|
Name |
Accession |
Description |
Interval |
E-value |
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-237 |
1.34e-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: 380.48 E-value: 1.34e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 3 EPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGI 82
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 83 AQAPEGRRIFPDMTVEENLLMGTIPIGSQFA-AEDMQTMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLL 161
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEvRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 162 DEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEVRKAYLGG 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 |
1.57e-117 |
|
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: 334.40 E-value: 1.57e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAQA 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 86 PEGRRIFPDMTVEENLLMGTIPIGSQFAAEDMQTMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2792998456 166 LGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGN 227
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-237 |
1.44e-100 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 292.17 E-value: 1.44e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASG 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 GIAQAPEGRRIFPDMTVEENLLMGTIPIGSQFAAEDMQTMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLL 160
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 161 LDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEVRKAYLGG 237
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLGG 237
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-235 |
7.11e-77 |
|
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: 231.65 E-value: 7.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAQA 85
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 86 PEGRRIFPDMTVEENLLMG--TIPIGSQFAAEDMqtmFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGlaALPRRSRKIPDEI---YELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2792998456 164 PSLGLAPIVVKQIFQTLSELA-RSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELlgNQEVRKAYL 235
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRaEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL--DEDKVRRYL 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-237 |
2.13e-58 |
|
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: 185.24 E-value: 2.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 2 NEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGG 81
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 82 IA---QAPegrRIFPDMTVEENLLMGT--------------IPIGSQFAAEDMQTMFDL--FPRLKERRKQRAMTMSGGE 142
Cdd:COG0411 81 IArtfQNP---RLFPELTVLENVLVAAharlgrgllaallrLPRARREEREARERAEELleRVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 143 QQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELAR-SGMTIFLVEqnaHH---ALKLSDRGYVMVNGQIRLS 218
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIE---HDmdlVMGLADRIVVLDFGRVIAE 234
|
250
....*....|....*....
gi 2792998456 219 GSGEELLGNQEVRKAYLGG 237
Cdd:COG0411 235 GTPAEVRADPRVIEAYLGE 253
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-236 |
5.85e-57 |
|
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: 180.82 E-value: 5.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 14 FYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAQAPEGRRIFP 93
Cdd:cd03218 9 RYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQEASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DMTVEENLL--MGTIPIGSQFAAEDMQTMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:cd03218 89 KLTVEENILavLEIRGLSKKEREEKLEELLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2792998456 172 VVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEVRKAYLG 236
Cdd:cd03218 168 AVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-230 |
3.46e-54 |
|
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: 173.78 E-value: 3.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIA-- 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 84 -QAPegrRIFPDMTVEENLLMGTIPIGSQFA---------AEDMQTMFDL--FPRLKERRKQRAMTMSGGEQQMLAIARA 151
Cdd:cd03219 81 fQIP---RLFPELTVLENVMVAAQARTGSGLllararreeREARERAEELleRVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEV 230
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
15-236 |
7.53e-53 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 170.60 E-value: 7.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGI---AQAPEgrrI 91
Cdd:COG1137 13 YGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIgylPQEAS---I 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 92 FPDMTVEENLL--MGTIPIGSQFAAEDMQTMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:COG1137 90 FRKLTVEDNILavLELRKLSKKEREERLEELLEEF-GITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 170 PIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEVRKAYLG 236
Cdd:COG1137 169 PIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLG 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
15-225 |
4.32e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 166.01 E-value: 4.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASggIAQAPEGRRIFPD 94
Cdd:COG1131 10 YGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR--IGYVPQEPALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 MTVEENL-LMGTI-PIGSQFAAEDMQTMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIV 172
Cdd:COG1131 88 LTVRENLrFFARLyGLPRKEARERIDELLELF-GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2792998456 173 VKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:COG1131 167 RRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
15-236 |
9.78e-50 |
|
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: 162.83 E-value: 9.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAQAPEGRRIFPD 94
Cdd:TIGR04406 11 YKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYLPQEASIFRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 MTVEENL-----LMGTIPIGSQfaAEDMQTMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:TIGR04406 91 LTVEENImavleIRKDLDRAER--EERLEALLEEF-QISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 170 PIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEVRKAYLG 236
Cdd:TIGR04406 168 PIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLG 234
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-234 |
3.72e-46 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 153.71 E-value: 3.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTH--YVA 78
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 79 sggiaQAPEGRRIFPdMTVEENLLMGTIPIGSqfaaedmqtmfdLFPRLKERRKQRAM-----------------TMSGG 141
Cdd:COG1121 82 -----QRAEVDWDFP-ITVRDVVLMGRYGRRG------------LFRRPSRADREAVDealervgledladrpigELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 142 EQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRgYVMVNGQIRLSGSG 221
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDR-VLLLNRGLVAHGPP 222
|
250
....*....|...
gi 2792998456 222 EELLGNQEVRKAY 234
Cdd:COG1121 223 EEVLTPENLSRAY 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-215 |
2.35e-42 |
|
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: 141.38 E-value: 2.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIshKSTHYVASGGIAQA 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI--KKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 86 PEGRRIFPDMTVEENLlmgtipigsqfaaedmqtmfdlfprlkerrkqramTMSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:cd03230 79 PEEPSLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2792998456 166 LGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-233 |
2.58e-42 |
|
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: 143.24 E-value: 2.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAsggiaq 84
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 85 apegRRI-----FPD-----MTVEENLLMGtiPIGSQFAAEDMQ-------TMFDLfprlKERRKQRAMTMSGGEQQMLA 147
Cdd:COG1122 75 ----RKVglvfqNPDdqlfaPTVEEDVAFG--PENLGLPREEIRerveealELVGL----EHLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 148 IARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGN 227
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSD 224
|
....*.
gi 2792998456 228 QEVRKA 233
Cdd:COG1122 225 YELLEE 230
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
15-235 |
3.95e-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: 140.76 E-value: 3.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASggIAQAPEGRRIFPD 94
Cdd:COG4555 11 YGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ--IGVLPDERGLYDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 MTVEENL-----LMGTIPIGSQFAAEDMQTMFDLFprlkERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:COG4555 89 LTVRENIryfaeLYGLFDEELKKRIEELIELLGLE----EFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 170 PIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELL---GNQEVRKAYL 235
Cdd:COG4555 165 VMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELReeiGEENLEDAFV 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-164 |
2.64e-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: 135.47 E-value: 2.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVaSGGIAQAPEGRRIFPDMTVEEN 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL-RKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 101 LLMGTIPIGSQFAAEDMQ-----TMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARaeealEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
19-214 |
3.87e-40 |
|
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: 137.21 E-value: 3.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVA--SGGIAQAPEGRRIFPdmT 96
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLVFQNPDDQFFGP--T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 97 VEENLLMGtiPIGSQFAAEDMQ----TMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIV 172
Cdd:cd03225 93 VEEEVAFG--LENLGLPEEEIEerveEALELV-GLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2792998456 173 VKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQ 214
Cdd:cd03225 170 RRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-234 |
1.58e-39 |
|
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: 136.71 E-value: 1.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 5 LLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS--GGI 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARriAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 83 AQAPEGRrifPDMTVEENLLMGTIP---IGSQFAAEDMQ------TMFDLFPrLKERrkqRAMTMSGGEQQMLAIARALM 153
Cdd:COG1120 81 PQEPPAP---FGLTVRELVALGRYPhlgLFGRPSAEDREaveealERTGLEH-LADR---PVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 154 SRPKLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVeqnAH---HALKLSDRGYVMVNGQIRLSGSGEELLGNQE 229
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMV---LHdlnLAARYADRLVLLKDGRIVAQGPPEEVLTPEL 230
|
....*
gi 2792998456 230 VRKAY 234
Cdd:COG1120 231 LEEVY 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-224 |
2.17e-39 |
|
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: 135.77 E-value: 2.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLL----MSIFGQPRIR-NGQILFSGEDISHKSTHYVAS- 79
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLrllnRLNDLIPGAPdEGEVLLDGKDIYDLDVDVLELr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 80 ---GGIAQAPEgrrIFPdMTVEENLLMGTIPIGSQFA------AEDMQTMFDLFPRLKerRKQRAMTMSGGEQQMLAIAR 150
Cdd:cd03260 81 rrvGMVFQKPN---PFP-GSIYDNVAYGLRLHGIKLKeelderVEEALRKAALWDEVK--DRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792998456 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSgMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-214 |
7.56e-39 |
|
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: 131.98 E-value: 7.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 8 FREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSthyvasggiaqape 87
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 88 grrifpdmtveenllmgtipigsqfaaedmqtmfdlfprLKERRKQRAMT--MSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:cd00267 68 ---------------------------------------LEELRRRIGYVpqLSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2792998456 166 LGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQ 214
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-224 |
2.64e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 133.64 E-value: 2.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 4 PLLAFREVDV-FYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSThyvasggi 82
Cdd:COG3638 1 PMLELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 83 AQAPEGRR----IF------PDMTVEENLLMGTIP-------IGSQFAAEDMQTMFDLFPR--LKERRKQRAMTMSGGEQ 143
Cdd:COG3638 73 RALRRLRRrigmIFqqfnlvPRLSVLTNVLAGRLGrtstwrsLLGLFPPEDRERALEALERvgLADKAYQRADQLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 144 QMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIfLVeqNAHH---ALKLSDRGYVMVNGQIRLSG 219
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITV-VV--NLHQvdlARRYADRIIGLRDGRVVFDG 229
|
....*
gi 2792998456 220 SGEEL 224
Cdd:COG3638 230 PPAEL 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-219 |
4.34e-38 |
|
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: 131.89 E-value: 4.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 13 VFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTH--YVAsggiaQAPEGRR 90
Cdd:cd03235 7 VSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigYVP-----QRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 91 IFPdMTVEENLLMGTIPigsqfaaedmqtMFDLFPRLKERRKQRAM-----------------TMSGGEQQMLAIARALM 153
Cdd:cd03235 82 DFP-ISVRDVVLMGLYG------------HKGLFRRLSKADKAKVDealervglseladrqigELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 154 SRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRgYVMVNGQIRLSG 219
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-238 |
6.03e-38 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 132.43 E-value: 6.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 5 LLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHyvasggIAQ 84
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKD------INK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 85 ApegRR----------IFPDMTVEENLLMGTIPIGSQFAAEDMQTMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARAL 152
Cdd:COG1126 75 L---RRkvgmvfqqfnLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERvgLADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGN-QEVR 231
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENpQHER 231
|
....*...
gi 2792998456 232 -KAYLGGV 238
Cdd:COG1126 232 tRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
15-215 |
6.62e-38 |
|
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: 131.50 E-value: 6.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSThyvasggiaQAPEGRR---- 90
Cdd:cd03262 10 FGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKK---------NINELRQkvgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 91 ------IFPDMTVEENLLMGTIPIGSQFAAEDMQTMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:cd03262 81 vfqqfnLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKvgLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2792998456 163 EPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-236 |
1.90e-37 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 131.65 E-value: 1.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASG 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 GIAQAPEGRRIFPDMTVEENLLMgtipigsqfaAEDMQTMFDLFPRLKE----RRKQR---------------------- 134
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLV----------AQHQQLKTGLFSGLLKtpafRRAESealdraatwlervgllehanrq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 135 AMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNG 213
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
250 260
....*....|....*....|...
