|
Name |
Accession |
Description |
Interval |
E-value |
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-237 |
1.14e-135 |
|
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: 380.87 E-value: 1.14e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 3 AALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGI 82
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 83 AQSPEGRRVFPDMSVEENLLMGTIPI-GMDHAEEDMQRMFELFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLL 161
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARrDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600102 162 DEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEVRNAYLGG 237
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 ... |
6-227 |
1.64e-118 |
|
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: 336.71 E-value: 1.64e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQS 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 PEGRRVFPDMSVEENLLMGTIPIGMDHAEEDMQRMFELFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 166 LGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGN 227
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-237 |
8.56e-100 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 290.24 E-value: 8.56e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASN 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 GIAQSPEGRRVFPDMSVEENLLMGTIPIGMDHAEEDMQRMFELFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLL 160
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600102 161 LDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEVRNAYLGG 237
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLGG 237
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-224 |
6.95e-72 |
|
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: 218.93 E-value: 6.95e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQS 85
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 PEGRRVFPDMSVEENLLMGTIPIGMDHAEEDmQRMFELFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRSRKIP-DEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 166 LGLAPIVVKQIFQTLRELA-RSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRaEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-238 |
1.44e-61 |
|
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: 193.33 E-value: 1.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 2 SAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNG 81
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 82 IA---QSPegrRVFPDMSVEENLLMGT--------------IPIGMDHAEEDMQRMFEL--FPRLKERRNQRAMTMSGGE 142
Cdd:COG0411 81 IArtfQNP---RLFPELTVLENVLVAAharlgrgllaallrLPRARREEREARERAEELleRVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 143 QQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELAR-SGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSG 221
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
250
....*....|....*..
gi 15600102 222 EELLGNQEVRNAYLGGH 238
Cdd:COG0411 238 AEVRADPRVIEAYLGEE 254
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-230 |
1.98e-58 |
|
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: 184.95 E-value: 1.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIA-- 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 84 -QSPegrRVFPDMSVEENLLMGTIPIG---------MDHAEEDMQRMFEL--FPRLKERRNQRAMTMSGGEQQMLAIARA 151
Cdd:cd03219 81 fQIP---RLFPELTVLENVMVAAQARTgsglllaraRREEREARERAEELleRVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEV 230
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-236 |
2.00e-54 |
|
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: 174.27 E-value: 2.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQS 85
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 PEGRRVFPDMSVEENLL--MGTIPIGMDHAEEDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:cd03218 81 PQEASIFRKLTVEENILavLEIRGLSKKEREEKLEELLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600102 164 PSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEVRNAYLG 236
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-225 |
3.87e-54 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 173.71 E-value: 3.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAqs 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 PEGRRVFPDMSVEENL-LMGTI-PIGMDHAEEDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:COG1131 79 PQEPALYPDLTVRENLrFFARLyGLPRKEARERIDELLELF-GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 164 PSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
15-238 |
1.31e-51 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 167.51 E-value: 1.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 15 YGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGI---AQSPEgrrV 91
Cdd:COG1137 13 YGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIgylPQEAS---I 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 92 FPDMSVEENLL--MGTIPIGMDHAEEDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:COG1137 90 FRKLTVEDNILavLELRKLSKKEREERLEELLEEF-GITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 170 PIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEVRNAYLGGH 238
Cdd:COG1137 169 PIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLGED 237
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
15-238 |
8.05e-49 |
|
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: 160.52 E-value: 8.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 15 YGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQSPEGRRVFPD 94
Cdd:TIGR04406 11 YKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYLPQEASIFRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 95 MSVEENLlMGTIPIGMDH-AEEDMQRMFELFPRL--KERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:TIGR04406 91 LTVEENI-MAVLEIRKDLdRAEREERLEALLEEFqiSHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600102 172 VVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEVRNAYLGGH 238
Cdd:TIGR04406 170 AVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLGEQ 236
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-229 |
1.46e-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: 154.03 E-value: 1.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFY-GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASN-GIa 83
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKvGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 84 qspegrrVF--PD-----MSVEENLLMGTIPIGMDHAE--EDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMS 154
Cdd:COG1122 80 -------VFqnPDdqlfaPTVEEDVAFGPENLGLPREEirERVEEALELV-GLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 155 RPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQE 229
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-215 |
3.72e-44 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 146.00 E-value: 3.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAqs 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 PEGRRVFPDMSVEENLlmgtipigmdhaeedmqrmfelfprlkerrnqramTMSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:cd03230 79 PEEPSLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600102 166 LGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-234 |
4.50e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 148.31 E-value: 4.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAH--YVA 78
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 79 sngiaQSPEGRRVFPdMSVEENLLMGTIP-IGM---------DHAEEDMQRMfelfpRLKERRNQRAMTMSGGEQQMLAI 148
Cdd:COG1121 82 -----QRAEVDWDFP-ITVRDVVLMGRYGrRGLfrrpsradrEAVDEALERV-----GLEDLADRPIGELSGGQQQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAyVMVTGEIRMSGSGEELLGNQ 228
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEEVLTPE 229
|
....*.
gi 15600102 229 EVRNAY 234
Cdd:COG1121 230 NLSRAY 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-210 |
6.08e-43 |
|
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: 144.15 E-value: 6.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 7 EFREVDVFY--GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASN-GIA 83
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 84 -QSPEGRRVFPdmSVEENLLMGTIPIGMDHAEEDM--QRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLL 160
Cdd:cd03225 81 fQNPDDQFFGP--TVEEEVAFGLENLGLPEEEIEErvEEALELV-GLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600102 161 LDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVM 210
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-234 |
2.24e-42 |
|
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: 144.03 E-value: 2.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNgIA- 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 84 --QSPEGRrvfPDMSVEENLLMGTIP-IGM---------DHAEEDMQRMfelfpRLKERRNQRAMTMSGGEQQMLAIARA 151
Cdd:COG1120 80 vpQEPPAP---FGLTVRELVALGRYPhLGLfgrpsaedrEAVEEALERT-----GLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEV 230
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELL 231
|
....
gi 15600102 231 RNAY 234
Cdd:COG1120 232 EEVY 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-235 |
1.06e-41 |
|
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: 142.30 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASngIAQ 84
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ--IGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 SPEGRRVFPDMSVEENLLM-GTI-PIGMDHAEEDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYfAELyGLFDEELKKRIEELIELL-GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600102 163 EPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELL---GNQEVRNAYL 235
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELReeiGEENLEDAFV 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-224 |
1.07e-41 |
|
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: 141.55 E-value: 1.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLL-----MSIFGQPRAAAGQILYRGQDIRQKSAHYVA-- 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 79 -SNGIA-QSPEgrrVFPdMSVEENLLMGTIPIGMDHAEEDMQRMFE------LFPRLKerRNQRAMTMSGGEQQMLAIAR 150
Cdd:cd03260 81 rRVGMVfQKPN---PFP-GSIYDNVAYGLRLHGIKLKEELDERVEEalrkaaLWDEVK--DRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600102 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSgMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-219 |
5.10e-41 |
|
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: 139.59 E-value: 5.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 7 EFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAH--YVAsngiaQ 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigYVP-----Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 SPEGRRVFPdMSVEENLLMGTIP-IGMDH--AEEDMQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIARALMSRPKLL 159
Cdd:cd03235 76 RRSIDRDFP-ISVRDVVLMGLYGhKGLFRrlSKADKAKVDEALERvgLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 160 LLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRaYVMVTGEIRMSG 219
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-215 |
1.04e-40 |
|
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: 138.78 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYG----PIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKS----AHYV 77
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 78 ASN-GIaqspegrrVF------PDMSVEENLLMGTIPIGmDHAEEDMQRMFELFPR--LKERRNQRAMTMSGGEQQMLAI 148
Cdd:cd03255 81 RRHiGF--------VFqsfnllPDLTALENVELPLLLAG-VPKKERRERAEELLERvgLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600102 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELAR-SGMTIFLVEQNANHAlKLSDRAYVMVTGEI 215
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-224 |
1.13e-40 |
|
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: 139.29 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQS 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 pegRRVFPDMSVEENLLMGTIPIGMDHAE--EDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:cd03300 81 ---YALFPHLTVFENIAFGLRLKKLPKAEikERVAEALDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 164 PSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-164 |
1.55e-40 |
|
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: 136.24 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVaSNGIAQSPEGRRVFPDMSVEEN 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL-RKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 101 LLMGTIPIGMDHAEEDMQ-----RMFELFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARaeealEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-214 |
7.82e-40 |
|
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: 134.68 E-value: 7.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 7 EFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSahyvasngiaqSP 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP-----------LE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 87 EGRRvfpdmsveenllmgtiPIGMdhaeedmqrMFELfprlkerrnqramtmSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:cd00267 70 ELRR----------------RIGY---------VPQL---------------SGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600102 167 GLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGE 214
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-236 |
8.93e-40 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 137.43 E-value: 8.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASN 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 GIAQSPEGRRVFPDMSVEENLLM------------GTIPI---------GMDHAEEDMQRMfelfpRLKERRNQRAMTMS 139
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVaqhqqlktglfsGLLKTpafrraeseALDRAATWLERV-----GLLEHANRQAGNLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 140 GGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMS 218
Cdd:PRK11300 156 YGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN 235
|
250
....*....|....*...
gi 15600102 219 GSGEELLGNQEVRNAYLG 236
Cdd:PRK11300 236 GTPEEIRNNPDVIKAYLG 253
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-215 |
1.25e-39 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 135.72 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHyvaSNGIAQS 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE---RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 PEGRRVFPDMSVEENLLMGTIPIGMDHAEED--MQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRarVRELLELV-GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600102 164 PSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:cd03259 157 PLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-227 |
1.59e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 136.28 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHyvasngIAQ 84
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKD------INK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 SpegRR----VF------PDMSVEENLLMGtiPI---GMDH--AEEDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIA 149
Cdd:COG1126 75 L---RRkvgmVFqqfnlfPHLTVLENVTLA--PIkvkKMSKaeAEERAMELLERV-GLADKADAYPAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600102 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGN 227
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-206 |
3.53e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 134.79 E-value: 3.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGP-IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVasngiaq 84
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREI------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 sPEGRR----VF------PDMSVEENLLMGTIPIGMDHAE--EDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARAL 152
Cdd:COG2884 75 -PYLRRrigvVFqdfrllPDRTVYENVALPLRVTGKSRKEirRRVREVLDLV-GLSDKAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600102 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLveqnANHALKLSDR 206
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLI----ATHDLELVDR 202
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-215 |
3.77e-39 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 134.94 E-value: 3.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFY----GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASN 80
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 G-----IAQSPeGRRVFPDMSVEENLLMGTIPIGMDHAEEDMQR----MFELFPRLKERRNQRAMTMSGGEQQMLAIARA 151
Cdd:cd03257 81 RkeiqmVFQDP-MSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEavllLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-215 |
5.23e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 134.79 E-value: 5.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 3 AALLEFREVDVFYG----PIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKS----A 74
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 75 HYvasngiaqspegRR-----VF------PDMSVEENLLMGTIPIGMDHAEeDMQRMFELFPR--LKERRNQRAMTMSGG 141
Cdd:COG1136 82 RL------------RRrhigfVFqffnllPELTALENVALPLLLAGVSRKE-RRERARELLERvgLGDRLDHRPSQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 142 EQQMLAIARALMSRPKLLLLDEP--SL----GlapivvKQIFQTLRELAR-SGMTIFLV---EQNANHAlklsDRAYVMV 211
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPtgNLdsktG------EEVLELLRELNReLGTTIVMVthdPELAARA----DRVIRLR 218
|
....
gi 15600102 212 TGEI 215
Cdd:COG1136 219 DGRI 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-215 |
6.16e-39 |
|
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: 134.19 E-value: 6.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAhyvasngiaQS 85
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKK---------NI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 PEGRR----------VFPDMSVEENLLMGTIPI-GMDHAEEDmQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIARAL 152
Cdd:cd03262 72 NELRQkvgmvfqqfnLFPHLTVLENITLAPIKVkGMSKAEAE-ERALELLEKvgLADKADAYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600102 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-210 |
6.35e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 140.54 E-value: 6.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 2 SAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNG 81
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 82 IA---QSPEgrrVFPDMSVEENLLMGTIPIG---MDHAEedMQRMF-ELFPRLKERRN--QRAMTMSGGEQQMLAIARAL 152
Cdd:COG1129 81 IAiihQELN---LVPNLSVAENIFLGREPRRgglIDWRA--MRRRArELLARLGLDIDpdTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVeqnaNHAL----KLSDRAYVM 210
Cdd:COG1129 156 SRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYI----SHRLdevfEIADRVTVL 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-224 |
7.31e-38 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 131.47 E-value: 7.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 20 ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHyvASNGIAQSPEGRRVFPDMSVEE 99
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA--ARQSLGYCPQFDALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 100 NL-LMGTIP-IGMDHAEEDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIF 177
Cdd:cd03263 95 HLrFYARLKgLPKSEIKEEVELLLRVL-GLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIW 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15600102 178 QTLRELaRSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:cd03263 174 DLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-229 |
2.49e-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: 136.57 E-value: 2.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 3 AALLEFREVDVFY--GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFG---QPRAAAGQILYRGQDIRQKSAHyV 77
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEA-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 78 ASNGIA---QSPEGRrvFPDMSVEENLLMGTIPIGMDHAE--EDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARAL 152
Cdd:COG1123 81 RGRRIGmvfQDPMTQ--LNPVTVGDQIAEALENLGLSRAEarARVLELLEAV-GLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600102 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLRELAR-SGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQE 229
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-224 |
2.58e-37 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 130.95 E-value: 2.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 4 ALLEFREVDV-FYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAhyvasngi 82
Cdd:COG3638 1 PMLELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 83 AQSPEGRR----VF------PDMSVEENLLMGTIP--------IGMdHAEEDMQRMFELFPR--LKERRNQRAMTMSGGE 142
Cdd:COG3638 73 RALRRLRRrigmIFqqfnlvPRLSVLTNVLAGRLGrtstwrslLGL-FPPEDRERALEALERvgLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 143 QQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSG 221
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPP 231
|
...
gi 15600102 222 EEL 224
Cdd:COG3638 232 AEL 234
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-224 |
3.16e-37 |
|
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: 130.38 E-value: 3.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYG-PIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVAS----- 79
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 80 NGIAQSPegrRVFPDMSVEENLLMGTIP--------IGMDHaEEDMQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIA 149
Cdd:cd03256 81 GMIFQQF---NLIERLSVLENVLSGRLGrrstwrslFGLFP-KEEKQRALAALERvgLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600102 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-236 |
9.09e-37 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 129.24 E-value: 9.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 19 QALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQSPEGRRVFPDMSVE 98
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEASIFRRLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 99 ENLlMGTIPIGMD-HAEEDMQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQ 175
Cdd:PRK10895 97 DNL-MAVLQIRDDlSAEQREDRANELMEEfhIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600102 176 IFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEVRNAYLG 236
Cdd:PRK10895 176 IKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-227 |
1.18e-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: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFY-----GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAH 75
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 76 YVASNG-----IAQSPEGrRVFPDMSVEENLLMGTIPIGMDHAEEDMQR------MFELFPRLKERrnqRAMTMSGGEQQ 144
Cdd:COG1123 336 SLRELRrrvqmVFQDPYS-SLNPRMTVGDIIAEPLRLHGLLSRAERRERvaelleRVGLPPDLADR---YPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 145 MLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEE 223
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
....
gi 15600102 224 LLGN 227
Cdd:COG1123 492 VFAN 495
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-214 |
1.26e-36 |
|
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: 126.92 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQksahyvasnGIAQS 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTD---------LEDEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 PEGRRvfpdmsveenllmgtiPIGMDHAEedmqrmFELFPRLKERRNqRAMTMSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:cd03229 72 PPLRR----------------RIGMVFQD------FALFPHLTVLEN-IALGLSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600102 166 LGLAPIVVKQIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVMVTGE 214
Cdd:cd03229 129 SALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-224 |
1.47e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 131.76 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIrqksahyvasN 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----------T 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 GIAqsPEGRRV---------FPDMSVEEN----LLMGtipiGMDHAE--EDMQRMFELFpRLKERRNQRAMTMSGGEQQM 145
Cdd:COG3842 71 GLP--PEKRNVgmvfqdyalFPHLTVAENvafgLRMR----GVPKAEirARVAELLELV-GLEGLADRYPHQLSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARSGMTIFLV-----EqnanhALKLSDRAYVMVTGEIRMSG 219
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVthdqeE-----ALALADRIAVMNDGRIEQVG 218
|
....*
gi 15600102 220 SGEEL 224
Cdd:COG3842 219 TPEEI 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-227 |
1.84e-36 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 128.67 E-value: 1.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSahyVASNGIAQ 84
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPK---VDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 spEGRRVF------PDMSVEENLLMGTIPI-GMDHAEEDMQRMfELFPR--LKERRNQRAMTMSGGEQQMLAIARALMSR 155
Cdd:PRK09493 78 --EAGMVFqqfylfPHLTALENVMFGPLRVrGASKEEAEKQAR-ELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 156 PKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGN 227
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-224 |
2.94e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 129.46 E-value: 2.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAH---YVasngi 82
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigYL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 83 aqsPEGRRVFPDMSVEENLL-MGTIPiGMDHAE--EDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLL 159
Cdd:COG4152 77 ---PEERGLYPKMKVGEQLVyLARLK-GLSKAEakRRADEWLERL-GLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 160 LLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
3.13e-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: 128.28 E-value: 3.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFY----GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAH- 75
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 76 -YVasngiAQSPegrRVFPDMSVEENLLMGTIPIGMDHAE--EDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARAL 152
Cdd:COG1116 83 gVV-----FQEP---ALLPWLTVLDNVALGLELRGVPKAErrERARELLELV-GLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600102 153 MSRPKLLLLDEPslglapivvkqiF-----QT--------LRELARSGMTIFLVEQNANHALKLSDRAYVM 210
Cdd:COG1116 154 ANDPEVLLMDEP------------FgaldaLTrerlqdelLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-234 |
4.79e-36 |
|
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: 127.61 E-value: 4.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGP----IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKsahyvasn 80
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 giaQSPEGRR----VF--------PDMSVEENLLMGTIPIGMDHAEEDMQRMFE---LFPRLKERR-NQramtMSGGEQQ 144
Cdd:COG1124 73 ---RRKAFRRrvqmVFqdpyaslhPRHTVDRILAEPLRIHGLPDREERIAELLEqvgLPPSFLDRYpHQ----LSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 145 MLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEE 223
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
250
....*....|.
gi 15600102 224 LLgnQEVRNAY 234
Cdd:COG1124 226 LL--AGPKHPY 234
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
15-224 |
1.38e-35 |
|
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: 125.56 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 15 YGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAqsPEGRRVFPD 94
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV--FQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 95 MSVEENLLMGTIPIGMDHAEEDmQRMFEL--FPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIV 172
Cdd:cd03265 88 LTGWENLYIHARLYGVPGAERR-ERIDELldFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600102 173 VKQIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:cd03265 167 RAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-225 |
1.51e-35 |
|
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: 126.35 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 4 ALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILY-----RGQ----DIRQKSA 74
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerRGGedvwELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 75 HYvasngiaqSPE-GRRVFPDMSVEENLLMG---TIPIGMDHAEEDMQRMFEL--FPRLKERRNQRAMTMSGGEQQMLAI 148
Cdd:COG1119 82 LV--------SPAlQLRFPRDETVLDVVLSGffdSIGLYREPTDEQRERARELleLLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSG-MTIFLVEQNA-------NHALKLSDrayvmvtGEIRMSGS 220
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVeeippgiTHVLLLKD-------GRVVAAGP 226
|
....*
gi 15600102 221 GEELL 225
Cdd:COG1119 227 KEEVL 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-219 |
2.04e-35 |
|
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: 125.09 E-value: 2.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGqdirqKSAHYVASNGIAQS 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-----KPLDIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 PEGRRVFPDMSVEENLLMGTIPIGMDHAE--EDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEarRRIDEWLERL-ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600102 164 PSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSG 219
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-210 |
2.15e-35 |
|
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: 123.31 E-value: 2.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAqs 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 pegrRVFpdmsveenllmgtipigmdhaeedmqrmfelfprlkerrnQramtMSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:cd03216 79 ----MVY----------------------------------------Q----LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600102 166 LGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVM 210
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVL 155
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-219 |
2.43e-35 |
|
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: 123.70 E-value: 2.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 7 EFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASngiaqsp 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 87 egrrvfpdmsveenlLMGTIP-----IGMDHaeedmqrmfelfprLKERRnqrAMTMSGGEQQMLAIARALMSRPKLLLL 161
Cdd:cd03214 74 ---------------KIAYVPqalelLGLAH--------------LADRP---FNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 162 DEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSG 219
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-224 |
3.53e-35 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 124.92 E-value: 3.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSahyvasnGIAQS 85
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLS-------EAELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 PEGRRV---------FPDMSVEENLLMgtiPIGMdHAEEDMQRMFEL------FPRLKERRNQRAMTMSGGEQQMLAIAR 150
Cdd:cd03261 74 RLRRRMgmlfqsgalFDSLTVFENVAF---PLRE-HTRLSEEEIREIvlekleAVGLRGAEDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-232 |
4.47e-35 |
|
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: 124.71 E-value: 4.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHyvasn 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 giAQSPEGRRV---------FPDMSVEENLlmgtipigmdhaeedmqrMFEL--FPRLKER-RNQRAMTM---------- 138
Cdd:COG1127 76 --ELYELRRRIgmlfqggalFDSLTVFENV------------------AFPLreHTDLSEAeIRELVLEKlelvglpgaa 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 139 -------SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVM 210
Cdd:COG1127 136 dkmpselSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVL 215
|
250 260
....*....|....*....|....
