|
Name |
Accession |
Description |
Interval |
E-value |
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-238 |
2.54e-152 |
|
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: 422.85 E-value: 2.54e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 3 DIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGI 82
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 83 ALVPEGRRIFPELTVYENLMMGAYNRKDKEGIKRDLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMM 162
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181651 163 DEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMVRKAYLGV 238
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLGV 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-228 |
1.18e-135 |
|
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: 380.24 E-value: 1.18e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGIALV 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRIFPELTVYENLMMGAYNRKdKEGIKRDLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEP 165
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARR-RAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181651 166 SLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDN 228
Cdd:cd03224 160 SEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-237 |
1.61e-93 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 274.06 E-value: 1.61e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRM 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 GIALVPEGRRIFPELTVYENLMMGAYnRKDKEGIKRDLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLL 160
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGF-FAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181651 161 MMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMVRKAYLG 237
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-238 |
3.79e-81 |
|
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: 242.43 E-value: 3.79e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGIALV 85
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRIFPELTVYENLMMGAYNRKDKEgiKRDLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEP 165
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRS--RKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181651 166 SLGLAPILVSEVFEVIQKINQEGT-TILLVEQNALGALKVAHYGYVLETGQIVLEGKASElLDNEMVRKaYLGV 238
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGAGDE-LDEDKVRR-YLAV 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-239 |
1.82e-71 |
|
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: 218.75 E-value: 1.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 2 SDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMG 81
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 82 IAlvpegR-----RIFPELTVYENLMMGAYNRkDKEGIKRDLEWIFSLFPR----------------LKERLKQLGGTLS 140
Cdd:COG0411 81 IA-----RtfqnpRLFPELTVLENVLVAAHAR-LGRGLLAALLRLPRARREereareraeellervgLADRADEPAGNLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 141 GGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNaLGAL-KVAHYGYVLETGQIVL 218
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHD-MDLVmGLADRIVVLDFGRVIA 233
|
250 260
....*....|....*....|.
gi 490181651 219 EGKASELLDNEMVRKAYLGVA 239
Cdd:COG0411 234 EGTPAEVRADPRVIEAYLGEE 254
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-231 |
2.04e-69 |
|
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: 212.68 E-value: 2.04e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGIalv 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 peGR-----RIFPELTVYENLMMGAYNR--------KDKEGIKRDLEWIFSL--FPRLKERLKQLGGTLSGGEQQMLAIG 150
Cdd:cd03219 78 --GRtfqipRLFPELTVLENVMVAAQARtgsglllaRARREEREARERAEELleRVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 151 RALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEM 230
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
.
gi 490181651 231 V 231
Cdd:cd03219 236 V 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-227 |
3.85e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 189.12 E-value: 3.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGIalV 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGY--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRIFPELTVYENL-MMGAYNRKDKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:COG1131 79 PQEPALYPDLTVRENLrFFARLYGLPRKEARERIDELLELF-GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181651 165 PSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLD 227
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-237 |
5.21e-60 |
|
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: 188.91 E-value: 5.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGIALV 85
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRIFPELTVYENLMMGA-YNRKDKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLeIRGLSKKEREEKLEELLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181651 165 PSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMVRKAYLG 237
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-237 |
1.60e-58 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 185.23 E-value: 1.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGIAL 84
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 VPEGRRIFPELTVYENLMMGA-YNRKDKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMD 163
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAVLeLRKLSKKEREERLEELLEEF-GITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181651 164 EPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMVRKAYLG 237
Cdd:COG1137 162 EPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLG 235
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-237 |
8.61e-56 |
|
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: 178.24 E-value: 8.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGIAL 84
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 VPEGRRIFPELTVYENLMMGAYNRKD--KEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMM 162
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLEIRKDldRAEREERLEALLEEF-QISHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 163 DEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMVRKAYLG 237
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLG 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-216 |
8.97e-50 |
|
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: 160.64 E-value: 8.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGIalV 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGY--L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRIFPELTVYENLMmgaynrkdkegikrdlewifslfprlkerlkqlggtLSGGEQQMLAIGRALMSRPKLLMMDEP 165
Cdd:cd03230 79 PEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490181651 166 SLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQI 216
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-237 |
4.11e-48 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 158.74 E-value: 4.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRM 80
Cdd:COG4674 6 MHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 GIalvpeGR-----RIFPELTVYENLMMgAYNRK--------------DKEGIKRDLEWIfslfpRLKERLKQLGGTLSG 141
Cdd:COG4674 86 GI-----GRkfqkpTVFEELTVFENLEL-ALKGDrgvfaslfarltaeERDRIEEVLETI-----GLTDKADRLAGLLSH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 142 GEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEgTTILLVEQN-----ALGAlKVAhygyVLETGQI 216
Cdd:COG4674 155 GQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGK-HSVVVVEHDmefvrQIAR-KVT----VLHQGSV 228
|
250 260
....*....|....*....|.
gi 490181651 217 VLEGKASELLDNEMVRKAYLG 237
Cdd:COG4674 229 LAEGSLDEVQADPRVIEVYLG 249
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-225 |
1.34e-47 |
|
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: 156.96 E-value: 1.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQK-----GKIIFNGQDITNKPAHVIN-R 79
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVLElR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 80 MGIALVPEGRRIFPeLTVYENLMMG--AYNRKDKEGIKRDLEWIFS---LFPRLKERLKQLGgtLSGGEQQMLAIGRALM 154
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGlrLHGIKLKEELDERVEEALRkaaLWDEVKDRLHALG--LSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181651 155 SRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEgTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASEL 225
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-235 |
4.85e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.02 E-value: 4.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHvinrm 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 gIALVPEGRRI---FPeLTVYENLMMGAYNRKdkegikrdlewifSLFPRLKER--------LKQLG---------GTLS 140
Cdd:COG1121 77 -IGYVPQRAEVdwdFP-ITVRDVVLMGRYGRR-------------GLFRRPSRAdreavdeaLERVGledladrpiGELS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 141 GGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNaLGALkVAHYGYVLE-TGQIVLE 219
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHD-LGAV-REYFDRVLLlNRGLVAH 219
|
250
....*....|....*.
gi 490181651 220 GKASELLDNEMVRKAY 235
Cdd:COG1121 220 GPPEEVLTPENLSRAY 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-229 |
2.22e-46 |
|
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: 153.64 E-value: 2.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYY-GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIAL 84
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 V---PEgRRIFpELTVYENLMMGAYNRK-DKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLL 160
Cdd:COG1122 80 VfqnPD-DQLF-APTVEEDVAFGPENLGlPREEIRERVEEALELV-GLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181651 161 MMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNE 229
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-237 |
2.94e-46 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 154.38 E-value: 2.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRM 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 GIALVPEGRRIFPELTVYENLMMG-----------------AYNRKDKEGIKRDLEWIFSLfpRLKERLKQLGGTLSGGE 143
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVAqhqqlktglfsgllktpAFRRAESEALDRAATWLERV--GLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 144 QQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKA 222
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
250
....*....|....*
gi 490181651 223 SELLDNEMVRKAYLG 237
Cdd:PRK11300 239 EEIRNNPDVIKAYLG 253
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-216 |
3.14e-46 |
|
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: 152.68 E-value: 3.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVIN-RMGIAL 84
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 VPEGRRIFPELTVYENLMMG---AYNRKDKEGIKRDLEwifsLFPR--LKERLKQLGGTLSGGEQQMLAIGRALMSRPKL 159
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLApikVKGMSKAEAEERALE----LLEKvgLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181651 160 LMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQI 216
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-228 |
4.75e-46 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 153.23 E-value: 4.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVIN-RMGIA 83
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKlRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 84 LVPEGRRIFPELTVYENLMMG---AYNRKDKEGIKRDLEwifsLFPR--LKERLKQLGGTLSGGEQQMLAIGRALMSRPK 158
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLApikVKKMSKAEAEERAME----LLERvgLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181651 159 LLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLV--EqnaLG-ALKVAHYGYVLETGQIVLEGKASELLDN 228
Cdd:COG1126 157 VMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVthE---MGfAREVADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-229 |
1.12e-45 |
|
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: 152.32 E-value: 1.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGIal 84
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 VPEGRRIFPELTVYENLMM-GAYNRKDKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMD 163
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYfAELYGLFDEELKKRIEELIELL-GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181651 164 EPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNE 229
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEI 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-235 |
2.32e-45 |
|
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: 151.73 E-value: 2.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIAL 84
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 VPEGRRIFPELTVYENLMMGAYNRKdkegikrdlewifSLFPRLKER--------LKQLG---------GTLSGGEQQML 147
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRYPHL-------------GLFGRPSAEdreaveeaLERTGlehladrpvDELSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 148 AIGRALMSRPKLLMMDEP--SLGLAPILvsEVFEVIQKINQE-GTTILLV----EQnalgALKVAHYGYVLETGQIVLEG 220
Cdd:COG1120 147 LIARALAQEPPLLLLDEPtsHLDLAHQL--EVLELLRRLARErGRTVVMVlhdlNL----AARYADRLVLLKDGRIVAQG 220
|
250
....*....|....*
gi 490181651 221 KASELLDNEMVRKAY 235
Cdd:COG1120 221 PPEEVLTPELLEEVY 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-220 |
1.55e-44 |
|
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: 148.44 E-value: 1.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHvinRMGIALV 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE---RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRIFPELTVYENLMMGAYNRKDKEG-IKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAeIRARVRELLELV-GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181651 165 PSLGLAPILVSEVFEVIQKI-NQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEG 220
Cdd:cd03259 157 PLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-165 |
3.98e-43 |
|
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: 142.79 E-value: 3.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRmGIALVPEGRRIFPELTVYEN 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 101 LMMGA-----YNRKDKEGIKRDLEWiFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEP 165
Cdd:pfam00005 80 LRLGLllkglSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-232 |
4.55e-43 |
|
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: 145.51 E-value: 4.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAH----V 76
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyeL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 77 INRMGI-----ALvpegrriFPELTVYENLMMG--AYNRKDKEGIKRdlewifslfpRLKERLKQLG--GT-------LS 140
Cdd:COG1127 81 RRRIGMlfqggAL-------FDSLTVFENVAFPlrEHTDLSEAEIRE----------LVLEKLELVGlpGAadkmpseLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 141 GGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLE 219
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
250
....*....|....*
gi 490181651 220 GKASELL--DNEMVR 232
Cdd:COG1127 224 GTPEELLasDDPWVR 238
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-194 |
1.02e-42 |
|
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: 144.17 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGA----IHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKP----AHVI 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 78 NR-MGIalvpegrrIF------PELTVYENLMMGA-YNRKDKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAI 149
Cdd:cd03255 81 RRhIGF--------VFqsfnllPDLTALENVELPLlLAGVPKKERRERAEELLERV-GLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490181651 150 GRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLV 194
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVV 197
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-194 |
4.18e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 142.49 E-value: 4.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 3 DIVLEVQSLHVYYG----AIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVIN 78
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 79 RMgialvpegRR-----IF------PELTVYENLMMGA-YNRKDKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQM 146
Cdd:COG1136 82 RL--------RRrhigfVFqffnllPELTALENVALPLlLAGVSRKERRERARELLERV-GLGDRLDHRPSQLSGGQQQR 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490181651 147 LAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLV 194
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMV 201
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-215 |
4.28e-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: 4.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 10 SLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIALV---P 86
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGLVfqnP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 87 EgRRIFpELTVYENLMMGAYNRK-DKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEP 165
Cdd:cd03225 85 D-DQFF-GPTVEEEVAFGLENLGlPEEEIEERVEEALELV-GLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490181651 166 SLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQ 215
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-225 |
6.65e-42 |
|
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: 142.12 E-value: 6.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVinRMGIALV 85
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREV--RRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRIFPELTVYENLMMGA--YNRKDKEGIKRDLEWIfsLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMD 163
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHArlYGVPGAERRERIDELL--DFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181651 164 EPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASEL 225
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-194 |
8.20e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 145.24 E-value: 8.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHvinRM 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE---KR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 GIALVPEGRRIFPELTVYENLMMGAYNRK-DKEGIKRdlewifslfpRLKERLKQLG---------GTLSGGEQQMLAIG 150
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAENVAFGLRMRGvPKAEIRA----------RVAELLELVGlegladrypHQLSGGQQQRVALA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490181651 151 RALMSRPKLLMMDEPsLG-----LAPILVSEVFEvIQKinQEGTTILLV 194
Cdd:COG3842 148 RALAPEPRVLLLDEP-LSaldakLREEMREELRR-LQR--ELGITFIYV 192
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-235 |
1.03e-41 |
|
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: 142.32 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAI-HAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVIN--RMGI 82
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 83 ALVPEGRRIFPELTVYENLMMGAYNRKDKegikrdLEWIFSLFPRL-KER----LKQLG---------GTLSGGEQQMLA 148
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRST------WRSLFGLFPKEeKQRalaaLERVGlldkayqraDQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 149 IGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASElLD 227
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LT 233
|
....*...
gi 490181651 228 NEMVRKAY 235
Cdd:cd03256 234 DEVLDEIY 241
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-237 |
3.65e-41 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 140.80 E-value: 3.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGIAL 84
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 VPEGRRIFPELTVYENLMMGAYNRKD--KEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMM 162
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDDlsAEQREDRANELMEEF-HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 163 DEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMVRKAYLG 237
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG 236
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-211 |
1.07e-40 |
|
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: 138.82 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 7 EVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHvinrmgIALVP 86
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 87 EGRRI---FPeLTVYENLMMGAY---------NRKDKEGIKRDLEwifslFPRLKERLKQLGGTLSGGEQQMLAIGRALM 154
Cdd:cd03235 75 QRRSIdrdFP-ISVRDVVLMGLYghkglfrrlSKADKAKVDEALE-----RVGLSELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181651 155 SRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNaLGALKvAHYGYVL 211
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHD-LGLVL-EYFDRVL 203
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-232 |
2.98e-40 |
|
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: 138.02 E-value: 2.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDIT-NKPA---HVINRMG 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISgLSEAelyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 82 I-----ALvpegrriFPELTVYENLMMGAY-NRKDKEGIKRD--LEWIFSLfpRLKERLKQLGGTLSGGEQQMLAIGRAL 153
Cdd:cd03261 81 MlfqsgAL-------FDSLTVFENVAFPLReHTRLSEEEIREivLEKLEAV--GLRGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 154 MSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELL--DNEM 230
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPL 231
|
..
gi 490181651 231 VR 232
Cdd:cd03261 232 VR 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-233 |
3.04e-40 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 144.01 E-value: 3.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 2 SDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMG 81
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 82 IALVPEGRRIFPELTVYENLMMGAYNRK----DKEGIKRdlewifslfpRLKERLKQLG---------GTLSGGEQQMLA 148
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRggliDWRAMRR----------RARELLARLGldidpdtpvGDLSVAQQQLVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 149 IGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLV-----EqnalgALKVAHYGYVLETGQIVLEGKAS 223
Cdd:COG1129 151 IARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYIshrldE-----VFEIADRVTVLRDGRLVGTGPVA 225
|
250
....*....|
gi 490181651 224 ELLDNEMVRK 233
Cdd:COG1129 226 ELTEDELVRL 235
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-225 |
1.56e-39 |
|
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: 135.71 E-value: 1.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSL-HVY-YGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGIa 83
Cdd:cd03263 1 LQIRNLtKTYkKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 84 lVPEGRRIFPELTVYENLMMgaYNR---KDKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLL 160
Cdd:cd03263 80 -CPQFDALFDELTVREHLRF--YARlkgLPKSEIKEEVELLLRVL-GLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 161 MMDEPSLGLAPILVSEVFEVIQKInQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASEL 225
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-194 |
6.50e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 134.41 E-value: 6.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 13 VYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVIN----RMGIalVPEG 88
Cdd:COG2884 10 RYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrrRIGV--VFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 89 RRIFPELTVYENLMMG-AYNRKDKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSL 167
Cdd:COG2884 88 FRLLPDRTVYENVALPlRVTGKSRKEIRRRVREVLDLV-GLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTG 166
|
170 180
....*....|....*....|....*..
gi 490181651 168 GLAPILVSEVFEVIQKINQEGTTILLV 194
Cdd:COG2884 167 NLDPETSWEIMELLEEINRRGTTVLIA 193
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-220 |
1.49e-38 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 133.11 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITnKPAHVINRMGiALV 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-KNIEALRRIG-ALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 pEGRRIFPELTVYENLMMGA-YNRKDKEGIKRDLEWIfslfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:cd03268 79 -EAPGFYPNLTARENLRLLArLLGIRKKRIDEVLDVV-----GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490181651 165 PSLGLAPILVSEVFEVIQKINQEGTTILLvEQNALGAL-KVA-HYGyVLETGQIVLEG 220
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGITVLI-SSHLLSEIqKVAdRIG-IINKGKLIEEG 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-215 |
3.36e-38 |
|
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: 131.16 E-value: 3.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDIT-NKPAHVINRMGIAL 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 VPEGRRIFPELTVYENLMMGaynrkdkegikrdlewifslfprlkerlkqlggtLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490181651 165 PSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQ 215
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-215 |
3.53e-38 |
|
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: 130.44 E-value: 3.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 7 EVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHvINRMGIALVP 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE-ELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 87 EgrrifpeltvyenlmmgaynrkdkegikrdlewifslfprlkerlkqlggtLSGGEQQMLAIGRALMSRPKLLMMDEPS 166
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490181651 167 LGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQ 215
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-228 |
1.89e-37 |
|
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: 136.96 E-value: 1.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYY-----GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAH 75
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 76 VINRMG--IALV---PEGrRIFPELTVYENLMMG--AYNRKDKEGIKRDLEWI---FSLFPRLKERlkqLGGTLSGGEQQ 145
Cdd:COG1123 336 SLRELRrrVQMVfqdPYS-SLNPRMTVGDIIAEPlrLHGLLSRAERRERVAELlerVGLPPDLADR---YPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 146 MLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTIL-------LVEQnalgalkVAHYGYVLETGQIV 217
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLfishdlaVVRY-------IADRVAVMYDGRIV 484
|
250
....*....|.
gi 490181651 218 LEGKASELLDN 228
Cdd:COG1123 485 EDGPTEEVFAN 495
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-220 |
3.04e-37 |
|
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: 129.80 E-value: 3.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGA----IHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMG 81
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 82 IalVPEGRRIFPELTVYENLMMGAynrkDKEGIKRD-----LEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSR 156
Cdd:cd03266 82 F--VSDSTGLYDRLTARENLEYFA----GLYGLKGDeltarLEELADRL-GMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181651 157 PKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEG 220
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-228 |
3.80e-37 |
|
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: 130.15 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHaIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAhvINRmGIALV 85
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP--EKR-DISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRIFPELTVYENLMMGAYNRK-DKEGIKRDLEWIfSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRKvDKKEIERKVLEI-AEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 165 PSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDN 228
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-194 |
4.11e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 132.89 E-value: 4.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEvqSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHviNRm 80
Cdd:COG3839 1 MASLELE--NVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 GIALVPEGRRIFPELTVYENLMMGAYNRK-DKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKL 159
Cdd:COG3839 76 NIAMVFQSYALYPHMTVYENIAFPLKLRKvPKAEIDRRVREAAELL-GLEDLLDRKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 490181651 160 LMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLV 194
Cdd:COG3839 155 FLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYV 190
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-219 |
4.74e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 130.59 E-value: 4.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGA-----IHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRM 80
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 gIAlvpegrRIF--------PELTVYENLMMgAYNRKDKEG----IKRDLEWIFslfprlKERLKQLG-----------G 137
Cdd:COG1101 82 -IG------RVFqdpmmgtaPSMTIEENLAL-AYRRGKRRGlrrgLTKKRRELF------RELLATLGlglenrldtkvG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 138 TLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKInqegttillVEQNALGALKVAH-------YG-- 208
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKI---------VEENNLTTLMVTHnmeqaldYGnr 218
|
250
....*....|..