gi 2792998456 214 QIRLSGSGEELLGNQEVRKAYLG 236
Cdd:PRK11300 231 TPLANGTPEEIRNNPDVIKAYLG 253
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-215 |
2.25e-37 |
|
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: 130.32 E-value: 2.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 5 LLAFREVDVFY----GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASG 80
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 G-----IAQAPeGRRIFPDMTVEENLLMG----TIPIGSQFAAEDMQTMFDLFPRLKERRKQRAMTMSGGEQQMLAIARA 151
Cdd:cd03257 81 RkeiqmVFQDP-MSSLNPRMTIGEQIAEPlrihGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2792998456 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLSEL-ARSGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-224 |
3.97e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 135.53 E-value: 3.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 2 NEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGG 81
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 82 IA---QAPEgrrIFPDMTVEENLLMGTIPIGSQF---------AAEDMQTM-FDLFPRlkerrkQRAMTMSGGEQQMLAI 148
Cdd:COG1129 81 IAiihQELN---LVPNLSVAENIFLGREPRRGGLidwramrrrARELLARLgLDIDPD------TPVGDLSVAQQQLVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVeqnAHH---ALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYI---SHRldeVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-224 |
4.30e-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: 130.00 E-value: 4.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYG-VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS----- 79
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 80 GGIAQAPegrRIFPDMTVEENLLMGTIP-------IGSQFAAEDMQTMFDLFPR--LKERRKQRAMTMSGGEQQMLAIAR 150
Cdd:cd03256 81 GMIFQQF---NLIERLSVLENVLSGRLGrrstwrsLFGLFPKEEKQRALAALERvgLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLveqNAHH---ALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIV---SLHQvdlAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-215 |
6.19e-37 |
|
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: 129.15 E-value: 6.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYG----VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHyvasgg 81
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEK------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 82 iAQAPEGRR----IF------PDMTVEENLLMGTIPIG--SQFAAEDMQTMFDLFpRLKERRKQRAMTMSGGEQQMLAIA 149
Cdd:cd03255 75 -ELAAFRRRhigfVFqsfnllPDLTALENVELPLLLAGvpKKERRERAEELLERV-GLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELAR-SGMTIFLVEQNaHHALKLSDRGYVMVNGQI 215
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-214 |
7.04e-37 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 127.69 E-value: 7.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIshksthyvASGGIAQA 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL--------TDLEDELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 86 PEGRRI---------FPDMTVEENLLMGtipigsqfaaedmqtmfdlfprlkerrkqramtMSGGEQQMLAIARALMSRP 156
Cdd:cd03229 73 PLRRRIgmvfqdfalFPHLTVLENIALG---------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 157 KLLLLDEPSLGLAPIVVKQIFQTLSEL-ARSGMTIFLVEQNAHHALKLSDRGYVMVNGQ 214
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-219 |
8.98e-37 |
|
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: 128.49 E-value: 8.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 9 REVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAQAPEg 88
Cdd:cd03268 4 NDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 89 rrIFPDMTVEENL-LMGTIPIGSQFAAEDMQTMFDlfprLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:cd03268 83 --FYPNLTARENLrLLARLLGIRKKRIDEVLDVVG----LKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 168 LAPIVVKQIFQTLSELARSGMTIFLveqnAHHAL----KLSDRGYVMVNGQIRLSG 219
Cdd:cd03268 157 LDPDGIKELRELILSLRDQGITVLI----SSHLLseiqKVADRIGIINKGKLIEEG 208
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-205 |
1.23e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.25 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 8 FREVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVasggiaqaP 86
Cdd:COG2884 4 FENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREI--------P 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 87 EGRR----IF------PDMTVEENLLMGTIPIG--SQFAAEDMQTMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMS 154
Cdd:COG2884 76 YLRRrigvVFqdfrllPDRTVYENVALPLRVTGksRKEIRRRVREVLDLV-GLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 155 RPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIF-------LVEQNAHHALKLSD 205
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLiathdleLVDRMPKRVLELED 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-224 |
1.33e-36 |
|
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: 128.39 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIshKSTHYVASGGIAQAPEGRRIFPDMTVEE 99
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQSLGYCPQFDALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 100 NL-LMGTIP-IGSQFAAEDMQTMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIF 177
Cdd:cd03263 95 HLrFYARLKgLPKSEIKEEVELLLRVL-GLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIW 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2792998456 178 QTLSELaRSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:cd03263 174 DLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-227 |
4.01e-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: 133.10 E-value: 4.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 3 EPLLAFREVDVFYGV-----IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSthyv 77
Cdd:COG1123 258 EPLLEVRNLSKRYPVrgkggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLS---- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 78 asgGIAQAPEGRRI-----------FPDMTVEENL-----LMGTIPIGSQFA-AEDMQTMFDLFPRLKERRkqrAMTMSG 140
Cdd:COG1123 334 ---RRSLRELRRRVqmvfqdpysslNPRMTVGDIIaeplrLHGLLSRAERRErVAELLERVGLPPDLADRY---PHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 141 GEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVeqnAHH---ALKLSDRGYVMVNGQIR 216
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFI---SHDlavVRYIADRVAVMYDGRIV 484
|
250
....*....|.
gi 2792998456 217 LSGSGEELLGN 227
Cdd:COG1123 485 EDGPTEEVFAN 495
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-224 |
4.13e-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: 130.60 E-value: 4.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHksthyvasg 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 giaQAPEGRRI---------FPDMTVEEN----LLMGTIPigSQFAAEDMQTMFDLFpRLKERRKQRAMTMSGGEQQMLA 147
Cdd:COG3842 72 ---LPPEKRNVgmvfqdyalFPHLTVAENvafgLRMRGVP--KAEIRARVAELLELV-GLEGLADRYPHQLSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 148 IARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSEL-ARSGMTIFLVeqnAHH---ALKLSDRGYVMVNGQIRLSGSGEE 223
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYV---THDqeeALALADRIAVMNDGRIEQVGTPEE 222
|
.
gi 2792998456 224 L 224
Cdd:COG3842 223 I 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-229 |
6.81e-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: 132.72 E-value: 6.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 3 EPLLAFREVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFG---QPRIRNGQILFSGEDISHKSTHYV 77
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 78 AS--GGIAQAPEgRRIFPdMTVEENLLMG--TIPIGSQFAAEDMQTMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALM 153
Cdd:COG1123 82 GRriGMVFQDPM-TQLNP-VTVGDQIAEAleNLGLSRAEARARVLELLEAV-GLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 154 SRPKLLLLDEPSLGLAPIVVKQIFQTLSELAR-SGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQE 229
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-215 |
1.47e-35 |
|
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: 125.32 E-value: 1.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHyvaSGGIAQA 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE---RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 86 PEGRRIFPDMTVEEN----LLMGTIPIGSQFAAEDMQT-MFDLFPRLKErrkqRAMTMSGGEQQMLAIARALMSRPKLLL 160
Cdd:cd03259 78 FQDYALFPHLTVAENiafgLKLRGVPKAEIRARVRELLeLVGLEGLLNR----YPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 161 LDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-215 |
2.27e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 125.16 E-value: 2.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 3 EPLLAFREVDVFYGV----IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSthyva 78
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLS----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 79 SGGIAQApegRR-----IF------PDMTVEENLLMGTIPIGSQFA-----AEDMQTMFDLfprlKERRKQRAMTMSGGE 142
Cdd:COG1136 77 ERELARL---RRrhigfVFqffnllPELTALENVALPLLLAGVSRKerrerARELLERVGL----GDRLDHRPSQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 143 QQMLAIARALMSRPKLLLLDEP--SL----GlapivvKQIFQTLSELAR-SGMTIFLV---EQNAHHAlklsDRGYVMVN 212
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPtgNLdsktG------EEVLELLRELNReLGTTIVMVthdPELAARA----DRVIRLRD 219
|
...
gi 2792998456 213 GQI 215
Cdd:COG1136 220 GRI 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-236 |
2.47e-35 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 125.78 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAQAPEGRRIFPDMTVE 98
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEASIFRRLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 99 ENLlMGTIPIGSQFAAEDMQ----TMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVK 174
Cdd:PRK10895 97 DNL-MAVLQIRDDLSAEQREdranELMEEF-HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2792998456 175 QIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEVRKAYLG 236
Cdd:PRK10895 175 DIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-214 |
1.83e-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: 121.34 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYG--VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS--GG 81
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKniAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 82 IAQAPEgrrIFpDMTVEENLLmgtipigsqfaaedmqtmfdlfprlkerrkqramtmSGGEQQMLAIARALMSRPKLLLL 161
Cdd:cd03228 81 VPQDPF---LF-SGTIRENIL------------------------------------SGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2792998456 162 DEPSLGLAPIVVKQIFQTLSELARsGMTIFLVeqnAH--HALKLSDRGYVMVNGQ 214
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK-GKTVIVI---AHrlSTIRDADRIIVLDDGR 171
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-215 |
3.34e-34 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 120.23 E-value: 3.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAqa 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 86 pegrrifpdmTVeenllmgtipigsqfaaedMQtmfdlfprlkerrkqramtMSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:cd03216 79 ----------MV-------------------YQ-------------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2792998456 166 LGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-227 |
3.59e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 122.51 E-value: 3.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 8 FREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIShksthyvasGGIAQAPE 87
Cdd:PRK09493 4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN---------DPKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 88 GRR----------IFPDMTVEENLLMGTIPIGSQFAAEDMQTMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSR 155
Cdd:PRK09493 75 IRQeagmvfqqfyLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2792998456 156 PKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGN 227
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-231 |
5.15e-34 |
|
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: 122.01 E-value: 5.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHyvasg 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 giAQAPEGRRI---------FPDMTVEENLlmgtipigsqfaaedmqtMFDL--FPRLKER-RKQRAMTM---------- 138
Cdd:COG1127 76 --ELYELRRRIgmlfqggalFDSLTVFENV------------------AFPLreHTDLSEAeIRELVLEKlelvglpgaa 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 139 -------SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVM 210
Cdd:COG1127 136 dkmpselSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVL 215
|
250 260
....*....|....*....|...