gi 15600102 211 VTGEIRMSGSGEELL--GNQEVRN 232
Cdd:COG1127 216 ADGKIIAEGTPEELLasDDPWVRQ 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-225 |
5.91e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 129.76 E-value: 5.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTlLMSI-FGQPRAAAGQILYRGQDIRQKSAHYVAS 79
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKST-LMKIlYGLYQPDSGEILIDGKPVRIRSPRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 80 NGIA---QSPegrRVFPDMSVEENLLMGTIP-----IGMDHAEEDMQRMFELFPrLKERRNQRAMTMSGGEQQMLAIARA 151
Cdd:COG3845 80 LGIGmvhQHF---MLVPNLTVAENIVLGLEPtkggrLDRKAARARIRELSERYG-LDVDPDAKVEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVeqnaNHALK----LSDRAYVM----VTGEIRMSGSGEE 223
Cdd:COG3845 156 LYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFI----THKLRevmaIADRVTVLrrgkVVGTVDTAETSEE 231
|
..
gi 15600102 224 LL 225
Cdd:COG3845 232 EL 233
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-215 |
6.02e-35 |
|
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: 122.93 E-value: 6.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 20 ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQSPEGRR---VFPDMS 96
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPEDRKregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 97 VEENLLMGTIpigmdhaeedmqrmfelfprlkerrnqramtMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQI 176
Cdd:cd03215 95 VAENIALSSL-------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEI 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15600102 177 FQTLRELARSGMTIFLV-----EqnanhALKLSDRAYVMVTGEI 215
Cdd:cd03215 144 YRLIRELADAGKAVLLIsseldE-----LLGLCDRILVMYEGRI 182
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-215 |
6.32e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.77 E-value: 6.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAH-------YVA 78
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPewrrqvaYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 79 sngiaQSPegrrVFPDMSVEENLLMgtiPIGMDHAEEDMQRMFELFPRL---KERRNQRAMTMSGGEQQMLAIARALMSR 155
Cdd:COG4619 81 -----QEP----ALWGGTVRDNLPF---PFQLRERKFDRERALELLERLglpPDILDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600102 156 PKLLLLDEPSLGLAPIVVKQIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-219 |
1.12e-34 |
|
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: 123.10 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAhyvASNGIAQS 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE---ALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 PEGRRVFPDMSVEENLLMGTIPIGMDHAEedMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKKR--IDEVLDVV-GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600102 166 LGLAPIVVKQIFQTLRELARSGMTIFLveqnANHAL----KLSDRAYVMVTGEIRMSG 219
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLI----SSHLLseiqKVADRIGIINKGKLIEEG 208
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-210 |
1.68e-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: 122.97 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYG----PIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAH--YVas 79
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDrgYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 80 ngiAQSPegrRVFPDMSVEENLLMGTIPIGMDHAE--EDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPK 157
Cdd:cd03293 79 ---FQQD---ALLPWLTVLDNVALGLELQGVPKAEarERAEELLELV-GLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600102 158 LLLLDEPSLGLAPIVVKQIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVM 210
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-210 |
2.17e-34 |
|
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: 120.95 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYG--PIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNgIA 83
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 84 ---QSPegrrVFPDMSVEENLLmgtipigmdhaeedmqrmfelfprlkerrnqramtmSGGEQQMLAIARALMSRPKLLL 160
Cdd:cd03228 80 yvpQDP----FLFSGTIRENIL------------------------------------SGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600102 161 LDEPSLGLAPIVVKQIFQTLRELARsGMTIFLVEQNAnHALKLSDRAYVM 210
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHRL-STIRDADRIIVL 167
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-215 |
5.48e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 127.06 E-value: 5.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 20 ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQSPEGRR---VFPDMS 96
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAYVPEDRKgegLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 97 VEENLLMGTIP-----IGMDHAEEDM--QRMFELFpRLK-ERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGl 168
Cdd:COG1129 347 IRENITLASLDrlsrgGLLDRRRERAlaEEYIKRL-RIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRG- 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 169 apIVV---KQIFQTLRELARSGMTIFLV-----EqnanhALKLSDRAYVMVTGEI 215
Cdd:COG1129 425 --IDVgakAEIYRLIRELAAEGKAVIVIsselpE-----LLGLSDRILVMREGRI 472
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-206 |
2.77e-33 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 119.66 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFY-GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVAS--NG 81
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLlrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 82 IAQSPEGRRVFPDMSVEENLLMGTIPIGMDhaEEDMQRMFELFPR---LKERRNQRAMTMSGGEQQMLAIARALMSRPKL 158
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKK--EREIQRRVGAALRqvgLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600102 159 LLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLveqnANHALKLSDR 206
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILDLLKRLNKRGTTVIV----ATHDLSLVDR 202
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-228 |
7.51e-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: 124.87 E-value: 7.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 2 SAALLEFREVDVFYGP-IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASN 80
Cdd:COG4988 333 GPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 G--IAQSPegrRVFPDmSVEENLLMGTipigMDHAEEDMQR------MFELFPRLKE----RRNQRAMTMSGGEQQMLAI 148
Cdd:COG4988 413 IawVPQNP---YLFAG-TIRENLRLGR----PDASDEELEAaleaagLDEFVAALPDgldtPLGEGGRGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARsGMTIFLVEQNAnHALKLSDRAYVMVTGEIRMSGSGEELLGNQ 228
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-223 |
8.10e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 122.36 E-value: 8.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQ 84
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 SpegRRVFPDMSVEEN----LLMGTIPigmdHAE-----EDMQRMFelfpRLKERRNQRAMTMSGGEQQMLAIARALMSR 155
Cdd:PRK09452 94 S---YALFPHMTVFENvafgLRMQKTP----AAEitprvMEALRMV----QLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 156 PKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEE 223
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-223 |
1.02e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 119.42 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 20 ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNgIAqspegrRVF------- 92
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY-IG------RVFqdpmmgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 93 -PDMSVEENLLMG-------TIPIGMDHAEEDMQRmfELFPRLK---ERR-NQRAMTMSGGEQQMLAIARALMSRPKLLL 160
Cdd:COG1101 94 aPSMTIEENLALAyrrgkrrGLRRGLTKKRRELFR--ELLATLGlglENRlDTKVGLLSGGQRQALSLLMATLTKPKLLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600102 161 LDEPSLGLAPIVVKQIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEE 223
Cdd:COG1101 172 LDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVSGEE 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-215 |
1.26e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 118.99 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMS-------IFGQprAAAGQILYRGQDIRQKSAhyva 78
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGA--RVEGEILLDGEDIYDPDV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 79 sngiaqSPEG--RRV---------FPdMSVEENLLMGtIPIGMDHAEEDMQRMFE-------LFPRLKERRNQRAMTMSG 140
Cdd:COG1117 86 ------DVVElrRRVgmvfqkpnpFP-KSIYDNVAYG-LRLHGIKSKSELDEIVEeslrkaaLWDEVKDRLKKSALGLSG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 141 GEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSgMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-207 |
1.95e-32 |
|
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: 117.19 E-value: 1.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 4 ALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVAS-NGI 82
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRlAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 83 AQSPEgrrVFPDMSVEENLLMGTIPIGMDHAEEDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:COG4133 81 GHADG---LKPELTVRENLRFWAALYGLRADREAIDEALEAV-GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600102 163 EPSLGLAPIVVKQIFQTLRELARSGMTIFL-----VEQNANHALKLSDRA 207
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLARGGAVLLtthqpLELAAARVLDLGDFK 206
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-225 |
2.22e-32 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 124.18 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGP--IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNgIA 83
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ-IG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 84 QSPEGRRVFPDmSVEENLLMGTIPIGMDH---------AEEDMQRM---FELfpRLKERrnqrAMTMSGGEQQMLAIARA 151
Cdd:COG2274 553 VVLQDVFLFSG-TIRENITLGDPDATDEEiieaarlagLHDFIEALpmgYDT--VVGEG----GSNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600102 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARsGMTIFLVEQNANHaLKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLST-IRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
16-219 |
4.44e-32 |
|
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: 116.70 E-value: 4.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 16 GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHyvASNGIAQSPEGRRVFPDM 95
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE--ARRRLGFVSDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 96 SVEENLLMGTIPIGMDHAEEDmQRMFELFPRL--KERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVV 173
Cdd:cd03266 94 TARENLEYFAGLYGLKGDELT-ARLEELADRLgmEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600102 174 KQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSG 219
Cdd:cd03266 173 RALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-235 |
5.94e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 117.87 E-value: 5.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 19 QALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASN---GIA-QSPEGRRVFPd 94
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRktvGIVfQNPDDQLFAP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 95 mSVEENLLMGtiPIGMDHAEEDMQRmfelfpRLKERRNQRAMT---------MSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:PRK13639 95 -TVEEDVAFG--PLNLGLSKEEVEK------RVKEALKAVGMEgfenkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600102 166 LGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQE-VRNAYL 235
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIEtIRKANL 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-229 |
1.41e-31 |
|
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: 121.41 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 2 SAALLEFREVDVFY--GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVAS 79
Cdd:COG4987 330 GGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 80 --NGIAQSPEgrrVFpDMSVEENLLMGTipigmDHA-EEDMQRMFE------LFPRLKERRN----QRAMTMSGGEQQML 146
Cdd:COG4987 410 riAVVPQRPH---LF-DTTLRENLRLAR-----PDAtDEELWAALErvglgdWLAALPDGLDtwlgEGGRRLSGGERRRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 147 AIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARsGMTIFLVeqnaNH---ALKLSDRAYVMVTGEIRMSGSGEE 223
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLI----THrlaGLERMDRILVLEDGRIVEQGTHEE 555
|
....*.
gi 15600102 224 LLGNQE 229
Cdd:COG4987 556 LLAQNG 561
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-227 |
1.74e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 116.03 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSI-----FGQPRAAAGQILYRGQDIRQKSAH 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 76 YVASNG----IAQSPEGrrvFPdMSVEENLLMGTIPIG------MDHAEEDMQRMFELFPRLKERRNQRAMTMSGGEQQM 145
Cdd:PRK14239 81 TVDLRKeigmVFQQPNP---FP-MSIYENVVYGLRLKGikdkqvLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELaRSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
..
gi 15600102 226 GN 227
Cdd:PRK14239 236 MN 237
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
11-215 |
9.90e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 113.57 E-value: 9.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 11 VDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLL--MSIFGQPRAaaGQIlyrgqDIRQKSAHYVASNGIAQSPEG 88
Cdd:PRK11124 8 INCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLrvLNLLEMPRS--GTL-----NIAGNHFDFSKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 89 RR----VF------PDMSVEENLLMGTIPI-GMDHaEEDMQRMFELFPRLkeRRNQRA----MTMSGGEQQMLAIARALM 153
Cdd:PRK11124 81 RRnvgmVFqqynlwPHLTVQQNLIEAPCRVlGLSK-DQALARAEKLLERL--RLKPYAdrfpLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 154 SRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-228 |
1.12e-30 |
|
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: 113.55 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQ-ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQksahyvasngiaQ 84
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE------------Q 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 SP-EGRR----------VFPDMSVEENLlmGTIP--IGMDHAEEDmQRMFELFPRL----KERRNQRAMTMSGGEQQMLA 147
Cdd:cd03295 69 DPvELRRkigyviqqigLFPHMTVEENI--ALVPklLKWPKEKIR-ERADELLALVgldpAEFADRYPHELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 148 IARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELAR-SGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLG 226
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQeLGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
..
gi 15600102 227 NQ 228
Cdd:cd03295 226 SP 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-228 |
4.55e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 113.36 E-value: 4.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASN 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 GIAqsPEGRRVFPDMSVEENLLMGTIPIGMDHAE--EDMQRMFElFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKL 158
Cdd:PRK13537 83 GVV--PQFDNLDPDFTVRENLLVFGRYFGLSAAAarALVPPLLE-FAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 159 LLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQ 228
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-215 |
1.41e-29 |
|
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: 109.65 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 14 FYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDI----RQKSAHYVAsngiaQSPeGR 89
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakeRRKSIGYVM-----QDV-DY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 90 RVFPDmSVEENLLMGT--IPIGMDHAEEDMQRMfELFpRLKERRnqrAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:cd03226 83 QLFTD-SVREELLLGLkeLDAGNEQAETVLKDL-DLY-ALKERH---PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600102 168 LAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:cd03226 157 LDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-225 |
2.23e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 112.55 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSaalLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRqksahyvasn 80
Cdd:COG1118 1 MS---IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 gIAQSPEGRRV---------FPDMSVEENllmgtIPIGMDHAeedmqrmfelfPRLKERRNQRAMTM------------- 138
Cdd:COG1118 68 -TNLPPRERRVgfvfqhyalFPHMTVAEN-----IAFGLRVR-----------PPSKAEIRARVEELlelvqlegladry 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 139 ----SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVMVTG 213
Cdd:COG1118 131 psqlSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQG 210
|
250
....*....|..
gi 15600102 214 EIRMSGSGEELL 225
Cdd:COG1118 211 RIEQVGTPDEVY 222
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-215 |
3.61e-29 |
|
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: 109.45 E-value: 3.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFY----GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSahy 76
Cdd:COG4181 4 SSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 77 vaSNGIAQspeGRR-----VF------PDMSVEENLLMgtiPI---GMDHAEEDMQRMFElfpR--LKERRNQRAMTMSG 140
Cdd:COG4181 81 --EDARAR---LRArhvgfVFqsfqllPTLTALENVML---PLelaGRRDARARARALLE---RvgLGHRLDHYPAQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 141 GEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELAR-SGMTIFLVeqnaNHALKL---SDRAYVMVTGEI 215
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLV----THDPALaarCDRVLRLRAGRL 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-215 |
4.31e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 109.33 E-value: 4.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLL--MSIFGQPRAaaGQILYRGQ--DIRQKSAHyvasng 81
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLrvLNLLETPDS--GQLNIAGHqfDFSQKPSE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 82 iAQSPEGRR----VF------PDMSVEENLLMGTIPIGMDHAEEDMQRMFELFPRLK--ERRNQRAMTMSGGEQQMLAIA 149
Cdd:COG4161 75 -KAIRLLRQkvgmVFqqynlwPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRltDKADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600102 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-224 |
1.11e-28 |
|
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: 108.20 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSA----------H 75
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVqernvgfvfqH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 76 YVAsngiaqspegrrvFPDMSVEENLLMG--TIPIGMDHAEEDM-QRMFEL--FPRLKERRNQRAMTMSGGEQQMLAIAR 150
Cdd:cd03296 83 YAL-------------FRHMTVFDNVAFGlrVKPRSERPPEAEIrAKVHELlkLVQLDWLADRYPAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELA-RSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-227 |
2.12e-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: 109.37 E-value: 2.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFY----GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFG---QPRAAAGQILYRGQDIRQKSAHYV 77
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 78 AS---NGIA---QSP---------------EGRRVFPDMSVEEnllmgtipigmdhAEEDMQRMFEL--FPRLKERRNQR 134
Cdd:COG0444 81 RKirgREIQmifQDPmtslnpvmtvgdqiaEPLRIHGGLSKAE-------------ARERAIELLERvgLPDPERRLDRY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 135 AMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTG 213
Cdd:COG0444 148 PHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAG 227
|
250
....*....|....
gi 15600102 214 EIRMSGSGEELLGN 227
Cdd:COG0444 228 RIVEEGPVEELFEN 241
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-225 |
4.05e-28 |
|
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: 106.65 E-value: 4.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHyvaSNGIAQSPEGRRVFPDMSVEEN 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---KRDISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 101 LLMGTIPIGMDHAEEDmQRMFELFPRLKERR--NQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQ 178
Cdd:cd03299 92 IAYGLKKRKVDKKEIE-RKVLEIAEMLGIDHllNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600102 179 TLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:cd03299 171 ELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-231 |
2.40e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 107.61 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQ 84
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 SpegRRVFPDMSVEENLLMGTIPIGMDHAE--EDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:PRK11607 99 S---YALFPHMTVEQNIAFGLKQDKLPKAEiaSRVNEMLGLV-HMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 163 EPSLGLAPIVVKQI-FQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEVR 231
Cdd:PRK11607 175 EPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-236 |
3.67e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.07 E-value: 3.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 25 SLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRqksahyvasngiAQSPEGRRV---------FPDM 95
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT------------ALPPAERPVsmlfqennlFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 96 SVEENLLMGTIPiGMDHAEEDMQRMFELFPR-----LKERRNQramTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAP 170
Cdd:COG3840 87 TVAQNIGLGLRP-GLKLTAEQRAQVEQALERvglagLLDRLPG---QLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 171 IVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLG--NQEVRNAYLG 236
Cdd:COG3840 163 ALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDgePPPALAAYLG 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-222 |
6.09e-27 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 107.78 E-value: 6.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 10 EVDVFYGPiqALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQSPEGR 89
Cdd:PRK10762 259 KVDNLSGP--GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDR 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 90 R---VFPDMSVEENLLMGTIP------IGMDHAEEDM--QRMFELFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKL 158
Cdd:PRK10762 337 KrdgLVLGMSVKENMSLTALRyfsragGSLKHADEQQavSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600102 159 LLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIrmsgSGE 222
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI----SGE 476
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-219 |
1.14e-26 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 102.37 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 23 KVSLQVNEgETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQ---DIRQKsahyvasngIAQSPEGRRV-------- 91
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKK---------INLPPQQRKIglvfqqya 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 92 -FPDMSVEENLLMGTIPIGMDHAEEDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAP 170
Cdd:cd03297 86 lFPHLNVRENLAFGLKRKRNREDRISVDELLDLL-GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600102 171 IVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSG 219
Cdd:cd03297 165 ALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-228 |
1.24e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 104.91 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAhyVASN 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR--LARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 GIAQSPEGRRVFPDMSVEENLLMGTIPIGMD--HAEEDMQRMFElFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKL 158
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLVFGRYFGMStrEIEAVIPSLLE-FARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 159 LLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQ 228
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-215 |
1.51e-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: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 3 AALLEFREVDVF-YGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNG 81
Cdd:COG3845 255 EVVLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 82 IAQSPEGRR---VFPDMSVEENLLMGTI---PIG----MDH--AEEDMQRMFELF----PRLkerrNQRAMTMSGGEQQM 145
Cdd:COG3845 335 VAYIPEDRLgrgLVPDMSVAENLILGRYrrpPFSrggfLDRkaIRAFAEELIEEFdvrtPGP----DTPARSLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-225 |
2.22e-26 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 101.06 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQP--RAAAGQILYRGQDIRqksahyvasngiaqspegrrvfpDMSVE 98
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDIT-----------------------DLPPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 99 ENLLMGtipIGMdhaeeDMQRMFElFPRLKERRNQRAMTM--SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQI 176
Cdd:cd03217 73 ERARLG---IFL-----AFQYPPE-IPGVKNADFLRYVNEgfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600102 177 FQTLRELARSGMTIFLVEQNANHALKL-SDRAYVMVTGEIRMSGSGEELL 225
Cdd:cd03217 144 AEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELAL 193
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-234 |
2.40e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 102.50 E-value: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASngiaq 84
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELAR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 spegRR-VFP-------DMSVEENLLMGTIPIGMDHAEED------MQRMfELfPRLKERRNQramTMSGGEQQMLAIAR 150
Cdd:COG4559 76 ----RRaVLPqhsslafPFTVEEVVALGRAPHGSSAAQDRqivreaLALV-GL-AHLAGRSYQ---TLSGGEQQRVQLAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 151 AL-------MSRPKLLLLDEP--SLGLAPivVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSG 221
Cdd:COG4559 147 VLaqlwepvDGGPRWLFLDEPtsALDLAH--QHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTP 224
|
250
....*....|...
gi 15600102 222 EELLGNQEVRNAY 234
Cdd:COG4559 225 EEVLTDELLERVY 237
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-227 |
3.30e-26 |
|
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: 101.50 E-value: 3.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGP----IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAhyvasn 80
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSG------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 giAQSPEGRR----------VFPDMSVEENLlmgTIPI---GMDHAEEDmQRMFEL--FPRLKERRNQRAMTMSGGEQQM 145
Cdd:cd03258 75 --KELRKARRrigmifqhfnLLSSRTVFENV---ALPLeiaGVPKAEIE-ERVLELleLVGLEDKADAYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
...
gi 15600102 225 LGN 227
Cdd:cd03258 229 FAN 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-206 |
3.84e-26 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 100.95 E-value: 3.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGP-IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDI----RQKSAHYVASN 80
Cdd:cd03292 1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 GIAQspEGRRVFPDMSVEENLLMGTIPIGMDHaEEDMQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIARALMSRPKL 158
Cdd:cd03292 81 GVVF--QDFRLLPDRNVYENVAFALEVTGVPP-REIRKRVPAALELvgLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600102 159 LLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLveqnANHALKLSDR 206
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVV----ATHAKELVDT 201
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-225 |
4.37e-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: 101.15 E-value: 4.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 7 EFREVDVFYGP-IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSaHYVASNGIAQS 85
Cdd:cd03254 4 EFENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS-RKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 PEGRRVFPDmSVEENLLMGTIPIGMDHAEEDMQ--RMFELFPRLKE----RRNQRAMTMSGGEQQMLAIARALMSRPKLL 159
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKeaGAHDFIMKLPNgydtVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600102 160 LLDEPSLGLAPIVVKQIFQTLRELaRSGMTIFLVeqnANH--ALKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKL-MKGRTSIII---AHRlsTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
3-234 |
6.93e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.77 E-value: 6.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 3 AALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHyVASNGI 82
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR-AASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 83 AQSPEGRRVFPDMSVEENLLMGTIP--IGMDHAEEDMQRMFElfpRLKERRN-----QRAMT-MSGGEQQMLAIARALMS 154
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMGRTPhrSRFDTWTETDRAAVE---RAMERTGvaqfaDRPVTsLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 155 RPKLLLLDEPSlglAPIVVKQIFQTL---RELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEVR 231
Cdd:PRK09536 157 ATPVLLLDEPT---ASLDINHQVRTLelvRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLR 233
|
...