gi 490181651 209 -YVLETGQIVLE 219
Cdd:COG1101 219 lIMMHEGRIILD 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-228 |
1.42e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 134.65 E-value: 1.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYY--GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQ---KGKIIFNGQDITNKPAHVINR 79
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 80 MgIALVP-EGRRIFPELTVYENLMMGAYNRK-DKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRP 157
Cdd:COG1123 84 R-IGMVFqDPMTQLNPVTVGDQIAEALENLGlSRAEARARVLELLEAV-GLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181651 158 KLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDN 228
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-220 |
1.48e-36 |
|
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: 128.39 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYY----GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRM 80
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 G--IALVPE--GRRIFPELTVYENL---MMGAYNRKDKEGIKRDLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRAL 153
Cdd:cd03257 81 RkeIQMVFQdpMSSLNPRMTIGEQIaepLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181651 154 MSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNaLGALK-VAHYGYVLETGQIVLEG 220
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHD-LGVVAkIADRVAVMYAGKIVEEG 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-228 |
1.57e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 131.42 E-value: 1.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSdivLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDI-TNKPAHviNR 79
Cdd:COG1118 1 MS---IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPR--ER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 80 mGIALVPEGRRIFPELTVYENLMMGAYNRK-DKEGIKRD-LEWIfslfprlkeRLKQLGG-------TLSGGEQQMLAIG 150
Cdd:COG1118 76 -RVGFVFQHYALFPHMTVAENIAFGLRVRPpSKAEIRARvEELL---------ELVQLEGladrypsQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 151 RALMSRPKLLMMDEPsLG-----LAPILVSEVFEVIQKInqeGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASEL 225
Cdd:COG1118 146 RALAVEPEVLLLDEP-FGaldakVRKELRRWLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
...
gi 490181651 226 LDN 228
Cdd:COG1118 222 YDR 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-227 |
2.05e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 129.84 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITnkpAHVINRMGiaL 84
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRRIG--Y 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 VPEGRRIFPELTVYENLM-MGAYNRKDKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMD 163
Cdd:COG4152 76 LPEERGLYPKMKVGEQLVyLARLKGLSKAEAKRRADEWLERL-GLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181651 164 EPSLGLAPILVSEVFEVIQKINQEGTTIL-------LVEQnalgaL--KVAhygyVLETGQIVLEGKASELLD 227
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAKGTTVIfsshqmeLVEE-----LcdRIV----IINKGRKVLSGSVDEIRR 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-194 |
4.94e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 127.90 E-value: 4.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYY----GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHv 76
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 77 inrmgIALVPEGRRIFPELTVYENLMMGA-YNRKDKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMS 155
Cdd:COG1116 82 -----RGVVFQEPALLPWLTVLDNVALGLeLRGVPKAERRERARELLELV-GLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490181651 156 RPKLLMMDEPsLG-LAPILVSEVFEVIQKINQE-GTTILLV 194
Cdd:COG1116 156 DPEVLLMDEP-FGaLDALTRERLQDELLRLWQEtGKTVLFV 195
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-228 |
8.68e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 127.27 E-value: 8.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQ-----KGKIIFNGQDITNKPAHVIN-R 79
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIEvR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 80 MGIALVPEGRRIFPELTVYENLMMGA-YNR--KDKEGIKRDLEWIF---SLFPRLKERLKQLGGTLSGGEQQMLAIGRAL 153
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVkLNGlvKSKKELDERVEWALkkaALWDEVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 154 MSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEgTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDN 228
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-217 |
8.90e-36 |
|
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: 125.83 E-value: 8.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAhviNRMGIALV 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP---KDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRIFPELTVYENLMMGAYNRK-DKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKvPKDEIDERVREVAELL-QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181651 165 PSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIV 217
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-216 |
1.26e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.31 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVInRMGIALV 85
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW-RRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRIFPElTVYENLMMGAYNRKDKEGIKRDLEWI--FSLFPRLkerLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMD 163
Cdd:COG4619 80 PQEPALWGG-TVRDNLPFPFQLRERKFDRERALELLerLGLPPDI---LDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181651 164 EPSLGLAPILVSEVFEVIQK-INQEGTTILLVEQNALGALKVAHYGYVLETGQI 216
Cdd:COG4619 156 EPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-228 |
1.33e-35 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 126.20 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHvinRMGIALV 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH---KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRIFPELTVYENLMMGAYNRK-DKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKlPKAEIKERVAEALDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 165 PSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDN 228
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
12-215 |
2.77e-35 |
|
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: 124.67 E-value: 2.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 12 HVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVIN--RMGIALVPEGR 89
Cdd:TIGR02673 9 KAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPllRRRIGVVFQDF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 90 RIFPELTVYENLMM-----GAYNRKDKEGIKRDLEWIfslfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:TIGR02673 89 RLLPDRTVYENVALplevrGKKEREIQRRVGAALRQV-----GLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490181651 165 PSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQ 215
Cdd:TIGR02673 164 PTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-219 |
1.65e-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: 121.00 E-value: 1.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNK-PAHVInRMGIAL 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPRDAR-RAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 VPEgrrifpeltvyenlmmgaynrkdkegikrdlewifslfprlkerlkqlggtLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:cd03216 80 VYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 165 PSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLE 219
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-220 |
1.79e-34 |
|
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: 122.39 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITnkpAHVINRMGiaLV 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIG--YL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRIFPELTVYENLMMGA--YNRKDKEGIKRDLEWI--FSLFPRLKERLKQlggtLSGGEQQMLAIGRALMSRPKLLM 161
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAqlKGLKKEEARRRIDEWLerLELSEYANKRVEE----LSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181651 162 MDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEG 220
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-194 |
2.88e-34 |
|
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: 121.00 E-value: 2.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 3 DIVLEVQSLHVyygaIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGI 82
Cdd:cd03215 2 EPVLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 83 ALVPEGRR---IFPELTVYENLMMGAYnrkdkegikrdlewifslfprlkerlkqlggtLSGGEQQMLAIGRALMSRPKL 159
Cdd:cd03215 78 AYVPEDRKregLVLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRV 125
|
170 180 190
....*....|....*....|....*....|....*
gi 490181651 160 LMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLV 194
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLI 160
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
15-228 |
7.08e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 121.74 E-value: 7.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 15 YGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVIN-RMGIALVPEGRRIFP 93
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLiRQEAGMVFQQFYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 94 ELTVYENLMMG-----AYNRKDKEGIKRDLEWIFSLfprlKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLG 168
Cdd:PRK09493 91 HLTALENVMFGplrvrGASKEEAEKQARELLAKVGL----AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 169 LAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDN 228
Cdd:PRK09493 167 LDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-207 |
8.15e-34 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 122.20 E-value: 8.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 2 SDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGL------VRAQkGKIIFNGQDITNK--- 72
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgFRVE-GKVTFHGKNLYAPdvd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 73 PAHVINRMGiaLVPEGRRIFPElTVYENLMMGA----YNRKDKEGIKRDLEWIfSLFPRLKERLKQLGGTLSGGEQQMLA 148
Cdd:PRK14243 86 PVEVRRRIG--MVFQKPNPFPK-SIYDNIAYGAringYKGDMDELVERSLRQA-ALWDEVKDKLKQSGLSLSGGQQQRLC 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181651 149 IGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEgTTILLVEQNALGALKVAHY 207
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDM 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-194 |
8.51e-34 |
|
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: 121.04 E-value: 8.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYG----AIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHvinrmg 81
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 82 IALVPEGRRIFPELTVYENLMMG--AYNRKDKEGIKRDLEWIfSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKL 159
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGleLQGVPKAEARERAEELL-ELV-GLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 490181651 160 LMMDEPSLGLAPILVSEVFEVIQKI-NQEGTTILLV 194
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIwRETGKTVLLV 188
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-237 |
1.25e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 121.02 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGaiHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPahvinrmgialv 85
Cdd:COG3840 2 LRLDDLTYRYG--DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRI---------FPELTVYENLMMG-----AYNRKDKEGIKRDLEwifslfpR--LKERLKQLGGTLSGGEQQMLAI 149
Cdd:COG3840 68 PAERPVsmlfqennlFPHLTVAQNIGLGlrpglKLTAEQRAQVEQALE-------RvgLAGLLDRLPGQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 150 GRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLD- 227
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDg 220
|
250
....*....|..
gi 490181651 228 --NEMVRkAYLG 237
Cdd:COG3840 221 epPPALA-AYLG 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-231 |
2.00e-33 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 125.93 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITN-KPAHViNRMGIA 83
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTPAKA-HQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 84 LVPEGRRIFPELTVYENLMMGAYNRKDKEgikrdlewifslfPRLKERLKQLG---------GTLSGGEQQMLAIGRALM 154
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGLPKRQASM-------------QKMKQLLAALGcqldldssaGSLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181651 155 SRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMV 231
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDII 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-228 |
3.37e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 120.53 E-value: 3.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 2 SDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGL------VRAqKGKIIFNGQDITNKPAH 75
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipgARV-EGEILLDGEDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 76 VIN-RMGIALVPEGRRIFPeLTVYENLMMGA--YNRKDKEGIKRDLEWifSL-----FPRLKERLKQLGGTLSGGEQQML 147
Cdd:COG1117 87 VVElRRRVGMVFQKPNPFP-KSIYDNVAYGLrlHGIKSKSELDEIVEE--SLrkaalWDEVKDRLKKSALGLSGGQQQRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 148 AIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEgTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLD 227
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFT 242
|
.
gi 490181651 228 N 228
Cdd:COG1117 243 N 243
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-220 |
3.61e-33 |
|
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: 118.31 E-value: 3.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 7 EVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIALVP 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 87 egrrifpelTVYENLmmgaynrkdkeGIKrdlewifslfpRLKERLKQlggTLSGGEQQMLAIGRALMSRPKLLMMDEPS 166
Cdd:cd03214 80 ---------QALELL-----------GLA-----------HLADRPFN---ELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 167 LGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEG 220
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-194 |
7.87e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 123.98 E-value: 7.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDIT-NKPAHVInR 79
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDAI-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 80 MGIALVPEGRRIFPELTVYENLMMGaynRKDKEGIKRDLEwifslfpRLKERLKQLG-------------GTLSGGEQQM 146
Cdd:COG3845 80 LGIGMVHQHFMLVPNLTVAENIVLG---LEPTKGGRLDRK-------AARARIRELSerygldvdpdakvEDLSVGEQQR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490181651 147 LAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLV 194
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFI 197
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-229 |
9.92e-33 |
|
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: 124.49 E-value: 9.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 2 SDIVLEVQSLHVYY-GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRM 80
Cdd:COG4988 333 GPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 gIALVPEGRRIFPElTVYENLMMGAYNRKDKEgIKRDL------EWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALM 154
Cdd:COG4988 413 -IAWVPQNPYLFAG-TIRENLRLGRPDASDEE-LEAALeaagldEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 155 SRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQnaLGALKVAHYGYVLETGQIVLEGKASELLDNE 229
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHR--LALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-194 |
5.15e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 121.66 E-value: 5.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 3 DIVLEVQSLHVYygaiHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNK-PAHVInRMG 81
Cdd:COG1129 254 EVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRsPRDAI-RAG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 82 IALVPEGRR---IFPELTVYENLMMGAYNRKDKEGIkRDLEWIFSLFPRLKERLK-------QLGGTLSGGEQQMLAIGR 151
Cdd:COG1129 329 IAYVPEDRKgegLVLDLSIRENITLASLDRLSRGGL-LDRRRERALAEEYIKRLRiktpspeQPVGNLSGGNQQKVVLAK 407
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490181651 152 ALMSRPKLLMMDEPSLGlapILV---SEVFEVIQKINQEGTTILLV 194
Cdd:COG1129 408 WLATDPKVLILDEPTRG---IDVgakAEIYRLIRELAAEGKAVIVI 450
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-230 |
1.31e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 117.60 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVinRM 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA--RQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 GIALVPEGRRIFPELTVYENLMM-GAYNRKDKEGIKRDLEWIFSlFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKL 159
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLLVfGRYFGLSAAAARALVPPLLE-FAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181651 160 LMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEM 230
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-217 |
3.22e-31 |
|
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: 113.89 E-value: 3.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 14 YYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPahviNRMGIALVP-EGRRIF 92
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE----RRKSIGYVMqDVDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 93 PELTVYENLMMGAYNRKDKEGIKRDLEWIFSLFpRLKERLKQlggTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPI 172
Cdd:cd03226 85 FTDSVREELLLGLKELDAGNEQAETVLKDLDLY-ALKERHPL---SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490181651 173 LVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIV 217
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-226 |
4.05e-31 |
|
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: 117.14 E-value: 4.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 24 IDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNkpahviNRMGIALVPEGRRI---------FPE 94
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD------SRKGIFLPPEKRRIgyvfqearlFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 95 LTVYENLMmgaYNRKDKEGIKRDLEW--IFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPI 172
Cdd:TIGR02142 90 LSVRGNLR---YGMKRARPSERRISFerVIELL-GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 173 LVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELL 226
Cdd:TIGR02142 166 RKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-215 |
6.02e-31 |
|
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: 112.09 E-value: 6.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYG--AIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIA 83
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 84 LVPEGRRIFPElTVYENLmmgaynrkdkegikrdlewifslfprlkerlkqlggtLSGGEQQMLAIGRALMSRPKLLMMD 163
Cdd:cd03228 80 YVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490181651 164 EPSLGLAPILVSEVFEVIQKInQEGTTILLVEQNaLGALKVAHYGYVLETGQ 215
Cdd:cd03228 122 EATSALDPETEALILEALRAL-AKGKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-228 |
9.99e-31 |
|
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: 113.59 E-value: 9.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPahvINRMGIALV 85
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP---VQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRIFPELTVYENLMMG-----AYNRKDKEGIKR---------DLEWIFSLFPrlkerlkqlgGTLSGGEQQMLAIGR 151
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGlrvkpRSERPPEAEIRAkvhellklvQLDWLADRYP----------AQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181651 152 ALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDN 228
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-227 |
1.49e-30 |
|
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: 113.36 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGA----IHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRmG 81
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR-R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 82 IALV---PEGRrIFPELTVYENLM--MGAYNRKD-KEGIKRDLEwIFSLFPRLKERLKQlggTLSGGEQQMLAIGRALMS 155
Cdd:COG1124 81 VQMVfqdPYAS-LHPRHTVDRILAepLRIHGLPDrEERIAELLE-QVGLPPSFLDRYPH---QLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181651 156 RPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNaLGAlkVAH---YGYVLETGQIVLEGKASELLD 227
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHD-LAV--VAHlcdRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-193 |
1.73e-30 |
|
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: 112.50 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 13 VYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVIN--RMGIALVPEGRR 90
Cdd:cd03292 9 TYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylRRKIGVVFQDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 91 IFPELTVYENLMM-----GAYNRKDKEGIKRDLEWIfslfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEP 165
Cdd:cd03292 89 LLPDRNVYENVAFalevtGVPPREIRKRVPAALELV-----GLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180
....*....|....*....|....*...
gi 490181651 166 SLGLAPILVSEVFEVIQKINQEGTTILL 193
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINKAGTTVVV 191
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-229 |
2.97e-30 |
|
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: 118.01 E-value: 2.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 20 AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITN-KPAHVinRMGIALVPEGRRIFPElTVY 98
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASL--RRQIGVVLQDVFLFSG-TIR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 99 ENLMMGAYNRKDKE--------GIKRDLEwifslfpRLKERLKQL----GGTLSGGEQQMLAIGRALMSRPKLLMMDEPS 166
Cdd:COG2274 567 ENITLGDPDATDEEiieaarlaGLHDFIE-------ALPMGYDTVvgegGSNLSGGQRQRLAIARALLRNPRILILDEAT 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181651 167 LGLAPILVSEVFEVIQKINQeGTTILLVEQNaLGALKVAHYGYVLETGQIVLEGKASELLDNE 229
Cdd:COG2274 640 SALDAETEAIILENLRRLLK-GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-228 |
6.97e-30 |
|
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: 111.13 E-value: 6.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYG----AIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDIT--NKPAHVIN 78
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 79 RMGIALVPEGRRIFPELTVYENLmmgAY----NRKDKEGIKRdlewifslfpRLKERLKQLG---------GTLSGGEQQ 145
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENV---ALpleiAGVPKAEIEE----------RVLELLELVGledkadaypAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 146 MLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLV--EQNALGAL--KVAhygyVLETGQIVLEG 220
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLIthEMEVVKRIcdRVA----VMEKGEVVEEG 223
|
....*...
gi 490181651 221 KASELLDN 228
Cdd:cd03258 224 TVEEVFAN 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-193 |
9.26e-30 |
|
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: 110.26 E-value: 9.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVinRMGIAL 84
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY--RRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 VPEGRRIFPELTVYENLMM--GAYNRK-DKEGIKRDLEWIfslfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLM 161
Cdd:COG4133 80 LGHADGLKPELTVRENLRFwaALYGLRaDREAIDEALEAV-----GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|..
gi 490181651 162 MDEPSLGLAPILVSEVFEVIQKINQEGTTILL 193
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-228 |
1.04e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 111.16 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQ-----KGKIIFNGQDITNKPAHVINR 79
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 80 MgIALVPEGRRIFPELTVYENLMMG-AYNR--KDKEGIKRDLEWIF---SLFPRLKERLKQLGGTLSGGEQQMLAIGRAL 153
Cdd:PRK14247 83 R-VQMVFQIPNPIPNLSIFENVALGlKLNRlvKSKKELQERVRWALekaQLWDEVKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 154 MSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEgTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDN 228
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-226 |
3.75e-29 |
|
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: 112.12 E-value: 3.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 24 IDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNG---QDitnkpahviNRMGIALVPEGRRI--------- 91
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQD---------SARGIFLPPHRRRIgyvfqearl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 92 FPELTVYENLMMGaYNRKDKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEP--SLGL 169
Cdd:COG4148 89 FPHLSVRGNLLYG-RKRAPRAERRISFDEVVELL-GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPlaALDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181651 170 ApiLVSEVFEVIQKINQE-GTTILLV-----EqnalgALKVAHYGYVLETGQIVLEGKASELL 226
Cdd:COG4148 167 A--RKAEILPYLERLRDElDIPILYVshsldE-----VARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-228 |
6.49e-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: 108.93 E-value: 6.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 13 VYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAhVINRMGIALVPEGRRIF 92
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP-VELRRKIGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 93 PELTVYENL-MMGAYNRKDKEGIKRdlewifslfpRLKERLKQLG-----------GTLSGGEQQMLAIGRALMSRPKLL 160
Cdd:cd03295 88 PHMTVEENIaLVPKLLKWPKEKIRE----------RADELLALVGldpaefadrypHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181651 161 MMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDN 228
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-220 |
7.46e-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: 108.05 E-value: 7.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGqIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGiaLV 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIG--YL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRIFPELTVYENL-----MMGAYNRKDKEGIKRDLEWIfSLFPRLKERLkqlgGTLSGGEQQMLAIGRALMSRPKLL 160
Cdd:cd03264 78 PQEFGVYPNFTVREFLdyiawLKGIPSKEVKARVDEVLELV-NLGDRAKKKI----GSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181651 161 MMDEPSLGLAPILVSEVFEVIQKINQEGTTIL---LVEQNALGALKVAhygyVLETGQIVLEG 220
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELGEDRIVILsthIVEDVESLCNQVA----VLNKGKLVFEG 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-220 |
1.01e-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: 107.58 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 25 DLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPahvINRMGIALVPEGRRIFPELTVYENLMMG 104
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP---PADRPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 105 A-----YNRKDKEGIKRDLEWIfslfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFE 179
Cdd:cd03298 95 LspglkLTAEDRQAIEVALARV-----GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490181651 180 VIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEG 220
Cdd:cd03298 170 LVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-235 |
1.10e-28 |
|
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: 112.94 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYY--GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIA 83
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR-IA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 84 LVPEGRRIFPElTVYENLMMGAYNRKDKEgIKRDLE------WIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRP 157
Cdd:COG4987 413 VVPQRPHLFDT-TLRENLRLARPDATDEE-LWAALErvglgdWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181651 158 KLLMMDEPSLGLAPILVSEVFEVIQKINQeGTTILLVEQNALGALKVAHYgYVLETGQIVLEGKASELL-DNEMVRKAY 235
Cdd:COG4987 491 PILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLERMDRI-LVLEDGRIVEQGTHEELLaQNGRYRQLY 567
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-228 |
2.77e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 108.99 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYY----GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQ---KGKIIFNGQDITNKPAHVI 77
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 78 NRMGialvpeGRR---IF--------PELTVYENLMMG--AYNRKDKEGIKRDLEWIFSL--FPRLKERLKQLGGTLSGG 142
Cdd:COG0444 81 RKIR------GREiqmIFqdpmtslnPVMTVGDQIAEPlrIHGGLSKAEARERAIELLERvgLPDPERRLDRYPHELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 143 EQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNaLGALK-VAHYGYVLETGQIVLEG 220
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHD-LGVVAeIADRVAVMYAGRIVEEG 233
|
....*...