gi 2792998456 211 VNGQIRLSGSGEELL--GNQEVR 231
Cdd:COG1127 216 ADGKIIAEGTPEELLasDDPWVR 238
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
5.62e-34 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 120.23 E-value: 5.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 2 NEPLLAFREVdvfyGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGG 81
Cdd:cd03215 1 GEPVLEVRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 82 IAQAPEGRR---IFPDMTVEENLLMGTIpigsqfaaedmqtmfdlfprlkerrkqramtMSGGEQQMLAIARALMSRPKL 158
Cdd:cd03215 77 IAYVPEDRKregLVLDLSVAENIALSSL-------------------------------LSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 159 LLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-224 |
1.31e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 122.52 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLmsifgqpRIRN-------GQILFSGEDISHKSTHyvasgGIAQAPE 87
Cdd:COG4152 11 FGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTI-------RIILgilapdsGEVLWDGEPLDPEDRR-----RIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 88 GRRIFPDMTVEENL-----LMGtipIGSQFAAEDMQTMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:COG4152 79 ERGLYPKMKVGEQLvylarLKG---LSKAEAKRRADEWLERL-GLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2792998456 163 EPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-224 |
1.36e-33 |
|
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: 120.80 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAQA 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 86 pegRRIFPDMTVEEN----LLMGTIPIGSQfaAEDMQTMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLL 161
Cdd:cd03300 81 ---YALFPHLTVFENiafgLRLKKLPKAEI--KERVAEALDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792998456 162 DEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
8-205 |
2.38e-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: 2.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 8 FREVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS--GGIAQ 84
Cdd:TIGR02673 4 FHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLlrRRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 85 APEGRRIFPDMTVEEN--LLMGTIPIGSQFAAEDMQTMFDLFPrLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:TIGR02673 84 VFQDFRLLPDRTVYENvaLPLEVRGKKEREIQRRVGAALRQVG-LEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2792998456 163 EPSLGLAPIVVKQIFQTLSELARSGMTIF-------LVEQNAHHALKLSD 205
Cdd:TIGR02673 163 EPTGNLDPDLSERILDLLKRLNKRGTTVIvathdlsLVDRVAHRVIILDD 212
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-215 |
3.55e-33 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 120.29 E-value: 3.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 5 LLAFREVDVFYGV----IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKST--HYVA 78
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkaFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 79 SGGIAQAPEGRrIFPDMTVEENL-----LMGTIPIGSQfAAEDMQTMfDLFPRLKERRKQramTMSGGEQQMLAIARALM 153
Cdd:COG1124 81 VQMVFQDPYAS-LHPRHTVDRILaeplrIHGLPDREER-IAELLEQV-GLPPSFLDRYPH---QLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2792998456 154 SRPKLLLLDEPSLGLAPIVVKQIFQTLSEL-ARSGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-215 |
3.69e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 124.75 E-value: 3.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 3 EPLLAFREVdvfyGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGI 82
Cdd:COG1129 254 EVVLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 83 AQAPEGRR---IFPDMTVEENLLMGTIPIGSQF----------AAEDMQTMFDLFPRlkeRRKQRAMTMSGGEQQMLAIA 149
Cdd:COG1129 330 AYVPEDRKgegLVLDLSIRENITLASLDRLSRGglldrrreraLAEEYIKRLRIKTP---SPEQPVGNLSGGNQQKVVLA 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792998456 150 RALMSRPKLLLLDEPSLGlapIVV---KQIFQTLSELARSGMTIFLV-----EqnahhALKLSDRGYVMVNGQI 215
Cdd:COG1129 407 KWLATDPKVLILDEPTRG---IDVgakAEIYRLIRELAAEGKAVIVIsselpE-----LLGLSDRILVMREGRI 472
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-224 |
3.99e-33 |
|
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: 119.53 E-value: 3.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 8 FREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSthyvasgGIAQAPE 87
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLS-------EAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 88 GRRI---------FPDMTVEEN----------LLMGTIpigSQFAAEDMQTMfdlfpRLKERRKQRAMTMSGGEQQMLAI 148
Cdd:cd03261 76 RRRMgmlfqsgalFDSLTVFENvafplrehtrLSEEEI---REIVLEKLEAV-----GLRGAEDLYPAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
15-224 |
4.18e-33 |
|
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: 119.40 E-value: 4.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAqaPEGRRIFPD 94
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV--FQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 MTVEENLLM-GTI-PIGSQFAAEDMQTMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIV 172
Cdd:cd03265 88 LTGWENLYIhARLyGVPGAERRERIDELLDFV-GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2792998456 173 VKQIFQTLSEL-ARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:cd03265 167 RAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
15-219 |
8.26e-33 |
|
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: 118.15 E-value: 8.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGE--DISHKSThyvasggIAQAPEGRRIF 92
Cdd:cd03269 10 FGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKplDIAARNR-------IGYLPEERGLY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 PDMTVEENL-----LMGtipIGSQFAAEDMQTMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:cd03269 83 PKMKVIDQLvylaqLKG---LKKEEARRRIDEWLERL-ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2792998456 168 LAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSG 219
Cdd:cd03269 159 LDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-225 |
3.81e-32 |
|
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: 117.49 E-value: 3.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 3 EPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLL--------------MSIFGQPRirngqilfSGED 68
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLslitgdlpptygndVRLFGERR--------GGED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 69 ISHKSTHYvasgGIAQAPEGRRIFPDMTVEENLLMG---TIPIGSQFAAEDMQTMFDLFPRLK-ERRKQRAM-TMSGGEQ 143
Cdd:COG1119 73 VWELRKRI----GLVSPALQLRFPRDETVLDVVLSGffdSIGLYREPTDEQRERARELLELLGlAHLADRPFgTLSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 144 QMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSG-MTIFLVeqnAHHA---LKLSDRGYVMVNGQIRLSG 219
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLV---THHVeeiPPGITHVLLLKDGRVVAAG 225
|
....*.
gi 2792998456 220 SGEELL 225
Cdd:COG1119 226 PKEEVL 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-235 |
5.02e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 117.87 E-value: 5.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS----GGIAQAPEGRRIFPd 94
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVrktvGIVFQNPDDQLFAP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 mTVEENLLMGtiPIGSQFAAEDMQTmfdlfpRLKERRKQRAMT---------MSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:PRK13639 95 -TVEEDVAFG--PLNLGLSKEEVEK------RVKEALKAVGMEgfenkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2792998456 166 LGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQE-VRKAYL 235
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIEtIRKANL 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-228 |
5.60e-32 |
|
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: 122.17 E-value: 5.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 4 PLLAFREVDVFYGV-IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS--G 80
Cdd:COG4988 335 PSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRqiA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 GIAQAPegrRIFPDmTVEENLLMGTipigSQFAAEDMQT------MFDLFPRLKE----RRKQRAMTMSGGEQQMLAIAR 150
Cdd:COG4988 415 WVPQNP---YLFAG-TIRENLRLGR----PDASDEELEAaleaagLDEFVAALPDgldtPLGEGGRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARsGMTIFLVeqnAH--HALKLSDRGYVMVNGQIRLSGSGEELLGNQ 228
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILI---THrlALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-229 |
6.30e-32 |
|
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: 122.18 E-value: 6.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 4 PLLAFREVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS-- 79
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRri 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 80 GGIAQAPEgrrIFpDMTVEENLLMGTiPIGSQfaaEDMQTMFD---LFPRLKERRK-------QRAMTMSGGEQQMLAIA 149
Cdd:COG4987 412 AVVPQRPH---LF-DTTLRENLRLAR-PDATD---EELWAALErvgLGDWLAALPDgldtwlgEGGRRLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARsGMTIFLVeqnAHH--ALKLSDRGYVMVNGQIRLSGSGEELLGN 227
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLI---THRlaGLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
..
gi 2792998456 228 QE 229
Cdd:COG4987 560 NG 561
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-223 |
2.18e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 115.95 E-value: 2.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTH----YVAsggiaqapegrRIF--- 92
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYkrakYIG-----------RVFqdp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 -----PDMTVEENLLM-----GTIPIGSQFAAEDMQTMFDLFPRLK---ERR-KQRAMTMSGGEQQMLAIARALMSRPKL 158
Cdd:COG1101 90 mmgtaPSMTIEENLALayrrgKRRGLRRGLTKKRRELFRELLATLGlglENRlDTKVGLLSGGQRQALSLLMATLTKPKL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 159 LLLDEPSLGLAPIVVKQIFQTLSEL-ARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEE 223
Cdd:COG1101 170 LLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVSGEE 235
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-219 |
2.72e-31 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 113.30 E-value: 2.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 9 REVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAsggiaqapeg 88
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 89 RRIfpdmtveenllmGTIPigsqfaaedmQTM--FDLFPrLKERRkqrAMTMSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:cd03214 73 RKI------------AYVP----------QALelLGLAH-LADRP---FNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2792998456 167 GLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSG 219
Cdd:cd03214 127 HLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-215 |
7.14e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 114.49 E-value: 7.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSI--FGQ--PRIR-NGQILFSGEDISHKSTH 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDlnPEVTiTGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 76 YV----ASGGIAQAPEGrriFPdMTVEENLLMGTIPIGSQ------FAAEDMQTMFDLFPRLKERRKQRAMTMSGGEQQM 145
Cdd:PRK14239 81 TVdlrkEIGMVFQQPNP---FP-MSIYENVVYGLRLKGIKdkqvldEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELaRSGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-215 |
1.15e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.60 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTH-------YVA 78
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPewrrqvaYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 79 sggiaQAPegrRIFPDmTVEENLLMGTIPIGSQFaaeDMQTMFDLFPRL---KERRKQRAMTMSGGEQQMLAIARALMSR 155
Cdd:COG4619 81 -----QEP---ALWGG-TVRDNLPFPFQLRERKF---DRERALELLERLglpPDILDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2792998456 156 PKLLLLDEPSLGLAPIVVKQIFQTLSEL-ARSGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-225 |
1.63e-30 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 118.78 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGgIAQAPEGRRIFPDmTVEE 99
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ-IGVVLQDVFLFSG-TIRE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 100 NLLMGTIPIGSQ---FAAED-------------MQTMfdlfprLKERrkqrAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:COG2274 568 NITLGDPDATDEeiiEAARLaglhdfiealpmgYDTV------VGEG----GSNLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792998456 164 PSLGLAPIVVKQIFQTLSELARsGMTIFLVeqnAH--HALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:COG2274 638 ATSALDAETEAIILENLRRLLK-GRTVIII---AHrlSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-215 |
5.01e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 112.05 E-value: 5.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 3 EPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSI------FGQPRIrNGQILFSGEDISHKSTHY 76
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlIPGARV-EGEILLDGEDIYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 77 VA----SGGIAQAPegrRIFPdMTVEENLLMGtipigsqfaaedmqtmfdlfPRL------------------------- 127
Cdd:COG1117 88 VElrrrVGMVFQKP---NPFP-KSIYDNVAYG--------------------LRLhgikskseldeiveeslrkaalwde 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 128 -KERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSgMTIFLVEQNAHHALKLSDR 206
Cdd:COG1117 144 vKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDY 222
|
....*....