gi 15600102 232 NAY 234
Cdd:PRK09536 234 AAF 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-219 |
1.52e-25 |
|
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: 99.59 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFY--GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSaHYVASNGIA 83
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD-PADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 84 QSPEGRRVFPDmSVEENLLMGtipiGMDHAEEDMQRMFEL---------FPRLKERR-NQRAMTMSGGEQQMLAIARALM 153
Cdd:cd03245 82 YVPQDVTLFYG-TLRDNITLG----APLADDERILRAAELagvtdfvnkHPNGLDLQiGERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 154 SRPKLLLLDEPSLGLAPIVVKQIFQTLRELARsGMTIFLVeqnaNH---ALKLSDRAYVMVTGEIRMSG 219
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIII----THrpsLLDLVDRIIVMDSGRIVADG 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-225 |
2.59e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 103.71 E-value: 2.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGP-IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNgIA- 83
Cdd:COG1132 340 IEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ-IGv 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 84 --QSPEgrrVFpDMSVEENLLMGTIPIGMD---------HAEEDMQRMfelfPR-LKERRNQRAMTMSGGEQQMLAIARA 151
Cdd:COG1132 419 vpQDTF---LF-SGTIRENIRYGRPDATDEeveeaakaaQAHEFIEAL----PDgYDTVVGERGVNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARsGMTIFLVeqnanhALKLS-----DRAYVMVTGEIRMSGSGEELL 225
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVI------AHRLStirnaDRILVLDDGRIVEQGTHEELL 562
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-225 |
2.67e-25 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 99.23 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGP-IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNgIAQ 84
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA-IGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 SPEGRRVFPDmSVEENLLMGTIpigmDHAEEDMQR------MFELFPRLKERRN----QRAMTMSGGEQQMLAIARALMS 154
Cdd:cd03253 80 VPQDTVLFND-TIGYNIRYGRP----DATDEEVIEaakaaqIHDKIMRFPDGYDtivgERGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600102 155 RPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVeqnanHALKL---SDRAYVMVTGEIRMSGSGEELL 225
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIA-----HRLSTivnADKIIVLKDGRIVERGTHEELL 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-189 |
2.80e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 103.09 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFG-QPRAA-AGQILYRGQDIRQKSAHYVA 78
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYPHGTyEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 79 SNGIAQSPEGRRVFPDMSVEENLLMGT--IPIGMDHAEEDMQRMFELFPRLKERRN--QRAMTMSGGEQQMLAIARALMS 154
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGNeiTPGGIMDYDAMYLRAQKLLAQLKLDINpaTPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190
....*....|....*....|....*....|....*
gi 15600102 155 RPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMT 189
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLKAHGIA 195
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-190 |
2.90e-25 |
|
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: 99.05 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 18 IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQD---------------IRQKSAHYVAsngi 82
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlaqaspreilaLRRRTIGYVS---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 83 aqspEGRRVFPDMS----VEENLLMgtipIGMDH--AEEDMQRMFELFpRLKERRNQRA-MTMSGGEQQMLAIARALMSR 155
Cdd:COG4778 100 ----QFLRVIPRVSaldvVAEPLLE----RGVDReeARARARELLARL-NLPERLWDLPpATFSGGEQQRVNIARGFIAD 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600102 156 PKLLLLDEPSLGLAP---IVVKQIfqtLRELARSGMTI 190
Cdd:COG4778 171 PPLLLLDEPTASLDAanrAVVVEL---IEEAKARGTAI 205
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-206 |
4.41e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 98.73 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVA---SNGIAQSPEGRRVFPDMSV 97
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrNQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 98 EENLLMGTIpIGMDHAEEDMQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQ 175
Cdd:PRK11629 105 LENVAMPLL-IGKKKPAEINSRALEMLAAvgLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190
....*....|....*....|....*....|.
gi 15600102 176 IFQTLRELARSGMTIFLVeqnANHALKLSDR 206
Cdd:PRK11629 184 IFQLLGELNRLQGTAFLV---VTHDLQLAKR 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-226 |
5.23e-25 |
|
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: 100.96 E-value: 5.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 23 KVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRG---QDIRQksahyvasnGIAQSPEGRRV-------- 91
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRK---------GIFLPPEKRRIgyvfqear 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 92 -FPDMSVEENLLMG---TIPIGMDHAEEDMQRMFELFPRLKERRNqramTMSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:TIGR02142 86 lFPHLSVRGNLRYGmkrARPSERRISFERVIELLGIGHLLGRLPG----RLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 168 LAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLG 226
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-224 |
5.52e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 102.44 E-value: 5.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQ 84
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 SPEGRRVFPDMSVEENLLmgtipIGMDHAEEDMQRMFELfprLKERRNQRAMTMSGG-----EQQMLAIARALMSRPKLL 159
Cdd:PRK15439 91 VPQEPLLFPNLSVKENIL-----FGLPKRQASMQKMKQL---LAALGCQLDLDSSAGslevaDRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 160 LLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-219 |
5.90e-25 |
|
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: 97.95 E-value: 5.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 25 SLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIrqkSAHYVASNGIAQSPEGRRVFPDMSVEENLLMG 104
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV---TAAPPADRPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 105 TIPiGMDHAEEDMQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRE 182
Cdd:cd03298 95 LSP-GLKLTAEDRQAIEVALARvgLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600102 183 L-ARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSG 219
Cdd:cd03298 174 LhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-224 |
9.87e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 98.72 E-value: 9.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFY-GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASN-GI 82
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFvGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 83 A-QSPEGRRVFPdmSVEENLLMGTIPIGMD-----HAEEDMQRMFELfprlKERRNQRAMTMSGGEQQMLAIARALMSRP 156
Cdd:PRK13652 83 VfQNPDDQIFSP--TVEQDIAFGPINLGLDeetvaHRVSSALHMLGL----EELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 157 KLLLLDEPSLGLAPIVVKQIFQTLRELA-RSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPeTYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-234 |
1.81e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.53 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 4 ALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNgia 83
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 84 qspegRRVFP-------DMSVEENLLMGTIPIGMDHAEED------MQRMfelfpRLKERRNQRAMTMSGGEQQMLAIAR 150
Cdd:PRK13548 78 -----RAVLPqhsslsfPFTVEEVVAMGRAPHGLSRAEDDalvaaaLAQV-----DLAHLAGRDYPQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 151 ALM------SRPKLLLLDEP--SLGLApivvKQ--IFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSG 219
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPtsALDLA----HQhhVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
250
....*....|....*
gi 15600102 220 SGEELLGNQEVRNAY 234
Cdd:PRK13548 224 TPAEVLTPETLRRVY 238
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-224 |
2.00e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 98.99 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 4 ALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIrqksahyvasNGIA 83
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV----------TDLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 84 qsPEGRRV---------FPDMSVEENLLMGTIPIGMDHAE-----EDMQRMFELFPRLkerrNQRAMTMSGGEQQMLAIA 149
Cdd:COG3839 72 --PKDRNIamvfqsyalYPHMTVYENIAFPLKLRKVPKAEidrrvREAAELLGLEDLL----DRKPKQLSGGQRQRVALG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 150 RALMSRPKLLLLDEPslgLAPIVVK---QIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:COG3839 146 RALVREPKVFLLDEP---LSNLDAKlrvEMRAEIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-205 |
2.74e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.16 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLL-----MSIFGQPRAAAGQILYRGQDIRQKSAHYVAS 79
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVTFHGKNLYAPDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 80 NgiaqspegRRV---------FPDmSVEENLLMGTIPIG----MDHAEEDMQRMFELFPRLKERRNQRAMTMSGGEQQML 146
Cdd:PRK14243 90 R--------RRIgmvfqkpnpFPK-SIYDNIAYGARINGykgdMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 147 AIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSgMTIFLVEQNANHALKLSD 205
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-227 |
3.86e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 96.58 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDI---RQKSAHY- 76
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvRDKDGQLk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 77 VASNGIAQSPEGR--------RVFPDMSVEENLLMGTIPI-GMDHAEEDMQRMFELFP-RLKER-RNQRAMTMSGGEQQM 145
Cdd:PRK10619 81 VADKNQLRLLRTRltmvfqhfNLWSHMTVLENVMEAPIQVlGLSKQEARERAVKYLAKvGIDERaQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
..
gi 15600102 226 GN 227
Cdd:PRK10619 241 GN 242
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-214 |
5.10e-24 |
|
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: 99.51 E-value: 5.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFG-QPRAA-AGQILYRGQDIRQKSAHYVASNGI 82
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvYPHGTwDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 83 AQSPEGRRVFPDMSVEENLLMG---TIPIGMDHAEEDMQRMFELFPRLK---ERRNQRAMTMSGGEQQMLAIARALMSRP 156
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGneiTLPGGRMAYNAMYLRAKNLLRELQldaDNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600102 157 KLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGE 214
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
19-231 |
5.71e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 95.97 E-value: 5.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 19 QALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQIlyRGQDI---------RQKSAHYVASNGIAQSPEGR 89
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI--RVGDItidtarslsQQKGLIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 90 RVFPDMSVEENLLMGTIPIGMDHAEEDMQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PRK11264 95 NLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKvgLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 168 LAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGN-QEVR 231
Cdd:PRK11264 175 LDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADpQQPR 239
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-213 |
7.45e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 99.09 E-value: 7.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASN 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 GIAQSPEGRRVFPDMSVEENLLMGTIPI----GMDHAE--EDMQRMFELFPRLKERR--NQRAMTMSGGEQQMLAIARAL 152
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIGRHLTkkvcGVNIIDwrEMRVRAAMMLLRVGLKVdlDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600102 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTG 213
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-218 |
1.49e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.10 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 14 FYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLL-----MSIFGQPRAAAGQILYRGQDI-----------RQKSAHYV 77
Cdd:PRK14258 16 YYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLkclnrMNELESEVRVEGRVEFFNQNIyerrvnlnrlrRQVSMVHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 78 ASNgiaqspegrrVFPdMSVEENLLMGTIPIG------MDHAEEDMQRMFELFPRLKERRNQRAMTMSGGEQQMLAIARA 151
Cdd:PRK14258 96 KPN----------LFP-MSVYDNVAYGVKIVGwrpkleIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 152 LMSRPKLLLLDEPSLGLAPIV---VKQIFQTLRelARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMS 218
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIAsmkVESLIQSLR--LRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIG 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-220 |
1.58e-23 |
|
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: 94.10 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGP--IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASN--G 81
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRisI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 82 IAQSPegrrvfpdmsveeNLLMGTI-----PIGMdHAEEDMQRMFELFpRLKERRNQRAMTM-----------SGGEQQM 145
Cdd:cd03244 83 IPQDP-------------VLFSGTIrsnldPFGE-YSDEELWQALERV-GLKEFVESLPGGLdtvveeggenlSVGQRQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRElARSGMTIFLVEQNANHALKlSDRAYVMVTGEIRMSGS 220
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-227 |
1.63e-23 |
|
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: 95.40 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 16 GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAhyvasngiAQSPEGRR----- 90
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSR--------KELRELRRkkism 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 91 ------VFPDMSVEENLLMGTIPIGMDHAEEdMQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:cd03294 107 vfqsfaLLPHRTVLENVAFGLEVQGVPRAER-EERAAEALELvgLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600102 163 EPSLGLAPIVVKQIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGN 227
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-213 |
2.57e-23 |
|
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: 94.07 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSahyvasngiaqsPEGRRVF------PD 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG------------PDRMVVFqnysllPW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 95 MSVEENLLMGTIPIGMDHAEEDMQRMFE---LFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:TIGR01184 69 LTVRENIALAVDRVLPDLSKSERRAIVEehiALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600102 172 VVKQIFQTLRELAR-SGMTIFLVEQNANHALKLSDRAYVMVTG 213
Cdd:TIGR01184 149 TRGNLQEELMQIWEeHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-229 |
3.11e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 94.73 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 20 ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSA---HYVASNGIA-QSPEgRRVFPDm 95
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVklsDIRKKVGLVfQYPE-YQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 96 SVEENLLMGtiPIGMDHAEEDMqrmfelfprlkERRNQRAMTM----------------SGGEQQMLAIARALMSRPKLL 159
Cdd:PRK13637 100 TIEKDIAFG--PINLGLSEEEI-----------ENRVKRAMNIvgldyedykdkspfelSGGQKRRVAIAGVVAMEPKIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600102 160 LLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQE 229
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVE 237
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-215 |
3.78e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.90 E-value: 3.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 24 VSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQSPEGRR---VFPDMSVEEN 100
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 101 LLMG----TIPIGM--------DHAEEDMQRMfelfpRLKER-RNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PRK11288 352 INISarrhHLRAGClinnrweaENADRFIRSL-----NIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600102 168 LAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:PRK11288 427 IDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-219 |
4.26e-23 |
|
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: 92.70 E-value: 4.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAhyvASNGIAQS 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP---KDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 PEGRRVFPDMSVEENLLMGTIPIGMDHAE--EDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEidERVREVAELL-QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600102 164 PSLGLAPIVVKQIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSG 219
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-237 |
5.54e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.44 E-value: 5.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 4 ALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLL------MSIFGQPRAAaGQILYRGQDIRQKSAHYV 77
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrlIELYPEARVS-GEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 78 AS--NGIAQSPEGrrvFPDMSVEENLLMGTIPIGMDHAEEDMQRMF-------ELFPRLKERRNQRAMTMSGGEQQMLAI 148
Cdd:PRK14247 81 RRrvQMVFQIPNP---IPNLSIFENVALGLKLNRLVKSKKELQERVrwalekaQLWDEVKDRLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSgMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGN- 227
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNp 236
|
250
....*....|.
gi 15600102 228 -QEVRNAYLGG 237
Cdd:PRK14247 237 rHELTEKYVTG 247
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-219 |
5.71e-23 |
|
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: 92.64 E-value: 5.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVsLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAqs 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 PEGRRVFPDMSVEENLLMGTIPIGMDHAEED--MQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKarVDEVLELV-NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 164 PSLGLAP---IVVKQIfqtLRELARSGMTIF---LVEQNANHAlklsDRAYVMVTGEIRMSG 219
Cdd:cd03264 157 PTAGLDPeerIRFRNL---LSELGEDRIVILsthIVEDVESLC----NQVAVLNKGKLVFEG 211
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-209 |
5.92e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.52 E-value: 5.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 2 SAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNG 81
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 82 IAQSPEGRRVFPDMSVEENLLMGTIP--IGMDHAEEDMQRMFELFPRLKER--RNQRAMTMSGGEQQMLAIARALMSRPK 157
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGQLPhkGGIVNRRLLNYEAREQLEHLGVDidPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600102 158 LLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYV 209
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITV 212
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
15-207 |
1.03e-22 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 91.52 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 15 YGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAhyvasngiAQSPEGRR---- 90
Cdd:TIGR03608 8 FGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNS--------KKASKFRReklg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 91 -VFPDM------SVEENLLMGTIPIGMDHAEEdMQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLL 161
Cdd:TIGR03608 80 yLFQNFalieneTVEENLDLGLKYKKLSKKEK-REKKKEALEKvgLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600102 162 DEPSLGLAPIVVKQIFQTLRELARSGMTIFLVeqnaNHALKLSDRA 207
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDEGKTIIIV----THDPEVAKQA 200
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-230 |
1.63e-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: 91.83 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 7 EFREVDVFYgP----IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSI--FGQPRAaaGQILYRGQDIRQKSAHYVASN 80
Cdd:cd03249 2 EFKNVSFRY-PsrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerFYDPTS--GEILLDGVDIRDLNLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 -GI-AQSPegrrVFPDMSVEENLLMGTIPIGMDHAEE-----DMQRMFELFP-RLKERRNQRAMTMSGGEQQMLAIARAL 152
Cdd:cd03249 79 iGLvSQEP----VLFDGTIAENIRYGKPDATDEEVEEaakkaNIHDFIMSLPdGYDTLVGERGSQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLrELARSGMTIFLVeqnanhALKLS-----DRAYVMVTGEIRMSGSGEELLGN 227
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEAL-DRAMKGRTTIVI------AHRLStirnaDLIAVLQNGQVVEQGTHDELMAQ 227
|
...
gi 15600102 228 QEV 230
Cdd:cd03249 228 KGV 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-226 |
2.02e-22 |
|
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: 91.52 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGP--IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIfgqPR---AAAGQILYRGQDIRQKSAHYVASN 80
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI---PRfydVDSGRILIDGHDVRDYTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 gIAQSPEGRRVFPDmSVEENLLMGTIPIGMD---------HAEEDMQRMFElfpRLKERRNQRAMTMSGGEQQMLAIARA 151
Cdd:cd03251 78 -IGLVSQDVFLFND-TVAENIAYGRPGATREeveeaaraaNAHEFIMELPE---GYDTVIGERGVKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARsGMTIFLVeqnanhALKLS-----DRAYVMVTGEIRMSGSGEELLG 226
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVI------AHRLStienaDRIVVLEDGKIVERGTHEELLA 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-227 |
2.65e-22 |
|
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: 94.75 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYG----PIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFG----QPRAAAGQILYRGQDIRQK 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRllpdPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 73 SAHyvASNGIaqspEGRR---VF--------PDMSVE----ENLLMGTipiGMDhAEEDMQRMFELF-----PRLKERRN 132
Cdd:COG4172 82 SER--ELRRI----RGNRiamIFqepmtslnPLHTIGkqiaEVLRLHR---GLS-GAAARARALELLervgiPDPERRLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 133 QRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVMV 211
Cdd:COG4172 152 AYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMR 231
|
250
....*....|....*.
gi 15600102 212 TGEIRMSGSGEELLGN 227
Cdd:COG4172 232 QGEIVEQGPTAELFAA 247
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-236 |
3.95e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.59 E-value: 3.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 20 ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASN--GIA-QSPE----GRRVF 92
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKlvGIVfQNPEtqfvGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 93 PDMSV-EENLLMGTIPIG--MDHAEEDMqrmfelfpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PRK13644 97 EDLAFgPENLCLPPIEIRkrVDRALAEI--------GLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600102 170 PIVVKQIFQTLRELARSGMTIFLVEQNANHaLKLSDRAYVMVTGEIRMSGSGEELLGNQEVRnaYLG 236
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ--TLG 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
21-164 |
4.14e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLmsifgqpRAAAGQI-LYRGQDIRQKSAH--YVasngiAQSPEgrrVFPDMSV 97
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLL-------KILAGELePDSGEVSIPKGLRigYL-----PQEPP---LDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 98 EENLLMGTIPIG------------MDHAEEDMQRMFELFPRLKER----------------------RNQRAMTMSGGEQ 143
Cdd:COG0488 79 LDTVLDGDAELRaleaeleeleakLAEPDEDLERLAELQEEFEALggweaearaeeilsglgfpeedLDRPVSELSGGWR 158
|
170 180
....*....|....*....|.
gi 15600102 144 QMLAIARALMSRPKLLLLDEP 164
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEP 179
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-216 |
5.58e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.84 E-value: 5.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVfYGPIQALKK----VSLQVNEGETVSLIGANGAGKSTLLMSIFGQ-PRAAAGQILYRGQDIRQKSAHYVASN 80
Cdd:PRK13549 260 LEVRNLTA-WDPVNPHIKrvddVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQAIAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 GIAQSPEGRR---VFPDMSVEENLLMGTI-----------PIGMDHAEEDMQRMfelfpRLKERRNQRAMT-MSGGEQQM 145
Cdd:PRK13549 339 GIAMVPEDRKrdgIVPVMGVGKNITLAALdrftggsriddAAELKTILESIQRL-----KVKTASPELAIArLSGGNQQK 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600102 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIR 216
Cdd:PRK13549 414 AVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-219 |
7.12e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 90.76 E-value: 7.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSahyvasn 80
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRD------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 gIAQSPEGRRVF------------------PDMSVEENL---LMGtipIGMDH-------AEEDMQRMfELFPrlkERRN 132
Cdd:PRK11701 75 -LYALSEAERRRllrtewgfvhqhprdglrMQVSAGGNIgerLMA---VGARHygdiratAGDWLERV-EIDA---ARID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 133 QRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMV 211
Cdd:PRK11701 147 DLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMK 226
|
....*...
gi 15600102 212 TGEIRMSG 219
Cdd:PRK11701 227 QGRVVESG 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-229 |
8.70e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 91.30 E-value: 8.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 18 IQALKKVSLQVNEGETVSLIGANGAGKSTLL--MSIFGQPRAAAGQILYRGQDIRQKSAHY--VASNGIAQSPEGRR--- 90
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIehLNALLLPDTGTIEWIFKDEKNKKKTKEKekVLEKLVIQKTRFKKikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 91 ----------VFP-------DMSVEENLLMGTIPIGMDHAE--EDMQRMFELFPrLKERRNQRA-MTMSGGEQQMLAIAR 150
Cdd:PRK13651 100 ikeirrrvgvVFQfaeyqlfEQTIEKDIIFGPVSMGVSKEEakKRAAKYIELVG-LDESYLQRSpFELSGGQKRRVALAG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQE 229
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNK 257
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-215 |
9.93e-22 |
|
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: 90.63 E-value: 9.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 19 QALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQksahyvasngiaQSPEGRRVF------ 92
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQ------------LDRKQRRAFrrdvql 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 93 ----------PDMSVE-------ENLLmgtipiGMDHAEE-----DMQRMFELFPRLKERRNQRamtMSGGEQQMLAIAR 150
Cdd:TIGR02769 93 vfqdspsavnPRMTVRqiigeplRHLT------SLDESEQkariaELLDMVGLRSEDADKLPRQ---LSGGQLQRINIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600102 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:TIGR02769 164 ALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-227 |
1.10e-21 |
|
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: 92.83 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFY-----------GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFG-QPraAAGQILYRGQDIRQK 72
Cdd:COG4172 275 LLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRlIP--SEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 73 SAHyvasngiAQSPEGRR---VF--------PDMSVEENLL--MGTIPIGMDHAEEDmQRMFELFPRL---KERRNQRAM 136
Cdd:COG4172 353 SRR-------ALRPLRRRmqvVFqdpfgslsPRMTVGQIIAegLRVHGPGLSAAERR-ARVAEALEEVgldPAARHRYPH 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 137 TMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARSGMT-IFLveqnaNHALK----LSDRAYVM 210
Cdd:COG4172 425 EFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAyLFI-----SHDLAvvraLAHRVMVM 499
|
250
....*....|....*..