gi 490181651 221 KASELLDN 228
Cdd:COG0444 234 PVEELFEN 241
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-194 |
5.11e-28 |
|
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: 106.36 E-value: 5.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYY----GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNkpahv 76
Cdd:COG4181 4 SSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 77 INRMGIALVpEGRRI------F---PELTVYENLMMGAYNRKDKEGIKRDLEWIfslfPR--LKERLKQLGGTLSGGEQQ 145
Cdd:COG4181 79 LDEDARARL-RARHVgfvfqsFqllPTLTALENVMLPLELAGRRDARARARALL----ERvgLGHRLDHYPAQLSGGEQQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 146 MLAIGRALMSRPKLLMMDEPSLGL-----APILvsevfEVIQKINQE-GTTILLV 194
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLdaatgEQII-----DLLFELNRErGTTLVLV 203
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-217 |
1.46e-27 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 104.68 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 24 IDLKVPrGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNkpahviNRMGIALVPEGRRI---------FPE 94
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD------SRKKINLPPQQRKIglvfqqyalFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 95 LTVYENLMMGAYNRKDKEgIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILV 174
Cdd:cd03297 90 LNVRENLAFGLKRKRNRE-DRISVDELLDLL-GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490181651 175 SEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIV 217
Cdd:cd03297 168 LQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
15-197 |
2.12e-27 |
|
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: 103.85 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 15 YGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQD---ITNKPAHVINRMGIALVPEGRRI 91
Cdd:TIGR03608 8 FGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQEtppLNSKKASKFRREKLGYLFQNFAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 92 FPELTVYENLMMGAYNRKDKEGIKRDLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAP 171
Cdd:TIGR03608 88 IENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDP 167
|
170 180
....*....|....*....|....*.
gi 490181651 172 ILVSEVFEVIQKINQEGTTILLVEQN 197
Cdd:TIGR03608 168 KNRDEVLDLLLELNDEGKTIIIVTHD 193
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-228 |
2.58e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 105.05 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDIT---------- 70
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 71 --NKPAHVINRMGIALVPEGRRIFPELTVYENLM------MGAYNRKDKEGIKRDLEWIfslfpRLKERLKQ-LGGTLSG 141
Cdd:PRK10619 81 vaDKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMeapiqvLGLSKQEARERAVKYLAKV-----GIDERAQGkYPVHLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 142 GEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGK 221
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
....*..
gi 490181651 222 ASELLDN 228
Cdd:PRK10619 236 PEQLFGN 242
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
15-225 |
4.11e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 106.34 E-value: 4.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 15 YGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPahvINRMGIALVPEGRRIFPE 94
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS---IQQRDICMVFQSYALFPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 95 LTVYENL-----MMGaynrKDKEGIKRdlewifslfpRLKERLK--QLGG-------TLSGGEQQMLAIGRALMSRPKLL 160
Cdd:PRK11432 93 MSLGENVgyglkMLG----VPKEERKQ----------RVKEALElvDLAGfedryvdQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181651 161 MMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASEL 225
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-227 |
6.24e-27 |
|
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: 102.61 E-value: 6.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGL--VRAQKGKIIFNGQDITNKPAHVINRMGIa 83
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 84 lvpegrrifpeltvyenlMMGAYNRKDKEGIKrdlewifslfprLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMD 163
Cdd:cd03217 80 ------------------FLAFQYPPEIPGVK------------NADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 164 EPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNA-LGALKVAHYGYVLETGQIVLEGKASELLD 227
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQrLLDYIKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-236 |
7.95e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.54 E-value: 7.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYG-AIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVIN- 78
Cdd:PRK13636 1 MEDYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 79 --RMGIALVPEGRRIFpELTVYENLMMGAYNRK-DKEGIKRDLEWIFSL--FPRLKERLKQlggTLSGGEQQMLAIGRAL 153
Cdd:PRK13636 81 reSVGMVFQDPDNQLF-SASVYQDVSFGAVNLKlPEDEVRKRVDNALKRtgIEHLKDKPTH---CLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 154 MSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELL-DNEMV 231
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFaEKEML 236
|
....*
gi 490181651 232 RKAYL 236
Cdd:PRK13636 237 RKVNL 241
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-230 |
8.60e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 105.68 E-value: 8.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDItnkPAHV-INR 79
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV---PARArLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 80 MGIALVPEGRRIFPELTVYENLMM-GAYNRKDKegikRDLEWIF-SL--FPRLKERLKQLGGTLSGGEQQMLAIGRALMS 155
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVfGRYFGMST----REIEAVIpSLleFARLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 156 RPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEM 230
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHI 264
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-165 |
1.52e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 105.41 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPA---HVi 77
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAenrHV- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 78 nrmgiALVPEGRRIFPELTVYENLMMGAYNRK-DKEGIKrdlewifslfPRLKERLK--QLGGT-------LSGGEQQML 147
Cdd:PRK09452 89 -----NTVFQSYALFPHMTVFENVAFGLRMQKtPAAEIT----------PRVMEALRmvQLEEFaqrkphqLSGGQQQRV 153
|
170
....*....|....*...
gi 490181651 148 AIGRALMSRPKLLMMDEP 165
Cdd:PRK09452 154 AIARAVVNKPKVLLLDES 171
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-194 |
1.67e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.65 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 3 DIVLEVQSLHVY-YGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMG 81
Cdd:COG3845 255 EVVLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 82 IALVPEGRR---IFPELTVYENLMMGAYNRK--------DKEGIKRDLEwifslfpRLKER-------LKQLGGTLSGGE 143
Cdd:COG3845 335 VAYIPEDRLgrgLVPDMSVAENLILGRYRRPpfsrggflDRKAIRAFAE-------ELIEEfdvrtpgPDTPARSLSGGN 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181651 144 QQMLAIGRALMSRPKLLMMDEPSLGL---ApilVSEVFEVIQKINQEGTTILLV 194
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLdvgA---IEFIHQRLLELRDAGAAVLLI 458
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-194 |
2.00e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.40 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQ---KGKIIFNGQDITNKPAHvinRMGI 82
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE---QRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 83 ALVPEGRRIFPELTVYENLMMG---AYNRKDKegikRDlewifslfpRLKERLKQLG---------GTLSGGEQQMLAIG 150
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFAlppTIGRAQR----RA---------RVEQALEEAGlagfadrdpATLSGGQRARVALL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490181651 151 RALMSRPKLLMMDEPSLGLAPILVSEVFE-VIQKINQEGTTILLV 194
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLV 190
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-223 |
2.81e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 102.01 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSdivLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKI-IFNGQ-DITNKP-AHVI 77
Cdd:PRK11124 1 MS---IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLnIAGNHfDFSKTPsDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 78 N--RMGIALVPEGRRIFPELTVYENLM---MGAYNRKDKEGIKRDLEWIFSLfpRLKERLKQLGGTLSGGEQQMLAIGRA 152
Cdd:PRK11124 78 RelRRNVGMVFQQYNLWPHLTVQQNLIeapCRVLGLSKDQALARAEKLLERL--RLKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181651 153 LMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKAS 223
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-223 |
2.93e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.01 E-value: 2.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQ--DITNKPAHVINRM--- 80
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAIRLlrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 GIALVPEGRRIFPELTVYENLM---MGAYNRKDKEGIKRDLEWIFSLfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRP 157
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIeapCKVLGLSKEQAREKAMKLLARL--RLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181651 158 KLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKAS 223
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-227 |
5.50e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 101.30 E-value: 5.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGL--VRAQKGKIIFNGQDITNKPAHVINRMGIA 83
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 84 LV----PEgrriFPELTVyENLMMGAYNRKDKEGIKrdlewIFSLFPRLKERLKQLG-----------GTLSGGEQ---- 144
Cdd:COG0396 81 LAfqypVE----IPGVSV-SNFLRTALNARRGEELS-----AREFLKLLKEKMKELGldedfldryvnEGFSGGEKkrne 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 145 --QMLAIgralmsRPKLLMMDEPSLGL---ApilVSEVFEVIQKINQEGTTILLV-EQNALGALKVAHYGYVLETGQIVL 218
Cdd:COG0396 151 ilQMLLL------EPKLAILDETDSGLdidA---LRIVAEGVNKLRSPDRGILIItHYQRILDYIKPDFVHVLVDGRIVK 221
|
....*....
gi 490181651 219 EGKAsELLD 227
Cdd:COG0396 222 SGGK-ELAL 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-237 |
5.68e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 101.66 E-value: 5.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQK------GKIIFNGQDITNKPAhVIN 78
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIFQIDA-IKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 79 RMGIALVPEGRRIFPELTVYENLM--MGAYNRKDKEGIKRDLEWIF---SLFPRLKERLKQLGGTLSGGEQQMLAIGRAL 153
Cdd:PRK14246 89 RKEVGMVFQQPNPFPHLSIYDNIAypLKSHGIKEKREIKKIVEECLrkvGLWKEVYDRLNSPASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 154 MSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEgTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELL---DNEM 230
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFtspKNEL 247
|
....*..
gi 490181651 231 VRKAYLG 237
Cdd:PRK14246 248 TEKYVIG 254
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-227 |
8.52e-26 |
|
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: 100.38 E-value: 8.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 14 YYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIALVPEGRRIFP 93
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM-IGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 94 ElTVYENLMMGAYNRKDKEGIK-----RDLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLG 168
Cdd:cd03254 91 G-TIMENIRLGRPNATDEEVIEaakeaGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181651 169 LAPILVSEVFEVIQKINQEGTTILLVEQnaLGALKVAHYGYVLETGQIVLEGKASELLD 227
Cdd:cd03254 170 IDTETEKLIQEALEKLMKGRTSIIIAHR--LSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-235 |
1.18e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 100.58 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIALV 85
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARR-RAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRI-FPeLTVYENLMMGAY-----NRKDKEGIKR-----DLEwifslfpRLKERLKQlggTLSGGEQQMLAIGRAL- 153
Cdd:COG4559 81 PQHSSLaFP-FTVEEVVALGRAphgssAAQDRQIVREalalvGLA-------HLAGRSYQ---TLSGGEQQRVQLARVLa 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 154 ------MSRPKLLMMDEP--SLGLAPILvsEVFEVIQKINQEGTTILLV--EQN--ALGALKVAhygyVLETGQIVLEGK 221
Cdd:COG4559 150 qlwepvDGGPRWLFLDEPtsALDLAHQH--AVLRLARQLARRGGGVVAVlhDLNlaAQYADRIL----LLHQGRLVAQGT 223
|
250
....*....|....
gi 490181651 222 ASELLDNEMVRKAY 235
Cdd:COG4559 224 PEEVLTDELLERVY 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-232 |
1.55e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.61 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHvinRMGIAL 84
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY---QRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 VPEGRRIFPELTVYENLMMG-AYNRKDKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMD 163
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGlKQDKLPKAEIASRVNEMLGLV-HMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 164 EPSLGLAPILVSEV-FEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMVR 232
Cdd:PRK11607 175 EPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-236 |
1.60e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.92 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYY-GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVIN---RM 80
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEvrkTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 GIALVPEGRRIFPElTVYENLMMGAYNRK-DKEGIKRdlewifslfpRLKERLKQLGGT---------LSGGEQQMLAIG 150
Cdd:PRK13639 81 GIVFQNPDDQLFAP-TVEEDVAFGPLNLGlSKEEVEK----------RVKEALKAVGMEgfenkpphhLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 151 RALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELL-DNE 229
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFsDIE 229
|
....*..
gi 490181651 230 MVRKAYL 236
Cdd:PRK13639 230 TIRKANL 236
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-224 |
2.44e-25 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 101.87 E-value: 2.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 24 IDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGqditnkpaHVIN--RMGIALVPEGRRI---------F 92
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG--------RVLFdaEKGICLPPEKRRIgyvfqdarlF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 93 PELTVYENLMMGaYNRKDKEgikrDLEWIFSLFPrLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEP--SLGLa 170
Cdd:PRK11144 89 PHYKVRGNLRYG-MAKSMVA----QFDKIVALLG-IEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPlaSLDL- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 171 PiLVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASE 224
Cdd:PRK11144 162 P-RKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-238 |
6.54e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.11 E-value: 6.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSL-HVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINR-MGI 82
Cdd:PRK13652 3 LIETRDLcYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKfVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 83 ALVPEGRRIFPElTVYENLMMGAYNRK-DKEGIKRDLEWIFSLFPrLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLM 161
Cdd:PRK13652 83 VFQNPDDQIFSP-TVEQDIAFGPINLGlDEETVAHRVSSALHMLG-LEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181651 162 MDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASEL-LDNEMVRKAYLGV 238
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPDLLARVHLDL 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-228 |
7.09e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 98.67 E-value: 7.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIvlEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAI-------AGLVRAqkGKIIFNGQDITNKP 73
Cdd:PRK11264 1 MSAI--EVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRV--GDITIDTARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 74 AHVIN--RMGIALVPEGRRIFPELTVYENLMMGAYNRKdkeGIKRDlewifSLFPRLKERLKQLGGT---------LSGG 142
Cdd:PRK11264 77 KGLIRqlRQHVGFVFQNFNLFPHRTVLENIIEGPVIVK---GEPKE-----EATARARELLAKVGLAgketsyprrLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 143 EQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKA 222
Cdd:PRK11264 149 QQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
|
....*.
gi 490181651 223 SELLDN 228
Cdd:PRK11264 229 KALFAD 234
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-226 |
1.02e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 99.77 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYY----GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPahvinrmG 81
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALS-------E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 82 IALVPEGRRI---------FPELTVYENLmmgAY----NRKDKEGIKRdlewifslfpRLKERLKQLG---------GTL 139
Cdd:COG1135 75 RELRAARRKIgmifqhfnlLSSRTVAENV---ALpleiAGVPKAEIRK----------RVAELLELVGlsdkadaypSQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 140 SGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLV--EQNALGAL--KVAhygyVLETG 214
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLIthEMDVVRRIcdRVA----VLENG 217
|
250
....*....|..
gi 490181651 215 QIVLEGKASELL 226
Cdd:COG1135 218 RIVEQGPVLDVF 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-197 |
1.15e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.92 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVR-----AQKGKIIFNGQDITNKPAH 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 76 VIN-RMGIALVPEGRRIFPeLTVYENLMMGAYNR--KDKEGIKRDLEWIF---SLFPRLKERLKQLGGTLSGGEQQMLAI 149
Cdd:PRK14239 81 TVDlRKEIGMVFQQPNPFP-MSIYENVVYGLRLKgiKDKQVLDEAVEKSLkgaSIWDEVKDRLHDSALGLSGGQQQRVCI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490181651 150 GRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEgTTILLVEQN 197
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRS 206
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-235 |
2.20e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.15 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 4 IVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIA 83
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR-RA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 84 LVPEGRRI-FPeLTVYENLMMGAY-----NRKDKEGIKR-----DLEwifslfpRLKERLKQlggTLSGGEQQMLAIGRA 152
Cdd:PRK13548 80 VLPQHSSLsFP-FTVEEVVAMGRAphglsRAEDDALVAAalaqvDLA-------HLAGRDYP---QLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 153 LM------SRPKLLMMDEP--SLGLApilvsevfeviqkiNQEGT-TIL--LVEQNALGALKV-------AHYG---YVL 211
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPtsALDLA--------------HQHHVlRLArqLAHERGLAVIVVlhdlnlaARYAdriVLL 214
|
250 260
....*....|....*....|....
gi 490181651 212 ETGQIVLEGKASELLDNEMVRKAY 235
Cdd:PRK13548 215 HQGRLVADGTPAEVLTPETLRRVY 238
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-239 |
3.51e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.19 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 25 DLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPahvINRMGIALVPEGRRIFPELTVYENLMMG 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP---PSRRPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 105 --------AYNRKDKEGIKRDLewifslfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSE 176
Cdd:PRK10771 96 lnpglklnAAQREKLHAIARQM--------GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181651 177 VFEVIQKI-NQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMVRKAYLGVA 239
Cdd:PRK10771 168 MLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLGIK 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-236 |
6.18e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 96.73 E-value: 6.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 3 DIVLEVQSLHVYY-GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVI-NRM 80
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 GIALVPEGRRIFpELTVYENLMMGAYN-RKDKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKL 159
Cdd:PRK13647 82 GLVFQDPDDQVF-SSTVWDDVAFGPVNmGLDKDEVERRVEEALKAV-RMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181651 160 LMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMVRKAYL 236
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQAGL 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-197 |
1.31e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.49 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIV--LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTL------SAIAGLVRAQkGKIIFNGQDITNK 72
Cdd:PRK14258 1 MSKLIpaIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLkclnrmNELESEVRVE-GRVEFFNQNIYER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 73 PAHvINRM--GIALVPEGRRIFPeLTVYENL-----MMGAYNRKDKEGIKRDLEWIFSLFPRLKERLKQLGGTLSGGEQQ 145
Cdd:PRK14258 80 RVN-LNRLrrQVSMVHPKPNLFP-MSVYDNVaygvkIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490181651 146 MLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKIN-QEGTTILLVEQN 197
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHN 210
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-194 |
2.22e-23 |
|
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: 97.82 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYY-GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIAL 84
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-VSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 VPEGRRIFpELTVYENLMMGAYNRKDKEgIKRDLE------WIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPK 158
Cdd:TIGR02868 414 CAQDAHLF-DTTVRENLRLARPDATDEE-LWAALErvgladWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAP 491
|
170 180 190
....*....|....*....|....*....|....*.
gi 490181651 159 LLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLV 194
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADELLEDLLAALSGRTVVLIT 527
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-235 |
2.47e-23 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 94.38 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 3 DIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKII------FNGQDITN-KPah 75
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWElRK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 76 vinRMGI---ALvpeGRRIFPELTVYENLM------MGAYNRKDKEGIKRDLEWIFSLfpRLKERLKQLGGTLSGGEQQM 146
Cdd:COG1119 79 ---RIGLvspAL---QLRFPRDETVLDVVLsgffdsIGLYREPTDEQRERARELLELL--GLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 147 LAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEG-TTILLveqnalgalkVAHY----------GYVLETGQ 215
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVL----------VTHHveeippgithVLLLKDGR 220
|
250 260
....*....|....*....|
gi 490181651 216 IVLEGKASELLDNEMVRKAY 235
Cdd:COG1119 221 VVAAGPKEEVLTSENLSEAF 240
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-228 |
3.45e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 97.54 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 14 YYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIALVPEGRRIFp 93
Cdd:COG1132 349 YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ-IGVVPQDTFLF- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 94 ELTVYENLMMGAYNRKDKEgIKRDL------EWIFSLfP-----RLKERlkqlGGTLSGGEQQMLAIGRALMSRPKLLMM 162
Cdd:COG1132 427 SGTIRENIRYGRPDATDEE-VEEAAkaaqahEFIEAL-PdgydtVVGER----GVNLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181651 163 DEPSLGLAPILVSEVFEVIQKINQEGTTILLveqnA--LGALKVAHYGYVLETGQIVLEGKASELLDN 228
Cdd:COG1132 501 DEATSALDTETEALIQEALERLMKGRTTIVI----AhrLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-232 |
1.04e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.01 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 14 YYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGIALVPEGRRIFP 93
Cdd:PRK09700 14 SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQELSVID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 94 ELTVYENLMMGAYNRKDKEGIK-------RDLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPS 166
Cdd:PRK09700 94 ELTVLENLYIGRHLTKKVCGVNiidwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181651 167 LGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMVR 232
Cdd:PRK09700 174 SSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-194 |
1.25e-22 |
|
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: 91.07 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQ--KGKIIFNGqdiTNKPAHVINRMgIALVPEGRRIFPELTVY 98
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLING---RPLDKRSFRKI-IGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 99 ENLMMGAynrkdkegikrdlewifslfprlkeRLKQlggtLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVF 178
Cdd:cd03213 101 ETLMFAA-------------------------KLRG----LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170
....*....|....*.