gi 2792998456 207 GYVMVNGQI 215
Cdd:COG1117 223 TAFFYLGEL 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
9.73e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 111.33 E-value: 9.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFY----GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTH- 75
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 76 -YVAsggiaQAPegrRIFPDMTVEENLLMG--TIPIGSQFAAEDMQTMFDLFpRLKERRKQRAMTMSGGEQQMLAIARAL 152
Cdd:COG1116 83 gVVF-----QEP---ALLPWLTVLDNVALGleLRGVPKAERRERARELLELV-GLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2792998456 153 MSRPKLLLLDEPslglapivvkqiF-----QT--------LSELARSGMTIFLVEQNAHHALKLSDRGYVM 210
Cdd:COG1116 154 ANDPEVLLMDEP------------FgaldaLTrerlqdelLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-210 |
1.65e-29 |
|
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: 109.87 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYG----VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHyvasgg 81
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 82 IAQAPEGRRIFPDMTVEENLLMG--TIPIGSQFAAEDMQTMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLL 159
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGleLQGVPKAEARERAEELLELV-GLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2792998456 160 LLDEPSLGLAPIVVKQIFQTLSEL-ARSGMTIFLVEQNAHHALKLSDRGYVM 210
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
11-215 |
1.70e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 110.49 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 11 VDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLL--MSIFGQPRirNGQILFSGE--DISHKSTHyvasggiAQAP 86
Cdd:COG4161 8 INCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLrvLNLLETPD--SGQLNIAGHqfDFSQKPSE-------KAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 87 EGRR----------IFPDMTVEENLLMGTIPIGSQFAAEDMQTMFDLFPRLKERRKQRA--MTMSGGEQQMLAIARALMS 154
Cdd:COG4161 79 LLRQkvgmvfqqynLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRfpLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2792998456 155 RPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
11-215 |
1.87e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 110.49 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 11 VDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLL-------MSIFGQPRIRNGQILFSgedishksthyvASGGIA 83
Cdd:PRK11124 8 INCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLrvlnlleMPRSGTLNIAGNHFDFS------------KTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 84 QAPEGRR----------IFPDMTVEENLLMGTIPIGSQFAAEDMQTMFDLFPRLkeRRKQRA----MTMSGGEQQMLAIA 149
Cdd:PRK11124 76 AIRELRRnvgmvfqqynLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERL--RLKPYAdrfpLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-223 |
1.91e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 113.12 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHksthyvasg 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 giaQAPEGRRI---------FPDMTVEEN----LLMGTIPigsqfAAEDMQTMFDLFP--RLKERRKQRAMTMSGGEQQM 145
Cdd:PRK09452 81 ---VPAENRHVntvfqsyalFPHMTVFENvafgLRMQKTP-----AAEITPRVMEALRmvQLEEFAQRKPHQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEE 223
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
19-225 |
3.02e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 112.16 E-value: 3.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIShksthyvasggIAQAPEGRRI------- 91
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-----------TNLPPRERRVgfvfqhy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 92 --FPDMTVEENLlmgtipigsQFAAEDMqtmfdlfPRLKERRKQRAMTM-----------------SGGEQQMLAIARAL 152
Cdd:COG1118 85 alFPHMTVAENI---------AFGLRVR-------PPSKAEIRARVEELlelvqlegladrypsqlSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 153 MSRPKLLLLDEPsLG-----LAPIVVKQIFQTLSELArsGMTIF----LVEqnahhALKLSDRGYVMVNGQIRLSGSGEE 223
Cdd:COG1118 149 AVEPEVLLLDEP-FGaldakVRKELRRWLRRLHDELG--GTTVFvthdQEE-----ALELADRVVVMNQGRIEQVGTPDE 220
|
..
gi 2792998456 224 LL 225
Cdd:COG1118 221 VY 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-228 |
5.75e-29 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 108.93 E-value: 5.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQ-ALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIS-------HKSTHYV 77
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqdpvelRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 78 asggIAQAPegrrIFPDMTVEENLlmGTIPigsqfaaedmqtmfDLFPRLKERRKQRAM-------------------TM 138
Cdd:cd03295 81 ----IQQIG----LFPHMTVEENI--ALVP--------------KLLKWPKEKIRERADellalvgldpaefadryphEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 139 SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELAR-SGMTIFLVEQNAHHALKLSDRGYVMVNGQIRL 217
Cdd:cd03295 137 SGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQeLGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQ 216
|
250
....*....|.
gi 2792998456 218 SGSGEELLGNQ 228
Cdd:cd03295 217 VGTPDEILRSP 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-225 |
1.56e-28 |
|
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: 106.84 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQP--RIRNGQILFSGEDIShksthyvasggiaqapegrrifpDMTVE 98
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDIT-----------------------DLPPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 99 ENLLMGtIPIGSQFAAEdmqtmfdlFPRLKERRKQRAMTM--SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQI 176
Cdd:cd03217 73 ERARLG-IFLAFQYPPE--------IPGVKNADFLRYVNEgfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2792998456 177 FQTLSELARSGMTIFLVeqnAHHA--LKL--SDRGYVMVNGQIRLSGSGEELL 225
Cdd:cd03217 144 AEVINKLREEGKSVLII---THYQrlLDYikPDRVHVLYDGRIVKSGDKELAL 193
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
15-224 |
1.84e-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: 107.81 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAQApegRRIFPD 94
Cdd:cd03296 12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH---YALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 MTVEENLLMG--TIPIGSQFAAEDMQ----TMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:cd03296 89 MTVFDNVAFGlrVKPRSERPPEAEIRakvhELLKLV-QLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 169 APIVVKQIFQTLSELA-RSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:cd03296 168 DAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-205 |
1.85e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 106.79 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 4 PLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS-GGI 82
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRlAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 83 AQAPEgrrIFPDMTVEENLLMGTIPIGSQFAAEDMQTMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:COG4133 81 GHADG---LKPELTVRENLRFWAALYGLRADREAIDEALEAV-GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2792998456 163 EPSLGLAPIVVKQIFQTLSELARSGMTIFLVeqnAHHALKLSD 205
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLARGGAVLLT---THQPLELAA 196
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-225 |
3.18e-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: 107.04 E-value: 3.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHyvaSGGIAQAPEGRRIFPDMTVEEN 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---KRDISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 101 LLMGTIPIG---SQFAAEDMQTMFDLFPRLKERRKQRamTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIF 177
Cdd:cd03299 92 IAYGLKKRKvdkKEIERKVLEIAEMLGIDHLLNRKPE--TLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2792998456 178 QTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:cd03299 170 EELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
16-219 |
4.39e-28 |
|
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: 106.30 E-value: 4.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 16 GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHyvASGGIAQAPEGRRIFPDM 95
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE--ARRRLGFVSDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 96 TVEENL-----LMGTIPIGSQFAAEDMQTMFDLfprlKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAP 170
Cdd:cd03266 94 TARENLeyfagLYGLKGDELTARLEELADRLGM----EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2792998456 171 IVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSG 219
Cdd:cd03266 170 MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-236 |
6.62e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.99 E-value: 6.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 25 SLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHksthyvasggiaQAPEGRRI---------FPDM 95
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA------------LPPAERPVsmlfqennlFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 96 TVEENLLMGTIPiGSQFAAEDMQTMFDLFPRL----KERRKQRAmtMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:COG3840 87 TVAQNIGLGLRP-GLKLTAEQRAQVEQALERVglagLLDRLPGQ--LSGGQRQRVALARCLVRKRPILLLDEPFSALDPA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2792998456 172 VVKQIFQTLSELARS-GMTIFLVeqnAHH---ALKLSDRGYVMVNGQIRLSGSGEELLG--NQEVRKAYLG 236
Cdd:COG3840 164 LRQEMLDLVDELCRErGLTVLMV---THDpedAARIADRVLLVADGRIAADGPTAALLDgePPPALAAYLG 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-231 |
1.13e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.38 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 4 PLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHyvasggia 83
Cdd:PRK11607 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 84 QAP-----EGRRIFPDMTVEENLLMG----TIPIGSqfAAEDMQTMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMS 154
Cdd:PRK11607 90 QRPinmmfQSYALFPHMTVEQNIAFGlkqdKLPKAE--IASRVNEMLGLV-HMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 155 RPKLLLLDEPSLGLAPIVVKQI-FQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEVR 231
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-215 |
1.20e-27 |
|
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: 104.65 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 14 FYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKsTHYVASGGIAQAPeGRRIFP 93
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK-ERRKSIGYVMQDV-DYQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DmTVEENLLMGT--IPIGSQFAAEDMQTMfDLFpRLKERRKQramTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:cd03226 87 D-SVREELLLGLkeLDAGNEQAETVLKDL-DLY-ALKERHPL---SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2792998456 172 VVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-214 |
1.62e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 109.35 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTlLMSI-FG--QPriRNGQILFSGEDISHKSTHYV 77
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKST-LMKIlYGlyQP--DSGEILIDGKPVRIRSPRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 78 ASGGIA---QAPegrRIFPDMTVEENLLMGTIPIGSqfaaedmqtmfdLFPRLKERRKQ----------------RAMTM 138
Cdd:COG3845 78 IALGIGmvhQHF---MLVPNLTVAENIVLGLEPTKG------------GRLDRKAARARirelserygldvdpdaKVEDL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 139 SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVeqnAHH---ALKLSDRGYVMVNGQ 214
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFI---THKlreVMAIADRVTVLRRGK 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-228 |
2.36e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 106.43 E-value: 2.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASG 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 GIAqaPEGRRIFPDMTVEENLLMGTIPIG--SQFAAEDMQTMFDlFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKL 158
Cdd:PRK13537 83 GVV--PQFDNLDPDFTVRENLLVFGRYFGlsAAAARALVPPLLE-FAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 159 LLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQ 228
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-227 |
7.48e-27 |
|
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: 105.14 E-value: 7.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 5 LLAFREVDVFY----GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFG---QPRIRNGQILFSGEDISHKSthyv 77
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKLS---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 78 asggiaqaPEGRR---------IFPD-MTVeenlLMGTIPIGSQFaAEDMQTMFDLfprLKERRKQRAMTM--------- 138
Cdd:COG0444 77 --------EKELRkirgreiqmIFQDpMTS----LNPVMTVGDQI-AEPLRIHGGL---SKAEARERAIELlervglpdp 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 139 -----------SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVeqnAHH---ALKL 203
Cdd:COG0444 141 errldryphelSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFI---THDlgvVAEI 217
|
250 260
....*....|....*....|....