gi 15600102 211 VTGEIRMSGSGEELLGN 227
Cdd:COG4172 500 KDGKVVEQGPTEQVFDA 516
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-231 |
1.14e-21 |
|
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: 91.70 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 24 VSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRG---QDirqksahyvASNGIAQSPEGRRV--------- 91
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQD---------SARGIFLPPHRRRIgyvfqearl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 92 FPDMSVEENLLMGTIPIGMDHAEEDMQRMFELF---PRLkerrNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEP--SL 166
Cdd:COG4148 89 FPHLSVRGNLLYGRKRAPRAERRISFDEVVELLgigHLL----DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPlaAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600102 167 GLApivVKQ-IFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEVR 231
Cdd:COG4148 165 DLA---RKAeILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLL 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-224 |
1.19e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.81 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 22 KKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQSPEGRRV---FPDMSVE 98
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSsglYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 99 EN---LLMGTIPIGMDHAEEdmQRMFELFPR---LK-ERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:PRK15439 360 WNvcaLTHNRRGFWIKPARE--NAVLERYRRalnIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600102 172 VVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
1.31e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 90.29 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYGP-IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDI---RQKSAHY 76
Cdd:PRK13636 1 MEDYILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 77 VASNGIA-QSPEgRRVFpDMSVEENLLMGtiPIGMDHAEEDMQRMFElfpRLKER------RNQRAMTMSGGEQQMLAIA 149
Cdd:PRK13636 81 RESVGMVfQDPD-NQLF-SASVYQDVSFG--AVNLKLPEDEVRKRVD---NALKRtgiehlKDKPTHCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQ 228
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
..
gi 15600102 229 EV 230
Cdd:PRK13636 234 EM 235
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-193 |
1.50e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 92.42 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQ-ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNgIAQ 84
Cdd:TIGR02868 335 LELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-VSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 SPEGRRVFpDMSVEENLLMGTipigMDHAEEDMQRMFE---LFPRLKERRN-------QRAMTMSGGEQQMLAIARALMS 154
Cdd:TIGR02868 414 CAQDAHLF-DTTVRENLRLAR----PDATDEELWAALErvgLADWLRALPDgldtvlgEGGARLSGGERQRLALARALLA 488
|
170 180 190
....*....|....*....|....*....|....*....
gi 15600102 155 RPKLLLLDEPSLGLAPIVVKQIFQTLRElARSGMTIFLV 193
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLI 526
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-229 |
2.42e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.13 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSI-----FGQPRAAAGQILYRGQDIRQKSAHYVASN 80
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 G----IAQSPEGrrvFPDMSVEENLLMGTIPIGMDHAEEDMQRMFE-------LFPRLKERRNQRAMTMSGGEQQMLAIA 149
Cdd:PRK14267 85 RevgmVFQYPNP---FPHLTIYDNVAIGVKLNGLVKSKKELDERVEwalkkaaLWDEVKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELaRSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQE 229
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-207 |
2.64e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 91.96 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFY-GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHyVASNGIAQ 84
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD-SWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 SPEGRRVFPDmSVEENLLMGTiPIGMDHAEEDMQRMFELFPRLKERRN-------QRAMTMSGGEQQMLAIARALMSRPK 157
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLAR-PDASDAEIREALERAGLDEFVAALPQgldtpigEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600102 158 LLLLDEPSLGLAPIVVKQIFQTLRELARsGMTIFLVeqnaNHALKLSDRA 207
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLV----THRLALAALA 523
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-224 |
2.97e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 89.30 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 19 QALKKVSLQVNEGETVSLIGANGAGKSTLL----------------MSIFGQPRAAAGQIlyrGQDIRQKSAHyvaSNGI 82
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsglitgdksagshIELLGRTVQREGRL---ARDIRKSRAN---TGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 83 AQSpegRRVFPDMSVEENLLMGTI---PIGMD----HAEEDMQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIARALM 153
Cdd:PRK09984 92 FQQ---FNLVNRLSVLENVLIGALgstPFWRTcfswFTREQKQRALQALTRvgMVHFAHQRVSTLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 154 SRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-230 |
3.05e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 89.38 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 20 ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQD---------IRQKSAHyvasngIAQSPEGRR 90
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenlwdIRNKAGM------VFQNPDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 91 VfpDMSVEENLLMGTIPIGMDhAEEDMQRMFELFPRLK--ERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:PRK13633 99 V--ATIVEEDVAFGPENLGIP-PEEIRERVDESLKKVGmyEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600102 169 APIVVKQIFQTLREL-ARSGMTIFLVEQNANHALKlSDRAYVMVTGEIRMSGSGEELLGNQEV 230
Cdd:PRK13633 176 DPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEM 237
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-236 |
3.85e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.10 E-value: 3.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 25 SLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRqksahyvasngiAQSPEGRRV---------FPDM 95
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT------------TTPPSRRPVsmlfqennlFSHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 96 SVEENLLMGTIP-IGMDHAEEDM-----QRMF--ELFPRLKERrnqramtMSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PRK10771 87 TVAQNIGLGLNPgLKLNAAQREKlhaiaRQMGieDLLARLPGQ-------LSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 168 LAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEVRNAYLG 236
Cdd:PRK10771 160 LDPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLG 229
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-219 |
3.99e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.01 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFY-GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVA--SNG 81
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 82 IAQSPEGRRVFPDMSVEENLLMGTIPIGMdhAEEDMQR----MFELFPRLKERRNqRAMTMSGGEQQMLAIARALMSRPK 157
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGA--SGDDIRRrvsaALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600102 158 LLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLveqnANHALKL-SDRAY-VMVTGEIRMSG 219
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLM----ATHDIGLiSRRSYrMLTLSDGHLHG 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-219 |
6.14e-21 |
|
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: 87.33 E-value: 6.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 19 QALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAA---GQILYRGQDIR----QKSAHYVASNGIaqspegrrV 91
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKpdqfQKCVAYVRQDDI--------L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 92 FPDMSVEENLLMGTIPIGMDHAEEDMQRMFELFPRLKE-----RRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:cd03234 93 LPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDlaltrIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600102 167 GLAPIVVKQIFQTLRELARSGMTIFL-VEQNANHALKLSDRAYVMVTGEIRMSG 219
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-228 |
6.43e-21 |
|
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: 90.65 E-value: 6.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 18 IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQ-PRAAAGQILYRGQDIRQKSAHYVASNGIAQSPEGRR---VFP 93
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 94 DMSVEENLLMGTIP----IGMDHAEEDMQRMFELFPRLKERRNQRAM---TMSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:TIGR02633 353 ILGVGKNITLSVLKsfcfKMRIDAAAELQIIGSAIQRLKVKTASPFLpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 167 GLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQ 228
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQ 494
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-231 |
7.09e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 88.53 E-value: 7.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 19 QALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQ--------DIRQKSAHyvasngIAQSPEGRr 90
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwDVRRQVGM------VFQNPDNQ- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 91 vFPDMSVEENLLMGTIPIGMDHaeEDMQRmfelfpRLKERRNQRAMT---------MSGGEQQMLAIARALMSRPKLLLL 161
Cdd:PRK13635 94 -FVGATVQDDVAFGLENIGVPR--EEMVE------RVDQALRQVGMEdflnrephrLSGGQKQRVAIAGVLALQPDIIIL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600102 162 DEPSLGLAPIVVKQIFQTLRELAR-SGMTIFLVEQNANHALKlSDRAYVMVTGEIRMSGSGEEL--LGNQEVR 231
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIfkSGHMLQE 236
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-229 |
8.11e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 88.25 E-value: 8.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQ--------DIRQKSAHyvasngIAQSPEGRrvF 92
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwDIRHKIGM------VFQNPDNQ--F 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 93 PDMSVEENLLMGTIPIGMDHAE--EDMQRMFEL--FPRLKERRNQRamtMSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:PRK13650 95 VGATVEDDVAFGLENKGIPHEEmkERVNEALELvgMQDFKEREPAR---LSGGQKQRVAIAGAVAMRPKIIILDEATSML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 169 APIVVKQIFQTLRELARS-GMTIFLVEQNANHaLKLSDRAYVMVTGEIRMSGSGEELLGNQE 229
Cdd:PRK13650 172 DPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-225 |
8.52e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.80 E-value: 8.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLL------MSIFGQPRAAAGQILYRGQDIRQKSAHYVASN--GIAQSPEGrrvF 92
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLkvlnrlIEIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEvgMVFQQPNP---F 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 93 PDMSVEENLLMGTIPIGMDHAEEDMQRMFE------LFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSl 166
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVEEclrkvgLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT- 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 167 GLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-224 |
1.25e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.99 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSaalLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSA------ 74
Cdd:PRK10851 1 MS---IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHArdrkvg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 75 ----HYVasngiaqspegrrVFPDMSVEENLLMGTI-------PIGMDHAEEDMQ--RMFELfPRLKERRNQRamtMSGG 141
Cdd:PRK10851 78 fvfqHYA-------------LFRHMTVFDNIAFGLTvlprrerPNAAAIKAKVTQllEMVQL-AHLADRYPAQ---LSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 142 EQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGS 220
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
....
gi 15600102 221 GEEL 224
Cdd:PRK10851 221 PDQV 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-215 |
1.37e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.84 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 22 KKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQSPEGRR---VFPDMSVE 98
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 99 ENL-------------LMGTIPIGMDHAEEDMQRmfELFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:PRK09700 360 QNMaisrslkdggykgAMGLFHEVDEQRTAENQR--ELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600102 166 LGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-230 |
1.60e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.37 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 15 YGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDI----------RQKSAhyvasnGIAQ 84
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskrgllalRQQVA------TVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 SPEGRRVFPDmsVEENLLMGTIPIGMdhAEEDMQRMFELFPRL---KERRNQRAMTMSGGEQQMLAIARALMSRPKLLLL 161
Cdd:PRK13638 85 DPEQQIFYTD--IDSDIAFSLRNLGV--PEAEITRRVDEALTLvdaQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 162 DEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEV 230
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-219 |
2.29e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 84.67 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGP--IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIR--QKS-AHYVASn 80
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSdlEKAlSSLISV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 gIAQSPegrrvfpdmsveeNLLMGTIpigmdhaeedmqrmfelfprlkerRNQRAMTMSGGEQQMLAIARALMSRPKLLL 160
Cdd:cd03247 80 -LNQRP-------------YLFDTTL------------------------RNNLGRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 161 LDEPSLGLAPIVVKQIFQTLRELARsGMTIFLVEQNANhALKLSDRAYVMVTGEIRMSG 219
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-215 |
2.55e-20 |
|
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: 85.54 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGP--IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNG-- 81
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLti 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 82 IAQSPegrrvfpdmsveeNLLMGTIPIGMDhaEEDMQRMFELFPRLkeRRNQRAMTMSGGEQQMLAIARALMSRPKLLLL 161
Cdd:cd03369 87 IPQDP-------------TLFSGTIRSNLD--PFDEYSDEEIYGAL--RVSEGGLNLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600102 162 DEPSLGLAPIVVKQIFQTLRELArSGMTIFLVEqnanHALKL---SDRAYVMVTGEI 215
Cdd:cd03369 150 DEATASIDYATDALIQKTIREEF-TNSTILTIA----HRLRTiidYDKILVMDAGEV 201
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
21-234 |
2.66e-20 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 86.16 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQP--RAAAGQILYRGQDIRQKSAHYVASNGI---AQSPEGrrvFPDM 95
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPsyEVTSGTILFKGQDLLELEPDERARAGLflaFQYPEE---IPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 96 SVEENL---------LMGTIPIGMDHAEEDMQRMFELFpRLKERRNQRAMT--MSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:TIGR01978 93 SNLEFLrsalnarrsARGEEPLDLLDFEKLLKEKLALL-DMDEEFLNRSVNegFSGGEKKRNEILQMALLEPKLAILDEI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 165 SLGLAPIVVKQIFQTLRELARSGMTIFLVeqnaNHALKL-----SDRAYVMVTGEIRMSGSGEelLGNQEVRNAY 234
Cdd:TIGR01978 172 DSGLDIDALKIVAEGINRLREPDRSFLII----THYQRLlnyikPDYVHVLLDGRIVKSGDVE--LAKELEAKGY 240
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
16-220 |
3.39e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.55 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 16 GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAhyvasngiAQSPEGRR----V 91
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSE--------KELRKARRqigmI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 92 FPDMsveeNLLMG-TI------PI---GMDHAEEDmQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIARALMSRPKLL 159
Cdd:PRK11153 88 FQHF----NLLSSrTVfdnvalPLelaGTPKAEIK-ARVTELLELvgLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600102 160 LLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVeqnaNHAL----KLSDRAYVMVTGEIRMSGS 220
Cdd:PRK11153 163 LCDEATSALDPATTRSILELLKDINRElGLTIVLI----THEMdvvkRICDRVAVIDAGRLVEQGT 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-225 |
5.00e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 85.28 E-value: 5.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 24 VSLQVNEGETVSLIGANGAGKSTLLMSIFGQpRAAAGQILYRGQDIRQKSAH-------YVASNgiaQSPEgrrvfPDMS 96
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAelarhraYLSQQ---QSPP-----FAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 97 VEENLLMGTIPIGmdHAEEDMQRMFELFPRL----KERRNqrAMTMSGGEQQMLAIARALM-------SRPKLLLLDEPS 165
Cdd:COG4138 86 VFQYLALHQPAGA--SSEAVEQLLAQLAEALgledKLSRP--LTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 166 LGLApiVVKQI--FQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:COG4138 162 NSLD--VAQQAalDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-224 |
5.69e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.08 E-value: 5.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSahyVASNGIAQS 85
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS---IQQRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 PEGRRVFPDMSVEEN----LLMGTIPigmdhAEEDMQRMFELFPRLK----ERR--NQramtMSGGEQQMLAIARALMSR 155
Cdd:PRK11432 84 FQSYALFPHMSLGENvgygLKMLGVP-----KEERKQRVKEALELVDlagfEDRyvDQ----ISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 156 PKLLLLDEPSLGLAPIVVKQIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-210 |
7.90e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 85.30 E-value: 7.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 4 ALLEFREVDVFYG----PIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIrqksahyvas 79
Cdd:COG4525 2 SMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 80 ngiaQSPEGRR--VF------PDMSVEENLLMGTIPIGMDHAEEDmQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIA 149
Cdd:COG4525 72 ----TGPGADRgvVFqkdallPWLNVLDNVAFGLRLRGVPKAERR-ARAEELLALvgLADFARRRIWQLSGGMRQRVGIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVM 210
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-220 |
8.49e-20 |
|
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: 88.15 E-value: 8.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 20 ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIrqKSAHYVASNGIAQSPEGRRVFPDMSVEE 99
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 100 NLLMGTIPIG--MDHAEEDMQRMFElFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIF 177
Cdd:TIGR01257 1023 HILFYAQLKGrsWEEAQLEMEAMLE-DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600102 178 QTLRELaRSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGS 220
Cdd:TIGR01257 1102 DLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-164 |
8.68e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.07 E-value: 8.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRA---AAGQILYRGQDIRqksahyvasngi 82
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLT------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 83 AQSPEGRRV---------FPDMSVEENLLMGtIPIGMDHAEE-----------DMQRMFELFPrlkerrnqraMTMSGGE 142
Cdd:COG4136 70 ALPAEQRRIgilfqddllFPHLSVGENLAFA-LPPTIGRAQRrarveqaleeaGLAGFADRDP----------ATLSGGQ 138
|
170 180
....*....|....*....|..
gi 15600102 143 QQMLAIARALMSRPKLLLLDEP 164
Cdd:COG4136 139 RARVALLRALLAEPRALLLDEP 160
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-230 |
1.30e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.79 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 19 QALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASN-GIA-QSPEGrRVFpDMS 96
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKvGLVfQDPDD-QVF-SST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 97 VEENLLMGTIPIGMDHAEEDmQRMFELFP--RLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVK 174
Cdd:PRK13647 97 VWDDVAFGPVNMGLDKDEVE-RRVEEALKavRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600102 175 QIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGsGEELLGNQEV 230
Cdd:PRK13647 176 TLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDEDI 230
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-228 |
1.63e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.80 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 2 SAALLEFREVDVFY--GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQ------KS 73
Cdd:PRK11160 335 DQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADyseaalRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 74 AHYVASngiaQSPEgrrVFPDmSVEENLLMGtIPIGMDHAEEDMQRMFELFPRLKERRNQRAMT------MSGGEQQMLA 147
Cdd:PRK11160 415 AISVVS----QRVH---LFSA-TLRDNLLLA-APNASDEALIEVLQQVGLEKLLEDDKGLNAWLgeggrqLSGGEQRRLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 148 IARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARsGMTIFLVEQNAnHALKLSDRAYVMVTGEIRMSGSGEELLGN 227
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
.
gi 15600102 228 Q 228
Cdd:PRK11160 564 Q 564
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-227 |
1.71e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 85.51 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFY----GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDI-----------R 70
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalserelraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 71 QK-----------SAHYVASNgIAqspegrrvFPdMSVEenllmgtipiGMDHAEEDmQRMFELFPR--LKERRNQRAMT 137
Cdd:COG1135 82 RKigmifqhfnllSSRTVAEN-VA--------LP-LEIA----------GVPKAEIR-KRVAELLELvgLSDKADAYPSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 138 MSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIR 216
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
250
....*....|.
gi 15600102 217 MSGSGEELLGN 227
Cdd:COG1135 221 EQGPVLDVFAN 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-215 |
2.11e-19 |
|
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: 82.60 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPI------QALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAA--GQILYRGQDIRQKSAHYV 77
Cdd:cd03213 4 LSFRNLTVTVKSSpsksgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 78 asngIAQSPEGRRVFPDMSVEENLLMgtipigmdHAEedmqrmfelfprLKerrnqramTMSGGEQQMLAIARALMSRPK 157
Cdd:cd03213 84 ----IGYVPQDDILHPTLTVRETLMF--------AAK------------LR--------GLSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 158 LLLLDEPSLGLAPIVVKQIFQTLRELARSGMT-IFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRLADTGRTiICSIHQPSSEIFELFDKLLLLSQGRV 190
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-190 |
2.26e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.21 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 4 ALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIA 83
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 84 QSPEGRRVFPDMSVEENLLMG---TIPIGmdhaEEDMQRMFE----LFPRLKERRNQRAM--TMSGGEQQMLAIARALMS 154
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIFLGrefVNRFG----RIDWKKMYAeadkLLARLNLRFSSDKLvgELSIGEQQMVEIAKVLSF 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 15600102 155 RPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTI 190
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGI 194
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-225 |
2.94e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 84.75 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 18 IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIaqspegrrVF----- 92
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGV--------VFgqrsq 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 93 --PDMSVEENL-LMGTI-PIGMDHAEEDMQRMFELFpRLKERRNQRAMTMSGGeQQMLA-IARALMSRPKLLLLDEPSLG 167
Cdd:COG4586 107 lwWDLPAIDSFrLLKAIyRIPDAEYKKRLDELVELL-DLGELLDTPVRQLSLG-QRMRCeLAAALLHRPKILFLDEPTIG 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600102 168 LAPIVVKQIFQTLREL-ARSGMTIFL-------VEQnanhalkLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:COG4586 185 LDVVSKEAIREFLKEYnRERGTTILLtshdmddIEA-------LCDRVIVIDHGRIIYDGSLEELK 243
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-225 |
3.06e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.87 E-value: 3.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLlMSIFGQPRAA----AGQILYRG-----QDIRQKSAhYVASNGIaqspegrrV 91
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTL-MNALAFRSPKgvkgSGSVLLNGmpidaKEMRAISA-YVQQDDL--------F 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 92 FPDMSVEENLL-MGTIPIGMDHA-EEDMQRMFELFPRLKERRNQ--------RAMTMSGGEQQMLAIARALMSRPKLLLL 161
Cdd:TIGR00955 111 IPTLTVREHLMfQAHLRMPRRVTkKEKRERVDEVLQALGLRKCAntrigvpgRVKGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 162 DEPSLGLAPIVVKQIFQTLRELARSGMTIFL-VEQNANHALKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICtIHQPSSELFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-230 |
4.41e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.54 E-value: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYgPI----QALKKVSLQVNEGETVSLIGANGAGKST--LLMSIFGQPraAAGQILYRGQDIRQKSAHY-- 76
Cdd:TIGR00958 478 LIEFQDVSFSY-PNrpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTvaALLQNLYQP--TGGQVLLDGVPLVQYDHHYlh 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 77 --VASngIAQSPegrrVFPDMSVEENllmgtIPIGMDHAEEDMQR----------MFELFPR-----LKERRNQramtMS 139
Cdd:TIGR00958 555 rqVAL--VGQEP----VLFSGSVREN-----IAYGLTDTPDEEIMaaakaanahdFIMEFPNgydteVGEKGSQ----LS 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 140 GGEQQMLAIARALMSRPKLLLLDEPSLGLaPIVVKQIFQTLRELArsGMTIFLVEQNAnHALKLSDRAYVMVTGEIRMSG 219
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSAL-DAECEQLLQESRSRA--SRTVLLIAHRL-STVERADQILVLKKGSVVEMG 695
|
250
....*....|.