gi 490181651 179 EVIQKINQEGTTILLV 194
Cdd:cd03213 152 SLLRRLADTGRTIICS 167
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-194 |
1.48e-22 |
|
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: 95.43 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 2 SDIVLEVQSL-HVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVInRM 80
Cdd:TIGR02857 318 PASSLEFSGVsVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 GIALVPEGRRIFPElTVYENLMMGAYNRKDKEgIKRDL------EWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALM 154
Cdd:TIGR02857 397 QIAWVPQHPFLFAG-TIAENIRLARPDASDAE-IREALeragldEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490181651 155 SRPKLLMMDEPSLGLAPILVSEVFEVIQKINQeGTTILLV 194
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLV 513
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-229 |
4.22e-22 |
|
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: 90.68 E-value: 4.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNkpahvIN----RMGIALVPEGRRIFpELT 96
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRD-----LNlrwlRSQIGLVSQEPVLF-DGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 97 VYENLMMGAYNRKDKEGIK--RD---LEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAp 171
Cdd:cd03249 93 IAENIRYGKPDATDEEVEEaaKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALD- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181651 172 ilvSEVFEVIQK-INQ--EGTTILLVEQNaLGALKVAHYGYVLETGQIVLEGKASELLDNE 229
Cdd:cd03249 172 ---AESEKLVQEaLDRamKGRTTIVIAHR-LSTIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-214 |
4.94e-22 |
|
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: 90.60 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITnKPAHviNRMgiaLVPEGRRIFPELTVYEN 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-EPGP--DRM---VVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 101 L------MMGAYNRKDKEGIKRD-LEWIfslfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPIL 173
Cdd:TIGR01184 75 IalavdrVLPDLSKSERRAIVEEhIALV-----GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490181651 174 VSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETG 214
Cdd:TIGR01184 150 RGNLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-196 |
5.85e-22 |
|
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: 90.02 E-value: 5.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQK---GKIIFNGQDitNKPAHVINRmgIALVPEGRRIFPELTV 97
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQP--RKPDQFQKC--VAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 98 YENLMMGAYNR---KDKEGIKRDLEWIFSLfprLKERLKQLGGT----LSGGEQQMLAIGRALMSRPKLLMMDEPSLGLA 170
Cdd:cd03234 99 RETLTYTAILRlprKSSDAIRKKRVEDVLL---RDLALTRIGGNlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180
....*....|....*....|....*..
gi 490181651 171 PILVSEVFEVIQKINQEGTTILL-VEQ 196
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILtIHQ 202
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-238 |
7.51e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 91.26 E-value: 7.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 20 AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVIN-RMGIALV---PEgRRIFPEl 95
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDiRKKVGLVfqyPE-YQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 96 TVYENLMMGAYNRK-DKEGIKRdlewifslfpRLKERLKQLGGT-----------LSGGEQQMLAIGRALMSRPKLLMMD 163
Cdd:PRK13637 100 TIEKDIAFGPINLGlSEEEIEN----------RVKRAMNIVGLDyedykdkspfeLSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181651 164 EPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDN-EMVRKAYLGV 238
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEvETLESIGLAV 246
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-220 |
8.34e-22 |
|
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: 90.08 E-value: 8.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 15 YGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQD-ITNKPAHViNRMGIALvpeGRR--I 91
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpWKRRKKFL-RRIGVVF---GQKtqL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 92 FPELTVYENL-MMGAYNRKDKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLA 170
Cdd:cd03267 107 WWDLPVIDSFyLLAAIYDLPPARFKKRLDELSELL-DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490181651 171 PILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEG 220
Cdd:cd03267 186 VVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-235 |
8.78e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.46 E-value: 8.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIALV 85
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEgRRIFPE-LTVYE---------NLMMGAYNRKDKEGIKRDLEWIfslfpRLKERLKQLGGTLSGGEQQMLAIGRALMS 155
Cdd:PRK11231 82 PQ-HHLTPEgITVRElvaygrspwLSLWGRLSAEDNARVNQAMEQT-----RINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 156 RPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMVRKAY 235
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVF 235
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-239 |
1.04e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 90.59 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 24 IDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDItnkPAHVINRM-----GIALVPEGRRIFPELTVY 98
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI---PAMSRSRLytvrkRMSMLFQSGALFTDMNVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 99 ENLmmgAYNRKDKEGIKRDLewifsLFPRLKERLKQLG---------GTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGL 169
Cdd:PRK11831 103 DNV---AYPLREHTQLPAPL-----LHSTVMMKLEAVGlrgaaklmpSELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181651 170 APILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNE--MVRKAYLGVA 239
Cdd:PRK11831 175 DPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPdpRVRQFLDGIA 247
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-224 |
1.50e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 91.40 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 7 EVQSLH-VYYGA---IHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHvinrmgi 82
Cdd:PRK11153 3 ELKNISkVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEK------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 83 ALVPEGRRI------FPEL---TVYEN--LMMGAYNrKDKEGIKRdlewifslfpRLKERLKQLGGT---------LSGG 142
Cdd:PRK11153 76 ELRKARRQIgmifqhFNLLssrTVFDNvaLPLELAG-TPKAEIKA----------RVTELLELVGLSdkadrypaqLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 143 EQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLV--EQNALGAL--KVAhygyVLETGQIV 217
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLIthEMDVVKRIcdRVA----VIDAGRLV 220
|
....*..
gi 490181651 218 LEGKASE 224
Cdd:PRK11153 221 EQGTVSE 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-165 |
3.20e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 89.15 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYG----AIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAhviNRmg 81
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA---DR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 82 iALVPEGRRIFPELTVYENLMMGAYNRKDKEGIKRDlewifslfpRLKERLKQLG---------GTLSGGEQQMLAIGRA 152
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRA---------RAEELLALVGladfarrriWQLSGGMRQRVGIARA 148
|
170
....*....|...
gi 490181651 153 LMSRPKLLMMDEP 165
Cdd:COG4525 149 LAADPRFLLMDEP 161
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-194 |
5.57e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 87.53 E-value: 5.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYG----AIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDIT--NKPAHVIN 78
Cdd:PRK10584 6 IVEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 79 RM-GIALVPEGRRIFPELTVYEN-----LMMGAYNRKDKEGIKRDLEWIfslfpRLKERLKQLGGTLSGGEQQMLAIGRA 152
Cdd:PRK10584 86 RAkHVGFVFQSFMLIPTLNALENvelpaLLRGESSRQSRNGAKALLEQL-----GLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490181651 153 LMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLV 194
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILV 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-165 |
5.88e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFnGQDITnkpahvinrm 80
Cdd:COG0488 311 LGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK---------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 gIALVPEGRRIF-PELTVYENLMMGAYNRKDKEgIKRDLEWiFsLFPRlkERLKQLGGTLSGGEQQMLAIGRALMSRPKL 159
Cdd:COG0488 380 -IGYFDQHQEELdPDKTVLDELRDGAPGGTEQE-VRGYLGR-F-LFSG--DDAFKPVGVLSGGEKARLALAKLLLSPPNV 453
|
....*.
gi 490181651 160 LMMDEP 165
Cdd:COG0488 454 LLLDEP 459
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-220 |
6.41e-21 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 87.26 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 18 IHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVInRMGIALVPEGRRIFPElTV 97
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL-RRNIGYVPQDVTLFYG-TL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 98 YENLMMGAYNRKDKEgIKRDLEWI------------FSLfpRLKERlkqlGGTLSGGEQQMLAIGRALMSRPKLLMMDEP 165
Cdd:cd03245 95 RDNITLGAPLADDER-ILRAAELAgvtdfvnkhpngLDL--QIGER----GRGLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 166 SLGLAPILVSEVFEVIQKINQEGTTILLVEQNALgaLKVAHYGYVLETGQIVLEG 220
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLLGDKTLIIITHRPSL--LDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-227 |
8.99e-21 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 87.29 E-value: 8.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 20 AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIALVPEGRRIFPElTVYE 99
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-IGLVSQDVFLFND-TVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 100 NLMMGAYNRKDKEGIK-----RDLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLApiLV 174
Cdd:cd03251 95 NIAYGRPGATREEVEEaaraaNAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALD--TE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 175 SE--VFEVIQKINQEGTTILLVEQnaLGALKVAHYGYVLETGQIVLEGKASELLD 227
Cdd:cd03251 173 SErlVQAALERLMKNRTTFVIAHR--LSTIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-238 |
1.76e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.99 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKgkiifngqditnKPAHVINRMGIAL 84
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK------------SAGSHIELLGRTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 VPEGRR-------------IFPE------LTVYENLMMGAYnrkdkeGIKRDLEWIFSLFPRLKER-----LKQLG---- 136
Cdd:PRK09984 72 QREGRLardirksrantgyIFQQfnlvnrLSVLENVLIGAL------GSTPFWRTCFSWFTREQKQralqaLTRVGmvhf 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 137 -----GTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQ-EGTTILLVEQNALGALKVAHYGYV 210
Cdd:PRK09984 146 ahqrvSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVA 225
|
250 260
....*....|....*....|....*...
gi 490181651 211 LETGQIVLEGkASELLDNEMVRKAYLGV 238
Cdd:PRK09984 226 LRQGHVFYDG-SSQQFDNERFDHLYRSI 252
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-211 |
1.84e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 85.77 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgiAL 84
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQL--CF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 VPEGRRIFPELTVYENLMMGAYNRKDKEGIKrDLEWIFSlfprLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDIHFSPGAVGIT-ELCRLFS----LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490181651 165 PSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVL 211
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKADYEEYHL 200
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-193 |
2.09e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.08 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 14 YYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVIN--RMGIALVPEGRRI 91
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflRRQIGMIFQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 92 FPELTVYENLMM-----GAYNRKDKEGIKRDLEWIfslfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPS 166
Cdd:PRK10908 91 LMDRTVYDNVAIpliiaGASGDDIRRRVSAALDKV-----GLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180
....*....|....*....|....*..
gi 490181651 167 LGLAPILVSEVFEVIQKINQEGTTILL 193
Cdd:PRK10908 166 GNLDDALSEGILRLFEEFNRVGVTVLM 192
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-239 |
2.67e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.96 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 20 AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITN--KPAHVINRMGIALV-PEGRriFPELT 96
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfsKLQGIRKLVGIVFQnPETQ--FVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 97 VYENLMMGAYNR-----KDKEGIKRDLEWIfslfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAP 171
Cdd:PRK13644 95 VEEDLAFGPENLclppiEIRKRVDRALAEI-----GLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181651 172 ILVSEVFEVIQKINQEGTTILLVEQNaLGALKVAHYGYVLETGQIVLEGKASELLDNEMVRkaYLGVA 239
Cdd:PRK13644 170 DSGIAVLERIKKLHEKGKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQ--TLGLT 234
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-235 |
3.65e-20 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 85.85 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQ--KGKIIFNGQDITNKPAHVIN 78
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 79 RMGIALVPEGRRIFPELTvYENLMMGAYNRKDKEGIKRDLEWIfSLFPRLKERLKQLGGT-----------LSGGEQQML 147
Cdd:CHL00131 83 HLGIFLAFQYPIEIPGVS-NADFLRLAYNSKRKFQGLPELDPL-EFLEIINEKLKLVGMDpsflsrnvnegFSGGEKKRN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 148 AIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVE--QNALGALKvAHYGYVLETGQIVLEGKASel 225
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILIThyQRLLDYIK-PDYVHVMQNGKIIKTGDAE-- 237
|
250
....*....|
gi 490181651 226 LDNEMVRKAY 235
Cdd:CHL00131 238 LAKELEKKGY 247
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-165 |
4.84e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.06 E-value: 4.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSdivLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNkpAHVINRM 80
Cdd:PRK10851 1 MS---IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARDRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 gIALVPEGRRIFPELTVYENLMMG-----AYNRKDKEGIKRDLEWIFSL--FPRLKERLKqlgGTLSGGEQQMLAIGRAL 153
Cdd:PRK10851 76 -VGFVFQHYALFRHMTVFDNIAFGltvlpRRERPNAAAIKAKVTQLLEMvqLAHLADRYP---AQLSGGQKQRVALARAL 151
|
170
....*....|..
gi 490181651 154 MSRPKLLMMDEP 165
Cdd:PRK10851 152 AVEPQILLLDEP 163
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-220 |
5.14e-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: 83.90 E-value: 5.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYG--AIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVinRMGIA 83
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL--SSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 84 LVPEGRRIFpELTVYENLmmgaynrkdkegikrdlewifslfprlkerlkqlGGTLSGGEQQMLAIGRALMSRPKLLMMD 163
Cdd:cd03247 79 VLNQRPYLF-DTTLRNNL----------------------------------GRRFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181651 164 EPSLGLAPI----LVSEVFEVIqkinqEGTTILLVEQNALGalkVAHYG--YVLETGQIVLEG 220
Cdd:cd03247 124 EPTVGLDPIterqLLSLIFEVL-----KDKTLIWITHHLTG---IEHMDkiLFLENGKIIMQG 178
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-165 |
6.62e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 86.82 E-value: 6.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 14 YYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITN-KPAhviNRmGIALVPEGRRIF 92
Cdd:PRK11650 13 YDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElEPA---DR-DIAMVFQNYALY 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181651 93 PELTVYENLMMGAYNRK-DKEGIKRDLE---WIFSLFPRLKERLKQlggtLSGGEQQMLAIGRALMSRPKLLMMDEP 165
Cdd:PRK11650 89 PHMSVRENMAYGLKIRGmPKAEIEERVAeaaRILELEPLLDRKPRE----LSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-190 |
7.63e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.68 E-value: 7.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGL--VRAQKGKIIFNGQDITNKPAHVIN 78
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 79 RMGIALVPEGRRIFPELTVYENLMMGayNRKDKEGIKRDLEwifsLFPRLKERLKQLG---------GTLSGGEQQMLAI 149
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLG--NEITPGGIMDYDA----MYLRAQKLLAQLKldinpatpvGNLGLGQQQLVEI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490181651 150 GRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTT 190
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIA 195
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-194 |
1.24e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.91 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 3 DIVLEVQSLHVYYGAIHAIKGID---LKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQK-GKIIFNGQDIT-NKPAHVI 77
Cdd:PRK13549 257 EVILEVRNLTAWDPVNPHIKRVDdvsFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKiRNPQQAI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 78 nRMGIALVPEGRR---IFPELTVYENLMMGAYNRKDKEGI---KRDLEWIFSLFPRLKER---LKQLGGTLSGGEQQMLA 148
Cdd:PRK13549 337 -AQGIAMVPEDRKrdgIVPVMGVGKNITLAALDRFTGGSRiddAAELKTILESIQRLKVKtasPELAIARLSGGNQQKAV 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490181651 149 IGRALMSRPKLLMMDEPSLGlapILVSEVFEVIQKINQ---EGTTILLV 194
Cdd:PRK13549 416 LAKCLLLNPKILILDEPTRG---IDVGAKYEIYKLINQlvqQGVAIIVI 461
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-238 |
1.41e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.80 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 20 AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDIT----NKPAHVInRMGIALV---PEGRrIF 92
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstskNKDIKQI-RKKVGLVfqfPESQ-LF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 93 PElTVYENLMMGAYN----RKDKEGIKRDLEWIFSLFPRLKERLKqlgGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLG 168
Cdd:PRK13649 100 EE-TVLKDVAFGPQNfgvsQEEAEALAREKLALVGISESLFEKNP---FELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181651 169 LAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELL-DNEMVRKAYLGV 238
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFqDVDFLEEKQLGV 246
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-194 |
1.59e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.05 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 15 YGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIifngqditnkpaHVINRMGIALVP---EGRRI 91
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGARVAYVPqrsEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 92 FPeLTVYENLMMGA---------YNRKDKEGIKRDLEWIfslfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMM 162
Cdd:NF040873 70 LP-LTVRDLVAMGRwarrglwrrLTRDDRAAVDDALERV-----GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190
....*....|....*....|....*....|..
gi 490181651 163 DEPSLGLAPILVSEVFEVIQKINQEGTTILLV 194
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARGATVVVV 175
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-228 |
1.94e-19 |
|
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: 84.23 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 16 GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPA---HVINRMGIALVPEGRRIF 92
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelRELRRKKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 93 PELTVYENLMMG--AYNRKDKEGIKRDLEWIFSLfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLA 170
Cdd:cd03294 115 PHRTVLENVAFGleVQGVPRAEREERAAEALELV--GLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181651 171 PILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDN 228
Cdd:cd03294 193 PLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-235 |
2.31e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.66 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIALV 85
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRIFPELTVYENLMMG---------AYNRKDKEGIKRDLEWIfslfpRLKERLKQLGGTLSGGEQQMLAIGRALMSR 156
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGrtphrsrfdTWTETDRAAVERAMERT-----GVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181651 157 PKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMVRKAY 235
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAF 236
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-194 |
2.48e-19 |
|
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: 82.93 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 20 AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVInRMGIALVPEGRRIFpELTVYE 99
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL-RSRISIIPQDPVLF-SGTIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 100 NLmmGAYNRKDKEGIKRDLE------WIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPil 173
Cdd:cd03244 97 NL--DPFGEYSDEELWQALErvglkeFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDP-- 172
|
170 180
....*....|....*....|....
gi 490181651 174 vsEVFEVIQKINQE---GTTILLV 194
Cdd:cd03244 173 --ETDALIQKTIREafkDCTVLTI 194
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
15-225 |
3.22e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.08 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 15 YGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAhviNRMGIALVPEGRRIFPE 94
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP---AERGVGMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 95 LTVYENLMMG-AYNRKDKEGIKRDLEW---IFSLFPRLKERLKqlggTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLA 170
Cdd:PRK11000 90 LSVAENMSFGlKLAGAKKEEINQRVNQvaeVLQLAHLLDRKPK----ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490181651 171 PILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASEL 225
Cdd:PRK11000 166 AALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-188 |
3.62e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 85.65 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVR--AQKGKIIFNGQDITNKPAHVINRMGI 82
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 83 ALVPEGRRIFPELTVYENLMMGayNRKDKEGIKRDLEwifSLFPRLKERLKQLG----------GTLSGGEQQMLAIGRA 152
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLG--NEITLPGGRMAYN---AMYLRAKNLLRELQldadnvtrpvGDYGGGQQQLVEIAKA 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 490181651 153 LMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEG 188
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHG 191
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-165 |
6.80e-19 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 83.63 E-value: 6.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYY-----------GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDI 69
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 70 TNKPAHVINRMgialvpegRR----IF--------PELTVYENLM--MGAYNRKDKEGIKRdlewifslfpRLKERLKQL 135
Cdd:COG4608 83 TGLSGRELRPL--------RRrmqmVFqdpyaslnPRMTVGDIIAepLRIHGLASKAERRE----------RVAELLELV 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490181651 136 G----------GTLSGGEQQMLAIGRALMSRPKLLMMDEP 165
Cdd:COG4608 145 GlrpehadrypHEFSGGQRQRIGIARALALNPKLIVCDEP 184
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-165 |
9.16e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.35 E-value: 9.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 8 VQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGqDITnkpahvinrmgIALVPE 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR-----------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 88 GRRIFPELTVYENLMMGAYNRKDKEGIKRDLE-------------------------WifSLFPRLKERLKQLG------ 136
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELRALEAELEELEaklaepdedlerlaelqeefealggW--EAEARAEEILSGLGfpeedl 146
|
170 180 190
....*....|....*....|....*....|...
gi 490181651 137 ----GTLSGGEQQMLAIGRALMSRPKLLMMDEP 165
Cdd:COG0488 147 drpvSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-238 |
9.19e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.86 E-value: 9.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 17 AIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAH-----VINRMGIALVPEGRRI 91
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpVRKKVGVVFQFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 92 FPElTVYENLMMGAYNRK-DKEGIKRDLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLA 170
Cdd:PRK13643 98 FEE-TVLKDVAFGPQNFGiPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181651 171 PILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMVRKAY-LGV 238
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHeLGV 245
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-165 |
9.28e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.05 E-value: 9.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 7 EVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIALVP 86
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKR-LAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 87 EGRRIFPELTVYENLMMGAY-------NRKDKEGIKRDLEWiFSLFPrLKER-LKQlggtLSGGEQQMLAIGRALMSRPK 158
Cdd:COG4604 82 QENHINSRLTVRELVAFGRFpyskgrlTAEDREIIDEAIAY-LDLED-LADRyLDE----LSGGQRQRAFIAMVLAQDTD 155
|
....*..
gi 490181651 159 LLMMDEP 165
Cdd:COG4604 156 YVLLDEP 162
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-194 |
9.37e-19 |
|
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: 81.30 E-value: 9.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGA--IHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVInRMGIA 83
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL-RSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 84 LVPEGRRIFPElTVYENLmmGAYNRKDKEGIKRDLewifslfprlkeRLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMD 163
Cdd:cd03369 86 IIPQDPTLFSG-TIRSNL--DPFDEYSDEEIYGAL------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190
....*....|....*....|....*....|.
