03240 4 LSIRNIRSFHERSEIEFFSPL-----TLIV--GQNGAGKTTIIEAL---------KYALTGE----LPPNSKGGAH---- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 84 peDRQVFPEHTVEENIELGKKDN-------SNSFD-------------DWPIDkiwetfpilvklknRLAGQLSGGEQQM 143
Cdd:cd03240 60 --DPKLIREGEVRAQVKLAFENAngkkytiTRSLAilenvifchqgesNWPLL--------------DMRGRCSGGEKVL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1347602354 144 LSI------ARTLVGNPEILLLDEPSEGL-APIIVEDIVKILENLKKLGV 186
Cdd:cd03240 124 ASLiirlalAETFGSNCGILALDEPTTNLdEENIEESLAEIIEERKSQKN 173
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
134-211 |
2.95e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 134 GQ----LSGGEQQMLSIA---------RTLvgnpeiLLLDEPSEGLAPiivEDIVKILENLKKL---GVTILLAEQNmhf 197
Cdd:COG0178 821 GQpattLSGGEAQRVKLAselskrstgKTL------YILDEPTTGLHF---HDIRKLLEVLHRLvdkGNTVVVIEHN--- 888
|
90
....*....|....*
gi 1347602354 198 cMEVAKEA-IIIDKG 211
Cdd:COG0178 889 -LDVIKTAdWIIDLG 902
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
13-166 |
4.14e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 36.78 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 13 YGNSQVLFDMSlKIKKNNIIALLGRNGAGKSSTFKAITGLIKVKSGSIKLKGEELIKKPTskralsgigYVpedrqvfpe 92
Cdd:cd03222 10 YGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQ---------YI--------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347602354 93 htveenielgkkdnsnsfddwpidkiwetfpilvklknrlagQLSGGEQQMLSIARTLVGNPEILLLDEPSEGL 166
Cdd:cd03222 71 ------------------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYL 102
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
126-211 |
6.31e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.36 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347602354 126 VKLknrlaGQ----LSGGEQQMLSIA---------RTLvgnpeiLLLDEPSEGLApiiVEDIVKILENLKKL---GVTIL 189
Cdd:PRK00349 822 IKL-----GQpattLSGGEAQRVKLAkelskrstgKTL------YILDEPTTGLH---FEDIRKLLEVLHRLvdkGNTVV 887
|
90 100
....*....|....*....|...
gi 1347602354 190 LAEQNmhfcMEVAKEA-IIIDKG 211
Cdd:PRK00349 888 VIEHN----LDVIKTAdWIIDLG 906
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
4-50 |
8.22e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 36.48 E-value: 8.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1347602354 4 LETKSMNAFYGNSQVLFDmslKIKKNNIIALLGRNGAGKSSTFKAIT 50
Cdd:cd03279 6 LELKNFGPFREEQVIDFT---GLDNNGLFLICGPTGAGKSTILDAIT 49
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
32-51 |
9.66e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 36.67 E-value: 9.66e-03
|
| |