gi 2792998456 204 SDRGYVMVNGQIRLSGSGEELLGN 227
Cdd:COG0444 218 ADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-219 |
9.55e-27 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 102.37 E-value: 9.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 23 QVSLEVNkGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGedishksTHYVASG-GIAQAPEGRRI---------F 92
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG-------TVLFDSRkKINLPPQQRKIglvfqqyalF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 PDMTVEENLLMGTIPIGS---QFAAEDMQTMFDLFPrLKERRKQramTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:cd03297 88 PHLNVRENLAFGLKRKRNredRISVDELLDLLGLDH-LLNRYPA---QLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2792998456 170 PIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSG 219
Cdd:cd03297 164 RALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-215 |
1.18e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.03 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 3 EPLLAFREVDVF--YGVIqALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASG 80
Cdd:COG3845 255 EVVLEVENLSVRddRGVP-ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 GIAQAPEGRR---IFPDMTVEENLLMGTI---PIGSQF---------AAEDMQTMFDLFPRlkeRRKQRAMTMSGGEQQM 145
Cdd:COG3845 334 GVAYIPEDRLgrgLVPDMSVAENLILGRYrrpPFSRGGfldrkairaFAEELIEEFDVRTP---GPDTPARSLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-215 |
1.23e-26 |
|
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: 102.51 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFY----GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHY 76
Cdd:COG4181 4 SSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 77 VAsggiaqAPEGRRI------F---PDMTVEENLLMgtiPIGSQFAAEDMQTMFDLFPR--LKERRKQRAMTMSGGEQQM 145
Cdd:COG4181 84 RA------RLRARHVgfvfqsFqllPTLTALENVML---PLELAGRRDARARARALLERvgLGHRLDHYPAQLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792998456 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELAR-SGMTIFLVEqnahHALKL---SDRGYVMVNGQI 215
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVT----HDPALaarCDRVLRLRAGRL 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-219 |
2.01e-26 |
|
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: 101.80 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 25 SLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSthyVASGGIAQAPEGRRIFPDMTVEENLLMG 104
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP---PADRPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 105 TIPiGSQFAAEDMQTMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSE 182
Cdd:cd03298 95 LSP-GLKLTAEDRQAIEVALARvgLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 2792998456 183 L-ARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSG 219
Cdd:cd03298 174 LhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-206 |
4.31e-26 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 101.43 E-value: 4.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFY--GVIQA--LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHY 76
Cdd:PRK11629 1 MNKILLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 77 VAS------GGIAQApegRRIFPDMTVEENLLMGTIpIGSQFAAEDMQTMFDLFPR--LKERRKQRAMTMSGGEQQMLAI 148
Cdd:PRK11629 81 KAElrnqklGFIYQF---HHLLPDFTALENVAMPLL-IGKKKPAEINSRALEMLAAvgLEHRANHRPSELSGGERQRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVeqnAHHALKLSDR 206
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLV---VTHDLQLAKR 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-224 |
1.27e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 103.98 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 4 PLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIA 83
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 84 QAPEGRRIFPDMTVEENLLMGTipigsQFAAEDMQTMFDLfprLKERRKQRAMTMSGG-----EQQMLAIARALMSRPKL 158
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGL-----PKRQASMQKMKQL---LAALGCQLDLDSSAGslevaDRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 159 LLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
21-234 |
3.41e-25 |
|
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: 99.26 E-value: 3.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQP--RIRNGQILFSGEDISHKSTHYVASGGI---AQAPEGrriFPDM 95
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPsyEVTSGTILFKGQDLLELEPDERARAGLflaFQYPEE---IPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 96 TVEEnLLMGTIPIGSQFAAEDMQTMFDLFPRLKERRKQRAMT-----------MSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:TIGR01978 93 SNLE-FLRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDeeflnrsvnegFSGGEKKRNEILQMALLEPKLAILDEI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792998456 165 SLGLAPIVVKQIFQTLSELARSGMTIFLVeqnAHHA--LKL--SDRGYVMVNGQIRLSGSGEelLGNQEVRKAY 234
Cdd:TIGR01978 172 DSGLDIDALKIVAEGINRLREPDRSFLII---THYQrlLNYikPDYVHVLLDGRIVKSGDVE--LAKELEAKGY 240
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-219 |
4.63e-25 |
|
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: 97.00 E-value: 4.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKS---THYVASggIAQAPegrRIFpDM 95
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEkalSSLISV--LNQRP---YLF-DT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 96 TVEENLlmgtipiGSQFaaedmqtmfdlfprlkerrkqramtmSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQ 175
Cdd:cd03247 90 TLRNNL-------GRRF--------------------------SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2792998456 176 IFQTLSELARsGMTIFLVeqnAHH--ALKLSDRGYVMVNGQIRLSG 219
Cdd:cd03247 137 LLSLIFEVLK-DKTLIWI---THHltGIEHMDKILFLENGKIIMQG 178
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-234 |
5.64e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.46 E-value: 5.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 4 PLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHyVASGGIA 83
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR-AASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 84 QAPEGRRIFPDMTVEENLLMGTIPIGSQFAAEDmqtmfdlfpRLKERRKQRAM--------------TMSGGEQQMLAIA 149
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWT---------ETDRAAVERAMertgvaqfadrpvtSLSGGERQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 150 RALMSRPKLLLLDEPSlglAPIVVKQIFQTLsELARSgmtifLVEQN-----AHHALKLSDRgY-----VMVNGQIRLSG 219
Cdd:PRK09536 152 RALAQATPVLLLDEPT---ASLDINHQVRTL-ELVRR-----LVDDGktavaAIHDLDLAAR-YcdelvLLADGRVRAAG 221
|
250
....*....|....*
gi 2792998456 220 SGEELLGNQEVRKAY 234
Cdd:PRK09536 222 PPADVLTADTLRAAF 236
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-222 |
7.95e-25 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 102.00 E-value: 7.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAQAPEGRR---IFPDMTV 97
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 98 EENLLMGTIPIGSQFA-----AEDMQTMFD---LFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PRK10762 348 KENMSLTALRYFSRAGgslkhADEQQAVSDfirLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2792998456 170 PIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIrlsgSGE 222
Cdd:PRK10762 428 VGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI----SGE 476
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-206 |
9.69e-25 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 97.09 E-value: 9.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 8 FREVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISH---KSTHYVASGgIA 83
Cdd:cd03292 3 FINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgRAIPYLRRK-IG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 84 QAPEGRRIFPDMTVEEN--LLMGTIPIGSQFAAEDMQTMFDLFPrLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLL 161
Cdd:cd03292 82 VVFQDFRLLPDRNVYENvaFALEVTGVPPREIRKRVPAALELVG-LSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2792998456 162 DEPSLGLAPIVVKQIFQTLSELARSGMTIFLveqnAHHALKLSDR 206
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVV----ATHAKELVDT 201
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-225 |
1.07e-24 |
|
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: 97.69 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGgIAQAPEGRRIFPDmTVE 98
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA-IGVVPQDTVLFND-TIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 99 ENLLMGTIPIGSQ--FAAEDMQTMFDLFPRLKERRK----QRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIV 172
Cdd:cd03253 93 YNIRYGRPDATDEevIEAAKAAQIHDKIMRFPDGYDtivgERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2792998456 173 VKQIFQTLSELARSGMTIFLveqnAH--HALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:cd03253 173 EREIQAALRDVSKGRTTIVI----AHrlSTIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-224 |
1.12e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 99.76 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKsthyvasggiaqA 85
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL------------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 86 PEGRRI---------FPDMTVEEN----LLMGTIPigsqfAAE------DMQTMFDLFPRLKERRKQramtMSGGEQQML 146
Cdd:COG3839 72 PKDRNIamvfqsyalYPHMTVYENiafpLKLRKVP-----KAEidrrvrEAAELLGLEDLLDRKPKQ----LSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 147 AIARALMSRPKLLLLDEPslgLAPIVVK---QIFQTLSEL-ARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGE 222
Cdd:COG3839 143 ALGRALVREPKVFLLDEP---LSNLDAKlrvEMRAEIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPE 219
|
..
gi 2792998456 223 EL 224
Cdd:COG3839 220 EL 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
15-216 |
1.12e-24 |
|
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: 96.94 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKsthYVASGGIAQAPEGRRIFPD 94
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL---PPKDRDIAMVFQNYALYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 MTVEENLLMG---------TIPIGSQFAAEDMQ--TMFDLFPRlkerrkqramTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:cd03301 87 MTVYDNIAFGlklrkvpkdEIDERVREVAELLQieHLLDRKPK----------QLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 164 PslgLAPIVVKQIFQTLSEL----ARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIR 216
Cdd:cd03301 157 P---LSNLDAKLRVQMRAELkrlqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-230 |
1.33e-24 |
|
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: 97.61 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 18 IQALKQVSLEVNKGETVALIGANGAGKSTLLMSI--FGQPRirNGQILFSGEDISHKSTHYVAS--GGIAQAPEgrrIFp 93
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerFYDPT--SGEILLDGVDIRDLNLRWLRSqiGLVSQEPV---LF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DMTVEENLLMGtipIGSQFAAEDMQ---------TMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:cd03249 90 DGTIAENIRYG---KPDATDEEVEEaakkanihdFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 165 SLGLAPIVVKQIFQTLsELARSGMTIFLVeqnAH--HALKLSDRGYVMVNGQIRLSGSGEELLGNQEV 230
Cdd:cd03249 167 TSALDAESEKLVQEAL-DRAMKGRTTIVI---AHrlSTIRNADLIAVLQNGQVVEQGTHDELMAQKGV 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-225 |
1.57e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 101.39 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS--GGI 82
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRqiGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 83 AQAPEgrrIFpDMTVEENLLMGTIPIGSQ---FAAEDMQ--TMFDLFP-----RLKERrkqrAMTMSGGEQQMLAIARAL 152
Cdd:COG1132 420 PQDTF---LF-SGTIRENIRYGRPDATDEeveEAAKAAQahEFIEALPdgydtVVGER----GVNLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2792998456 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARsGMTIFLVeqnAH--HALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:COG1132 492 LKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVI---AHrlSTIRNADRILVLDDGRIVEQGTHEELL 562
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-226 |
2.29e-24 |
|
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: 99.03 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 24 VSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEdishksTHYVASGGIAQAPEGRRI---------FPD 94
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR------TLFDSRKGIFLPPEKRRIgyvfqearlFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 MTVEENLLMG---TIPIGSQFAAEDMQTMFDLFPrLKERRKQRamtMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:TIGR02142 90 LSVRGNLRYGmkrARPSERRISFERVIELLGIGH-LLGRLPGR---LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 172 VVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLG 226
Cdd:TIGR02142 166 RKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-234 |
3.31e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 96.72 E-value: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 9 REVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVA--------SG 80
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELArrravlpqHS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 GIAqapegrriFPdMTVEENLLMGTIPIGSQFAAED------MQTMfDLfPRLKERRKQramTMSGGEQQMLAIARAL-- 152
Cdd:COG4559 85 SLA--------FP-FTVEEVVALGRAPHGSSAAQDRqivreaLALV-GL-AHLAGRSYQ---TLSGGEQQRVQLARVLaq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 153 -----MSRPKLLLLDEP--SLGLAPivVKQIFQTLSELARSGMTIFLVeqnaHHALKL----SDRGYVMVNGQIRLSGSG 221
Cdd:COG4559 151 lwepvDGGPRWLFLDEPtsALDLAH--QHAVLRLARQLARRGGGVVAV----LHDLNLaaqyADRILLLHQGRLVAQGTP 224
|
250
....*....|...
gi 2792998456 222 EELLGNQEVRKAY 234
Cdd:COG4559 225 EEVLTDELLERVY 237
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-229 |
4.74e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.04 E-value: 4.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYV----ASGGIAQAPEgRRIFPDm 95
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdirkKVGLVFQYPE-YQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 96 TVEENLLMGTIPIGsqfaAEDMQTmfdlfprlkERRKQRAMTM----------------SGGEQQMLAIARALMSRPKLL 159
Cdd:PRK13637 100 TIEKDIAFGPINLG----LSEEEI---------ENRVKRAMNIvgldyedykdkspfelSGGQKRRVAIAGVVAMEPKIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2792998456 160 LLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQE 229
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVE 237
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-225 |
6.11e-24 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 95.37 E-value: 6.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 8 FREVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIsHKSTHYVASGGIAQAP 86
Cdd:cd03254 5 FENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI-RDISRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 87 EGRRIFPDmTVEENLLMGT-IPIGSQFAAEDMQTMFDLFPR-----LKERRKQRAMTMSGGEQQMLAIARALMSRPKLLL 160
Cdd:cd03254 84 QDTFLFSG-TIMENIRLGRpNATDEEVIEAAKEAGAHDFIMklpngYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 161 LDEPSLGLAPIVVKQIFQTLSELaRSGMTIFLVeqnAHH--ALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKL-MKGRTSIII---AHRlsTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-225 |
8.11e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 95.52 E-value: 8.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQP--RIRNGQILFSGEDISHKSTHYVASGGIA---QAPEgrRIfPDM 95
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERARAGIFlafQYPV--EI-PGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 96 TVEeNLLMgtIPIGSQfaAEDMQTMFDLFPRLKERRKQRAMTM-----------SGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:COG0396 93 SVS-NFLR--TALNAR--RGEELSAREFLKLLKEKMKELGLDEdfldryvnegfSGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2792998456 165 SLGLAPIVVKQIFQTLSELARSGMTIFLVeqnAHHA--LKL--SDRGYVMVNGQIRLSGsGEELL 225
Cdd:COG0396 168 DSGLDIDALRIVAEGVNKLRSPDRGILII---THYQriLDYikPDFVHVLVDGRIVKSG-GKELA 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-166 |
1.41e-23 |
|
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: 94.42 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 17 VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILfsgedishksthyVASGG----IAQAPEgRRIF 92
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL-------------VRHDGgwvdLAQASP-REIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 pdmtveeNLLMGTIPIGSQF-------AAED--MQTMFDL-FPRLKERRKQRAM----------------TMSGGEQQML 146
Cdd:COG4778 89 -------ALRRRTIGYVSQFlrviprvSALDvvAEPLLERgVDREEARARARELlarlnlperlwdlppaTFSGGEQQRV 161
|
170 180
....*....|....*....|..