gi 490181651 164 EPSLGLAPILVSEVFEVIQKINQeGTTILLV 194
Cdd:cd03369 151 EATASIDYATDALIQKTIREEFT-NSTILTI 180
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-219 |
1.09e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.03 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 4 IVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNgqditNKPAHVInRMGIA 83
Cdd:PRK11247 11 TPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEA-REDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 84 LVPEGRRIFPELTVYENLMMGAynRKD-KEGIKRDLEWIfslfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMM 162
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLGL--KGQwRDAALQALAAV-----GLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490181651 163 DEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLE 219
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-194 |
1.24e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.19 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 24 IDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDIT-NKPAHVInRMGIALVPEGRR---IFPELTVYE 99
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAI-RAGIMLCPEDRKaegIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 100 NLMMGAYNRKDKEGIKRDLEWIFSLFPRLKERLK-------QLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGlapI 172
Cdd:PRK11288 351 NINISARRHHLRAGCLINNRWEAENADRFIRSLNiktpsreQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG---I 427
|
170 180
....*....|....*....|....*
gi 490181651 173 LV---SEVFEVIQKINQEGTTILLV 194
Cdd:PRK11288 428 DVgakHEIYNVIYELAAQGVAVLFV 452
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-229 |
1.29e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 82.98 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 3 DIVLEVQSLHVYYGA-----IHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKI----IFNGQDIT-NK 72
Cdd:PRK13631 19 DIILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNnHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 73 PAHVINRMGIALVPEGRRI------FPEL-----TVYENLMMGAYNRKDKEGIKRDLEWIFSLFPRLKER-LKQLGGTLS 140
Cdd:PRK13631 99 LITNPYSKKIKNFKELRRRvsmvfqFPEYqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 141 GGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEG 220
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
....*....
gi 490181651 221 KASELLDNE 229
Cdd:PRK13631 259 TPYEIFTDQ 267
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-227 |
1.81e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.94 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 19 HAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIA-----GLVRAqkGKIIFNGQDITNKPAHVINrmgiALVPEGRRIFP 93
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrspkGVKGS--GSVLLNGMPIDAKEMRAIS----AYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 94 ELTVYENLMMGAYNRKDKEGIKRDLEwifslfPRLKERLKQLG---------GT------LSGGEQQMLAIGRALMSRPK 158
Cdd:TIGR00955 113 TLTVREHLMFQAHLRMPRRVTKKEKR------ERVDEVLQALGlrkcantriGVpgrvkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 159 LLMMDEPSLGLAPILVSEVFEVIQKINQEGTT-ILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLD 227
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTiICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-216 |
2.47e-18 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 83.34 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 3 DIVLEVQSLHVYYGAIHAIKGID---LKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQ-KGKIIFNGQDI-TNKPAHVI 77
Cdd:TIGR02633 255 DVILEARNLTCWDVINPHRKRVDdvsFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVdIRNPAQAI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 78 nRMGIALVPEGRR---IFPELTVYENLMMGAYNRKDKEGI---KRDLEWIFSLFPRLKERLKQLG---GTLSGGEQQMLA 148
Cdd:TIGR02633 335 -RAGIAMVPEDRKrhgIVPILGVGKNITLSVLKSFCFKMRidaAAELQIIGSAIQRLKVKTASPFlpiGRLSGGNQQKAV 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181651 149 IGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQI 216
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-191 |
2.48e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.13 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGIAL 84
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 VPEGRRIFPELTVYENLMMGaynRKDKEGIKRdLEW--IFSLFPRLKERL------KQLGGTLSGGEQQMLAIGRALMSR 156
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLG---REFVNRFGR-IDWkkMYAEADKLLARLnlrfssDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190
....*....|....*....|....*....|....*
gi 490181651 157 PKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTI 191
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELKSQGRGI 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-194 |
2.72e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQditnkPAHVINRM----- 80
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-----EMRFASTTaalaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 GIALVPEGRRIFPELTVYENLMMGAYNRK----DKEGIKRdlewifslfpRLKERLKQLG---------GTLSGGEQQML 147
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENLYLGQLPHKggivNRRLLNY----------EAREQLEHLGvdidpdtplKYLSIGQRQMV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490181651 148 AIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLV 194
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYV 196
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-171 |
3.95e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.86 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKpAH---VINRmg 81
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADA-RHrraVCPR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 82 IALVPE--GRRIFPELTVYENLmmgaynrkdkegikrdlewifSLFPRL-----KER-------LKQLG---------GT 138
Cdd:NF033858 78 IAYMPQglGKNLYPTLSVFENL---------------------DFFGRLfgqdaAERrrridelLRATGlapfadrpaGK 136
|
170 180 190
....*....|....*....|....*....|...
gi 490181651 139 LSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAP 171
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-236 |
4.93e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.44 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGqditnKPAHVINRMGIAL 84
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-----KPLDYSKRGLLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 VPEGRRIF--PELTVYENLMMG--AYNRKD----KEGIKRDLEWIFSLFPRLKERlKQLGGTLSGGEQQMLAIGRALMSR 156
Cdd:PRK13638 76 RQQVATVFqdPEQQIFYTDIDSdiAFSLRNlgvpEAEITRRVDEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 157 PKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLD-NEMVRKAY 235
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAcTEAMEQAG 234
|
.
gi 490181651 236 L 236
Cdd:PRK13638 235 L 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-234 |
5.02e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 82.47 E-value: 5.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 3 DIVLEVQSLHVYYGAihAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGI 82
Cdd:PRK10982 248 EVILEVRNLTSLRQP--SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGF 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 83 ALVPEGRR---IFPELTVYENLM---MGAYNRK----DKEGIKRDLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRA 152
Cdd:PRK10982 326 ALVTEERRstgIYAYLDIGFNSLisnIRNYKNKvgllDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRW 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 153 LMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMVR 232
Cdd:PRK10982 406 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQNEILR 485
|
..
gi 490181651 233 KA 234
Cdd:PRK10982 486 LA 487
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-228 |
5.78e-18 |
|
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: 82.04 E-value: 5.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYGA----IHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGL----VRAQKGKIIFNGQDITNK 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 73 PAHVINRMgialvpEGRRI---FPE--------LTV----YENLMM-GAYNRKDKEgiKRDLEW-----IfslfPRLKER 131
Cdd:COG4172 82 SERELRRI------RGNRIamiFQEpmtslnplHTIgkqiAEVLRLhRGLSGAAAR--ARALELlervgI----PDPERR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 132 LKQLGGTLSGGEQQ--MLAIgrALMSRPKLLMMDEPSLGL-----APILvsevfEVIQKINQE-GTTILLVEQNaLGAL- 202
Cdd:COG4172 150 LDAYPHQLSGGQRQrvMIAM--ALANEPDLLIADEPTTALdvtvqAQIL-----DLLKDLQRElGMALLLITHD-LGVVr 221
|
250 260
....*....|....*....|....*.
gi 490181651 203 KVAHYGYVLETGQIVLEGKASELLDN 228
Cdd:COG4172 222 RFADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-228 |
6.54e-18 |
|
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: 82.04 E-value: 6.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 3 DIVLEVQSLHVYY-----------GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQkGKIIFNGQDITN 71
Cdd:COG4172 273 PPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 72 KPAHvinrmgiALVPEGRRI---F--------PELTVYENLMmgaynrkdkEGIKrdlewifSLFPRL--KERLKQLGGT 138
Cdd:COG4172 352 LSRR-------ALRPLRRRMqvvFqdpfgslsPRMTVGQIIA---------EGLR-------VHGPGLsaAERRARVAEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 139 L-----------------SGGEQQMLAIGRALMSRPKLLMMDEPslglapilVS--------EVFEVIQKINQE-GTTIL 192
Cdd:COG4172 409 LeevgldpaarhryphefSGGQRQRIAIARALILEPKLLVLDEP--------TSaldvsvqaQILDLLRDLQREhGLAYL 480
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 490181651 193 LVEQNalgaLKV----AHYGYVLETGQIVLEGKASELLDN 228
Cdd:COG4172 481 FISHD----LAVvralAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-193 |
7.24e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 80.90 E-value: 7.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 18 IHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDIT-NKPAHVINrmgIALVpEGRR--IFPE 94
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFkRRKEFARR---IGVV-FGQRsqLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 95 LTVYENL-MMGAYNRKDKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGeQQMLA-IGRALMSRPKLLMMDEPSLGLAPI 172
Cdd:COG4586 111 LPAIDSFrLLKAIYRIPDAEYKKRLDELVELL-DLGELLDTPVRQLSLG-QRMRCeLAAALLHRPKILFLDEPTIGLDVV 188
|
170 180
....*....|....*....|..
gi 490181651 173 LVSEVFEVIQKINQE-GTTILL 193
Cdd:COG4586 189 SKEAIREFLKEYNRErGTTILL 210
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-194 |
9.89e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 81.31 E-value: 9.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 18 IHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGIALVPEGRRIFPELTV 97
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 98 YENLMMGAYNRK----DKEGIKRDLEWIFS-----LFPRLKerlkqlGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLG 168
Cdd:PRK10982 91 MDNMWLGRYPTKgmfvDQDKMYRDTKAIFDeldidIDPRAK------VATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180
....*....|....*....|....*.
gi 490181651 169 LAPILVSEVFEVIQKINQEGTTILLV 194
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKERGCGIVYI 190
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
23-226 |
1.04e-17 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 79.46 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 23 GIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNkpahvinrmgiaLVPEGRRIF---------- 92
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQ------------LDRKQRRAFrrdvqlvfqd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 93 ------PELTVYENLM--MGAYNRKDKEGIKRDLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:TIGR02769 97 spsavnPRMTVRQIIGepLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181651 165 PSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELL 226
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLL 239
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-194 |
1.10e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGIALVPEGRR---IFPELTV 97
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 98 YENL-------------MMGAYNRKDKEGIKRDLEWIFSLfprLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:PRK09700 359 AQNMaisrslkdggykgAMGLFHEVDEQRTAENQRELLAL---KCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190
....*....|....*....|....*....|
gi 490181651 165 PSLGLAPILVSEVFEVIQKINQEGTTILLV 194
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDGKVILMV 465
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-229 |
1.25e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.13 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 17 AIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDI-TNKPAHVINRMGIALV---PEGRRI- 91
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEkNKKKTKEKEKVLEKLViqkTRFKKIk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 92 --------------FPEL-----TVYENLMMGA--YNRKDKEGIKRDLEWIfSLFPRLKERLKQLGGTLSGGEQQMLAIG 150
Cdd:PRK13651 99 kikeirrrvgvvfqFAEYqlfeqTIEKDIIFGPvsMGVSKEEAKKRAAKYI-ELVGLDESYLQRSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181651 151 RALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNE 229
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDN 256
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-220 |
1.38e-17 |
|
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: 78.34 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 15 YGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDitnkpahvinrmgIALVPEGRRIFPE 94
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV-------------SSLLGLGGGFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 95 LTVYENLMMGA--YNRKDKEgIKRDLEWIFSlFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEpslGLApi 172
Cdd:cd03220 99 LTGRENIYLNGrlLGLSRKE-IDEKIDEIIE-FSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE---VLA-- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181651 173 lVSEVF------EVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEG 220
Cdd:cd03220 172 -VGDAAfqekcqRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-194 |
1.46e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.20 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGIALVPEGRR---IFPELTV 97
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 98 YENLMMGAYNRKDKEG--IKRDLEWI-----FSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLA 170
Cdd:PRK10762 348 KENMSLTALRYFSRAGgsLKHADEQQavsdfIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180
....*....|....*....|....
gi 490181651 171 PILVSEVFEVIQKINQEGTTILLV 194
Cdd:PRK10762 428 VGAKKEIYQLINQFKAEGLSIILV 451
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-192 |
1.50e-17 |
|
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: 78.24 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 4 IVLEVQS------LHVYYGA-IHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQ----DITNK 72
Cdd:COG4778 3 TLLEVENlsktftLHLQGGKrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 73 PAHVI---NRMGIALVPEGRRIFPELT----VYENLMMGAYNRKDKEGIKRDLewiFSLFpRLKERLKQLG-GTLSGGEQ 144
Cdd:COG4778 83 SPREIlalRRRTIGYVSQFLRVIPRVSaldvVAEPLLERGVDREEARARAREL---LARL-NLPERLWDLPpATFSGGEQ 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490181651 145 QMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTIL 192
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-194 |
1.87e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.32 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITN----KPAHVINRMgIALVPEGRRIFPELT 96
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaAKAELRNQK-LGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 97 VYENLMMGAY--NRKDKEGIKRDLEWIFSLfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILV 174
Cdd:PRK11629 104 ALENVAMPLLigKKKPAEINSRALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180
....*....|....*....|.
gi 490181651 175 SEVFEVIQKIN-QEGTTILLV 194
Cdd:PRK11629 182 DSIFQLLGELNrLQGTAFLVV 202
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-236 |
2.02e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.10 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 24 IDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDIT----NKPAHVInRMGIALV---PEGRrIFpELT 96
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKL-RKKVSLVfqfPEAQ-LF-ENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 97 VYENLMMGAYN--RKDKEGIKRDLEWIFSLfpRLKERLKQLGG-TLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPIL 173
Cdd:PRK13641 103 VLKDVEFGPKNfgFSEDEAKEKALKWLKKV--GLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181651 174 VSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELL-DNEMVRKAYL 236
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFsDKEWLKKHYL 244
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-229 |
2.04e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.64 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYY--GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVInRMGIA 83
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL-RQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 84 LVPEGRRIFPElTVYENLMMGAYNRKDKEGI----KRDLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKL 159
Cdd:PRK11160 418 VVSQRVHLFSA-TLRDNLLLAAPNASDEALIevlqQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 160 LMMDEPSLGLAPILVSEVFEVIQKINQeGTTILLVEQNALGALKVAHYgYVLETGQIVLEGKASELLDNE 229
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRLTGLEQFDRI-CVMDNGQIIEQGTHQELLAQQ 564
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-238 |
2.07e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.77 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYYGAIH-AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDiTNKpahVINR 79
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHtALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-TRQ---ALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 80 MGIALVPEGRRI---FPELtVYENLMMGAYN-----RKDKEGIKRDLEWIFSLFPRLKERLKQLgGTLSGGEQQMLAIGR 151
Cdd:PRK15056 78 NLVAYVPQSEEVdwsFPVL-VEDVVMMGRYGhmgwlRRAKKRDRQIVTAALARVDMVEFRHRQI-GELSGGQKKRVFLAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 152 ALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNaLGALKVAHYGYVLETGQIVLEGKASELLDNEMV 231
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN-LGSVTEFCDYTVMVKGTVLASGPTETTFTAENL 234
|
....*..
gi 490181651 232 RKAYLGV 238
Cdd:PRK15056 235 ELAFSGV 241
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-232 |
2.23e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 78.90 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQslHVYY----GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHV 76
Cdd:PRK13635 1 MKEEIIRVE--HISFrypdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 77 INRMgIALV---PEGRriFPELTVYENLMMGAYNRkdkeGIKRDlewifSLFPRLKERLKQLGGT---------LSGGEQ 144
Cdd:PRK13635 79 VRRQ-VGMVfqnPDNQ--FVGATVQDDVAFGLENI----GVPRE-----EMVERVDQALRQVGMEdflnrephrLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 145 QMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGT-TILLVEQNALGALKvAHYGYVLETGQIVLEGKAS 223
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPE 225
|
250
....*....|.
gi 490181651 224 EL--LDNEMVR 232
Cdd:PRK13635 226 EIfkSGHMLQE 236
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-227 |
7.71e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.66 E-value: 7.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 14 YYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGqditnKPAHVINrMGIALVpegrrifP 93
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-----RVSALLE-LGAGFH-------P 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 94 ELTVYENLMMGA----YNRKDkegIKRDLEWI--FSlfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEpsl 167
Cdd:COG1134 102 ELTGRENIYLNGrllgLSRKE---IDEKFDEIveFA---ELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE--- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181651 168 GLApilV-SEVF-----EVIQKINQEGTTILLVEQNaLGALK-VAHYGYVLETGQIVLEGKASELLD 227
Cdd:COG1134 173 VLA---VgDAAFqkkclARIRELRESGRTVIFVSHS-MGAVRrLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-215 |
8.56e-17 |
|
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: 75.97 E-value: 8.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 20 AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGqditnkpahvinrmGIALVPEGRRIFPElTVYE 99
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEPWIQNG-TIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 100 NLMMGA--YNRKDKEGIK-----RDLEwifsLFP-----RLKERlkqlGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSL 167
Cdd:cd03250 85 NILFGKpfDEERYEKVIKacalePDLE----ILPdgdltEIGEK----GINLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490181651 168 GLAPILVSEVFE-VIQKINQEGTTILLVEQNaLGALKVAHYGYVLETGQ 215
Cdd:cd03250 157 AVDAHVGRHIFEnCILGLLLNNKTRILVTHQ-LQLLPHADQIVVLDNGR 204
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-225 |
2.12e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 77.08 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAgktttlSAIAGLVRAQkgkiiFNGQDITNKPAHVI----NRMG 81
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GA------A**RGALPAH-----V*GPDAGRRPWRF*twcaNRRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 82 IAL-------VPEGRRifPELTVYENLMMGA----YNRKDKEGIKRDLEWIFSLfprlKERLKQLGGTLSGGEQQMLAIG 150
Cdd:NF000106 83 LRRtig*hrpVR*GRR--ESFSGRENLYMIGr*ldLSRKDARARADELLERFSL----TEAAGRAAAKYSGGMRRRLDLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 151 RALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASEL 225
Cdd:NF000106 157 ASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-228 |
3.99e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.52 E-value: 3.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 24 IDLKVPRGQIVTLIGANGAGKTT---TLSAIAGLVRAQK--GKIIFNGQDITNKPAHVINRMGIALVPEGRRIFPeLTVY 98
Cdd:PRK14271 40 VSMGFPARAVTSLMGPTGSGKTTflrTLNRMNDKVSGYRysGDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFP-MSIM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 99 ENLMMGA-----YNRKDKEGIKRDLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPIL 173
Cdd:PRK14271 119 DNVLAGVrahklVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTT 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 174 VSEVFEVIQKInQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDN 228
Cdd:PRK14271 199 TEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-235 |
5.45e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.02 E-value: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIV--LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVIN 78
Cdd:PRK10253 1 MTESVarLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 79 RMgIALVPEGRRIFPELTVYENLMMGAY---------NRKDKEGIKRDLEWIfslfpRLKERLKQLGGTLSGGEQQMLAI 149
Cdd:PRK10253 81 RR-IGLLAQNATTPGDITVQELVARGRYphqplftrwRKEDEEAVTKAMQAT-----GITHLADQSVDTLSGGQRQRAWI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 150 GRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDN 228
Cdd:PRK10253 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
....*..
gi 490181651 229 EMVRKAY 235
Cdd:PRK10253 235 ELIERIY 241
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-236 |
1.21e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 73.87 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 2 SDIVLEVQSLHVYYGAIH--AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVI-N 78
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIrK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 79 RMGIALV-PEGRriFPELTVYENLMMGAYNRK-DKEGIKRDLEwIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSR 156
Cdd:PRK13632 84 KIGIIFQnPDNQ--FIGATVEDDIAFGLENKKvPPKKMKDIID-DLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 157 PKLLMMDEPSLGLAPILVSEVFEVIQKINQEGT-TILLVEQNALGALKvAHYGYVLETGQIVLEGKASELLDN-EMVRKA 234
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNkEILEKA 239
|
..
gi 490181651 235 YL 236
Cdd:PRK13632 240 KI 241
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-238 |
1.70e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.58 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 20 AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDiTNKPAHVI---NRMGIALVPEGRRIFPELt 96
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENLWdirNKAGMVFQNPDNQIVATI- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 97 VYENLMMGAYNRkdkeGIKRDlewifSLFPRLKERLKQLG---------GTLSGGEQQMLAIGRALMSRPKLLMMDEPSL 167
Cdd:PRK13633 103 VEEDVAFGPENL----GIPPE-----EIRERVDESLKKVGmyeyrrhapHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181651 168 GLAPILVSEVFEVIQKINQE-GTTILLVE---QNALGALKVAhygyVLETGQIVLEGKASELLDN-EMVRKAYLGV 238
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKyGITIILIThymEEAVEADRII----VMDSGKVVMEGTPKEIFKEvEMMKKIGLDV 245
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-165 |
1.83e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.20 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAhvinRMGIALV 85
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA----ERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGrrIFPELTVYEN----LMMGAYNRKDKEGIKRDLEWIFSLFPRLKERLKQlggtLSGGEQQMLAIGRALMSRPKLLM 161
Cdd:PRK11248 78 NEG--LLPWRNVQDNvafgLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQ----LSGGQRQRVGIARALAANPQLLL 151
|
....