gi 15600102 220 SGEELLGNQEV 230
Cdd:TIGR00958 696 THKQLMEDQGC 706
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-225 |
5.90e-19 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 85.18 E-value: 5.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYG-PIQALKKVSLQVNEGETVSLIGANGAGKSTL--LMSIFGQPRAaaGQILYRGQDIRQKSAHYVAS--N 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLakLLVGFFQARS--GEILLNGFSLKDIDRHTLRQfiN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 GIAQSPegrrVFPDMSVEENLLMGTIPigmDHAEEDMQRMFEL---------FPR-LKERRNQRAMTMSGGEQQMLAIAR 150
Cdd:TIGR01193 552 YLPQEP----YIFSGSILENLLLGAKE---NVSQDEIWAACEIaeikddienMPLgYQTELSEEGSSISGGQKQRIALAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSgmTIFLVEQNANHAlKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELL 696
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-223 |
6.56e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.16 E-value: 6.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 3 AALLEFREVDVFY----GPIQALKKVSLQVNEGETVSLIGANGAGKSTLlMSIFG-QPRAAAGQILYRGQDIRQksahyV 77
Cdd:PRK10535 2 TALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTL-MNILGcLDKPTSGTYRVAGQDVAT-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 78 ASNGIAQSpegRR-----------VFPDMSVEENLLMGTIPIGMDHAEEdMQRMFELFPRL--KERRNQRAMTMSGGEQQ 144
Cdd:PRK10535 76 DADALAQL---RRehfgfifqryhLLSHLTAAQNVEVPAVYAGLERKQR-LLRAQELLQRLglEDRVEYQPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 145 MLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKlSDRAYVMVTGEIrMSGSGEE 223
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEI-VRNPPAQ 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-229 |
7.39e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.91 E-value: 7.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 19 QALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSA-----HYVASNGIA-QSPEGRrVF 92
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirPVRKRIGMVfQFPESQ-LF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 93 PDmSVEENLLMGTIPIGMDhAEEDMQRMFELFPRLKERRN---QRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PRK13646 100 ED-TVEREIIFGPKNFKMN-LDEVKNYAHRLLMDLGFSRDvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600102 170 PIVVKQIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQE 229
Cdd:PRK13646 178 PQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-225 |
1.05e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 81.65 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQP--RAAAGQILYRGQDIRQKSAHYVASNGIA---QSPEgrrVFPDM 95
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERARAGIFlafQYPV---EIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 96 SVEeNLL---MGTIPIGMDHAEEDMQRMFELFPRLKERRN--QRAM--TMSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:COG0396 93 SVS-NFLrtaLNARRGEELSAREFLKLLKEKMKELGLDEDflDRYVneGFSGGEKKRNEILQMLLLEPKLAILDETDSGL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 169 APIVVKQIFQTLRELARSGMTIFLVeqnaNHALKL-----SDRAYVMVTGEIRMSGsGEELL 225
Cdd:COG0396 172 DIDALRIVAEGVNKLRSPDRGILII----THYQRIldyikPDFVHVLVDGRIVKSG-GKELA 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-223 |
1.08e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.67 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 15 YGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQdirqksahyVAS----NGIaqspegrr 90
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR---------VSAllelGAG-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 91 vF-PDMSVEENL-LMGTIpIGMDHAEedMQRMF---ELFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEps 165
Cdd:COG1134 99 -FhPELTGRENIyLNGRL-LGLSRKE--IDEKFdeiVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE-- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600102 166 lGLApiVVKQIFQT-----LRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEE 223
Cdd:COG1134 173 -VLA--VGDAAFQKkclarIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-236 |
1.71e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.85 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 20 ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKsahyVASNGIAQSPEGRRV---FPDMs 96
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNLVAYVPQSEEVdwsFPVL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 97 VEENLLMGTIP-IGMDH--AEEDMQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:PRK15056 97 VEDVVMMGRYGhMGWLRraKKRDRQIVTAALARvdMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 172 VVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAyVMVTGEIRMSGSGEELLGNQEVRNAYLG 236
Cdd:PRK15056 177 TEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFTAENLELAFSG 240
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-219 |
1.82e-18 |
|
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: 80.65 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 15 YGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDirqkSAHYVASNGIAqspegrrvfPD 94
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV----SSLLGLGGGFN---------PE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 95 MSVEENL-LMGTIpIGMDHAEEDmQRMFEL--FPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEpslGLApi 171
Cdd:cd03220 99 LTGRENIyLNGRL-LGLSRKEID-EKIDEIieFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE---VLA-- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600102 172 VVKQIFQ-----TLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSG 219
Cdd:cd03220 172 VGDAAFQekcqrRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-214 |
2.12e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 83.24 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 18 IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQSPEGRRVFPDMSV 97
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 98 EENLLMGTIPI-GM--DHAE--EDMQRMFE-----LFPRLKerrnqrAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PRK10982 91 MDNMWLGRYPTkGMfvDQDKmyRDTKAIFDeldidIDPRAK------VATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15600102 168 LAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGE 214
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-227 |
2.92e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.06 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDV----------FYGPIQALKKV---SLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQ 71
Cdd:PRK15079 8 LLEVADLKVhfdikdgkqwFWQPPKTLKAVdgvTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 72 KSA---HYVASN--GIAQSP---------------EGRRVF-PDMSVEENllmgtipigMDHAEEDMQRMfELFPRLKer 130
Cdd:PRK15079 88 MKDdewRAVRSDiqMIFQDPlaslnprmtigeiiaEPLRTYhPKLSRQEV---------KDRVKAMMLKV-GLLPNLI-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 131 rNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYV 209
Cdd:PRK15079 156 -NRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLV 234
|
250
....*....|....*...
gi 15600102 210 MVTGEIRMSGSGEELLGN 227
Cdd:PRK15079 235 MYLGHAVELGTYDEVYHN 252
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
6-229 |
3.27e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 81.41 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGP-----IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQdirqksaHYVASN 80
Cdd:PRK13641 3 IKFENVDYIYSPgtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGY-------HITPET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 GIAQSPEGRR------VFPDMSVEENLLMGTIPIG-------MDHAEEDMQRMFELFPRLKERRNQRAMTMSGGEQQMLA 147
Cdd:PRK13641 76 GNKNLKKLRKkvslvfQFPEAQLFENTVLKDVEFGpknfgfsEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 148 IARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGN 227
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSD 235
|
..
gi 15600102 228 QE 229
Cdd:PRK13641 236 KE 237
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-230 |
3.36e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 80.81 E-value: 3.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 2 SAALLEFREVDVFYGPIQ--ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVAS 79
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 80 N-GIA-QSPEGRrvFPDMSVEENllmgtIPIGMDHAEEDMQRMFELFPRLKERRN------QRAMTMSGGEQQMLAIARA 151
Cdd:PRK13632 84 KiGIIfQNPDNQ--FIGATVEDD-----IAFGLENKKVPPKKMKDIIDDLAKKVGmedyldKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGM-TIFLVEQNANHALkLSDRAYVMVTGEIRMSGSGEELLGNQEV 230
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-214 |
6.30e-18 |
|
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: 79.05 E-value: 6.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 8 FREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGqdirqkSAHYVASNGIAQSpe 87
Cdd:cd03250 8 FTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------SIAYVSQEPWIQN-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 88 grrvfpdMSVEENLLMGtipigmdhAEEDMQRM------------FELFPRLKERR-NQRAMTMSGGEQQMLAIARALMS 154
Cdd:cd03250 80 -------GTIRENILFG--------KPFDEERYekvikacalepdLEILPDGDLTEiGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600102 155 RPKLLLLDEPSLGLAPIVVKQIFQT-LRELARSGMTIFLVEQNAnHALKLSDRAYVMVTGE 214
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFENcILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-232 |
6.54e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.05 E-value: 6.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 17 PIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQI----LYRGQDIR-QKSAHYVASNGIAQSPEGRRV 91
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNnHELITNPYSKKIKNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 92 ------FPDM-----SVEENLLMGTIPIGMdHAEEDMQRMFELFPR--LKERRNQRA-MTMSGGEQQMLAIARALMSRPK 157
Cdd:PRK13631 118 vsmvfqFPEYqlfkdTIEKDIMFGPVALGV-KKSEAKKLAKFYLNKmgLDDSYLERSpFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 158 LLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEVRN 232
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-215 |
8.07e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 79.73 E-value: 8.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 19 QALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDI-----RQKSAHYVASNGIAQSPEGrRVFP 93
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnrAQRKAFRRDIQMVFQDSIS-AVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 94 DMSVEENL------LMGTIPIGMDHAEEDMQRMFELFPRLKERRNQRamtMSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PRK10419 105 RKTVREIIreplrhLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ---LSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600102 168 LAPIVVKQIFQTLRELARSGMTIFLVeqnANHALKLSD----RAYVMVTGEI 215
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQFGTACLF---ITHDLRLVErfcqRVMVMDNGQI 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-224 |
1.23e-17 |
|
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: 81.39 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFG--QPRAAAGQILYR------------------ 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 66 -----GQDIRQKSAHYVASNGIAQSPEGRRV----------FPDMSVEENLLMGTIPIGMDhAEEDMQRMFELFP--RLK 128
Cdd:TIGR03269 81 pcpvcGGTLEPEEVDFWNLSDKLRRRIRKRIaimlqrtfalYGDDTVLDNVLEALEEIGYE-GKEAVGRAVDLIEmvQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 129 ERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELAR-SGMTIFLVEQNANHALKLSDRA 207
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKaSGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*..
gi 15600102 208 YVMVTGEIRMSGSGEEL 224
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEV 256
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-219 |
1.42e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 80.93 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 20 ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQSPEGRR---VFPDMS 96
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEERRstgIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 97 VEENLLMGTI-----PIGM---DHAEEDMQRMFELFpRLKERRNQRAM-TMSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PRK10982 343 IGFNSLISNIrnyknKVGLldnSRMKSDTQWVIDSM-RVKTPGHRTQIgSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600102 168 LAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGeiRMSG 219
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG--LVAG 471
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-225 |
1.73e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.78 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 3 AALLEFREVDVFY-GPIQALKKVSLQVNEGETVSLIGANGAGKST---LLMSIFgQPraAAGQILYRGQDIRQKSahyVA 78
Cdd:PRK13657 332 KGAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTlinLLQRVF-DP--QSGRILIDGTDIRTVT---RA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 79 S--NGIAQspegrrVFPDM-----SVEENLLMGTipigMDHAEEDMQRMFELFPRLK--ERRNQRAMTM--------SGG 141
Cdd:PRK13657 406 SlrRNIAV------VFQDAglfnrSIEDNIRVGR----PDATDEEMRAAAERAQAHDfiERKPDGYDTVvgergrqlSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 142 EQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELaRSGMTIFLVeqnanhALKLS-----DRAYVMVTGEIR 216
Cdd:PRK13657 476 ERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFII------AHRLStvrnaDRILVFDNGRVV 548
|
....*....
gi 15600102 217 MSGSGEELL 225
Cdd:PRK13657 549 ESGSFDELV 557
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-225 |
1.91e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.56 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 4 ALLEFR----EVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQP----RAAAGQILYRGQDIrqksah 75
Cdd:COG4170 2 PLLDIRnltiEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDL------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 76 yvasngIAQSPEGRR---------VF--------PDMSVEENLlMGTIPIG------MDHAEEDMQRMFELFPRLKERRN 132
Cdd:COG4170 76 ------LKLSPRERRkiigreiamIFqepsscldPSAKIGDQL-IEAIPSWtfkgkwWQRFKWRKKRAIELLHRVGIKDH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 133 QRAMT-----MSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELAR-SGMTIFLVEQNANHALKLSDR 206
Cdd:COG4170 149 KDIMNsypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADT 228
|
250
....*....|....*....
gi 15600102 207 AYVMVTGEIRMSGSGEELL 225
Cdd:COG4170 229 ITVLYCGQTVESGPTEQIL 247
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-227 |
3.28e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.60 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAG-----QILYRGQDIRQKSAHYVASNGIAQSPEGRRVFPdM 95
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFP-M 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 96 SVEENLLMGTIPIGMDHAEE----DMQRMFE--LFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEfrgvAQARLTEvgLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600102 170 PIVVKQIFQTLRELARSgMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGN 227
Cdd:PRK14271 196 PTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-231 |
3.54e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 78.27 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 2 SAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQ--KSAHYVAS 79
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 80 NGIAQSPEGRRVFPDMSVEENLlmgTIPIgMDHAE--EDMQR---MFELFP-RLKERRNQRAMTMSGGEQQMLAIARALM 153
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNV---AYPL-REHTQlpAPLLHstvMMKLEAvGLRGAAKLMPSELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 154 SRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEVR 231
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR 238
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-225 |
3.70e-17 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 77.53 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGP--IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQ-KSAHYVASNGI 82
Cdd:cd03252 1 ITFEHVRFRYKPdgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 83 AQSpegRRVFPDMSVEENLLMGTIPIGMDHAEE--DMQRMFELFPRLKERRNQ----RAMTMSGGEQQMLAIARALMSRP 156
Cdd:cd03252 81 VLQ---ENVLFNRSIRDNIALADPGMSMERVIEaaKLAGAHDFISELPEGYDTivgeQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 157 KLLLLDEPSLGLAPIVVKQIFQTLRELArSGMTIFLVEQNANhALKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-226 |
7.40e-17 |
|
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: 79.08 E-value: 7.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFY-----GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYR-----------GQD 68
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkpGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 69 IRQKSAHYVasnGIAQSPEGrrVFPDMSVEENLlmgTIPIGMDHAEE--DMQRMFEL----FPRLKERR--NQRAMTMSG 140
Cdd:TIGR03269 359 GRGRAKRYI---GILHQEYD--LYPHRTVLDNL---TEAIGLELPDElaRMKAVITLkmvgFDEEKAEEilDKYPDELSE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 141 GEQQMLAIARALMSRPKLLLLDEPSLGLAPI----VVKQIFQTLRELarsGMTIFLVEQNANHALKLSDRAYVMVTGEIR 216
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPItkvdVTHSILKAREEM---EQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
250
....*....|
gi 15600102 217 MSGSGEELLG 226
Cdd:TIGR03269 508 KIGDPEEIVE 517
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
5-230 |
9.31e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.47 E-value: 9.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGP-----IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQIlyRGQDIRQKSAhyvaS 79
Cdd:PRK13643 1 MIKFEKVNYTYQPnspfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV--TVGDIVVSST----S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 80 NGIAQSPEGRRV-----FPDMSVEENLLMGTIPIG-------MDHAEEDMQRMFELFPRLKERRNQRAMTMSGGEQQMLA 147
Cdd:PRK13643 75 KQKEIKPVRKKVgvvfqFPESQLFEETVLKDVAFGpqnfgipKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 148 IARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLgn 227
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF-- 232
|
...
gi 15600102 228 QEV 230
Cdd:PRK13643 233 QEV 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
6-224 |
1.01e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 77.37 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGP-----IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQI------LYRG------QD 68
Cdd:PRK13634 3 ITFQKVEHRYQYktpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervITAGkknkklKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 69 IRQKSahyvasnGIA-QSPEgRRVFPDmSVEENLLMGTIPIGM--DHAEEDMQRMFELFPRLKERRNQRAMTMSGGEQQM 145
Cdd:PRK13634 83 LRKKV-------GIVfQFPE-HQLFEE-TVEKDICFGPMNFGVseEDAKQKAREMIELVGLPEELLARSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELAR-SGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-213 |
1.37e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.21 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYGPIQALKKV----SLQVNEGETVSLIGANGAGKSTLLMSIFG---QPRAA--AGQILYRGQDIRQ 71
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVvndvSLQIEAGETLALVGESGSGKSVTALSILRllpSPPVVypSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 72 KSA---HYVASNGIA---QSPEgRRVFPDMSVEENLL-MGTIPIGMDHaEEDMQRMFELFPRL-----KERRNQRAMTMS 139
Cdd:PRK15134 81 ASEqtlRGVRGNKIAmifQEPM-VSLNPLHTLEKQLYeVLSLHRGMRR-EAARGEILNCLDRVgirqaAKRLTDYPHQLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 140 GGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTG 213
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-215 |
1.60e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 77.91 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 15 YGPIQA----LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQP--RAAAGQILYRGQDIRQKSAHYVASNGIAQSPEG 88
Cdd:NF040905 266 YHPLHPerkvVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDVSTVSDAIDAGLAYVTED 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 89 RRVFP---DMSVEENLLMGTIPIGMDHAEEDMQRMFELFPRLKERRN-------QRAMTMSGGEQQMLAIARALMSRPKL 158
Cdd:NF040905 346 RKGYGlnlIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKMNiktpsvfQKVGNLSGGNQQKVVLSKWLFTDPDV 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 159 LLLDEPSLGlapIVV--K-QIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:NF040905 426 LILDEPTRG---IDVgaKyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-215 |
1.67e-16 |
|
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: 75.83 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 15 YGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQspeGRR--VF 92
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVF---GQKtqLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 93 PDMSVEE--NLLMGTIPIGMDHAEEDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAP 170
Cdd:cd03267 108 WDLPVIDsfYLLAAIYDLPPARFKKRLDELSELL-DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600102 171 IVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:cd03267 187 VAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-190 |
1.81e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.86 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 7 EFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQSP 86
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAYMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 87 E--GRRVFPDMSVEENL-LMGTIpIGMDHAEEDmQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLL 161
Cdd:NF033858 83 QglGKNLYPTLSVFENLdFFGRL-FGQDAAERR-RRIDELLRAtgLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160
|
170 180 190
....*....|....*....|....*....|..
gi 15600102 162 DEPSLGLAPIVVKQIFQ---TLRElARSGMTI 190
Cdd:NF033858 161 DEPTTGVDPLSRRQFWElidRIRA-ERPGMSV 191
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-206 |
2.11e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 77.52 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTlLMSI------FGQpraAAGQILYRGQ-----DIRQKS 73
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKST-LMKVlsgvypHGS---YEGEILFDGEvcrfkDIRDSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 74 AHyvasnGI-------AQSPEgrrvfpdMSVEENLLMGTIPI--GMDHAEEDMQRMFELFPR--LKERRNQRAMTMSGGE 142
Cdd:NF040905 77 AL-----GIviihqelALIPY-------LSIAENIFLGNERAkrGVIDWNETNRRARELLAKvgLDESPDTLVTDIGVGK 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600102 143 QQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDR 206
Cdd:NF040905 145 QQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADS 208
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-225 |
2.15e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.50 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 7 EFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDI-RQKS---AHYVA---- 78
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVaTTPSrelAKRLAilrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 79 SNGIAqspegrrvfPDMSVEENLLMGTIPigmdHA-----EED---MQRMFELFpRLKERRNQRAMTMSGGEQQMLAIAR 150
Cdd:COG4604 83 ENHIN---------SRLTVRELVAFGRFP----YSkgrltAEDreiIDEAIAYL-DLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600102 151 ALMSRPKLLLLDEP--SLGLAPIVvkQIFQTLRELAR-SGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:COG4604 149 VLAQDTDYVLLDEPlnNLDMKHSV--QMMKLLRRLADeLGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-164 |
4.28e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 4.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQIlYRGQDIRQksAHYvasngiAQ 84
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGETVKI--GYF------DQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 SpegRRVF-PDMSVEENLlmgtipigMDHAEED--------MQRMfeLFPRlkERRNQRAMTMSGGEQQMLAIARALMSR 155
Cdd:COG0488 386 H---QEELdPDKTVLDEL--------RDGAPGGteqevrgyLGRF--LFSG--DDAFKPVGVLSGGEKARLALAKLLLSP 450
|
....*....
gi 15600102 156 PKLLLLDEP 164
Cdd:COG0488 451 PNVLLLDEP 459
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-225 |
4.59e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 75.99 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFY----GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQP----RAAAGQILYRGQDIRQKSA-- 74
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 75 ------HYVASngIAQSPEGRrVFPDMSVEENLlMGTIPiGMDHAEEDMQRM-------FELFPRLKERRNQRAM----- 136
Cdd:PRK15093 83 rrklvgHNVSM--IFQEPQSC-LDPSERVGRQL-MQNIP-GWTYKGRWWQRFgwrkrraIELLHRVGIKDHKDAMrsfpy 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 137 TMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELAR-SGMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
250
....*....|
gi 15600102 216 RMSGSGEELL 225
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
15-215 |
4.68e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 74.71 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 15 YGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQksahyvASNGIAQSPEGRRVFPD 94
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE------AREDTRLMFQDARLLPW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 95 MSVEENLLMGTIPIGMDHAEEDMQRMfelfpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPsLG----LAP 170
Cdd:PRK11247 96 KKVIDNVGLGLKGQWRDAALQALAAV-----GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP-LGaldaLTR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600102 171 IVVKQIFQTLRElaRSGMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:PRK11247 170 IEMQDLIESLWQ--QHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-224 |
4.80e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 75.92 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFY----GPIQALKKVSLQVNEGETVSLIGANGAGKSTL---LMSIFGQPRAAAGQILYRGQDI---R 70
Cdd:PRK09473 8 QADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTafaLMGLLAANGRIGGSATFNGREIlnlP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 71 QKSAHYVASNGIA---QSPEgRRVFPDMSVEENL---LMgtIPIGMDHAE--EDMQRMFEL--FPRLKERRNQRAMTMSG 140
Cdd:PRK09473 88 EKELNKLRAEQISmifQDPM-TSLNPYMRVGEQLmevLM--LHKGMSKAEafEESVRMLDAvkMPEARKRMKMYPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 141 GEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSG 219
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 244
|
....*
gi 15600102 220 SGEEL 224
Cdd:PRK09473 245 NARDV 249
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-230 |
5.44e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.04 E-value: 5.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 19 QALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYrgqdirqksAHYVASNGIAQSPEGRRV------- 91
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV---------GDYAIPANLKKIKEVKRLrkeiglv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 92 --FPDMSVEENLLMGTIPIGMDHAEEDMQRMFELFPRL-------KERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:PRK13645 96 fqFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELlklvqlpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 163 EPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEV 230
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-225 |
6.00e-16 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 76.29 E-value: 6.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGP--IQALKKVSLQVNEGETVSLIGANGAGKSTL--LMSIFGQPraAAGQILYRGQDIrqksAHYVASN 80
Cdd:TIGR02203 330 DVEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLvnLIPRFYEP--DSGQILLDGHDL----ADYTLAS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 ---GIAQSPEGRRVFPDmSVEENLLMGTiPIGMDHAE-EDMQRM---FELFPRLKERRN----QRAMTMSGGEQQMLAIA 149
Cdd:TIGR02203 404 lrrQVALVSQDVVLFND-TIANNIAYGR-TEQADRAEiERALAAayaQDFVDKLPLGLDtpigENGVLLSGGQRQRLAIA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVeqnanHAL---KLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIA-----HRLstiEKADRIVVMDDGRIVERGTHNELL 555
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-227 |
6.83e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 75.15 E-value: 6.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFY-----------GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDI 69
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 70 RQKSAHYVAsngiaqspEGRR----VF--------PDMSVEENLlmgtipigmdhaEEDMqRMFELFPRlKERRnQRAMT 137
Cdd:COG4608 83 TGLSGRELR--------PLRRrmqmVFqdpyaslnPRMTVGDII------------AEPL-RIHGLASK-AERR-ERVAE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 138 M------------------SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARSGMT-IF------ 191
Cdd:COG4608 140 LlelvglrpehadryphefSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLqDELGLTyLFishdls 219
|
250 260 270
....*....|....*....|....*....|....*.