gi 2792998456 147 AIARALMSRPKLLLLDEP--SL 166
Cdd:COG4778 162 NIARGFIADPPLLLLDEPtaSL 183
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-205 |
2.99e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 94.33 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 4 PLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIF------GQPRIRnGQILFSGEDISHKSTHY- 76
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVRVE-GRVEFFNQNIYERRVNLn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 77 VASGGIAQAPEGRRIFPdMTVEENLLMGTIPIGSQFA------AEDMQTMFDLFPRLKERRKQRAMTMSGGEQQMLAIAR 150
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKleiddiVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELA-RSGMTIFLVEQNAHHALKLSD 205
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSD 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
16-227 |
3.19e-23 |
|
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: 93.80 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 16 GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSthyvasgGIAQAPEGRRI---- 91
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLS-------GKELRKARRRIgmif 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 92 -----FPDMTVEENLlmgTIP--IGSQFAAEDMQTMFDL--FPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:cd03258 89 qhfnlLSSRTVFENV---ALPleIAGVPKAEIEERVLELleLVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 163 EPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGN 227
Cdd:cd03258 166 EATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-231 |
3.85e-23 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 95.94 E-value: 3.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 23 QVSLEVNKGETVALIGANGAGKSTLLMSIFG--QP---RIR-NGQILFSGEdishksthyvasGGIAQAPEGRRI----- 91
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGleRPdsgRIRlGGEVLQDSA------------RGIFLPPHRRRIgyvfq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 92 ----FPDMTVEENLLMG---TIPIGSQFAAEDMQTMFDLFPRLKerrkQRAMTMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:COG4148 85 earlFPHLSVRGNLLYGrkrAPRAERRISFDEVVELLGIGHLLD----RRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2792998456 165 --SLGLApivVKQ-IFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEVR 231
Cdd:COG4148 161 laALDLA---RKAeILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLL 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-205 |
3.97e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.08 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 3 EPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLmSIFGQ-----PRIR-NGQILFSGEDISHKSTHY 76
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTIL-RCFNRlndliPGFRvEGKVTFHGKNLYAPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 77 VAS----GGIAQAPEGrriFPDmTVEENLLMGTIPIGSQfaaEDMQTMFD-------LFPRLKERRKQRAMTMSGGEQQM 145
Cdd:PRK14243 87 VEVrrriGMVFQKPNP---FPK-SIYDNIAYGARINGYK---GDMDELVErslrqaaLWDEVKDKLKQSGLSLSGGQQQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSgMTIFLVEQNAHHALKLSD 205
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-219 |
4.30e-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: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETvALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASggIAQA 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR--IGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 86 PEGRRIFPDMTVEENL----LMGTIPiGSQFAAEDMQTMFDLfpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLL 161
Cdd:cd03264 78 PQEFGVYPNFTVREFLdyiaWLKGIP-SKEVKARVDEVLELV--NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792998456 162 DEPSLGLAP---IVVKQIfqtLSELARSGMTIF---LVEQNAHHALKLSdrgyVMVNGQIRLSG 219
Cdd:cd03264 155 DEPTAGLDPeerIRFRNL---LSELGEDRIVILsthIVEDVESLCNQVA----VLNKGKLVFEG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-234 |
8.36e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.91 E-value: 8.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 4 PLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASggia 83
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 84 qapegRR---------IFPdMTVEENLLMGTIPiGSQFAAEDMQTMFDLFPR-----LKERRKQramTMSGGEQQMLAIA 149
Cdd:PRK13548 77 -----RRavlpqhsslSFP-FTVEEVVAMGRAP-HGLSRAEDDALVAAALAQvdlahLAGRDYP---QLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 150 RALM------SRPKLLLLDEP--SLGLApivvKQifQTLSELARSgmtiFLVEQNAH-----HALKL----SDRGYVMVN 212
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPtsALDLA----HQ--HHVLRLARQ----LAHERGLAvivvlHDLNLaaryADRIVLLHQ 216
|
250 260
....*....|....*....|..
gi 2792998456 213 GQIRLSGSGEELLGNQEVRKAY 234
Cdd:PRK13548 217 GRLVADGTPAEVLTPETLRRVY 238
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
15-228 |
1.11e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 94.51 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSThyVASGGIAQAPEGRRIFPD 94
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR--LARARIGVVPQFDNLDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 MTVEENLLMgtipIGSQF--AAEDMQTMFDL---FPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PRK13536 129 FTVRENLLV----FGRYFgmSTREIEAVIPSlleFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 170 PIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQ 228
Cdd:PRK13536 205 PHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
19-231 |
1.79e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 92.12 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSI--FGQP---RIRNGQILF-SGEDISHKSTHYVA----SGGIAQapeG 88
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlLEQPeagTIRVGDITIdTARSLSQQKGLIRQlrqhVGFVFQ---N 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 89 RRIFPDMTVEENLLMGTIPIGSQFAAEDMQTMFDLFPRLKERRKQRAMT--MSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:PRK11264 94 FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPrrLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 167 GLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGN-QEVR 231
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADpQQPR 239
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-226 |
2.10e-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: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYG--VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIfgqPR---IRNGQILFSGEDISHKSTHYVASg 80
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI---PRfydVDSGRILIDGHDVRDYTLASLRR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 GIAQAPEGRRIFPDmTVEENLLMGTIPIGSQ---FAAEDMQTMfDLFPRLKE----RRKQRAMTMSGGEQQMLAIARALM 153
Cdd:cd03251 77 QIGLVSQDVFLFND-TVAENIAYGRPGATREeveEAARAANAH-EFIMELPEgydtVIGERGVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2792998456 154 SRPKLLLLDEPSLGLAPIVVKQIFQTLSELARsGMTIFLVeqnAHH--ALKLSDRGYVMVNGQIRLSGSGEELLG 226
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVI---AHRlsTIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-224 |
2.36e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.17 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 14 FYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS--GGIAQAPEGRRI 91
Cdd:PRK13652 13 YSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKfvGLVFQNPDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 92 FPdmTVEENLLMGTIPIG--SQFAAEDMQTMFDLFPrLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PRK13652 93 SP--TVEQDIAFGPINLGldEETVAHRVSSALHMLG-LEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 170 PIVVKQIFQTLSELA-RSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:PRK13652 170 PQGVKELIDFLNDLPeTYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-227 |
2.50e-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: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYG----VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFG----QPRIRNGQILFSGEDISHk 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRllpdPAAHPSGSILFDGQDLLG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 73 sthyvasggiaqAPE-------GRRI---F--------PDMTVE----ENLLMGTiPIGSQFAAEDMQTMFDL--FPRLK 128
Cdd:COG4172 81 ------------LSErelrrirGNRIamiFqepmtslnPLHTIGkqiaEVLRLHR-GLSGAAARARALELLERvgIPDPE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 129 ERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSEL-ARSGMTIFLVEqnahHAL----KL 203
Cdd:COG4172 148 RRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLIT----HDLgvvrRF 223
|
250 260
....*....|....*....|....
gi 2792998456 204 SDRGYVMVNGQIRLSGSGEELLGN 227
Cdd:COG4172 224 ADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-189 |
2.52e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 94.61 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTlLMSI------FGQpriRNGQILFSGEDISHKST 74
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKST-LMKVlsgvypHGT---YEGEIIFEGEELQASNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 75 HYVASGGIAQAPEGRRIFPDMTVEENLLMGTIPigSQFAAEDMQTMFDLFPRLKERRK------QRAMTMSGGEQQMLAI 148
Cdd:PRK13549 77 RDTERAGIAIIHQELALVKELSVLENIFLGNEI--TPGGIMDYDAMYLRAQKLLAQLKldinpaTPVGNLGLGQQQLVEI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2792998456 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMT 189
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIA 195
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-236 |
4.15e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.59 E-value: 4.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS---GGIAQAPEGRriFPDMT 96
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRklvGIVFQNPETQ--FVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 97 VEENLLMGtiPIGSQFAAEDMQTMFDLF---PRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVV 173
Cdd:PRK13644 95 VEEDLAFG--PENLCLPPIEIRKRVDRAlaeIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2792998456 174 KQIFQTLSELARSGMTIFLVEQNAHHaLKLSDRGYVMVNGQIRLSGSGEELLGNQEVRkaYLG 236
Cdd:PRK13644 173 IAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ--TLG 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-220 |
4.27e-22 |
|
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: 90.25 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 8 FREVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS--GGIA 83
Cdd:cd03244 5 FKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSriSIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 84 QAPEgrrIFPDmTVEENLlmgtIPIGSQFAAEDMQTMFDLfpRLKERRKQRAMTM-----------SGGEQQMLAIARAL 152
Cdd:cd03244 85 QDPV---LFSG-TIRSNL----DPFGEYSDEELWQALERV--GLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLSElARSGMTIFLVeqnAH--HALKLSDRGYVMVNGQIRLSGS 220
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTI---AHrlDTIIDSDRILVLDKGRVVEFDS 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-215 |
5.15e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.82 E-value: 5.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 24 VSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAQAPEGRR---IFPDMTVEEN 100
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 101 LLMG----TIPIG--------SQFAAEDMQTMfdlfpRLKER-RKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PRK11288 352 INISarrhHLRAGclinnrweAENADRFIRSL-----NIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2792998456 168 LAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:PRK11288 427 IDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
15-196 |
5.28e-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: 89.98 E-value: 5.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSThyvasggiAQAPEGRR---- 90
Cdd:TIGR03608 8 FGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNS--------KKASKFRReklg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 91 -IFPDM------TVEENLLMGTIpiGSQFAAEDMQTM-------FDLFPRLKerrkQRAMTMSGGEQQMLAIARALMSRP 156
Cdd:TIGR03608 80 yLFQNFalieneTVEENLDLGLK--YKKLSKKEKREKkkealekVGLNLKLK----QKIYELSGGEQQRVALARAILKPP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2792998456 157 KLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQN 196
Cdd:TIGR03608 154 PLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHD 193
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-224 |
5.78e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.45 E-value: 5.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 14 FYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAQApegRRIFP 93
Cdd:PRK10851 11 SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH---YALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DMTVEENLLMG-TI------PIGSQFAAEDMQ--TMFDLfPRLKERRKQRamtMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:PRK10851 88 HMTVFDNIAFGlTVlprrerPNAAAIKAKVTQllEMVQL-AHLADRYPAQ---LSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2792998456 165 SLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-236 |
6.50e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 90.03 E-value: 6.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 25 SLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDisHKSThyvasgGIAQAP-----EGRRIFPDMTVEE 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTT------PPSRRPvsmlfQENNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 100 NLLMGTIPiGSQFAAEDMQTM---------FDLFPRLKERrkqramtMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAP 170
Cdd:PRK10771 91 NIGLGLNP-GLKLNAAQREKLhaiarqmgiEDLLARLPGQ-------LSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 171 IVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEVRKAYLG 236
Cdd:PRK10771 163 ALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLG 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-216 |
6.98e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.46 E-value: 6.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 24 VSLEVNKGETVALIGANGAGKSTLLMSIFGQ-PRIRNGQILFSGEDISHKSTHYVASGGIAQAPEGRR---IFPDMTVEE 99
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKrdgIVPVMGVGK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 100 NLlmgTIPIGSQFA-------AEDMQTMFDLFPRLKERR---KQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PRK13549 361 NI---TLAALDRFTggsriddAAELKTILESIQRLKVKTaspELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2792998456 170 PIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIR 216
Cdd:PRK13549 438 VGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-213 |
8.29e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.31 E-value: 8.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASG 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 GIAQAPEGRRIFPDMTVEENLLMGTIPIGSQFAA-----EDMQ---TMFDLFPRLKERRKQRAMTMSGGEQQMLAIARAL 152
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIGRHLTKKVCGVniidwREMRvraAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2792998456 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNG 213
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-213 |
9.40e-22 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 89.83 E-value: 9.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIShksthyvasggiAQAPEGRRIF------PD 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT------------EPGPDRMVVFqnysllPW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 MTVEENLLMGTIPIGSQFAAEDMQTMFD---LFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:TIGR01184 69 LTVRENIALAVDRVLPDLSKSERRAIVEehiALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2792998456 172 VVKQIFQTLSELAR-SGMTIFLVEQNAHHALKLSDRGYVMVNG 213
Cdd:TIGR01184 149 TRGNLQEELMQIWEeHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-227 |
1.12e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 90.03 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIS---------- 70
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 71 --HKSTHYVASGGIAQAPEGRRIFPDMTVEENLLMGTIPI---GSQFAAEDMQTMFDLFPRLKERRKQRAMTMSGGEQQM 145
Cdd:PRK10619 81 vaDKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVlglSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
..