gi 490181651 162 MDEP 165
Cdd:PRK11248 152 LDEP 155
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-194 |
1.99e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 73.99 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYY----GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVrAQKGKI----IFNGQDITNK 72
Cdd:PRK09473 8 QADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIggsaTFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 73 PAHVINRM---GIALvpegrrIF--------PELTVYENLM--------MG---AYNRKDK--EGIKrdlewifslFPRL 128
Cdd:PRK09473 87 PEKELNKLraeQISM------IFqdpmtslnPYMRVGEQLMevlmlhkgMSkaeAFEESVRmlDAVK---------MPEA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181651 129 KERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLV 194
Cdd:PRK09473 152 RKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMI 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-193 |
2.69e-15 |
|
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: 74.66 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 20 AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVinRMGIALVPEGRRIFPELTVYE 99
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV--RQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 100 NLMMGAYNR-KDKEGIKRDLEWIFSlFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVF 178
Cdd:TIGR01257 1023 HILFYAQLKgRSWEEAQLEMEAMLE-DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170
....*....|....*
gi 490181651 179 EVIQKInQEGTTILL 193
Cdd:TIGR01257 1102 DLLLKY-RSGRTIIM 1115
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-226 |
2.72e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.20 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYY---GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMG 81
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 82 IALVPEGRRIFPELTVYENLMMGAYNR--KDKEGIKRDLEWIFSLfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKL 159
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVAFGMENQgiPREEMIKRVDEALLAV--NMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181651 160 LMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELL 226
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-233 |
6.06e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 72.35 E-value: 6.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 20 AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDItnkPAhvinrmGIALVPEGRRI-------- 91
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI---PA------NLKKIKEVKRLrkeiglvf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 92 -FPEL-----TVYENLMMGAYNR-KDKEGIKRDLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:PRK13645 97 qFPEYqlfqeTIEKDIAFGPVNLgENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181651 165 PSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDN-EMVRK 233
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNqELLTK 247
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-235 |
1.61e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.01 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 24 IDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMGIALVPEGRR---IFPELTVYEN 100
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQssgLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 101 LMMGAYNR--------KDK---EGIKRDLEWIFSlfprlkeRLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGL 169
Cdd:PRK15439 362 VCALTHNRrgfwikpaRENavlERYRRALNIKFN-------HAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181651 170 APILVSEVFEVIQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMVRKAY 235
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRLAF 500
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-229 |
1.73e-14 |
|
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: 70.21 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 20 AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDI-TNKPAHVINRMGIALvpeGRRIFPELTVY 98
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGVVL---QENVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 99 ENLMMG--AYNRKDKEGIKR---DLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPIL 173
Cdd:cd03252 94 DNIALAdpGMSMERVIEAAKlagAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490181651 174 VSEVFEVIQKINQEGTTILLVEQnaLGALKVAHYGYVLETGQIVLEGKASELLDNE 229
Cdd:cd03252 174 EHAIMRNMHDICAGRTVIIIAHR--LSTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-238 |
2.25e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 71.60 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 20 AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDI---TNKPAHVINRMGIALVPEGRRIFPELT 96
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakiSDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 97 VYENLMMGAYNRKDKEGIKRDlewifslfpRLKERLKQLG---------GTLSGGEQQMLAIGRALMSRPKLLMMDEPSL 167
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERRE---------KALDALRQVGlenyahsypDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 168 GLAPILVSEVFEVIQKIN-QEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLD---NEMVRKAYLGV 238
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNnpaNDYVRTFFRGV 268
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-238 |
2.37e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.58 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 20 AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPA-----HVINRMGIAL-VPEGrRIFp 93
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirPVRKRIGMVFqFPES-QLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 94 ELTVYENLMMGAYNRK-DKEGIKrdlEWIFSL-----FPRlkERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSL 167
Cdd:PRK13646 100 EDTVEREIIFGPKNFKmNLDEVK---NYAHRLlmdlgFSR--DVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181651 168 GLAPILVSEVFEVIQKIN-QEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELL-DNEMVRKAYLGV 238
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFkDKKKLADWHIGL 247
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-226 |
3.91e-14 |
|
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: 70.99 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYY-----GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFN-GQ---DITNKPAH 75
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDewvDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 76 VINRMG--IALVPEGRRIFPELTVYENLmmgaynrkdKEGIKRDLEWIFSLF-------------PRLKERLKQLGGTLS 140
Cdd:TIGR03269 359 GRGRAKryIGILHQEYDLYPHRTVLDNL---------TEAIGLELPDELARMkavitlkmvgfdeEKAEEILDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 141 GGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLE 219
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
....*..
gi 490181651 220 GKASELL 226
Cdd:TIGR03269 510 GDPEEIV 516
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
21-226 |
6.95e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.95 E-value: 6.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITnkpahvinrmgiALVPEGRRIFPELT--VY 98
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLA------------KLNRAQRKAFRRDIqmVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 99 ENlMMGAYN-RKD-KEGIKRDLEWIFSLFP-----RLKERLKQLG----------GTLSGGEQQMLAIGRALMSRPKLLM 161
Cdd:PRK10419 96 QD-SISAVNpRKTvREIIREPLRHLLSLDKaerlaRASEMLRAVDlddsvldkrpPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181651 162 MDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELL 226
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKL 240
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-225 |
7.35e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 69.28 E-value: 7.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 20 AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDIT----NKPAHVI-NRMGIAL-VPEgRRIFP 93
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKPLrKKVGIVFqFPE-HQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 94 ElTVYENLMMGAYN--RKDKEGIKRDLEWIfSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAP 171
Cdd:PRK13634 101 E-TVEKDICFGPMNfgVSEEDAKQKAREMI-ELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 172 ILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASEL 225
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-187 |
8.59e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.35 E-value: 8.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 4 IVLEVQSLHVYYG-------------AIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDIT 70
Cdd:PRK15079 7 VLLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 71 NK------------------PAHVIN-RMGIA-LVPEGRRIF-PELTVYE------NLMMgaynrkdKEGikrdlewifs 123
Cdd:PRK15079 87 GMkddewravrsdiqmifqdPLASLNpRMTIGeIIAEPLRTYhPKLSRQEvkdrvkAMML-------KVG---------- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181651 124 LFPRLKERLKQlggTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE 187
Cdd:PRK15079 150 LLPNLINRYPH---EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRE 210
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-225 |
9.87e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.39 E-value: 9.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYG----AIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLV----RAQKGKIIFNGQD---ITNKP 73
Cdd:PRK11022 3 LLNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDlqrISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 74 AHVINRMGIALVPE------------GRRIFPELTVYEnlmmgAYNRKDKEGIKRDLEWIFSLfPRLKERLKQLGGTLSG 141
Cdd:PRK11022 83 RRNLVGAEVAMIFQdpmtslnpcytvGFQIMEAIKVHQ-----GGNKKTRRQRAIDLLNQVGI-PDPASRLDVYPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 142 GEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQ-EGTTILLVEQNALGALKVAHYGYVLETGQIVLEG 220
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
....*
gi 490181651 221 KASEL 225
Cdd:PRK11022 237 KAHDI 241
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-228 |
1.13e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.00 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 24 IDLKVPRGQIVTLIGANGAGKTTTLSAIAG-LVRAQKGKIIFNGQditnkpahvinrmgIALVPEGRRIFpELTVYENLM 102
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS--------------VAYVPQVSWIF-NATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 103 MGA------YNRK-DKEGIKRDLEwifsLFP-RLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILV 174
Cdd:PLN03232 701 FGSdfeserYWRAiDVTALQHDLD----LLPgRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVA 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181651 175 SEVFEVIQKINQEGTTILLVeQNALGALKVAHYGYVLETGQIVLEGKASELLDN 228
Cdd:PLN03232 777 HQVFDSCMKDELKGKTRVLV-TNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-165 |
1.19e-13 |
|
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: 67.38 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDI---TNKPAHVINRMGI 82
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 83 AlvpEGrrIFPELTVYENLmmgAYNRKDKEGIKRDLEwifslfprlkERLKQLG---------GTLSGGEQQMLAIGRAL 153
Cdd:TIGR01189 81 L---PG--LKPELSALENL---HFWAAIHGGAQRTIE----------DALAAVGltgfedlpaAQLSAGQQRRLALARLW 142
|
170
....*....|..
gi 490181651 154 MSRPKLLMMDEP 165
Cdd:TIGR01189 143 LSRRPLWILDEP 154
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-197 |
1.45e-13 |
|
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: 69.66 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 2 SDIVLEVQSLHVYYGAIH-AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRM 80
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 GIAlvPEGRRIFPELTVYENLMMGAYNRK-DKEGIKRDLEW-IFSLfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPK 158
Cdd:TIGR01257 2015 GYC--PQFDAIDDLLTGREHLYLYARLRGvPAEEIEKVANWsIQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190
....*....|....*....|....*....|....*....
gi 490181651 159 LLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQN 197
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHS 2129
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-194 |
3.01e-13 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 65.70 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHA--IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITN-KPAHVinRMGI 82
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNEL--GDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 83 ALVPEGRRIFPElTVYENLmmgaynrkdkegikrdlewifslfprlkerlkqlggtLSGGEQQMLAIGRALMSRPKLLMM 162
Cdd:cd03246 79 GYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190
....*....|....*....|....*....|..
gi 490181651 163 DEPSLGLAPILVSEVFEVIQKINQEGTTILLV 194
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAAGATRIVI 152
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-224 |
3.15e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 31 GQIVTLIGANGAGKTTTLSAIAGLVRAQ--KGKIIFNGQDITNKpahVINRMGiaLVPEGRRIFPELTVYENLMMGAYNR 108
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQ---ILKRTG--FVTQDDILYPHLTVRETLVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 109 KDKEGIKRD----LEWIFSLFPRLKERLKQLGGT----LSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEV 180
Cdd:PLN03211 169 LPKSLTKQEkilvAESVISELGLTKCENTIIGNSfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490181651 181 IQKINQEGTTILL-VEQNALGALKVAHYGYVLETGQIVLEGKASE 224
Cdd:PLN03211 249 LGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-230 |
3.31e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.61 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 24 IDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGkiifngqditnkpAHVINRMGIALVPEGRRIFpELTVYENLMM 103
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD-------------ASVVIRGTVAYVPQVSWIF-NATVRDNILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 104 GA------YNRK-DKEGIKRDLEwifsLFP-----RLKERlkqlGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAP 171
Cdd:PLN03130 702 GSpfdperYERAiDVTALQHDLD----LLPggdltEIGER----GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181651 172 ILVSEVFEVIQKINQEGTTILLVeQNALGALKVAHYGYVLETGQIVLEGKASELLDNEM 230
Cdd:PLN03130 774 HVGRQVFDKCIKDELRGKTRVLV-TNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGP 831
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-169 |
3.60e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVlEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQditnkpahvinrM 80
Cdd:PRK09544 1 MTSLV-SLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 GIALVPEGRRIFPE--LTVYENLMMgaynrkdKEGIKRDlewifSLFPRLK-----ERLKQLGGTLSGGEQQMLAIGRAL 153
Cdd:PRK09544 68 RIGYVPQKLYLDTTlpLTVNRFLRL-------RPGTKKE-----DILPALKrvqagHLIDAPMQKLSGGETQRVLLARAL 135
|
170
....*....|....*.
gi 490181651 154 MSRPKLLMMDEPSLGL 169
Cdd:PRK09544 136 LNRPQLLVLDEPTQGV 151
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-220 |
3.92e-13 |
|
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: 65.75 E-value: 3.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQ---KGKIIFNGqdITNKPAHVINRMGIALVPEGRRIFPELTV 97
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG--IPYKEFAEKYPGEIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 98 YENLMmgaynrkdkegikrdlewiFSLFPRLKERLKqlggTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPilvSEV 177
Cdd:cd03233 101 RETLD-------------------FALRCKGNEFVR----GISGGERKRVSIAEALVSRASVLCWDNSTRGLDS---STA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490181651 178 FEVIQKINQ-----EGTTILLVEQNALGALKVAHYGYVLETGQIVLEG 220
Cdd:cd03233 155 LEILKCIRTmadvlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-228 |
3.97e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 18 IHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINrmgiALVPEGRRIF----- 92
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQ----ALRRDIQFIFqdpya 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 93 ---PELTVYENLM--MGAYNRKDKEGIKRDLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSL 167
Cdd:PRK10261 413 sldPRQTVGDSIMepLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181651 168 GLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDN 228
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFEN 554
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-225 |
4.05e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.95 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 24 IDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQkGKIIFNGQDITN-KPAHVinRMGIALVPEGRRIFPElTVYENLM 102
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRElDPESW--RKHLSWVGQNPQLPHG-TLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 103 MGAYNRKDKEgIKRDLE--WIFSLFPRLKERL----KQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLApiLVSE 176
Cdd:PRK11174 445 LGNPDASDEQ-LQQALEnaWVSEFLPLLPQGLdtpiGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD--AHSE 521
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490181651 177 --VFEVIQKINQEGTTILLVEQnaLGALKVAHYGYVLETGQIVLEGKASEL 225
Cdd:PRK11174 522 qlVMQALNAASRRQTTLMVTHQ--LEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-194 |
4.07e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.91 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFngqditnkPAHvinrMGIALVPEgRRIFPELTVYEN 100
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--------PAG----ARVLFLPQ-RPYLPLGTLREA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 101 LmmgAY----NRKDKEGIKRDLEWIfSLfPRLKERLKQ---LGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPIL 173
Cdd:COG4178 446 L---LYpataEAFSDAELREALEAV-GL-GHLAERLDEeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN 520
|
170 180
....*....|....*....|.
gi 490181651 174 VSEVFEVIQKiNQEGTTILLV 194
Cdd:COG4178 521 EAALYQLLRE-ELPGTTVISV 540
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-169 |
4.49e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.67 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNkpAHVINRMGIAl 84
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDD--PDVAEACHYL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 85 vpeGRRIF--PELTVYENL-----MMGAYNRKDKEGIKR-DLEWIFSLfprlkerlkqLGGTLSGGEQQMLAIGRALMSR 156
Cdd:PRK13539 79 ---GHRNAmkPALTVAENLefwaaFLGGEELDIAAALEAvGLAPLAHL----------PFGYLSAGQKRRVALARLLVSN 145
|
170
....*....|...
gi 490181651 157 PKLLMMDEPSLGL 169
Cdd:PRK13539 146 RPIWILDEPTAAL 158
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-169 |
5.09e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.49 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPahvinrmgIALV 85
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRD--------LYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRIFPELT----------------------VYENLM-MGA--YNRKDKEGikrdLEWIfslfPRLK---ERLKQLGG 137
Cdd:PRK11701 79 SEAERRRLLRTewgfvhqhprdglrmqvsaggnIGERLMaVGArhYGDIRATA----GDWL----ERVEidaARIDDLPT 150
|
170 180 190
....*....|....*....|....*....|..
gi 490181651 138 TLSGGEQQMLAIGRALMSRPKLLMMDEPSLGL 169
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGL 182
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-226 |
5.18e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.82 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKpAHVINRMGIALVPEGRRIFPElTVYEN 100
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL-SHSVLRQGVAMVQQDPVVLAD-TFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 101 LMMGaynRK-DKEGIKRDLE------WIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPIL 173
Cdd:PRK10790 435 VTLG---RDiSEEQVWQALEtvqlaeLARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490181651 174 VSEVFEVIQKINQEgtTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELL 226
Cdd:PRK10790 512 EQAIQQALAAVREH--TTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-229 |
7.45e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 66.31 E-value: 7.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 20 AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVInRMGIALV---PEGRriFPELT 96
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL-RKHIGIVfqnPDNQ--FVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 97 VYENLMMGAYN-----RKDKEGIKRDLEWIFSLfprlkERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAP 171
Cdd:PRK13648 101 VKYDVAFGLENhavpyDEMHRRVSEALKQVDML-----ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181651 172 ILVSEVFEVIQKINQE-GTTILLVEQNALGALKvAHYGYVLETGQIVLEGKASELLDNE 229
Cdd:PRK13648 176 DARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-226 |
8.15e-13 |
|
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: 67.08 E-value: 8.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIALVPEGrrifPEL---TV 97
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH-IGYLPQD----VELfdgTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 98 YENL--MMGAynrkDKEGIKR-----DL-EWIFSLfP-----RLKERlkqlGGTLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:COG4618 423 AENIarFGDA----DPEKVVAaaklaGVhEMILRL-PdgydtRIGEG----GARLSGGQRQRIGLARALYGDPRLVVLDE 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181651 165 PSLGLAPILVSEVFEVIQKINQEGTTILLVEQNaLGALKVAHYGYVLETGQIVLEGKASELL 226
Cdd:COG4618 494 PNSNLDDEGEAALAAAIRALKARGATVVVITHR-PSLLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-187 |
1.13e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.12 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 2 SDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITnkpahvinrmg 81
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIS----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 82 iALVPEGRR-----------IFPElTVYENLMMGAYNRK---DKEGIKRDLEWiFSLfPrlKERLKQLGGTLSGGEQQML 147
Cdd:PRK10247 73 -TLKPEIYRqqvsycaqtptLFGD-TVYDNLIFPWQIRNqqpDPAIFLDDLER-FAL-P--DTILTKNIAELSGGEKQRI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490181651 148 AIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE 187
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVRE 186
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-235 |
1.31e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.34 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 28 VPRGQIVTLIGANGAGKTTTLSAIAGLVrAQKGKIIFNGQDITNKPAHVINRMGIALVPEGRRIFpELTVYENLMMGAYN 107
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPF-AMPVFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 108 RKDKEGIKRDLEWIFSLFpRLKERLKQLGGTLSGGEQQ-------MLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEV 180
Cdd:PRK03695 97 KTRTEAVASALNEVAEAL-GLDDKLGRSVNQLSGGEWQrvrlaavVLQVWPDINPAGQLLLLDEPMNSLDVAQQAALDRL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 181 IQKINQEGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMVRKAY 235
Cdd:PRK03695 176 LSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-187 |
1.68e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.27 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYY-----------GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQkGKIIFNGQditnkP 73
Cdd:PRK15134 275 LLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQ-----P 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 74 AHVINRMgiALVPEGRRI---F--------PELTVYENLMMG-AYNRKDKEGIKRDLEWI-----FSLFPRLKERLKqlg 136
Cdd:PRK15134 349 LHNLNRR--QLLPVRHRIqvvFqdpnsslnPRLNVLQIIEEGlRVHQPTLSAAQREQQVIavmeeVGLDPETRHRYP--- 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490181651 137 GTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE 187
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQK 474
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-187 |
2.22e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 64.75 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVlEVQSLHVYYGA---IHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVI 77
Cdd:PRK13650 1 MSNII-EVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 78 nRMGIALV---PEGRriFPELTVYENLMMGAYNRkdkeGIKRDLewifsLFPRLKERLKQLGGT---------LSGGEQQ 145
Cdd:PRK13650 80 -RHKIGMVfqnPDNQ--FVGATVEDDVAFGLENK----GIPHEE-----MKERVNEALELVGMQdfkereparLSGGQKQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490181651 146 MLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE 187
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDD 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-230 |
2.54e-12 |
|
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: 65.59 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGL--VRAQKGKIIFN------------------ 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 66 -----GQDITNKPAHVIN-----------RMGIALvpegRRIFP---ELTVYENLM--MGAYNRKDKEGIKRDLEWIFSL 124
Cdd:TIGR03269 81 pcpvcGGTLEPEEVDFWNlsdklrrrirkRIAIML----QRTFAlygDDTVLDNVLeaLEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 125 fpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQK-INQEGTTILLVEQNALGALK 203
Cdd:TIGR03269 157 --QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVIED 234
|
250 260
....*....|....*....|....*..