gi 15600102 192 LVEqnanHalkLSDRAYVMVTGEIRMSGSGEELLGN 227
Cdd:COG4608 220 VVR----H---ISDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-190 |
7.68e-16 |
|
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: 73.16 E-value: 7.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILY------RGQDIRQKSAHYVA- 78
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWngtplaEQRDEPHENILYLGh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 79 SNGIAqspegrrvfPDMSVEENL-----LMGTIPIGMDHAEEDMQrmfelfprLKERRNQRAMTMSGGEQQMLAIARALM 153
Cdd:TIGR01189 81 LPGLK---------PELSALENLhfwaaIHGGAQRTIEDALAAVG--------LTGFEDLPAAQLSAGQQRRLALARLWL 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600102 154 SRPKLLLLDEPSLGLAPIVVKQIFQTLRE-LARSGMTI 190
Cdd:TIGR01189 144 SRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVL 181
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-225 |
8.03e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.20 E-value: 8.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQpRAAAGQILYRGQDIRQKS----AHYVASNGIAQSPEgrrvfPDMS 96
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSaaelARHRAYLSQQQTPP-----FAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 97 VEENLLM----GTIPIGMDHAEEDMQRMFELFPRLKERRNQramtMSGGEQQ-------MLAIARALMSRPKLLLLDEPS 165
Cdd:PRK03695 86 VFQYLTLhqpdKTRTEAVASALNEVAEALGLDDKLGRSVNQ----LSGGEWQrvrlaavVLQVWPDINPAGQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 166 LGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-230 |
9.92e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.40 E-value: 9.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 14 FYGPiqALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASN-----GIA-QSPE 87
Cdd:PRK13649 18 FEGR--ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQirkkvGLVfQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 88 GRrVFpDMSVEENLLMGTIPIGM--DHAEEDMQRMFELFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:PRK13649 96 SQ-LF-EETVLKDVAFGPQNFGVsqEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 166 LGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLgnQEV 230
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF--QDV 236
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-227 |
9.95e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.45 E-value: 9.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 20 ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKS---AHYVASNGIAQSPEGRRVFPDMS 96
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 97 VEENLLMGTIPIGMDhAEEDMQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVK 174
Cdd:PRK10070 123 VLDNTAFGMELAGIN-AEERREKALDALRQvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600102 175 QIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGN 227
Cdd:PRK10070 202 EMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-225 |
1.09e-15 |
|
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: 75.55 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQ-------KSAHYVAsngiaQSPEgrrVFP 93
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwdreelgRHIGYLP-----QDVE---LFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 94 DmSVEENllmgtipIGMdHAEEDMQRMF---------ELFPRLKE----RRNQRAMTMSGGEQQMLAIARALMSRPKLLL 160
Cdd:COG4618 420 G-TIAEN-------IAR-FGDADPEKVVaaaklagvhEMILRLPDgydtRIGEGGARLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 161 LDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANhALKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-201 |
1.75e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.88 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 15 YGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGqilyrgqDIRQKSAHYVASngIAQSPEGRRVFPd 94
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG-------TVRRAGGARVAY--VPQRSEVPDSLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 95 MSVEENLLMGTIP--------IGMDHA--EEDMQRMfelfpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:NF040873 72 LTVRDLVAMGRWArrglwrrlTRDDRAavDDALERV-----GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 15600102 165 SLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHAL 201
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTHDLELVR 183
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-225 |
1.83e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.12 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNgIAQS 85
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 PEGRRVFPDMSVEENLLMGTIPI--------GMDHA--EEDMQRMfelfpRLKERRNQRAMTMSGGEQQMLAIARALMSR 155
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSPWlslwgrlsAEDNArvNQAMEQT-----RINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 156 PKLLLLDEPS--LGLAPIVvkQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:PRK11231 157 TPVVLLDEPTtyLDINHQV--ELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-231 |
2.34e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.14 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 19 QALKKVSLQVNE---GETVSLI-GANGAGKSTLLMSIFGQPRAAAGQILYRGQDIrqksahYVASNGIAQSPEGRRV--- 91
Cdd:PRK11144 8 QQLGDLCLTVNLtlpAQGITAIfGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL------FDAEKGICLPPEKRRIgyv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 92 ------FPDMSVEENLLMGtipigMDHAeedMQRMFE----------LFPRLkerrnqrAMTMSGGEQQMLAIARALMSR 155
Cdd:PRK11144 82 fqdarlFPHYKVRGNLRYG-----MAKS---MVAQFDkivallgiepLLDRY-------PGSLSGGEKQRVAIGRALLTA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 156 PKLLLLDEP--SLGLAPivVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEVR 231
Cdd:PRK11144 147 PELLLMDEPlaSLDLPR--KRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-215 |
2.40e-15 |
|
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: 71.09 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQA--LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQ-KSAHYVASngI 82
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDH--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 83 AQSPEGRRVFPDmSVEENLLmgtipigmdhaeedmqrmfelfprlkerrnqramtmSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:cd03246 79 GYLPQDDELFSG-SIAENIL------------------------------------SGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600102 163 EPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANhALKLSDRAYVMVTGEI 215
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-190 |
2.60e-15 |
|
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: 71.76 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQ------DIRQKSAHYVA- 78
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrDSIARGLLYLGh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 79 SNGIAQSpegrrvfpdMSVEENLLMGTIPIGMDHAEEDMQRM----FELFPrlkerrnqrAMTMSGGEQQMLAIARALMS 154
Cdd:cd03231 81 APGIKTT---------LSVLENLRFWHADHSDEQVEEALARVglngFEDRP---------VAQLSAGQQRRVALARLLLS 142
|
170 180 190
....*....|....*....|....*....|....*..
gi 15600102 155 RPKLLLLDEPSLGLAPIVVKQIFQTLR-ELARSGMTI 190
Cdd:cd03231 143 GRPLWILDEPTTALDKAGVARFAEAMAgHCARGGMVV 179
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-224 |
2.85e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.91 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 8 FREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAhyvASNGIAQSPE 87
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP---AERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 88 GRRVFPDMSVEENLLMGTIPIGMDHAE-----EDMQRMFELfPRLKERRNQramTMSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAGAKKEEinqrvNQVAEVLQL-AHLLDRKPK---ALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600102 163 EPSLGL-APIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:PRK11000 159 EPLSNLdAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-215 |
3.51e-15 |
|
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: 71.52 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 18 IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAA---GQILYRGQDIRQKSAHYVASngIAQSPEGRRVFPD 94
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGE--IIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 95 MSVEENLlmgtipigmDHAeedmqrmfelfprLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVK 174
Cdd:cd03233 98 LTVRETL---------DFA-------------LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600102 175 QIFQTLRELAR-SGMTIFL-VEQNANHALKLSDRAYVMVTGEI 215
Cdd:cd03233 156 EILKCIRTMADvLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
6-225 |
6.24e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 73.32 E-value: 6.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPI-QALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYV-ASNGIA 83
Cdd:COG5265 358 VRFENVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLrAAIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 84 qsPEGRRVFPDmSVEENLLMGTipIGMDHAE-EDMQRMFELFP---RLKE----RRNQRAMTMSGGEQQMLAIARALMSR 155
Cdd:COG5265 438 --PQDTVLFND-TIAYNIAYGR--PDASEEEvEAAARAAQIHDfieSLPDgydtRVGERGLKLSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 156 PKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLveqnanhALKLS-----DRAYVMVTGEIRMSGSGEELL 225
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALREVARGRTTLVI-------AHRLStivdaDEILVLEAGRIVERGTHAELL 580
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-164 |
8.06e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.57 E-value: 8.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 4 ALLEFREVDVFY-GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAhyvASNGI 82
Cdd:PRK11650 2 AGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP---ADRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 83 AQspegrrVF------PDMSVEENLLMGTIPIGMDHAE-----EDMQRMFELFPRLKERRNQramtMSGGEQQMLAIARA 151
Cdd:PRK11650 79 AM------VFqnyalyPHMSVRENMAYGLKIRGMPKAEieervAEAARILELEPLLDRKPRE----LSGGQRQRVAMGRA 148
|
170
....*....|...
gi 15600102 152 LMSRPKLLLLDEP 164
Cdd:PRK11650 149 IVREPAVFLFDEP 161
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-230 |
9.50e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.09 E-value: 9.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQ-PRAAAGQILYRGQdirqksahyvasngIAQSPEGRRVFpDMSVEE 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGElSHAETSSVVIRGS--------------VAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 100 NLLMGTipigmDHAEED---------MQRMFELFP-RLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PLN03232 698 NILFGS-----DFESERywraidvtaLQHDLDLLPgRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600102 170 PIVVKQIFQTLRELARSGMTIFLVeQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEV 230
Cdd:PLN03232 773 AHVAHQVFDSCMKDELKGKTRVLV-TNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSL 832
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-191 |
1.02e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.22 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 25 SLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVAS-------NGIAqspegrrvfPDMSV 97
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllylghqPGIK---------TELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 98 EENLLMgtipIGMDHAEEDMQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQ 175
Cdd:PRK13538 92 LENLRF----YQRLHGPGDDEALWEALAQvgLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVAR 167
|
170
....*....|....*..
gi 15600102 176 IFQTLRE-LARSGMTIF 191
Cdd:PRK13538 168 LEALLAQhAEQGGMVIL 184
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
1.23e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 71.32 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYGPIQA--LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVA 78
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 79 SN-GIA-QSPegrrvfpdmsveENLLMGTI-----PIGMDHAEEDMQRMFELFPR------LKERRNQRAMTMSGGEQQM 145
Cdd:PRK13648 83 KHiGIVfQNP------------DNQFVGSIvkydvAFGLENHAVPYDEMHRRVSEalkqvdMLERADYEPNALSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLREL-ARSGMTIFLVEQNANHALKlSDRAYVMVTGEIRMSGSGEEL 224
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
....*
gi 15600102 225 LGNQE 229
Cdd:PRK13648 230 FDHAE 234
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-224 |
1.24e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 72.08 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAG--KSTLLMSIFG-----QPRAAAGQILYRGQDIRQKSAHYVA 78
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GpdagrRPWRF*TWCANRRALRRTIG*HRPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 79 SNGIAQSPEGRrvfpdmsveENLLMgtIPIGMDHAEEDMQ-RMFELFPR--LKERRNQRAMTMSGGEQQMLAIARALMSR 155
Cdd:NF000106 94 R*GRRESFSGR---------ENLYM--IGR*LDLSRKDARaRADELLERfsLTEAAGRAAAKYSGGMRRRLDLAASMIGR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 156 PKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:NF000106 163 PAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-224 |
1.63e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.18 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 19 QALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFG----QpraaaGQILYRGQDIRQ-------KSAHYVASNgiAQSPE 87
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyQ-----GSLKINGIELREldpeswrKHLSWVGQN--PQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 88 GrrvfpdmSVEENLLMGTIPIGMDHAEEDMQRMF--ELFPRLKERRN----QRAMTMSGGEQQMLAIARALMSRPKLLLL 161
Cdd:PRK11174 437 G-------TLRDNVLLGNPDASDEQLQQALENAWvsEFLPLLPQGLDtpigDQAAGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600102 162 DEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANhaLKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLED--LAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-190 |
2.45e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.13 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQ----KSAHYVA-SNGIAqspegrrvfPDM 95
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpdvaEACHYLGhRNAMK---------PAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 96 SVEENL-----LMGTIPIGMDHAEEDM--QRMFELfprlkerrnqRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:PRK13539 89 TVAENLefwaaFLGGEELDIAAALEAVglAPLAHL----------PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|...
gi 15600102 169 APIVVKQIFQTLRE-LARSGMTI 190
Cdd:PRK13539 159 DAAAVALFAELIRAhLAQGGIVI 181
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-230 |
3.24e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 70.21 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFY--GPIQALKKVSLQVNEGETVSLIGANGAGKST---LLMSIFGQPRAAAGQILYRGQDIRQKSAH 75
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 76 YVASN-GIA-QSPEGRrvFPDMSVEENllmgtIPIGMDHAEEDMQRMFELFPR------LKERRNQRAMTMSGGEQQMLA 147
Cdd:PRK13640 81 DIREKvGIVfQNPDNQ--FVGATVGDD-----VAFGLENRAVPRPEMIKIVRDvladvgMLDYIDSEPANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 148 IARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELAR-SGMTIFLVEQNANHAlKLSDRAYVMVTGEIRMSGSGEELLG 226
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFS 232
|
....
gi 15600102 227 NQEV 230
Cdd:PRK13640 233 KVEM 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-228 |
3.86e-14 |
|
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: 71.48 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQdirqksahyvasngIAQSPEGRRVFPDmSVEEN 100
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 101 LLMG--------TIPIGMDHAEEDMQrmfeLFP-RLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:TIGR01271 507 IIFGlsydeyryTSVIKACQLEEDIA----LFPeKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600102 172 VVKQIFQTLRELARSGMTIFLVEQNANHaLKLSDRAYVMVTGEIRMSGSGEELLGNQ 228
Cdd:TIGR01271 583 TEKEIFESCLCKLMSNKTRILVTSKLEH-LKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-192 |
5.46e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.05 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQ 84
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 SPEGrrVFPDMSVEENLLMGTIPIGMDHAEEDMQRMFEL-----FPrlkerrnqrAMTMSGGEQQMLAIARALMSRPKLL 159
Cdd:PRK13540 81 HRSG--INPYLTLRENCLYDIHFSPGAVGITELCRLFSLehlidYP---------CGLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190
....*....|....*....|....*....|...
gi 15600102 160 LLDEPSLGLAPIVVKQIFQTLRELARSGMTIFL 192
Cdd:PRK13540 150 LLDEPLVALDELSLLTIITKIQEHRAKGGAVLL 182
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-165 |
5.65e-14 |
|
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: 66.70 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQIlyrgqdirqksahyvasngiaqs 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 pegrrvfpdmsveenLLMGTIPIGmdhaeedmqrmfeLFPRLkerrnqramtmSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:cd03221 58 ---------------TWGSTVKIG-------------YFEQL-----------SGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-225 |
5.98e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.09 E-value: 5.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQ------PRAAA--GQILYRGQDIRQKSAHYVASNGIAQSPEGRRVF 92
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggaPRGARvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 93 PdMSVEENLLMGTIPigmdHAE---EDMQRMFELFPRLKERRNQRAM------TMSGGEQQMLAIARAL---------MS 154
Cdd:PRK13547 97 A-FSAREIVLLGRYP----HARragALTHRDGEIAWQALALAGATALvgrdvtTLSGGELARVQFARVLaqlwpphdaAQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 155 RPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-228 |
6.36e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.78 E-value: 6.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 2 SAALLEFREVDVFYGP--IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDirqksahyVAS 79
Cdd:PLN03232 1231 SRGSIKFEDVHLRYRPglPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD--------VAK 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 80 NGIAqspEGRRVFPDMSVEENLLMGTIPIGMD----HAEEDMQRMFELfPRLKE--RRNQRAM---------TMSGGEQQ 144
Cdd:PLN03232 1303 FGLT---DLRRVLSIIPQSPVLFSGTVRFNIDpfseHNDADLWEALER-AHIKDviDRNPFGLdaevseggeNFSVGQRQ 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 145 MLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSgMTIFLVEQNANHALKlSDRAYVMVTGEIRMSGSGEEL 224
Cdd:PLN03232 1379 LLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS-CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQEL 1456
|
....
gi 15600102 225 LGNQ 228
Cdd:PLN03232 1457 LSRD 1460
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-229 |
8.23e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.97 E-value: 8.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 18 IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASN--GIAQSPEGRrvFPDM 95
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKigMVFQNPDNQ--FVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 96 SVEENLLMGTIPIGMDHaEEDMQRMFE--LFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVV 173
Cdd:PRK13642 98 TVEDDVAFGMENQGIPR-EEMIKRVDEalLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600102 174 KQIFQTLRELA-RSGMTIFLVEQNANHALKlSDRAYVMVTGEIRMSGSGEELLGNQE 229
Cdd:PRK13642 177 QEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-229 |
1.36e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.77 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 2 SAALLEFREVDVFYGP--IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKsahyvas 79
Cdd:PLN03130 1234 SSGSIKFEDVVLRYRPelPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF------- 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 80 nGIAQSPEGRRVFPDMSVeenLLMGTIPIGMD----HAEEDMQRMFELfPRLKE--RRNQRAM---------TMSGGEQQ 144
Cdd:PLN03130 1307 -GLMDLRKVLGIIPQAPV---LFSGTVRFNLDpfneHNDADLWESLER-AHLKDviRRNSLGLdaevseageNFSVGQRQ 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 145 MLAIARALMSRPKLLLLDEPSlglAPIVVKQ---IFQTLRELARSgMTIFLVEQNANHALKlSDRAYVMVTGEIRMSGSG 221
Cdd:PLN03130 1382 LLSLARALLRRSKILVLDEAT---AAVDVRTdalIQKTIREEFKS-CTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTP 1456
|
....*...
gi 15600102 222 EELLGNQE 229
Cdd:PLN03130 1457 ENLLSNEG 1464
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-204 |
1.71e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 67.80 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAhyvaSNGIAQ 84
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA----ERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 SPEGrrVFPDMSVEENLLMGTIPIGMDHAE--EDMQRMFELFPrLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:PRK11248 77 QNEG--LLPWRNVQDNVAFGLQLAGVEKMQrlEIAHQMLKKVG-LEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15600102 163 EPSLGLAPIVVKQIfQT--LRELARSGMTIFLVEQNANHALKLS 204
Cdd:PRK11248 154 EPFGALDAFTREQM-QTllLKLWQETGKQVLLITHDIEEAVFMA 196
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-211 |
2.57e-13 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 66.73 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFY---GPIQALKKVSLQVNEGETVSLIGANGAGKSTL--LMSIFGQPRAaaGQILYRGQDIRQKSAHYVAS 79
Cdd:cd03248 11 IVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVvaLLENFYQPQG--GQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 80 --NGIAQSPegrrVFPDMSVEENLLMGTIPIGMDHAEEDMQR------MFELFPRLKERRNQRAMTMSGGEQQMLAIARA 151
Cdd:cd03248 89 kvSLVGQEP----VLFARSLQDNIAYGLQSCSFECVKEAAQKahahsfISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSgMTIFLVEqnanHALKLSDRAYVMV 211
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIA----HRLSTVERADQIL 219
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-224 |
3.12e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 67.84 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 4 ALLEFREVDVFYG----PIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFG----QPRAAAGQILYRGQD---IRQK 72
Cdd:PRK11022 2 ALLNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlidyPGRVMAEKLEFNGQDlqrISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 73 SAHYVASNGIAQspegrrVFPDMSVEEN-------LLMGTIPI--GMDHAEEdMQRMFELF-----PRLKERRNQRAMTM 138
Cdd:PRK11022 82 ERRNLVGAEVAM------IFQDPMTSLNpcytvgfQIMEAIKVhqGGNKKTR-RQRAIDLLnqvgiPDPASRLDVYPHQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 139 SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELAR-SGMTIFLVEQNANHALKLSDRAYVMVTGEIRM 217
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
....*..
gi 15600102 218 SGSGEEL 224
Cdd:PRK11022 235 TGKAHDI 241
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-216 |
4.34e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.34 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 18 IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQ----KSAHYVASNgIAQSPEGRRVFP 93
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARAKLRAKH-VGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 94 DMSVEENLLMGTIPIGMDHAEEDmQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:PRK10584 102 TLNALENVELPALLRGESSRQSR-NGAKALLEQlgLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600102 172 VVKQIFQTLRELARS-GMTIFLVEQNANHALKlSDRAYVMVTGEIR 216
Cdd:PRK10584 181 TGDKIADLLFSLNREhGTTLILVTHDLQLAAR-CDRRLRLVNGQLQ 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-182 |
5.82e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.52 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 3 AALLEFREVDVF---YGPIqaLKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILY-RGQDI---RQKSah 75
Cdd:COG4178 360 DGALALEDLTLRtpdGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVlflPQRP-- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 76 YVASNGIAQS---PEGRRVFPDMSVEENLLMgtipIGMDHaeedmqrmfeLFPRLKERRNqRAMTMSGGEQQMLAIARAL 152
Cdd:COG4178 436 YLPLGTLREAllyPATAEAFSDAELREALEA----VGLGH----------LAERLDEEAD-WDQVLSLGEQQRLAFARLL 500
|
170 180 190
....*....|....*....|....*....|
gi 15600102 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLRE 182
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-207 |
1.31e-12 |
|
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: 63.71 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLmsifgqpRAAAGqiLYRgqdirqksahyvASNGIAQSPEGRRVFpdmsveen 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLF-------RALAG--LWP------------WGSGRIGMPEGEDLL-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 101 llmgTIPigmdhaeedmQRMFelFPR--LKErrnQRA----MTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVK 174
Cdd:cd03223 68 ----FLP----------QRPY--LPLgtLRE---QLIypwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180 190
....*....|....*....|....*....|....*....