gi 2792998456 226 GN 227
Cdd:PRK10619 241 GN 242
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-219 |
1.22e-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: 89.25 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGqpRIRN-----GQILFSGEDISHKSTHYVasggIAQAPEGRRIFP 93
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG--RVEGggttsGQILFNGQPRKPDQFQKC----VAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DMTVEENLL-MGTIPIGSQFAaEDMQTMFDLFPRLKER-----RKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:cd03234 95 GLTVRETLTyTAILRLPRKSS-DAIRKKRVEDVLLRDLaltriGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2792998456 168 LAPIVVKQIFQTLSELARSGMTIFL-VEQNAHHALKLSDRGYVMVNGQIRLSG 219
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-215 |
1.69e-21 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 88.80 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKStHYVASGGIA 83
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD-PADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 84 QAPEGRRIFPDmTVEENLLMGTIPIGSQ--FAAEDMQTMFDLFPR----LKERRKQRAMTMSGGEQQMLAIARALMSRPK 157
Cdd:cd03245 82 YVPQDVTLFYG-TLRDNITLGAPLADDEriLRAAELAGVTDFVNKhpngLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 158 LLLLDEPSLGLAPIVVKQIFQTLSELARsGMTIFLVeqnAHH--ALKLSDRGYVMVNGQI 215
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIII---THRpsLLDLVDRIIVMDSGRI 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-237 |
1.76e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.59 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLL------MSIFGQPRIRnGQILFSGEDISHKSTHYVAS 79
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrlIELYPEARVS-GEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 80 --GGIAQAPEGrriFPDMTVEENLLMG-----------TIPIGSQFAAEDMQtmfdLFPRLKERRKQRAMTMSGGEQQML 146
Cdd:PRK14247 83 rvQMVFQIPNP---IPNLSIFENVALGlklnrlvkskkELQERVRWALEKAQ----LWDEVKDRLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 147 AIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSgMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLG 226
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
250
....*....|...
gi 2792998456 227 N--QEVRKAYLGG 237
Cdd:PRK14247 235 NprHELTEKYVTG 247
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-214 |
1.96e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 92.28 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 3 EPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGI 82
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 83 AQAPEGRRIFPDMTVEENLLMGTIP--IGS-------QFAAEDMQTM-FDLFPRLKERRkqramtMSGGEQQMLAIARAL 152
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLGQLPhkGGIvnrrllnYEAREQLEHLgVDIDPDTPLKY------LSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2792998456 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQ 214
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-219 |
4.12e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.01 E-value: 4.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 5 LLAFREVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVA--SGG 81
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 82 IAQAPEGRRIFPDMTVEENLLMGTIPIGSqfAAEDMQ----TMFDLFPRLkERRKQRAMTMSGGEQQMLAIARALMSRPK 157
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGA--SGDDIRrrvsAALDKVGLL-DKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2792998456 158 LLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVeqnAHHALKLSDRGY-VMVNGQIRLSG 219
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMA---THDIGLISRRSYrMLTLSDGHLHG 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-228 |
4.60e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 91.27 E-value: 4.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 22 KQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAQAPEGRR---IFPDMTVE 98
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQssgLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 99 EN---LLMGTIPIGSQFAAEdmQTMFDLFPR---LK-ERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:PRK15439 360 WNvcaLTHNRRGFWIKPARE--NAVLERYRRalnIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 172 VVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIrlsgsGEELLGNQ 228
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI-----SGALTGAA 489
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-231 |
5.36e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.93 E-value: 5.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVN-----KGETvALIGANGAGKSTLLMSIFG-----QPRIR-NGQILFSGEdishksthyvasGGIAQAPE 87
Cdd:PRK11144 8 QQLGDLCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGltrpqKGRIVlNGRVLFDAE------------KGICLPPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 88 GRRI---------FPDMTVEENLLMGTipigsqfaAEDMQTMFD----------LFPRLkerrkqrAMTMSGGEQQMLAI 148
Cdd:PRK11144 75 KRRIgyvfqdarlFPHYKVRGNLRYGM--------AKSMVAQFDkivallgiepLLDRY-------PGSLSGGEKQRVAI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 149 ARALMSRPKLLLLDEP--SLGLAPivVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:PRK11144 140 GRALLTAPELLLMDEPlaSLDLPR--KRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVW 217
|
....*.
gi 2792998456 226 GNQEVR 231
Cdd:PRK11144 218 ASSAMR 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-215 |
5.88e-21 |
|
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: 86.84 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQ--PRIRNGQILFSGEDISHKSTHYVasggIAQAPEGRRIFPDMTVE 98
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKI----IGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 99 ENLlmgtipigsQFAAEdmqtmfdlfprLKerrkqramTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQ 178
Cdd:cd03213 101 ETL---------MFAAK-----------LR--------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 2792998456 179 TLSELARSGMT-IFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03213 153 LLRRLADTGRTiICSIHQPSSEIFELFDKLLLLSQGRV 190
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-227 |
6.78e-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: 90.51 E-value: 6.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 3 EPLLAFREVDVFY-----------GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFG-QPRirNGQILFSGEDIS 70
Cdd:COG4172 273 PPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRlIPS--EGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 71 HKSTHyvasggiAQAPEGRRI---F--------PDMTVEEnllmgTIpigsqfaAEDMQTmfdLFPRLKER-RKQRAMTM 138
Cdd:COG4172 351 GLSRR-------ALRPLRRRMqvvFqdpfgslsPRMTVGQ-----II-------AEGLRV---HGPGLSAAeRRARVAEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 139 ------------------SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSEL-ARSGMT-IFLveqnaH 198
Cdd:COG4172 409 leevgldpaarhryphefSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAyLFI-----S 483
|
250 260 270
....*....|....*....|....*....|...
gi 2792998456 199 HALK----LSDRGYVMVNGQIRLSGSGEELLGN 227
Cdd:COG4172 484 HDLAvvraLAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-227 |
6.93e-21 |
|
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: 88.08 E-value: 6.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 16 GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDI---SHKSTHYVASGGIAQAPEGRRIF 92
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamSRKELRELRRKKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 PDMTVEENLLMGT----IP--IGSQFAAEDMQTMfdlfpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:cd03294 115 PHRTVLENVAFGLevqgVPraEREERAAEALELV-----GLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2792998456 167 GLAPIVVKQIFQTLSEL-ARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGN 227
Cdd:cd03294 190 ALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-224 |
8.22e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.15 E-value: 8.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLL----------------MSIFGQPRIRNGQIlfsGEDISHKSTHyvaSGGI 82
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsglitgdksagshIELLGRTVQREGRL---ARDIRKSRAN---TGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 83 AQApegRRIFPDMTVEENLLMGTIpiGSqfaAEDMQTMFDLFPRLKERRK--------------QRAMTMSGGEQQMLAI 148
Cdd:PRK09984 92 FQQ---FNLVNRLSVLENVLIGAL--GS---TPFWRTCFSWFTREQKQRAlqaltrvgmvhfahQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-214 |
9.73e-21 |
|
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: 86.37 E-value: 9.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGedishkSTHYVasggiAQAPegrRIFPDmTVEE 99
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------SIAYV-----SQEP---WIQNG-TIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 100 NLLMgtipiGSQFAAEDMQTM---------FDLFPRLKERR-KQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:cd03250 85 NILF-----GKPFDEERYEKVikacalepdLEILPDGDLTEiGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2792998456 170 PIVVKQIFQT-LSELARSGMTIFLVEQNAHHaLKLSDRGYVMVNGQ 214
Cdd:cd03250 160 AHVGRHIFENcILGLLLNNKTRILVTHQLQL-LPHADQIVVLDNGR 204
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-200 |
1.04e-20 |
|
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: 90.04 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHyVASGGIAQ 84
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD-SWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 85 APEGRRIFPDmTVEENLLMGTiPIGSQFAAEDMQTMFDLFPRLKERRK-------QRAMTMSGGEQQMLAIARALMSRPK 157
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLAR-PDASDAEIREALERAGLDEFVAALPQgldtpigEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2792998456 158 LLLLDEPSLGLAPIVVKQIFQTLSELARsGMTIFLVEQNAHHA 200
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALA 520
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-199 |
1.96e-20 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 89.34 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 3 EPLLAFREVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS-- 79
Cdd:TIGR02868 332 KPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRrv 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 80 GGIAQAPEgrrIFpDMTVEENLLMGTiPIGSQFAAEDMQTMFDLFPRLKERRK-------QRAMTMSGGEQQMLAIARAL 152
Cdd:TIGR02868 412 SVCAQDAH---LF-DTTVRENLRLAR-PDATDEELWAALERVGLADWLRALPDgldtvlgEGGARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2792998456 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLSElARSGMTIFLVeqnAHH 199
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLI---THH 529
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
2.85e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.83 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGV-IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGE--DISHKSTHYV 77
Cdd:PRK13636 1 MEDYILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 78 --ASGGIAQAPEgRRIFpDMTVEENLLMGtiPIGSQFAAEDMQTMFDlfpRLKER------RKQRAMTMSGGEQQMLAIA 149
Cdd:PRK13636 81 reSVGMVFQDPD-NQLF-SASVYQDVSFG--AVNLKLPEDEVRKRVD---NALKRtgiehlKDKPTHCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 150 RALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQ 228
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
....*...