gi 490181651 204 VAHYGYVLETGQIVLEGKASELLDNEM 230
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTPDEVVAVFM 261
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-227 |
2.71e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 65.75 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 7 EVQSLHV---YYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTlsaIAGLVRA---QKGKIIFNGQDITNkpahvINRM 80
Cdd:PRK13657 334 AVEFDDVsfsYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRVfdpQSGRILIDGTDIRT-----VTRA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 G----IALVPEGRRIFPElTVYENLMMGAYNRKDKE-----GIKRDLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGR 151
Cdd:PRK13657 406 SlrrnIAVVFQDAGLFNR-SIEDNIRVGRPDATDEEmraaaERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181651 152 ALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQnaLGALKVAHYGYVLETGQIVLEGKASELLD 227
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHR--LSTVRNADRILVFDNGRVVESGSFDELVA 558
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-234 |
5.09e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 64.74 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIALVPEGRRIFPElTVYEN 100
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ-VALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 101 LMMGaYNRKDKEGIKRDL------EWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLApilv 174
Cdd:TIGR00958 575 IAYG-LTDTPDEEIMAAAkaanahDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD---- 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181651 175 SEVFEVIQKI-NQEGTTILLVEQNaLGALKVAHYGYVLETGQIVLEGKASELLDNEMVRKA 234
Cdd:TIGR00958 650 AECEQLLQESrSRASRTVLLIAHR-LSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-197 |
5.38e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 64.75 E-value: 5.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYY----GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDIT---NKPAHVIN 78
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtldADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 79 RMGIALVPEGRRIFPELTVYENLMMGA-YNRKDKegiKRDLEWIFSLFPRL--KERLKQLGGTLSGGEQQMLAIGRALMS 155
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVPAvYAGLER---KQRLLRAQELLQRLglEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490181651 156 RPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQN 197
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-235 |
6.27e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.65 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 24 IDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIALVPEGRRIFPELTVYENLMM 103
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQLPAAEGMTVRELVAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 104 GAY---------NRKDKEGIKRDLEWIfslfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILV 174
Cdd:PRK10575 109 GRYpwhgalgrfGAADREKVEEAISLV-----GLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181651 175 SEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNEMVRKAY 235
Cdd:PRK10575 184 VDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-225 |
9.84e-12 |
|
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: 64.16 E-value: 9.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQditnkpahvinrmgIALVPEGRRIFPElTVYEN 100
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 101 LMMG-AYNRKDKEGIKR--DLEWIFSLFP-RLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSE 176
Cdd:TIGR01271 507 IIFGlSYDEYRYTSVIKacQLEEDIALFPeKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490181651 177 VFE-VIQKINQEGTTILLVEQnaLGALKVAHYGYVLETGQIVLEGKASEL 225
Cdd:TIGR01271 587 IFEsCLCKLMSNKTRILVTSK--LEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-194 |
1.68e-11 |
|
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: 60.63 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIfngqditnKPAHvinrMGIALVPEgRRIFPELTVYEN 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG--------MPEG----EDLLFLPQ-RPYLPLGTLREQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 101 LmmgaynrkdkegikrdlewifsLFPRLKErlkqlggtLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPilvsEV-FE 179
Cdd:cd03223 84 L----------------------IYPWDDV--------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ESeDR 129
|
170
....*....|....*
gi 490181651 180 VIQKINQEGTTILLV 194
Cdd:cd03223 130 LYQLLKELGITVISV 144
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-226 |
1.90e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.11 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 20 AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITN-KPAHVinRMGIALVPEGRRIFPElTVY 98
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASL--RNQVALVSQNVHLFND-TIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 99 ENLmmgAYNRKDK---EGIKR------DLEWIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGL 169
Cdd:PRK11176 435 NNI---AYARTEQysrEQIEEaarmayAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 170 ApilvSEVFEVIQK---INQEGTTILLVEQNaLGALKVAHYGYVLETGQIVLEGKASELL 226
Cdd:PRK11176 512 D----TESERAIQAaldELQKNRTSLVIAHR-LSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-236 |
2.20e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.12 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYY--GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLV---RAQKGKIIFNGQDITNKPA- 74
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 75 HVINRMGIALV-PEGRriFPELTVYENLMMGAYNRkdkeGIKRDlewifSLFPRLKERLKQLGGT---------LSGGEQ 144
Cdd:PRK13640 81 DIREKVGIVFQnPDNQ--FVGATVGDDVAFGLENR----AVPRP-----EMIKIVRDVLADVGMLdyidsepanLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 145 QMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKI-NQEGTTILLVEQN---ALGALKVahygYVLETGQIVLEG 220
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDideANMADQV----LVLDDGKLLAQG 225
|
250
....*....|....*..
gi 490181651 221 KASELLDN-EMVRKAYL 236
Cdd:PRK13640 226 SPVEIFSKvEMLKEIGL 242
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-230 |
2.52e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 62.23 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 16 GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGL------VRAQKgkIIFNGQDITnkpahvinrmgiALVPEGR 89
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGItkdnwhVTADR--FRWNGIDLL------------KLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 90 R---------IF--------PELTVYENLMMGAYN-------------RKD-------KEGIKrDLEWIFSLFPRlkerl 132
Cdd:COG4170 84 RkiigreiamIFqepsscldPSAKIGDQLIEAIPSwtfkgkwwqrfkwRKKraiellhRVGIK-DHKDIMNSYPH----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 133 kqlggTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQ-EGTTILLVEQNALGALKVAHYGYVL 211
Cdd:COG4170 158 -----ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVL 232
|
250
....*....|....*....
gi 490181651 212 ETGQIVLEGKASELLDNEM 230
Cdd:COG4170 233 YCGQTVESGPTEQILKSPH 251
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-225 |
4.32e-11 |
|
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: 61.41 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQditnkpahvinrmgIALVPEGRRIFPElTVYEN 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 101 LMMG-AYNR-KDKEGIKR-DLEWIFSLFP-RLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSE 176
Cdd:cd03291 118 IIFGvSYDEyRYKSVVKAcQLEEDITKFPeKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490181651 177 VFE-VIQKINQEGTTILLVeqNALGALKVAHYGYVLETGQIVLEGKASEL 225
Cdd:cd03291 198 IFEsCVCKLMANKTRILVT--SKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-216 |
6.42e-11 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 60.18 E-value: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIALVPEGRRIFPElTVYEN 100
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-VSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 101 LMMGAYNRKDKE----GIKRDLEWIFSLFPR-LKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLApilvS 175
Cdd:cd03248 108 IAYGLQSCSFECvkeaAQKAHAHSFISELASgYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD----A 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490181651 176 EVFEVIQKINQEG---TTILLVEQNaLGALKVAHYGYVLETGQI 216
Cdd:cd03248 184 ESEQQVQQALYDWperRTVLVIAHR-LSTVERADQILVLDGGRI 226
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-165 |
7.58e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 7.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 25 DLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNgQDIT------NKPAHVINRM------GIALVPEGRRIF 92
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIvarlqqDPPRNVEGTVydfvaeGIEEQAEYLKRY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 93 PELTvyeNLMMGAY---NRKDKEGIKRDLE----WIFSlfPRLKERLKQLG-------GTLSGGEQQMLAIGRALMSRPK 158
Cdd:PRK11147 102 HDIS---HLVETDPsekNLNELAKLQEQLDhhnlWQLE--NRINEVLAQLGldpdaalSSLSGGWLRKAALGRALVSNPD 176
|
....*..
gi 490181651 159 LLMMDEP 165
Cdd:PRK11147 177 VLLLDEP 183
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-169 |
8.56e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.43 E-value: 8.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAhvINRMGIALV 85
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD--SIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEGRRIFPELTVYENLMMGAYNRKDkEGIkrdlewifslfprlKERLKQLG---------GTLSGGEQQMLAIGRALMSR 156
Cdd:cd03231 79 GHAPGIKTTLSVLENLRFWHADHSD-EQV--------------EEALARVGlngfedrpvAQLSAGQQRRVALARLLLSG 143
|
170
....*....|...
gi 490181651 157 PKLLMMDEPSLGL 169
Cdd:cd03231 144 RPLWILDEPTTAL 156
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-166 |
8.60e-11 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 58.23 E-value: 8.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIifngqditnkpaHVINRMGIALV 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------TWGSTVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 86 PEgrrifpeltvyenlmmgaynrkdkegikrdlewifslfprlkerlkqlggtLSGGEQQMLAIGRALMSRPKLLMMDEP 165
Cdd:cd03221 69 EQ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
.
gi 490181651 166 S 166
Cdd:cd03221 98 T 98
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-169 |
1.18e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.84 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQ--------KGKIIFNGQDITNKPAHV 76
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 77 INRMGIALVPEGRRIFPeLTVYENLMMGAY--NRKDKEGIKRDLEWIFSLFPRLKErlKQLGG----TLSGGEQQMLAIG 150
Cdd:PRK13547 81 LARLRAVLPQAAQPAFA-FSAREIVLLGRYphARRAGALTHRDGEIAWQALALAGA--TALVGrdvtTLSGGELARVQFA 157
|
170 180
....*....|....*....|....*...
gi 490181651 151 RAL---------MSRPKLLMMDEPSLGL 169
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAAL 185
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-216 |
2.02e-10 |
|
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: 59.48 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYY--GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQkGKIIFNGQDITNKPAHVInRMGIA 83
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKW-RKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 84 LVPEGRRIFPElTVYENLmmGAYNRKDKEGIKR-----DLEWIFSLFP-RLKERLKQLGGTLSGGEQQMLAIGRALMSRP 157
Cdd:cd03289 81 VIPQKVFIFSG-TFRKNL--DPYGKWSDEEIWKvaeevGLKSVIEQFPgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181651 158 KLLMMDEPSLGLAPIlvseVFEVIQKINQE---GTTILLVEQNALGALKVAHYgYVLETGQI 216
Cdd:cd03289 158 KILLLDEPSAHLDPI----TYQVIRKTLKQafaDCTVILSEHRIEAMLECQRF-LVIEENKV 214
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-165 |
2.26e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.28 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 23 GIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITnkpahvinrmgiALVPEGRR----------IF 92
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR------------RQRDEYHQdllylghqpgIK 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181651 93 PELTVYENL--MMGAYNRKDKEGIKRDLEWIfslfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEP 165
Cdd:PRK13538 87 TELTALENLrfYQRLHGPGDDEALWEALAQV-----GLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
31-192 |
2.61e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 58.02 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 31 GQIVTLIGANGAGKTTTLSAIA-----GLVraqKGKIIFNGQDITnkpahvIN-RMGIALVPEGRRIFPELTVYENLMMG 104
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAgrktaGVI---TGEILINGRPLD------KNfQRSTGYVEQQDVHSPNLTVREALRFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 105 AYNRKdkegikrdlewifslfprlkerlkqlggtLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKI 184
Cdd:cd03232 104 ALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
....*...
gi 490181651 185 NQEGTTIL 192
Cdd:cd03232 155 ADSGQAIL 162
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-165 |
3.36e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRA--QKGKIIFNGQ-----DITNKPAH-- 75
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGEvcrfkDIRDSEALgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 76 VINRMGIALVpegrrifPELTVYENLMMGayNRKDKEGIkrdLEWIfSLFPRLKERLKQLG-----GTLSG----GEQQM 146
Cdd:NF040905 81 VIIHQELALI-------PYLSIAENIFLG--NERAKRGV---IDWN-ETNRRARELLAKVGldespDTLVTdigvGKQQL 147
|
170
....*....|....*....
gi 490181651 147 LAIGRALMSRPKLLMMDEP 165
Cdd:NF040905 148 VEIAKALSKDVKLLILDEP 166
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-183 |
4.05e-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: 59.54 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYY--GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQkGKIIFNG---QDITNKPAhvinRM 80
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvswNSVTLQTW----RK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 GIALVPEGRRIFPElTVYENLmmGAYNRKDKEGIKR-----DLEWIFSLFP-RLKERLKQLGGTLSGGEQQMLAIGRALM 154
Cdd:TIGR01271 1293 AFGVIPQKVFIFSG-TFRKNL--DPYEQWSDEEIWKvaeevGLKSVIEQFPdKLDFVLVDGGYVLSNGHKQLMCLARSIL 1369
|
170 180
....*....|....*....|....*....
gi 490181651 155 SRPKLLMMDEPSLGLAPIlvseVFEVIQK 183
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDPV----TLQIIRK 1394
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-197 |
4.56e-10 |
|
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: 56.95 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 19 HAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIaglvraqkgkiifngqditnkpahvINRMGIALVPEGRRIFPELTVy 98
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG-------------------------LYASGKARLISFLPKFSRNKL- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 99 enLMMGaynrKDKEGIKRDLEWIfslfprlkeRLKQLGGTLSGGEQQMLAIGRALMSRPK--LLMMDEPSLGLAPILVSE 176
Cdd:cd03238 63 --IFID----QLQFLIDVGLGYL---------TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQ 127
|
170 180
....*....|....*....|.
gi 490181651 177 VFEVIQKINQEGTTILLVEQN 197
Cdd:cd03238 128 LLEVIKGLIDLGNTVILIEHN 148
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-165 |
6.20e-10 |
|
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: 57.34 E-value: 6.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 18 IHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVI---NRMGIALVPEGRRIFpE 94
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrNRYSVAYAAQKPWLL-N 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181651 95 LTVYENLMMGA-YNRK------DKEGIKRDLEWI-FSLFPRLKERlkqlGGTLSGGEQQMLAIGRALMSRPKLLMMDEP 165
Cdd:cd03290 93 ATVEENITFGSpFNKQrykavtDACSLQPDIDLLpFGDQTEIGER----GINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-229 |
9.43e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 9.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVINRMgIALVPEGRRIFPElTVYEN 100
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV-LSIIPQSPVLFSG-TVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 101 LmmGAYNRKDKEGIKRDLE--WIFSLFPR----LKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSlglAPILV 174
Cdd:PLN03232 1330 I--DPFSEHNDADLWEALEraHIKDVIDRnpfgLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEAT---ASVDV 1404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181651 175 sEVFEVIQKINQE--GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELLDNE 229
Cdd:PLN03232 1405 -RTDSLIQRTIREefKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
5-225 |
1.19e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.02 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYyGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGL----VRAQKGKIIFNGQDITnkPAHVINRM 80
Cdd:PRK10418 4 QIELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVA--PCALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 gIALVPEG-RRIF-PELTvyenlmMGAYNRKDKEGIKR-----------------DLEWIFSLFPRlkerlkqlggTLSG 141
Cdd:PRK10418 81 -IATIMQNpRSAFnPLHT------MHTHARETCLALGKpaddatltaaleavgleNAARVLKLYPF----------EMSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 142 GEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEG 220
Cdd:PRK10418 144 GMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQG 223
|
....*
gi 490181651 221 KASEL 225
Cdd:PRK10418 224 DVETL 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-166 |
1.78e-09 |
|
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: 57.25 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 3 DIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFnGQDITnkpahvinrmgI 82
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK-----------L 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 83 ALVPEGR-RIFPELTVYEN-------LMMGAYNRKDKEGIKRdlewiFSLfpRLKERLKQLgGTLSGGEQQMLAIGRALM 154
Cdd:TIGR03719 388 AYVDQSRdALDPNKTVWEEisggldiIKLGKREIPSRAYVGR-----FNF--KGSDQQKKV-GQLSGGERNRVHLAKTLK 459
|
170
....*....|..
gi 490181651 155 SRPKLLMMDEPS 166
Cdd:TIGR03719 460 SGGNVLLLDEPT 471
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-226 |
4.97e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.87 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGL-----VRAQKGKIIFNGQDITNKPAHVI-----NRMGIalvpegrr 90
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTLrgvrgNKIAM-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 91 IFPELTV------------YENLMMGAYNRK-----------DKEGIKRdlewifslfprLKERLKQLGGTLSGGEQQML 147
Cdd:PRK15134 97 IFQEPMVslnplhtlekqlYEVLSLHRGMRReaargeilnclDRVGIRQ-----------AAKRLTDYPHQLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 148 AIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASELL 226
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLF 245
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-216 |
5.29e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.67 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 19 HAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQditnkpahvinrmgIALVPEGRRIFPELTVY 98
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS--------------AALIAISSGLNGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 99 EN-----LMMGAYNRKDKEGIKRDLEwifslFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEP-SLGlAPI 172
Cdd:PRK13545 104 ENielkgLMMGLTKEKIKEIIPEIIE-----FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAlSVG-DQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490181651 173 LVSEVFEVIQKINQEGTTILLVeQNALGALKV-------AHYGYVLETGQI 216
Cdd:PRK13545 178 FTKKCLDKMNEFKEQGKTIFFI-SHSLSQVKSfctkalwLHYGQVKEYGDI 227
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-195 |
5.46e-09 |
|
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: 55.07 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 26 LKVPR-GQIVTLIGANGAGKTTTLSAIAGLVRAQKGK---------II--FNGQDITNKPAHVIN-RMGIALVPEGRRIF 92
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeILdeFRGSELQNYFTKLLEgDVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 93 PEL---TVYENLmmgayNRKDKEGIKRDLEWIFSLFPRLKERLKQLggtlSGGEQQMLAIGRALMSRPKLLMMDEPSLGL 169
Cdd:cd03236 100 PKAvkgKVGELL-----KKKDERGKLDELVDQLELRHVLDRNIDQL----SGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180
....*....|....*....|....*.
gi 490181651 170 APILVSEVFEVIQKINQEGTTILLVE 195
Cdd:cd03236 171 DIKQRLNAARLIRELAEDDNYVLVVE 196
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-70 |
1.51e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 54.42 E-value: 1.51e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 490181651 24 IDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDIT 70
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT 397
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
60-169 |
1.78e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 60 GKIIFNGQDITNKPAHVINRMgIALVPEGRRIFpELTVYENLMMGAYNrKDKEGIKRDL------EWIFSLFPRLKERLK 133
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNL-FSIVSQEPMLF-NMSIYENIKFGKED-ATREDVKRACkfaaidEFIESLPNKYDTNVG 1353
|
90 100 110
....*....|....*....|....*....|....*.
gi 490181651 134 QLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGL 169
Cdd:PTZ00265 1354 PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSL 1389
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
10-166 |
2.09e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 10 SLHVYYGAIHaikgidlkvpRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNgQDITNKPAHVinrmgialvpegr 89
Cdd:PRK13409 354 SLEVEGGEIY----------EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKPQYI------------- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 90 RIFPELTVYENLMMgaynrkdkegIKRDLE--WIFS--LFP-RLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:PRK13409 410 KPDYDGTVEDLLRS----------ITDDLGssYYKSeiIKPlQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 479
|
..
gi 490181651 165 PS 166
Cdd:PRK13409 480 PS 481
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-227 |
2.26e-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: 54.18 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQditnkpahvinrmgIALVPEGRRIfPELTVYEN 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQQAWI-QNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 101 LMMGaynRKDKEGIKRDLEWIFSLFPRL-------KERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPIL 173
Cdd:TIGR00957 719 ILFG---KALNEKYYQQVLEACALLPDLeilpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181651 174 VSEVFEVIqkINQEG-----TTILLVeqNALGALKVAHYGYVLETGQIVLEGKASELLD 227
Cdd:TIGR00957 796 GKHIFEHV--IGPEGvlknkTRILVT--HGISYLPQVDVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
16-226 |
2.45e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 53.65 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 16 GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLV----RAQKGKIIFNGQDItnkpahvinrmgIALVPEGRR- 90
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDL------------LRLSPRERRk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 91 --------IF--------PELTVYENLMMGAYNRKDKEGIKRDLEW----IFSLFPRL-----KERLKQLGGTLSGGEQQ 145
Cdd:PRK15093 86 lvghnvsmIFqepqscldPSERVGRQLMQNIPGWTYKGRWWQRFGWrkrrAIELLHRVgikdhKDAMRSFPYELTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 146 MLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQ-EGTTILLVEQNALGALKVAHYGYVLETGQIVLEGKASE 224
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKE 245
|
..
gi 490181651 225 LL 226
Cdd:PRK15093 246 LV 247
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-194 |
2.51e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.65 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 19 HAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITnkpahvinrmgialvpegrrIFPELTVY 98
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ--------------------FGREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 99 ENLmmgaynrkdkeGIKRDlewifslFPRLKERLKQLG-----------GTLSGGEQQMLAIGRALMSRPKLLMMDEPSL 167
Cdd:COG2401 104 DAI-----------GRKGD-------FKDAVELLNAVGlsdavlwlrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180
....*....|....*....|....*...
gi 490181651 168 GLAPILVSEVFEVIQKINQE-GTTILLV 194
Cdd:COG2401 166 HLDRQTAKRVARNLQKLARRaGITLVVA 193
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-166 |
2.65e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 3 DIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFnGQdiTNKPAHV-INRMG 81
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE--TVKLAYVdQSRDA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 82 IAlvpegrrifPELTVYEN-------LMMG-------AY----NRKDKEGIKRdlewifslfprlkerlkqlGGTLSGGE 143
Cdd:PRK11819 399 LD---------PNKTVWEEisggldiIKVGnreipsrAYvgrfNFKGGDQQKK-------------------VGVLSGGE 450
|
170 180
....*....|....*....|...