gi 15600102 175 QIFQTLRELarsGMTIFLV------EQNANHALKLSDRA 207
Cdd:cd03223 129 RLYQLLKEL---GITVISVghrpslWKFHDRVLDLDGEG 164
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-225 |
1.38e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.20 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 18 IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYvasngiaQSPEGRRVFPDMSV 97
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-------RSQRIRMIFQDPST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 98 EEN------------LLMGTIPIGMDHAEEDMQ--RMFELFPrlkERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:PRK15112 99 SLNprqrisqildfpLRLNTDLEPEQREKQIIEtlRQVGLLP---DHASYYPHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600102 164 PSLGLAPIVVKQIFQTLREL-ARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-234 |
1.43e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.39 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 2 SAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNg 81
Cdd:PRK10253 4 SVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 82 IAQSPEGRRVFPDMSVEENLLMGTIPigmdhaeedMQRMFELFPRLKERRNQRAM--------------TMSGGEQQMLA 147
Cdd:PRK10253 83 IGLLAQNATTPGDITVQELVARGRYP---------HQPLFTRWRKEDEEAVTKAMqatgithladqsvdTLSGGQRQRAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 148 IARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLG 226
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
....*...
gi 15600102 227 NQEVRNAY 234
Cdd:PRK10253 234 AELIERIY 241
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-164 |
1.52e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.76 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFY----------GPIQALKKVSLQVNEGETVSLIGANGAGKSTL--LMSIFGQPraAAGQILYRGQD 68
Cdd:PRK11308 1 SQQPLLQAIDLKKHYpvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLarLLTMIETP--TGGELYYQGQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 69 IRQKSAHYVAS-----NGIAQSPEG----RRVFPDMsVEENLLMGTipigMDHAEEDMQRMFELFPR--LKERRNQRAMT 137
Cdd:PRK11308 79 LLKADPEAQKLlrqkiQIVFQNPYGslnpRKKVGQI-LEEPLLINT----SLSAAERREKALAMMAKvgLRPEHYDRYPH 153
|
170 180
....*....|....*....|....*...
gi 15600102 138 M-SGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:PRK11308 154 MfSGGQRQRIAIARALMLDPDVVVADEP 181
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-234 |
1.79e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.66 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQP--RAAAGQILYRGQDIRQKSAHYVA 78
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 79 SNGI---AQSP-EgrrvFPDMSVEENLLMG--TIPIGMDHAEEDMQRMFELfprLKERRNQRAMT-----------MSGG 141
Cdd:CHL00131 83 HLGIflaFQYPiE----IPGVSNADFLRLAynSKRKFQGLPELDPLEFLEI---INEKLKLVGMDpsflsrnvnegFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 142 EQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVeqnaNHALKL-----SDRAYVMVTGEIR 216
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILI----THYQRLldyikPDYVHVMQNGKII 231
|
250
....*....|....*...
gi 15600102 217 MSGSGEelLGNQEVRNAY 234
Cdd:CHL00131 232 KTGDAE--LAKELEKKGY 247
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-224 |
2.09e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 16 GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGIAQSPEGRRVFPDM 95
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMRHVRGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 96 SV--EENL--LMGTIPIGMDHAEE--------------DMQRMFEL--FPRLKERRNQRAMTMSGGEQQMLAIARALMSR 155
Cdd:PRK10261 107 AMifQEPMtsLNPVFTVGEQIAESirlhqgasreeamvEAKRMLDQvrIPEAQTILSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 156 PKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-225 |
2.34e-12 |
|
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: 66.12 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQ--ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVAS--NG 81
Cdd:TIGR00957 1285 VEFRNYCLRYREDLdlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFkiTI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 82 IAQSPEgrrvfpdmsveenLLMGTIPIGMD----HAEEDMQRMFEL---------FP-RLKERRNQRAMTMSGGEQQMLA 147
Cdd:TIGR00957 1365 IPQDPV-------------LFSGSLRMNLDpfsqYSDEEVWWALELahlktfvsaLPdKLDHECAEGGENLSVGQRQLVC 1431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600102 148 IARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSgMTIFLVEQNANHALKLSdRAYVMVTGEIRMSGSGEELL 225
Cdd:TIGR00957 1432 LARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLL 1507
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-224 |
2.69e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 65.81 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 20 ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAG-------QILYRGQDIRQKSAHYVASNGIAQSPEGR--- 89
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdatvagkSILTNISDVHQNMGYCPQFDAIDDLLTGRehl 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 90 ------RVFPDMSVEENLLMGTIPIGMDHAEEDMqrmfelfprlkerrnqrAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:TIGR01257 2034 ylyarlRGVPAEEIEKVANWSIQSLGLSLYADRL-----------------AGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600102 164 PSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-163 |
2.76e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.96 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 2 SAALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDI--------RQKS 73
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIstlkpeiyRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 74 AHyvasngIAQSPEgrrVFPDmSVEENLLMgtiPIGMDHAEEDMQRM------FELfPrlKERRNQRAMTMSGGEQQMLA 147
Cdd:PRK10247 84 SY------CAQTPT---LFGD-TVYDNLIF---PWQIRNQQPDPAIFlddlerFAL-P--DTILTKNIAELSGGEKQRIS 147
|
170
....*....|....*.
gi 15600102 148 IARALMSRPKLLLLDE 163
Cdd:PRK10247 148 LIRNLQFMPKVLLLDE 163
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-195 |
2.81e-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: 65.70 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLmSIFGQPRAAAGQILYRGqdirqksahyVASNGIAQSpEGRRVFPDMSVEEN 100
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLL-SALLRLLSTEGEIQIDG----------VSWNSVTLQ-TWRKAFGVIPQKVF 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 101 LLMGTIPIGMDH------------AEE-DMQRMFELFP-RLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:TIGR01271 1303 IFSGTFRKNLDPyeqwsdeeiwkvAEEvGLKSVIEQFPdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
170 180
....*....|....*....|....*....
gi 15600102 167 GLAPIVVKQIFQTLRElARSGMTIFLVEQ 195
Cdd:TIGR01271 1383 HLDPVTLQIIRKTLKQ-SFSNCTVILSEH 1410
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-228 |
2.86e-12 |
|
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: 64.49 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQdirqksahyvasngIAQSPEGRRVFPDmSVEEN 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 101 LLMGTI--------PIGMDHAEEDMQRMFElfpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIV 172
Cdd:cd03291 118 IIFGVSydeyryksVVKACQLEEDITKFPE---KDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600102 173 VKQIFQTLRELARSGMTIFLVEQNANHaLKLSDRAYVMVTGEIRMSGSGEELLGNQ 228
Cdd:cd03291 195 EKEIFESCVCKLMANKTRILVTSKMEH-LKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-171 |
3.27e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.42 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 3 AALLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLL--------------MSIFGQPRAAaGQILYrgqD 68
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLslitgdhpqgysndLTLFGRRRGS-GETIW---D 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 69 IRQKSAhYVASngiaQSPEGRRVfpDMSVEENLLMGTI-PIGMDHAEEDMQRMF--ELFPRL---KERRNQRAMTMSGGE 142
Cdd:PRK10938 334 IKKHIG-YVSS----SLHLDYRV--STSVRNVILSGFFdSIGIYQAVSDRQQKLaqQWLDILgidKRTADAPFHSLSWGQ 406
|
170 180
....*....|....*....|....*....
gi 15600102 143 QQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:PRK10938 407 QRLALIVRALVKHPTLLILDEPLQGLDPL 435
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-193 |
3.94e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.04 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 25 SLQVNEGETVSLIGANGAGKSTLlmsifgqPRAAAGQ-ILYRGQdiRQKSAHYVASNGIAQ-----SPEGRRVFPDM--- 95
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSAL-------ARALAGElPLLSGE--RQSQFSHITRLSFEQlqklvSDEWQRNNTDMlsp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 96 -------SVEENLLMGTipigmdHAEEDMQRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:PRK10938 94 geddtgrTTAEIIQDEV------KDPARCEQLAQQF-GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180
....*....|....*....|....*
gi 15600102 169 APIVVKQIFQTLRELARSGMTIFLV 193
Cdd:PRK10938 167 DVASRQQLAELLASLHQSGITLVLV 191
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-225 |
7.08e-12 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 63.33 E-value: 7.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFgqpraaagQILYRGQDIrqkSAHYVASNGIAQSpEGRRVFPDMSVEEN 100
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFL--------RLLNTEGDI---QIDGVSWNSVPLQ-KWRKAFGVIPQKVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 101 LLMGTIPIGMD----HAEEDMQR---------MFELFP-RLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:cd03289 88 IFSGTFRKNLDpygkWSDEEIWKvaeevglksVIEQFPgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 167 GLAPIVVKQIFQTLRElARSGMTIFLVEQNANHALKlSDRAYVMVTGEIRMSGSGEELL 225
Cdd:cd03289 168 HLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLL 224
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-207 |
2.04e-11 |
|
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: 60.80 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 20 ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFgqprAAAGQILYRgqdirqksahyvasngiaqspEGRRVFPDMSvee 99
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLI---------------------SFLPKFSRNK--- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 100 nllmgTIPIGmdhaeeDMQRMFEL---FPRLkerrNQRAMTMSGGEQQMLAIARALMSRPK--LLLLDEPSLGLAPIVVK 174
Cdd:cd03238 62 -----LIFID------QLQFLIDVglgYLTL----GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|...
gi 15600102 175 QIFQTLRELARSGMTIFLVEqnanHALKLSDRA 207
Cdd:cd03238 127 QLLEVIKGLIDLGNTVILIE----HNLDVLSSA 155
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-234 |
2.68e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNgIAQSPEGRRVFPDMSVEEN 100
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 101 LLMGTIP----IGMdHAEEDMQRMFELFPR--LKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVK 174
Cdd:PRK10575 106 VAIGRYPwhgaLGR-FGAADREKVEEAISLvgLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600102 175 QIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQEVRNAY 234
Cdd:PRK10575 185 DVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-227 |
4.13e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.45 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQ-PRAAAGQILYRGqdirqkSAHYVasngiaqsPEGRRVFpDMSVEE 99
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGElPPRSDASVVIRG------TVAYV--------PQVSWIF-NATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 100 NLLMGTiPIGMDHAEE-----DMQRMFELFP--RLKERrNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIV 172
Cdd:PLN03130 698 NILFGS-PFDPERYERaidvtALQHDLDLLPggDLTEI-GERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 173 VKQIFQTLRELARSGMTIFLVeQNANHALKLSDRAYVMVTGEIRMSGSGEELLGN 227
Cdd:PLN03130 776 GRQVFDKCIKDELRGKTRVLV-TNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-225 |
5.83e-11 |
|
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: 61.89 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGqdirqkSAHYVASNGIAQspegrrvfpDMSVEEN 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------SVAYVPQQAWIQ---------NDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 101 LLMGTiPIGMDHAEEDMQRMfELFPRL-------KERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVV 173
Cdd:TIGR00957 719 ILFGK-ALNEKYYQQVLEAC-ALLPDLeilpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600102 174 KQIFQTL--RELARSGMTIFLVEQNANHaLKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:TIGR00957 797 KHIFEHVigPEGVLKNKTRILVTHGISY-LPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-164 |
8.18e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 8.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRgQDIR------------QKSAH-YVASnGIAQSPE 87
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIvarlqqdpprnvEGTVYdFVAE-GIEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 88 GRRVFPDMSV-------EENL-LMGTIPIGMDHAE----EDmqRMFELFPRLKERRNQRAMTMSGGEQQMLAIARALMSR 155
Cdd:PRK11147 97 YLKRYHDISHlvetdpsEKNLnELAKLQEQLDHHNlwqlEN--RINEVLAQLGLDPDAALSSLSGGWLRKAALGRALVSN 174
|
....*....
gi 15600102 156 PKLLLLDEP 164
Cdd:PRK11147 175 PDVLLLDEP 183
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-224 |
8.73e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.10 E-value: 8.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 24 VSLQVNEGETVSLIGANGAGKS-TLLMSIFGQP---RAAAGQILYRGQDIRQKSAHYVASNGIAQSPEGR----RVFPDM 95
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGKPVAPCALRGRKIATIMQNPRSAfnplHTMHTH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 96 SVEENLLMG------TIPIGMDHAE-EDMQRMFELFPrlkerrnqraMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:PRK10418 102 ARETCLALGkpaddaTLTAALEAVGlENAARVLKLYP----------FEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600102 169 APIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:PRK10418 172 DVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-215 |
1.10e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 18 IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVAS-----NGIAQSPEGrRVF 92
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAlrrdiQFIFQDPYA-SLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 93 PDMSVEENLLMGTIPIGMDHAEEDMQRMFELFPR---LKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERvglLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15600102 170 PIVVKQIFQTLRELARS-GMTIFLVEQNANHALKLSDRAYVMVTGEI 215
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-168 |
1.54e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.36 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILyRGQDIRqksahyvasngIAQ 84
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-RNGKLR-----------IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 SPEGRRVFPDMSVEENLLMGTIPiGMDHAEedmqrmfeLFPRLKERR-----NQRAMTMSGGEQQMLAIARALMSRPKLL 159
Cdd:PRK09544 72 VPQKLYLDTTLPLTVNRFLRLRP-GTKKED--------ILPALKRVQaghliDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
....*....
gi 15600102 160 LLDEPSLGL 168
Cdd:PRK09544 143 VLDEPTQGV 151
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-183 |
1.85e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.10 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 16 GPIQALKKVSLQVNEGETVSLIGANGAGKST----LLMSIfgqprAAAGQILYRGQDIRQKSAHyvasngiAQSPEGRR- 90
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRR-------QLLPVRHRi 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 91 --VF--------PDMSV----EENLLMGTIPIGMDHAEEDMQRMFELFPRLKERRNQRAMTMSGGEQQMLAIARALMSRP 156
Cdd:PRK15134 365 qvVFqdpnsslnPRLNVlqiiEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKP 444
|
170 180
....*....|....*....|....*..
gi 15600102 157 KLLLLDEPSLGLAPIVVKQIFQTLREL 183
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSL 471
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-163 |
2.42e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 59.73 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSaHYVASNGIAQspegrrVFPDMSVEEN 100
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAM------VQQDPVVLAD 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600102 101 LLMGTIPIGMDHAEEDMQRMFE--------------LFPRLKERRNqramTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:PRK10790 430 TFLANVTLGRDISEEQVWQALEtvqlaelarslpdgLYTPLGEQGN----NLSVGQKQLLALARVLVQTPQILILDE 502
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-229 |
5.84e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.02 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 3 AALLEFREVDVFY--GPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIrqksahyvASN 80
Cdd:PTZ00243 1306 AGSLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI--------GAY 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 GIAqspEGRRVFPDMSVEENLLMGTIPIGMD----HAEEDMQRMFELFPrLKERRNQRA-----------MTMSGGEQQM 145
Cdd:PTZ00243 1378 GLR---ELRRQFSMIPQDPVLFDGTVRQNVDpfleASSAEVWAALELVG-LRERVASESegidsrvleggSNYSVGQRQL 1453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 146 LAIARALMSR-PKLLLLDEPSLGLAPIVVKQIFQTLRElARSGMTIFLVEQNAnHALKLSDRAYVMVTGEIRMSGSGEEL 224
Cdd:PTZ00243 1454 MCMARALLKKgSGFILMDEATANIDPALDRQIQATVMS-AFSAYTVITIAHRL-HTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
....*
gi 15600102 225 LGNQE 229
Cdd:PTZ00243 1532 VMNRQ 1536
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-164 |
8.97e-10 |
|
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: 58.02 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLL--MS-----IFGQPRAAAG-QILYrgqdirqksahyvasngIAQSPEgrrVF 92
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLriMAgvdkdFNGEARPQPGiKVGY-----------------LPQEPQ---LD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 93 PDMSVEENLLMGTIP----------IGMDHAEED------MQRMFELFPRLK-------ERRNQRAM------------- 136
Cdd:TIGR03719 81 PTKTVRENVEEGVAEikdaldrfneISAKYAEPDadfdklAAEQAELQEIIDaadawdlDSQLEIAMdalrcppwdadvt 160
|
170 180
....*....|....*....|....*...
gi 15600102 137 TMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEP 188
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-225 |
1.49e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 57.34 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFY--GPIQALKKVSLQVNEGETVSLIGANGAGKSTL--LMSIFGQprAAAGQILYRGQDIRQ---------- 71
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYD--IDEGEILLDGHDLRDytlaslrnqv 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 72 ----KSAHY----VASNgIAQSPEGRrvFPDMSVEENLLMGtipigmdHAEEDMQRMFELFPRLKerrNQRAMTMSGGEQ 143
Cdd:PRK11176 420 alvsQNVHLfndtIANN-IAYARTEQ--YSREQIEEAARMA-------YAMDFINKMDNGLDTVI---GENGVLLSGGQR 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 144 QMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELA--RSGMTIflveqnanhALKLS-----DRAYVMVTGEIR 216
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQknRTSLVI---------AHRLStiekaDEILVVEDGEIV 557
|
....*....
gi 15600102 217 MSGSGEELL 225
Cdd:PRK11176 558 ERGTHAELL 566
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
10-190 |
2.23e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 55.33 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 10 EVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLmSIFGQPRAAA---GQILYRGQDIR---QKSAHYVASNGIA 83
Cdd:cd03232 12 TVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLL-DVLAGRKTAGvitGEILINGRPLDknfQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 84 qspegrrvFPDMSVEENLLMgtipigmdHAeedmqrmfelfprlkerrNQRAMTMSggEQQMLAIARALMSRPKLLLLDE 163
Cdd:cd03232 91 --------SPNLTVREALRF--------SA------------------LLRGLSVE--QRKRLTIGVELAAKPSILFLDE 134
|
170 180
....*....|....*....|....*..
gi 15600102 164 PSLGLAPIVVKQIFQTLRELARSGMTI 190
Cdd:cd03232 135 PTSGLDSQAAYNIVRFLKKLADSGQAI 161
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-215 |
2.41e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 8 FREVDVFygpiQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQP----RAAAGQILYRGQDIRQKSAHYVASngIA 83
Cdd:TIGR00956 68 FRDTKTF----DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGITPEEIKKHYRGD--VV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 84 QSPEGRRVFPDMSVEENLLM-------GTIPIGMDHaEEDMQRMFELFPR---LKERRNQRAMT-----MSGGEQQMLAI 148
Cdd:TIGR00956 142 YNAETDVHFPHLTVGETLDFaarcktpQNRPDGVSR-EEYAKHIADVYMAtygLSHTRNTKVGNdfvrgVSGGERKRVSI 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600102 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELAR-SGMTIFL-VEQNANHALKLSDRAYVMVTGEI 215
Cdd:TIGR00956 221 AEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVaIYQCSQDAYELFDKVIVLYEGYQ 289
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-223 |
2.53e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.81 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFG--QPRAAAGQILYRGQDIRQ---KSAHYVASNGIaqspegrrVFPDM 95
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNRKPTKqilKRTGFVTQDDI--------LYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 96 SVEENLLMGTI---PIGMDHAEEDM---QRMFELFPRLKERR---NQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:PLN03211 156 TVRETLVFCSLlrlPKSLTKQEKILvaeSVISELGLTKCENTiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600102 167 GLAPIVVKQIFQTLRELARSGMTIFL-VEQNANHALKLSDRAYVMVTGEIRMSGSGEE 223
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-164 |
4.81e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 4.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQIlYRGQDIRqksahyvasngIAQSPEGRRVF-PDMSVEE 99
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTKLE-----------VAYFDQHRAELdPEKTVMD 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600102 100 NLLMG--TIPI-GMD-HAEEDMQRMfeLFPrlkerrNQRAMT----MSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:PRK11147 403 NLAEGkqEVMVnGRPrHVLGYLQDF--LFH------PKRAMTpvkaLSGGERNRLLLARLFLKPSNLLILDEP 467
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-164 |
5.16e-09 |
|
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: 54.64 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 15 YGP-IQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNG------IAQSPE 87
Cdd:cd03290 10 WGSgLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysvayAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 88 grrvFPDMSVEENLLMGTiPIGMDHAEE-----DMQRMFELFPRLKERR-NQRAMTMSGGEQQMLAIARALMSRPKLLLL 161
Cdd:cd03290 90 ----LLNATVEENITFGS-PFNKQRYKAvtdacSLQPDIDLLPFGDQTEiGERGINLSGGQRQRICVARALYQNTNIVFL 164
|
...
gi 15600102 162 DEP 164
Cdd:cd03290 165 DDP 167
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-216 |
6.41e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.36 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYG-PIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRqksahyvasngiAQ 84
Cdd:PRK10522 323 LELRNVTFAYQdNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT------------AE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 85 SPEGRR-----VFPDMSVEENLLmgtipiGMDHAEEDMQRMFELFPRLK-----ERRNQRAMT--MSGGEQQMLAIARAL 152
Cdd:PRK10522 391 QPEDYRklfsaVFTDFHLFDQLL------GPEGKPANPALVEKWLERLKmahklELEDGRISNlkLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600102 153 MSRPKLLLLDEPSLGLAPiVVKQIF--QTLRELARSGMTIFLVEQNaNHALKLSDRAYVMVTGEIR 216
Cdd:PRK10522 465 AEERDILLLDEWAADQDP-HFRREFyqVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLS 528
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
21-205 |
8.15e-09 |
|
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: 54.54 E-value: 8.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGqprAAAGQILYRGQdirQKSAHYVASNG---------IAQSPEGR-- 89
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLY---PALARRLHLKK---EQPGNHDRIEGlehidkvivIDQSPIGRtp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 90 --------RVFP---------------------------------DMSVEEnllmgtipigmdhAEEdmqrMFELFPRLK 128
Cdd:cd03271 85 rsnpatytGVFDeirelfcevckgkrynretlevrykgksiadvlDMTVEE-------------ALE----FFENIPKIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 129 ERRN-------------QRAMTMSGGEQQMLAIARALMSR---PKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFL 192
Cdd:cd03271 148 RKLQtlcdvglgyiklgQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVV 227
|
250
....*....|...