gi 490181651 144 QQMLAIGRALMSRPKLLMMDEPS 166
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPT 473
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-192 |
2.68e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGlvRAQKGkIIFNGQDITNkpahvinrmGIALVPEGRRI--------- 91
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTG-VITGGDRLVN---------GRPLDSSFQRSigyvqqqdl 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 92 -FPELTVYENLMMGAYNRKDKEGIKRD----LEWIFSLF--PRLKERLKQLGGT-LSGGEQQMLAIGRALMSRPKLLM-M 162
Cdd:TIGR00956 847 hLPTSTVRESLRFSAYLRQPKSVSKSEkmeyVEEVIKLLemESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfL 926
|
170 180 190
....*....|....*....|....*....|
gi 490181651 163 DEPSLGLAPILVSEVFEVIQKINQEGTTIL 192
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLADHGQAIL 956
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-197 |
3.40e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 53.68 E-value: 3.40e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181651 138 TLSGGEQQMLAIGRALMSRPKLLM--MDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQN 197
Cdd:PRK00635 476 TLSGGEQERTALAKHLGAELIGITyiLDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD 537
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-195 |
7.41e-08 |
|
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: 52.48 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 26 LKVPR-GQIVTLIGANGAGKTTTLSAIAGL-----------------VRAQKGKIIFNG-QDITN---KPAHVINRmgIA 83
Cdd:COG1245 93 LPVPKkGKVTGILGPNGIGKSTALKILSGElkpnlgdydeepswdevLKRFRGTELQDYfKKLANgeiKVAHKPQY--VD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 84 LVPegrRIFpELTVYEnLMMGAYNRKDKEGIKRDLEwifslfprLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMD 163
Cdd:COG1245 171 LIP---KVF-KGTVRE-LLEKVDERGKLDELAEKLG--------LENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*.
gi 490181651 164 EPSlglaPIL-VSE---VFEVIQKINQEGTTILLVE 195
Cdd:COG1245 238 EPS----SYLdIYQrlnVARLIRELAEEGKYVLVVE 269
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-204 |
7.68e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 24 IDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIifngqDITNKPAHVINRMG-IALVPEGRRIFPELTVYENL- 101
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI-----QIDGKTATRGDRSRfMAYLGHLPGLKADLSTLENLh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 102 -MMGAYNRKDKEGIKRDLEwIFSLFPRLKERLKQlggtLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEV 180
Cdd:PRK13543 105 fLCGLHGRRAKQMPGSALA-IVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRM 179
|
170 180
....*....|....*....|....
gi 490181651 181 IQKINQEGTTILLVEQNALGALKV 204
Cdd:PRK13543 180 ISAHLRGGGAALVTTHGAYAAPPV 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-194 |
9.78e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.10 E-value: 9.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 3 DIVLEVQSLHVYYgAIHA----IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQK--GKIIFNGQDI-TNKPAH 75
Cdd:NF040905 255 EVVFEVKNWTVYH-PLHPerkvVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNisGTVFKDGKEVdVSTVSD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 76 VINRmGIALVPEGRR----IFPElTVYENLMMGAYNRKDKEGIKRDLEWIfSLFPRLKERLK-------QLGGTLSGGEQ 144
Cdd:NF040905 334 AIDA-GLAYVTEDRKgyglNLID-DIKRNITLANLGKVSRRGVIDENEEI-KVAEEYRKKMNiktpsvfQKVGNLSGGNQ 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490181651 145 QMLAIGRALMSRPKLLMMDEPSLGlapILVS---EVFEVIQKINQEGTTILLV 194
Cdd:NF040905 411 QKVVLSKWLFTDPDVLILDEPTRG---IDVGakyEIYTIINELAAEGKGVIVI 460
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-165 |
1.19e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 4 IVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIifngqditnkpaHVINRMGIA 83
Cdd:PRK11147 318 IVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------------HCGTKLEVA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 84 LVPEGRRIF-PELTVYENLMMGaynRKDKE--GIKRDlewIFS-----LFPRLKER--LKqlggTLSGGEQQMLAIGRAL 153
Cdd:PRK11147 386 YFDQHRAELdPEKTVMDNLAEG---KQEVMvnGRPRH---VLGylqdfLFHPKRAMtpVK----ALSGGERNRLLLARLF 455
|
170
....*....|..
gi 490181651 154 MSRPKLLMMDEP 165
Cdd:PRK11147 456 LKPSNLLILDEP 467
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-164 |
1.62e-07 |
|
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: 51.48 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVInRMGIALVPEGRRIFPElTVYEN 100
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL-RFKITIIPQDPVLFSG-SLRMN 1379
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 101 LmmGAYNRKDKEGIKRDLE------WIFSLFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:TIGR00957 1380 L--DPFSQYSDEEVWWALElahlktFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDE 1447
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-214 |
2.79e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.98 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 138 TLSGGEQQMLAIGRALMS---RPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNaLGALKVAHygYVLETG 214
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHN-MHVVKVAD--YVLELG 885
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
16-195 |
2.81e-07 |
|
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: 49.56 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 16 GA-IHAIKGIDLKVPRGQIVTLIGANGAGKTT----TLSAiaglvRAQKgkiifngQDITNKPAHVINRMGIALVPEGRR 90
Cdd:cd03270 5 GArEHNLKNVDVDIPRNKLVVITGVSGSGKSSlafdTIYA-----EGQR-------RYVESLSAYARQFLGQMDKPDVDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 91 I---FPELTVYENLmmGAYNRKDKEGIKRDL-EWIFSLFPR--LKERLKQL-------------GGTLSGGEQQMLA--- 148
Cdd:cd03270 73 IeglSPAIAIDQKT--TSRNPRSTVGTVTEIyDYLRLLFARvgIRERLGFLvdvglgyltlsrsAPTLSGGEAQRIRlat 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490181651 149 -IGRALMSrpKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVE 195
Cdd:cd03270 151 qIGSGLTG--VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVE 196
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-165 |
3.30e-07 |
|
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: 50.32 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 19 HAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAqkgkiiFNGQditNKPAHVINrmgIALVPEGRRIFPELTVY 98
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD------FNGE---ARPQPGIK---VGYLPQEPQLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 99 ENLMMGAYNRKDKegIKRdLEWIFSLFP--------------RLKERLKQLGG------------------------TLS 140
Cdd:TIGR03719 87 ENVEEGVAEIKDA--LDR-FNEISAKYAepdadfdklaaeqaELQEIIDAADAwdldsqleiamdalrcppwdadvtKLS 163
|
170 180
....*....|....*....|....*
gi 490181651 141 GGEQQMLAIGRALMSRPKLLMMDEP 165
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEP 188
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
33-164 |
5.70e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 33 IVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITN--KP--AHVINRMGIALvpegrrifpELTVYENLMMGAYNR 108
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiaKPycTYIGHNLGLKL---------EMTVFENLKFWSEIY 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 490181651 109 KDKEGIKRDLEWIfslfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDE 164
Cdd:PRK13541 99 NSAETLYAAIHYF-----KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-70 |
6.69e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.59 E-value: 6.69e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181651 6 LEVQSLHVYYGAIH-AIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDIT 70
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-165 |
7.12e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 6 LEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKG--------KIIFNGQDITNKpahvi 77
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGtvkwsenaNIGYYAQDHAYD----- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 78 nrmgialvpegrriFPE-LTVYEnlMMGAYNR-KDKEGIKRdlewifSLFPRL---KERLKQLGGTLSGGEQQMLAIGRA 152
Cdd:PRK15064 395 --------------FENdLTLFD--WMSQWRQeGDDEQAVR------GTLGRLlfsQDDIKKSVKVLSGGEKGRMLFGKL 452
|
170
....*....|...
gi 490181651 153 LMSRPKLLMMDEP 165
Cdd:PRK15064 453 MMQKPNVLVMDEP 465
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
10-166 |
7.39e-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: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 10 SLHVYYGAIHaikgidlkvpRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNgQDITNKPAHVinrmgialvpegr 89
Cdd:COG1245 355 SLEVEGGEIR----------EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISYKPQYI------------- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 90 RIFPELTVYENLMMGAYNRKD----KEGIKRDLewifslfpRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEP 165
Cdd:COG1245 411 SPDYDGTVEEFLRSANTDDFGssyyKTEIIKPL--------GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
.
gi 490181651 166 S 166
Cdd:COG1245 483 S 483
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
131-225 |
1.46e-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: 48.47 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 131 RLKQLGGTLSGGEQQMLAIGRALMSR---PKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNaLGALKVAHy 207
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHN-LDVIKTAD- 899
|
90 100
....*....|....*....|....*.
gi 490181651 208 gYVLET--------GQIVLEGKASEL 225
Cdd:TIGR00630 900 -YIIDLgpeggdggGTVVASGTPEEV 924
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-172 |
2.37e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.81 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 2 SDIVLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITnkpAHVIN-RM 80
Cdd:NF033858 263 DEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDIAtRR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 81 GIALVPEGRRIFPELTVYENLMMGA--YNRKDKEGIKRdlewIFSLFPR--LKERLKQLGGTLSGGEQQMLAIGRALMSR 156
Cdd:NF033858 340 RVGYMSQAFSLYGELTVRQNLELHArlFHLPAAEIAAR----VAEMLERfdLADVADALPDSLPLGIRQRLSLAVAVIHK 415
|
170
....*....|....*.
gi 490181651 157 PKLLMMDEPSLGLAPI 172
Cdd:NF033858 416 PELLILDEPTSGVDPV 431
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-216 |
3.39e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.54 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 5 VLEVQSLHVYY----GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVI--N 78
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIelS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 79 RMGIALVPEGR-----RIF--------PELTVYEN------LMMGAYNRKDKEGIKRDLEWIfsLFPRLKERLKQLGGTL 139
Cdd:PRK10261 92 EQSAAQMRHVRgadmaMIFqepmtslnPVFTVGEQiaesirLHQGASREEAMVEAKRMLDQV--RIPEAQTILSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 140 SGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNALGALK-------VAHYGYVLE 212
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAeiadrvlVMYQGEAVE 249
|
....
gi 490181651 213 TGQI 216
Cdd:PRK10261 250 TGSV 253
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
31-166 |
9.08e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 31 GQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQ---DITNKPAHVINRMGIALVPEGRRIFPELtvyENLMMGAYN 107
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlAWVNQETPALPQPALEYVIDGDREYRQL---EAQLHDANE 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181651 108 RKDKEGI-----KRDL--EWIF-----SLFPRL---KERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEPS 166
Cdd:PRK10636 104 RNDGHAIatihgKLDAidAWTIrsraaSLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPT 177
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-193 |
1.06e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 45.76 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGqIVTLIGANGAGKTTTLSAIAGLVRAQKGKII----FNGQDITNKPAHVInrmgialvpegrrifpELT 96
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFdeedFYLGDDPDLPEIEI----------------ELT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 97 ---VYENLMMGAYNRKDKEGIKRDLEW----IFSLFPRLKERLKQLGGTLSG---------------------------- 141
Cdd:COG3593 77 fgsLLSRLLRLLLKEEDKEELEEALEElneeLKEALKALNELLSEYLKELLDgldlelelsldeledllkslslriedgk 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181651 142 ---------GEQQM--LAIGRALM-----SRPKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILL 193
Cdd:COG3593 157 elpldrlgsGFQRLilLALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVII 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-226 |
1.20e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 45.17 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 18 IHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVIN---RM-----GIALVPEgR 89
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqriRMifqdpSTSLNPR-Q 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 90 RIFPELTVYENLmmgaynRKDKEGIKRDlewifslfPRLKERLKQLG----------GTLSGGEQQMLAIGRALMSRPKL 159
Cdd:PRK15112 105 RISQILDFPLRL------NTDLEPEQRE--------KQIIETLRQVGllpdhasyypHMLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181651 160 LMMDEPSLGLAPILVSEVFEVIQKINQE-GTTILLVEQNaLGALK-VAHYGYVLETGQIVLEGKASELL 226
Cdd:PRK15112 171 IIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQH-LGMMKhISDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-166 |
1.27e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 26 LKVPR-GQIVTLIGANGAGKTTTLSAIAG-----------------LVRAQKGKIIFNG-QDITN---KPAHVINRmgIA 83
Cdd:PRK13409 93 LPIPKeGKVTGILGPNGIGKTTAVKILSGelipnlgdyeeepswdeVLKRFRGTELQNYfKKLYNgeiKVVHKPQY--VD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 84 LVPE---GrrifpelTVYENLMmgaynRKDKEGIKRDLEWIFSLFPRLKERLKQlggtLSGGEQQMLAIGRALMSRPKLL 160
Cdd:PRK13409 171 LIPKvfkG-------KVRELLK-----KVDERGKLDEVVERLGLENILDRDISE----LSGGELQRVAIAAALLRDADFY 234
|
....*.
gi 490181651 161 MMDEPS 166
Cdd:PRK13409 235 FFDEPT 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-165 |
1.36e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.34 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 1 MSDIVLEVQSLHVYY----------GAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDIT 70
Cdd:PRK11308 1 SQQPLLQAIDLKKHYpvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 71 NKPAHVIN--RMGIALV---PEG----RR----IFPE-LTVYENLmmGAYNRKDKegiKRDLEWIFSLFPRLKERLKQLg 136
Cdd:PRK11308 81 KADPEAQKllRQKIQIVfqnPYGslnpRKkvgqILEEpLLINTSL--SAAERREK---ALAMMAKVGLRPEHYDRYPHM- 154
|
170 180
....*....|....*....|....*....
gi 490181651 137 gtLSGGEQQMLAIGRALMSRPKLLMMDEP 165
Cdd:PRK11308 155 --FSGGQRQRIAIARALMLDPDVVVADEP 181
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
122-207 |
2.90e-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: 44.14 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 122 FSLFPRLKERLK----------QLG---GTLSGGEQQMLAIGRALMSR---PKLLMMDEPSLGLAPILVSEVFEVIQKIN 185
Cdd:cd03271 140 FENIPKIARKLQtlcdvglgyiKLGqpaTTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLV 219
|
90 100
....*....|....*....|..
gi 490181651 186 QEGTTILLVEQNaLGALKVAHY 207
Cdd:cd03271 220 DKGNTVVVIEHN-LDVIKCADW 240
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-194 |
6.27e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 25 DLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITN----KPAHVIN----RMGIALVPEGRRIFpELT 96
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRlsfeQLQKLVSdewqRNNTDMLSPGEDDT-GRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 97 VYENLMMGAynrkDKEGIKRDLEWIFSLFPRLKERLKQLggtlSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSE 176
Cdd:PRK10938 102 TAEIIQDEV----KDPARCEQLAQQFGITALLDRRFKYL----STGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170
....*....|....*...
gi 490181651 177 VFEVIQKINQEGTTILLV 194
Cdd:PRK10938 174 LAELLASLHQSGITLVLV 191
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
139-198 |
8.01e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 8.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181651 139 LSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPI---LVSEVFEVIqkINQEGTTILLVEQNA 198
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLnrqLVRRFVDVL--ISEGETQLLFVSHHA 462
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-70 |
1.29e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.09 E-value: 1.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181651 5 VLEVQSLHVYYGAIHAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGL--VRAQKGKIIFNGQDIT 70
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLL 68
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
36-165 |
1.76e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.03 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 36 LIGANGAGKTTTLSAIAGL-------VRAQKGkiifngqdITnkpahvinrmgIALVPEGRRIFPELTVYENLMMGAYNR 108
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVdkefegeARPAPG--------IK-----------VGYLPQEPQLDPEKTVRENVEEGVAEV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 109 KDKegIKRdLEWIFSLFP--------------RLKERLKQLGG------------------------TLSGGEQQMLAIG 150
Cdd:PRK11819 99 KAA--LDR-FNEIYAAYAepdadfdalaaeqgELQEIIDAADAwdldsqleiamdalrcppwdakvtKLSGGERRRVALC 175
|
170
....*....|....*
gi 490181651 151 RALMSRPKLLMMDEP 165
Cdd:PRK11819 176 RLLLEKPDMLLLDEP 190
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-185 |
4.77e-04 |
|
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: 40.89 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 21 IKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRaqkgkiIFNGqdITNKPAhvinRMGIALVPE----GRRIFPELT 96
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP------VYGG--RLTKPA----KGKLFYVPQrpymTLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 97 VYEnlmMGAYNRKDKEGIKRDLEWIFSLFpRLKERLKQLGG---------TLSGGEQQMLAIGRALMSRPKLLMMDEPSL 167
Cdd:TIGR00954 536 IYP---DSSEDMKRRGLSDKDLEQILDNV-QLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170
....*....|....*...
gi 490181651 168 GLAPILVSEVFEVIQKIN 185
Cdd:TIGR00954 612 AVSVDVEGYMYRLCREFG 629
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-64 |
5.89e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 39.28 E-value: 5.89e-04
10 20 30
....*....|....*....|....*....|....*
gi 490181651 30 RGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIF 64
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY 35
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-237 |
6.27e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 137 GTLSGGEQQMLA----IGRALMSrpKLLMMDEPSLGLAPILVSEVFEVIQKINQEGTTILLVEQNAlGALKVAHY----- 207
Cdd:TIGR00630 487 GTLSGGEAQRIRlatqIGSGLTG--VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDE-DTIRAADYvidig 563
|
90 100 110
....*....|....*....|....*....|..
gi 490181651 208 -GYVLETGQIVLEGKASELL-DNEMVRKAYLG 237
Cdd:TIGR00630 564 pGAGEHGGEVVASGTPEEILaNPDSLTGQYLS 595
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
139-211 |
1.06e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 1.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181651 139 LSGGEQQMLAIGRALMSRPKLLMMDEPSLGL---APILVSEVFEVIqKINQEGTTILLVEQnaLGALKVAHYGYVL 211
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLdnkSEYLVQKTINNL-KGNENRITIIIAHR--LSTIRYANTIFVL 652
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
8-134 |
1.16e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.21 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 8 VQSLHVY-YGAIHAIKgIDLKVPRGQIVtLIGANGAGKTTTLSAIAGLVRAQKGKI---------IFNGQDITNKPAhvi 77
Cdd:COG3950 3 IKSLTIEnFRGFEDLE-IDFDNPPRLTV-LVGENGSGKTTLLEAIALALSGLLSRLddvkfrkllIRNGEFGDSAKL--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181651 78 nrmgIALVPEGRRIF-PELTVYENLMMGAYNRKD--------KEGIKRDLEWIFSLFPRLKERLKQ 134
Cdd:COG3950 78 ----ILYYGTSRLLLdGPLKKLERLKEEYFSRLDgydslldeDSNLREFLEWLREYLEDLENKLSD 139
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-224 |
3.91e-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: 37.17 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 28 VPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQDITNKPAHVinrmgialvpegrrifpeltvyenlmmgayn 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 108 rkdkegikrdlewifslfprlkerlkqlggTLSGGEQQMLAIGRALMSRPKLLMMDEPSLGLAPILVSEVFEVIQKINQE 187
Cdd:cd03222 71 ------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180 190
....*....|....*....|....*....|....*...
gi 490181651 188 GT-TILLVEQNALGALKVAHYGYVLEtGQIVLEGKASE 224
Cdd:cd03222 121 GKkTALVVEHDLAVLDYLSDRIHVFE-GEPGVYGIASQ 157
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-197 |
7.45e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 36.72 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 19 HAIKGIDLKVPRGQIVTLIGANGAGKTTTLSAIAGLVRAQKGKIIFNGQditnkpahvINRMGIALVPEGRRIFPELTVY 98
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE---------VSVIAISAGLSGQLTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181651 99 ENLMMGaYNRKDkegIKRDLEWIFSlFPRLKERLKQLGGTLSGGEQQMLAIGRALMSRPKLLMMDEP-SLGlAPILVSEV 177
Cdd:PRK13546 109 KMLCMG-FKRKE---IKAMTPKIIE-FSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSVG-DQTFAQKC 182
|
170 180
....*....|....*....|
gi 490181651 178 FEVIQKINQEGTTILLVEQN 197
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHN 202
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
21-64 |
7.78e-03 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 36.57 E-value: 7.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 490181651 21 IKGIDLKVP--RGQIVTLIGANGAGKTTTLSAIAGlvRAQKGKIIF 64
Cdd:pfam00006 2 IRAIDGLLPigRGQRIGIFGGSGVGKTVLAGMIAR--QASADVVVY 45
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
17-52 |
9.33e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 36.28 E-value: 9.33e-03
10 20 30
....*....|....*....|....*....|....*..
gi 490181651 17 AIHAIKGIDLKVPrgqiVT-LIGANGAGKTTTLSAIA 52
Cdd:COG3910 26 AVRNLEGLEFHPP----VTfFVGENGSGKSTLLEAIA 58
|
|
| |