gi 15600102 193 VEQNAnHALKLSD 205
Cdd:cd03271 228 IEHNL-DVIKCAD 239
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-227 |
2.13e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 20 ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQIlyrgqDIRQKSAHYVASNGIAQSPEGRRvfpdmSVE- 98
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAISSGLNGQLTGIE-----NIEl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 99 ENLLMGtipIGMDHAEEDMQRMFElFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEP-SLGlAPIVVKQIF 177
Cdd:PRK13545 109 KGLMMG---LTKEKIKEIIPEIIE-FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAlSVG-DQTFTKKCL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600102 178 QTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGN 227
Cdd:PRK13545 184 DKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-214 |
3.01e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 27 QVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILyrgQDIRqksahyvasngIAQSPEGRRVFPDMSVEENLLMGTI 106
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD---PELK-----------ISYKPQYIKPDYDGTVEDLLRSITD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 107 PIGMDHAEEDMQRMFELfPRLKERRnqrAMTMSGGEQQMLAIARALMSRPKLLLLDEPSlglAPIVVKQIFQTLRELAR- 185
Cdd:PRK13409 427 DLGSSYYKSEIIKPLQL-ERLLDKN---VKDLSGGELQRVAIAACLSRDADLYLLDEPS---AHLDVEQRLAVAKAIRRi 499
|
170 180 190
....*....|....*....|....*....|....*..
gi 15600102 186 ---SGMTIFLVEqnanHALK----LSDRayVMV-TGE 214
Cdd:PRK13409 500 aeeREATALVVD----HDIYmidyISDR--LMVfEGE 530
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
132-237 |
4.25e-08 |
|
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: 53.09 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 132 NQRAMTMSGGEQQMLAIARALMSRPK--LLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQN------ANHALKL 203
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDedtiraADYVIDI 562
|
90 100 110
....*....|....*....|....*....|....*
gi 15600102 204 SDRAYVMvTGEIRMSGSGEELLGNQE-VRNAYLGG 237
Cdd:TIGR00630 563 GPGAGEH-GGEVVASGTPEEILANPDsLTGQYLSG 596
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-164 |
4.80e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 19 QALKKVSLQVNEGETVSLIGANGAGKSTLL--M-----SIFGQPRAAAGqilyrgqdirqksahyvASNGI-AQSPEgrr 90
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLriMagvdkEFEGEARPAPG-----------------IKVGYlPQEPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 91 VFPDMSVEENLLMGTIP----------IGMDHAEED------MQRMFELFPRLK-------ERRNQRAM----------- 136
Cdd:PRK11819 81 LDPEKTVRENVEEGVAEvkaaldrfneIYAAYAEPDadfdalAAEQGELQEIIDaadawdlDSQLEIAMdalrcppwdak 160
|
170 180 190
....*....|....*....|....*....|
gi 15600102 137 --TMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:PRK11819 161 vtKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-209 |
4.89e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 52.03 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 28 VNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSaHYVASNgiaqspegrrvfPDMSVEEnLLMGTIP 107
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP-QYIKAD------------YEGTVRD-LLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 108 IGMDHAEEDMQRMFELfpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSlglAPIVVKQIFQTLRELARSG 187
Cdd:cd03237 88 DFYTHPYFKTEIAKPL--QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPS---AYLDVEQRLMASKVIRRFA 162
|
170 180
....*....|....*....|....*.
gi 15600102 188 M----TIFLVEQNANHALKLSDRAYV 209
Cdd:cd03237 163 EnnekTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-225 |
6.98e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.41 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 20 ALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQ------KSAHYVASngiaQSPegrRVFP 93
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqldswRSRLAVVS----QTP---FLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 94 DmSVEENLLMGTiPigmDHAEEDMQRMFEL------FPRLKE----RRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:PRK10789 403 D-TVANNIALGR-P---DATQQEIEHVARLasvhddILRLPQgydtEVGERGVMLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 164 PSLGLAPIVVKQIFQTLRELaRSGMTIFLVEQNANhALKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:PRK10789 478 ALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-214 |
8.86e-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: 52.09 E-value: 8.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 27 QVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQ------ILYRGQDIRQKSahyvasngiaqspegrrvfpDMSVEEn 100
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEvdedlkISYKPQYISPDY--------------------DGTVEE- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 101 LLMGTIPIGMD---HAEEDMQRMfelfpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSlglAPIVVKQIF 177
Cdd:COG1245 421 FLRSANTDDFGssyYKTEIIKPL-----GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS---AHLDVEQRL 492
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600102 178 QT---LRELARS-GMTIFLVEqnanHALKL----SDRayVMV-TGE 214
Cdd:COG1245 493 AVakaIRRFAENrGKTAMVVD----HDIYLidyiSDR--LMVfEGE 532
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-213 |
1.18e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.14 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 137 TMSGGEQQMLAIARALMS---RPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNAnHALKLSDraYVMVTG 213
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVAD--YVLELG 885
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-227 |
1.20e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.14 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 133 QRAM-TMSGGEQQMLAIARALMSRPK--LLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNaNHALKLSDR--- 206
Cdd:PRK00635 471 ERALaTLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRiid 549
|
90 100
....*....|....*....|....
gi 15600102 207 ---AYVMVTGEIRMSGSGEELLGN 227
Cdd:PRK00635 550 igpGAGIFGGEVLFNGSPREFLAK 573
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
82-229 |
1.66e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 82 IAQSPegrrVFPDMSVEENLLMGTipigMDHAEEDMQR------MFELFPRLKERRNQR----AMTMSGGEQQMLAIARA 151
Cdd:PTZ00265 1301 VSQEP----MLFNMSIYENIKFGK----EDATREDVKRackfaaIDEFIESLPNKYDTNvgpyGKSLSGGQKQRIAIARA 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELA-RSGMTIFLVEQNANhALKLSDRAYVM----VTGE-IRMSGSGEELL 225
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIA-SIKRSDKIVVFnnpdRTGSfVQAHGTHEELL 1451
|
....
gi 15600102 226 GNQE 229
Cdd:PTZ00265 1452 SVQD 1455
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
133-224 |
3.40e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.40 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 133 QRAMTMSGGEQQMLAIARALMSR---PKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNAnHALKLSDraYV 209
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL-DVIKTAD--YI 901
|
90 100
....*....|....*....|...
gi 15600102 210 --------MVTGEIRMSGSGEEL 224
Cdd:TIGR00630 902 idlgpeggDGGGTVVASGTPEEV 924
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-163 |
7.53e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.94 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 38 GANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQKSAHYVASNGiaqSPEGRRVfpDMSVEENLLMGTipiGMDHAEEDM 117
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG---HNLGLKL--EMTVFENLKFWS---EIYNSAETL 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15600102 118 QRMFELFpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:PRK13541 105 YAAIHYF-KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-193 |
1.01e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.03 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQilyrgqdirqksahyvasngiaqspeGRRVFPDMSVEEN 100
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA--------------------------GCVDVPDNQFGRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 101 L-LMGTIPIGMDHAE----------EDMQRMFELFPRLkerrnqramtmSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:COG2401 100 AsLIDAIGRKGDFKDavellnavglSDAVLWLRRFKEL-----------STGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180
....*....|....*....|....
gi 15600102 170 PIVVKQIFQTLRELARSGMTIFLV 193
Cdd:COG2401 169 RQTAKRVARNLQKLARRAGITLVV 192
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
132-194 |
1.39e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.64 E-value: 1.39e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600102 132 NQRAMTMSGGEQQMLAIARALMSRPK--LLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVE 194
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVE 196
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-192 |
1.40e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 20 ALKKVSLQVNEGETVSLIGANGAGKST-------LL------MSIFGQPraaagqilyrgqdirqksahyVASNGIAQSp 86
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLpasegeAWLFGQP---------------------VDAGDIATR- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 87 egRRV---------FPDMSVEENLLMgtipigmdHA-------EEDMQRMFELFPR--LKERRNQRAMTMSGGEQQMLAI 148
Cdd:NF033858 339 --RRVgymsqafslYGELTVRQNLEL--------HArlfhlpaAEIAARVAEMLERfdLADVADALPDSLPLGIRQRLSL 408
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600102 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLRELARS-GMTIFL 192
Cdd:NF033858 409 AVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREdGVTIFI 453
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
16-180 |
2.51e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 16 GPIqALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQIlYRGQDIRQK--SAHYVASNGIAQSP--EGRRV 91
Cdd:PLN03073 521 GPL-LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKVRMAvfSQHHVDGLDLSSNPllYMMRC 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 92 FPdmSVEENLL---MGTIPIGMDHAeedMQRMFelfprlkerrnqramTMSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:PLN03073 599 FP--GVPEQKLrahLGSFGVTGNLA---LQPMY---------------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
170
....*....|..
gi 15600102 169 APIVVKQIFQTL 180
Cdd:PLN03073 659 DLDAVEALIQGL 670
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-210 |
2.73e-06 |
|
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: 47.47 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 30 EGETVSLIGANGAGKSTLLmSI--------FGQPRAAAG--QIL--YRG---QDIRQKsahyVASNGI--AQSPEG---- 88
Cdd:COG1245 98 KGKVTGILGPNGIGKSTAL-KIlsgelkpnLGDYDEEPSwdEVLkrFRGtelQDYFKK----LANGEIkvAHKPQYvdli 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 89 RRVFpDMSVEEnLLMGTIPIGMdhAEEDMQRMfelfpRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:COG1245 173 PKVF-KGTVRE-LLEKVDERGK--LDELAEKL-----GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600102 169 apivvkQIFQ------TLRELARSGMTIFLVEqnanHAL----KLSDRAYVM 210
Cdd:COG1245 244 ------DIYQrlnvarLIRELAEEGKYVLVVE----HDLaildYLADYVHIL 285
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-164 |
2.97e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAG--------QILYRGQDirqksaHYvasngiAQSPEGRRVF 92
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGtvkwsenaNIGYYAQD------HA------YDFENDLTLF 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600102 93 PDMSV------EENLLMGTipigmdhaeedMQRMfeLFPrlKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:PRK15064 403 DWMSQwrqegdDEQAVRGT-----------LGRL--LFS--QDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-225 |
1.22e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.93 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 17 PIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILyrgqdirqksahyvASNGIAQSPEGRRVFpDMS 96
Cdd:PTZ00243 672 PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--------------AERSIAYVPQQAWIM-NAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 97 VEENLLMGTipigmdhaEEDMQRMFE-------------LFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:PTZ00243 737 VRGNILFFD--------EEDAARLADavrvsqleadlaqLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 164 PSLGLAPIVVKQIFQTLRELARSGMTIFLVEQNAnHALKLSDRAYVMVTGEIRMSGSGEELL 225
Cdd:PTZ00243 809 PLSALDAHVGERVVEECFLGALAGKTRVLATHQV-HVVPRADYVVALGDGRVEFSGSSADFM 869
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-195 |
1.41e-05 |
|
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: 45.51 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 23 KVSLQVNEGETVSLIGANGAGKSTL------LMSIFGQPRA--AAGQILYrgqdirqksahyvasngIAQSPE-GRRVFP 93
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLfrilgeLWPVYGGRLTkpAKGKLFY-----------------VPQRPYmTLGTLR 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 94 D-----MSVEENLLMGtipigmdHAEEDMQRMFE---LFPRLKERRNQRAM-----TMSGGEQQMLAIARALMSRPKLLL 160
Cdd:TIGR00954 533 DqiiypDSSEDMKRRG-------LSDKDLEQILDnvqLTHILEREGGWSAVqdwmdVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190
....*....|....*....|....*....|....*
gi 15600102 161 LDEPSLGLAPIVVKQIFQTLRELarsGMTIFLVEQ 195
Cdd:TIGR00954 606 LDECTSAVSVDVEGYMYRLCREF---GITLFSVSH 637
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-170 |
1.52e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.45 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEF-REVDVFYGPIQalkkvsLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQDIRQ-KSAHYVA 78
Cdd:PRK13543 12 LAAHALAFsRNEEPVFGPLD------FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgDRSRFMA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 79 SngIAQSPEGRrvfPDMSVEENL-----LMGTIP----------IGMDHAEEDMQRMfelfprlkerrnqramtMSGGEQ 143
Cdd:PRK13543 86 Y--LGHLPGLK---ADLSTLENLhflcgLHGRRAkqmpgsalaiVGLAGYEDTLVRQ-----------------LSAGQK 143
|
170 180
....*....|....*....|....*..
gi 15600102 144 QMLAIARALMSRPKLLLLDEPSLGLAP 170
Cdd:PRK13543 144 KRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-190 |
2.51e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 19 QALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGqpRAAAGQI-----LYRGQDIR---QKSAHYVASNGIAqspegrr 90
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVItggdrLVNGRPLDssfQRSIGYVQQQDLH------- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 91 vFPDMSVEENL-------LMGTIPIG--MDHAEEDMqRMFELfPRLKErrnqrAMTMSGGE------QQMLAIARALMSR 155
Cdd:TIGR00956 848 -LPTSTVRESLrfsaylrQPKSVSKSekMEYVEEVI-KLLEM-ESYAD-----AVVGVPGEglnveqRKRLTIGVELVAK 919
|
170 180 190
....*....|....*....|....*....|....*.
gi 15600102 156 PKLLL-LDEPSLGLAPIVVKQIFQTLRELARSGMTI 190
Cdd:TIGR00956 920 PKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAI 955
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-192 |
5.08e-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: 43.45 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVsLIGANGAGKSTLLMSI---FGQPRAAAGQI--LYRGQDIRQKSAH---YVAS--NGIAQSPEGRR 90
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALrllLGPSSSRKFDEedFYLGDDPDLPEIEielTFGSllSRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 91 VFPDMSVEENLLMGTIPIGMDHAEEDMQRMF---------ELFPRLKERRNQRAMT--------------MSGGEQQMLA 147
Cdd:COG3593 93 DKEELEEALEELNEELKEALKALNELLSEYLkelldgldlELELSLDELEDLLKSLslriedgkelpldrLGSGFQRLIL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600102 148 IA--RALM-----SRPKLLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFL 192
Cdd:COG3593 173 LAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVII 224
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-165 |
7.34e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 5 LLEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQI-LYRGQDIRQKSAHYVASNGIA 83
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 84 QSPEGR--RVFPDmSVEENL--LMGTIPIGMDHAEEDMQRmfelfprlkerrnqramtMSGGEQQMLAIARALMSRPKLL 159
Cdd:PRK10636 392 ESPLQHlaRLAPQ-ELEQKLrdYLGGFGFQGDKVTEETRR------------------FSGGEKARLVLALIVWQRPNLL 452
|
....*.
gi 15600102 160 LLDEPS 165
Cdd:PRK10636 453 LLDEPT 458
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-228 |
1.06e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.09 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQP--RAAAGQILYRGQDIRQKSAHYVASNGIAQSPEGRRVFPDMSVE 98
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYPVEIPGVSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 99 ENLLMGTIPIGMDHAEEDMQRmFELFPRLKERRNQRAMT-----------MSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PRK09580 97 FFLQTALNAVRSYRGQEPLDR-FDFQDLMEEKIALLKMPedlltrsvnvgFSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600102 168 L---APIVVKQIFQTLRELARSgmtiFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQ 228
Cdd:PRK09580 176 LdidALKIVADGVNSLRDGKRS----FIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQ 235
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
17-70 |
1.42e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 42.23 E-value: 1.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 15600102 17 PIQALKKVslqVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQIlyRGQDIR 70
Cdd:PRK01889 184 GLDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV--REDDSK 232
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-229 |
1.44e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.11 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 1 MSAALLEFREVDVFYgpiqALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQdirqksahyVASN 80
Cdd:PRK13546 24 MKDALIPKHKNKTFF----ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE---------VSVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 81 GIAQSPEGRrvfpdMSVEENLLMGTIPIGMDHAE--EDMQRMFElFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKL 158
Cdd:PRK13546 91 AISAGLSGQ-----LTGIENIEFKMLCMGFKRKEikAMTPKIIE-FSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600102 159 LLLDEP-SLGLAPIVVKQIfQTLRELARSGMTIFLVEQNANHALKLSDRAYVMVTGEIRMSGSGEELLGNQE 229
Cdd:PRK13546 165 LVIDEAlSVGDQTFAQKCL-DKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYE 235
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
25-165 |
1.46e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 25 SLQVNEGETVSLIGANGAGKSTLLM-----SIFGQPRAAagQILYRGQDI---RQKSAHYVASNGIAQS----PEGRRVF 92
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGIPKNC--QILHVEQEVvgdDTTALQCVLNTDIERTqlleEEAQLVA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 93 PDMSVEENLLMGTIPIGMDHA-EEDM--QRMFELFPRLK----------------------ERRNQRAMTMSGGEQQMLA 147
Cdd:PLN03073 275 QQRELEFETETGKGKGANKDGvDKDAvsQRLEEIYKRLElidaytaearaasilaglsftpEMQVKATKTFSGGWRMRIA 354
|
170
....*....|....*...
gi 15600102 148 IARALMSRPKLLLLDEPS 165
Cdd:PLN03073 355 LARALFIEPDLLLLDEPT 372
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-165 |
1.70e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 42.23 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 6 LEFREVDVFYGPIQALKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYrGQDIRqksAHYVasngiAQS 85
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK---LAYV-----DQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 86 PEGrrVFPDMSVEEnllmgTIPIGMDHAE----EDMQRMF-ELFPRLKERRNQRAMTMSGGEQQMLAIARALMSRPKLLL 160
Cdd:TIGR03719 394 RDA--LDPNKTVWE-----EISGGLDIIKlgkrEIPSRAYvGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
....*
gi 15600102 161 LDEPS 165
Cdd:TIGR03719 467 LDEPT 471
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
136-237 |
2.29e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 40.63 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 136 MTMSGGEQQMLAIARALMSRPKLLLLDEPSlglAPIVVKQIFQTLRELARSGM----TIFLVEQNANHALKLSDRAYVmV 211
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPS---AYLDIEQRLNAARAIRRLSEegkkTALVVEHDLAVLDYLSDRIHV-F 145
|
90 100
....*....|....*....|....*.
gi 15600102 212 TGEIRMSGSGEELLGNQEVRNAYLGG 237
Cdd:cd03222 146 EGEPGVYGIASQPKGTREGINRFLRG 171
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
135-168 |
2.61e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 2.61e-04
10 20 30
....*....|....*....|....*....|....
gi 15600102 135 AMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-165 |
4.87e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 21 LKKVSLQVNEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQILYRGQ-----------DIRQKSAHYVAsngiaqspEGR 89
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqetpALPQPALEYVI--------DGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 90 RVFPDMsvEENLLMGTI-----PIGMDHAEEDMQRMFELFPRL----------KERRNQRAMTMSGGEQQMLAIARALMS 154
Cdd:PRK10636 89 REYRQL--EAQLHDANErndghAIATIHGKLDAIDAWTIRSRAasllhglgfsNEQLERPVSDFSGGWRMRLNLAQALIC 166
|
170
....*....|.
gi 15600102 155 RPKLLLLDEPS 165
Cdd:PRK10636 167 RSDLLLLDEPT 177
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
15-194 |
5.47e-04 |
|
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: 40.04 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 15 YGPiQALKKVSLQV-NEGETVSLIGANGAGKSTLLMSIFGQPRAAAGQ---------IL--YRGQDIrQKSAHYVASNGI 82
Cdd:cd03236 10 YGP-NSFKLHRLPVpREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeILdeFRGSEL-QNYFTKLLEGDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 83 --AQSPEGRRVFP---DMSVEEnLLMGTIPIGMdhAEEDMQRMfelfpRLKERRNQRAMTMSGGEQQMLAIARALMSRPK 157
Cdd:cd03236 88 kvIVKPQYVDLIPkavKGKVGE-LLKKKDERGK--LDELVDQL-----ELRHVLDRNIDQLSGGELQRVAIAAALARDAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15600102 158 LLLLDEPSLGLApivVKQIF---QTLRELARSGMTIFLVE 194
Cdd:cd03236 160 FYFFDEPSSYLD---IKQRLnaaRLIRELAEDDNYVLVVE 196
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
133-196 |
1.41e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 1.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600102 133 QRAMTMSGGEQQMLAIARALMSRPK---LLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQN 196
Cdd:COG0178 822 QPATTLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHN 888
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
29-194 |
4.37e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 36.57 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 29 NEGETVSLIGANGAGKSTLLmsifgqpraaagqilyrgqdirqKSAHYVAsnGIAQSPEGRRvfpdmsveenllmGTIPI 108
Cdd:cd03227 19 GEGSLTIITGPNGSGKSTIL-----------------------DAIGLAL--GGAQSATRRR-------------SGVKA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 109 GMDHAEEDMQRMFELfprlkerrnqraMTMSGGEQQMLAIA-----RALMSRPkLLLLDEPSLGLAPIVVKQIFQTLREL 183
Cdd:cd03227 61 GCIVAAVSAELIFTR------------LQLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEH 127
|
170
....*....|.
gi 15600102 184 ARSGMTIFLVE 194
Cdd:cd03227 128 LVKGAQVIVIT 138
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
94-196 |
8.35e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 36.97 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600102 94 DMSVEEnllmgtipigmdhAEEdmqrMFELFPRLKERRN-------------QRAMTMSGGEQQMLAIARALMSRPK--- 157
Cdd:PRK00349 791 DMTVEE-------------ALE----FFEAIPKIARKLQtlvdvglgyiklgQPATTLSGGEAQRVKLAKELSKRSTgkt 853
|
90 100 110
....*....|....*....|....*....|....*....
gi 15600102 158 LLLLDEPSLGLAPIVVKQIFQTLRELARSGMTIFLVEQN 196
Cdd:PRK00349 854 LYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHN 892
|
|
| |