gi 2792998456 229 EV-RKAYL 235
Cdd:PRK13636 234 EMlRKVNL 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-220 |
3.93e-20 |
|
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: 88.34 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 18 IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQ-PRIRNGQILFSGEDISHKSTHYVASGGIAQAPEGRR---IFP 93
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DMTVEENLLMGTIP----IGSQFAAEDMQTMFDLFPRLKERRKQRAM---TMSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:TIGR02633 353 ILGVGKNITLSVLKsfcfKMRIDAAAELQIIGSAIQRLKVKTASPFLpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2792998456 167 GLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRgyVMVNGQIRLSGS 220
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDR--VLVIGEGKLKGD 484
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-164 |
5.91e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.46 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQ--PRIR-NGQILFSGEDISHKsthyvasggi 82
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSaSGEVLLNGRRLTAL---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 83 aqAPEGRRI---------FPDMTVEENLLmgtipigsqfaaedmqtmFDLFPRL-KERRKQRAM---------------- 136
Cdd:COG4136 72 --PAEQRRIgilfqddllFPHLSVGENLA------------------FALPPTIgRAQRRARVEqaleeaglagfadrdp 131
|
170 180
....*....|....*....|....*....
gi 2792998456 137 -TMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:COG4136 132 aTLSGGQRARVALLRALLAEPRALLLDEP 160
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-228 |
6.39e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.96 E-value: 6.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 2 NEPLLAFREVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS 79
Cdd:PRK11160 335 DQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 80 GgIAQAPEGRRIFPDmTVEENLLMGtIPIGSQFAAEDMQTMFDLFPRLKERRKQRAMT------MSGGEQQMLAIARALM 153
Cdd:PRK11160 415 A-ISVVSQRVHLFSA-TLRDNLLLA-APNASDEALIEVLQQVGLEKLLEDDKGLNAWLgeggrqLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2792998456 154 SRPKLLLLDEPSLGLAPIVVKQIFQTLSELARsGMTIFLVEQNAhHALKLSDRGYVMVNGQIRLSGSGEELLGNQ 228
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELLAQQ 564
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-215 |
6.94e-20 |
|
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: 85.63 E-value: 6.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSthyvasggiaqaPEGRRIF------ 92
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD------------RKQRRAFrrdvql 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 ----------PDMTVEENL------LMGTIPIGSQFAAEDMQTMFDLFPRLKERRKQRamtMSGGEQQMLAIARALMSRP 156
Cdd:TIGR02769 93 vfqdspsavnPRMTVRQIIgeplrhLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ---LSGGQLQRINIARALAVKP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 157 KLLLLDEPSLGLAPIVVKQIFQTLSEL-ARSGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:TIGR02769 170 KLIVLDEAVSNLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-238 |
1.05e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 84.89 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 9 REVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSI-----FGQPRIRNGQILFSGEDISHKSTHYV----AS 79
Cdd:PRK14267 8 VNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIevrrEV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 80 GGIAQAPEGrriFPDMTVEENLLMGTIPIGSQFAAEDMQTMFD-------LFPRLKERRKQRAMTMSGGEQQMLAIARAL 152
Cdd:PRK14267 88 GMVFQYPNP---FPHLTIYDNVAIGVKLNGLVKSKKELDERVEwalkkaaLWDEVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 153 MSRPKLLLLDEPSLGLAPIVVKQIFQTLSELaRSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGN--QEV 230
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENpeHEL 243
|
....*...
gi 2792998456 231 RKAYLGGV 238
Cdd:PRK14267 244 TEKYVTGA 251
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-215 |
1.09e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.15 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 22 KQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAQAPEGRR---IFPDMTVE 98
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 99 ENllmgtIPIGSQFAAEDMQTMFDLFPRLKERR---KQRAM-------------TMSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:PRK09700 360 QN-----MAISRSLKDGGYKGAMGLFHEVDEQRtaeNQRELlalkchsvnqnitELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2792998456 163 EPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-163 |
1.19e-19 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 83.62 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS--GGIAQAPegrrifpdmt 96
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSslTIIPQDP---------- 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 97 veeNLLMGTIPigSQFAAEDMQTMFDLFPRLkeRRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:cd03369 92 ---TLFSGTIR--SNLDPFDEYSDEEIYGAL--RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-214 |
1.54e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 86.80 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 5 LLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFG-QPR-IRNGQILFSGEDISHKSTHYVASGGI 82
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvYPHgTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 83 AQAPEGRRIFPDMTVEENLLMG---TIPIGSQFAAEDMQTMFDLFPRLK---ERRKQRAMTMSGGEQQMLAIARALMSRP 156
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGneiTLPGGRMAYNAMYLRAKNLLRELQldaDNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 157 KLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQ 214
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-230 |
1.72e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.67 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVA----SGGIAQAPEGRRIFPD 94
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrqqVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 MTVE-----ENLLMGTIPIGSQfaAEDMQTMFDLfprlKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PRK13638 95 IDSDiafslRNLGVPEAEITRR--VDEALTLVDA----QHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2792998456 170 PIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEV 230
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-224 |
1.90e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 85.54 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSthyVASG 80
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS---IQQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 GIAQAPEGRRIFPDMTVEENLLMGTipigsqfaaeDMQTmfdlfpRLKERRKQR---AMTM--------------SGGEQ 143
Cdd:PRK11432 79 DICMVFQSYALFPHMSLGENVGYGL----------KMLG------VPKEERKQRvkeALELvdlagfedryvdqiSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 144 QMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSEL-ARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGE 222
Cdd:PRK11432 143 QRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQ 222
|
..
gi 2792998456 223 EL 224
Cdd:PRK11432 223 EL 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-238 |
2.14e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 84.05 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 23 QVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTH--YVASGGIAQAPEGRRIFPDMTVEEN 100
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 101 L-------------------LMGTIPIGSQFAAEDMQTmfdlfprlkerrkqramTMSGGEQQMLAIARALMSRPKLLLL 161
Cdd:PRK11831 105 VayplrehtqlpapllhstvMMKLEAVGLRGAAKLMPS-----------------ELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 162 DEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEVR-KAYLGGV 238
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRvRQFLDGI 246
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
21-164 |
2.20e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.27 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLmsifgqpRIRNGQI-LFSGEdISHKSTHYVASggIAQAPEgrrIFPDMTVEE 99
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLL-------KILAGELePDSGE-VSIPKGLRIGY--LPQEPP---LDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 100 NLLMGTIPIGS------------QFAAEDMQTMFDLFPRLK-------ERRKQRAM---------------TMSGGEQQM 145
Cdd:COG0488 81 TVLDGDAELRAleaeleeleaklAEPDEDLERLAELQEEFEalggweaEARAEEILsglgfpeedldrpvsELSGGWRRR 160
|
170
....*....|....*....
gi 2792998456 146 LAIARALMSRPKLLLLDEP 164
Cdd:COG0488 161 VALARALLSEPDLLLLDEP 179
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-229 |
2.52e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 84.75 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 17 VIQALKQVSLEVNKGETVALIGANGAGKSTLL--MSIFGQPRIRNGQILFSGEDISHKSTHY--VASGGIAQAPEGRRI- 91
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIehLNALLLPDTGTIEWIFKDEKNKKKTKEKekVLEKLVIQKTRFKKIk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 92 --------------FPDM-----TVEENLLMGTIPIG--SQFAAEDMQTMFDLFPRLKERRKQRAMTMSGGEQQMLAIAR 150
Cdd:PRK13651 99 kikeirrrvgvvfqFAEYqlfeqTIEKDIIFGPVSMGvsKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQE 229
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNK 257
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-214 |
3.44e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 2 NEPLLAFREVD-VFYGViQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASG 80
Cdd:PRK10762 1 MQALLQLKGIDkAFPGV-KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 GIAQAPEGRRIFPDMTVEENLLMGTIPIGSqFAAEDMQTMFD----LFPRLKERR--KQRAMTMSGGEQQMLAIARALMS 154
Cdd:PRK10762 80 GIGIIHQELNLIPQLTIAENIFLGREFVNR-FGRIDWKKMYAeadkLLARLNLRFssDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792998456 155 RPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEqnahHALK----LSDRGYVMVNGQ 214
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYIS----HRLKeifeICDDVTVFRDGQ 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-233 |
3.63e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.60 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 20 ALKQVSLEVNKGETVALIGANGAGKST-------LLMSIFGQPRIRNgqilFSGEDISHKSTHYVASGGIAQAPEGRRIf 92
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTiakhmnaLLIPSEGKVYVDG----LDTSDEENLWDIRNKAGMVFQNPDNQIV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 pDMTVEENLLMGTIPIGSQfaAEDMQTMFDlfPRLK-----ERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PRK13633 100 -ATIVEEDVAFGPENLGIP--PEEIRERVD--ESLKkvgmyEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 168 LAPIVVKQIFQTLSEL-ARSGMTIFLVEQNAHHALKlSDRGYVMVNGQIRLSGSGEELLGNQEVRKA 233
Cdd:PRK13633 175 LDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMMKK 240
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-164 |
7.35e-19 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 83.63 E-value: 7.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFY-----------GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDI 69
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 70 SHKSTHyvasggiAQAPEGRR---IF--------PDMTVEENLlmgtipigsqfaAE--DMQTMFDlfprlKERRKQRAM 136
Cdd:COG4608 83 TGLSGR-------ELRPLRRRmqmVFqdpyaslnPRMTVGDII------------AEplRIHGLAS-----KAERRERVA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2792998456 137 TM------------------SGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:COG4608 139 ELlelvglrpehadryphefSGGQRQRIGIARALALNPKLIVCDEP 184
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-232 |
8.81e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 85.03 E-value: 8.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQprirngqilfsgedISH-KSTHYVASGGIAQAPEGRRIFpDMTVEE 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGE--------------LSHaETSSVVIRGSVAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 100 NLLMGTIPIGSQFA----AEDMQTMFDLFP-RLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVK 174
Cdd:PLN03232 698 NILFGSDFESERYWraidVTALQHDLDLLPgRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 175 QIFQTLSELARSGMTIFLVeQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEVRK 232
Cdd:PLN03232 778 QVFDSCMKDELKGKTRVLV-TNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFK 834
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-214 |
1.53e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 84.01 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 14 FYGViQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAQAPEGRRIFP 93
Cdd:PRK10982 8 FPGV-KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DMTVEENLLMGTIPIGSQFAAE-----DMQTMF-----DLFPRLKerrkqrAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:PRK10982 87 QRSVMDNMWLGRYPTKGMFVDQdkmyrDTKAIFdeldiDIDPRAK------VATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2792998456 164 PSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQ 214
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-225 |
2.22e-18 |
|
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: 83.61 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 3 EPLLAFREVDVFYGV--IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIfgqPR---IRNGQILFSGEDISHKSTHYV 77
Cdd:TIGR02203 328 RGDVEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLI---PRfyePDSGQILLDGHDLADYTLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 78 ASGgIAQAPEGRRIFPDmTVEENLL---MGTIP---IGSQFAAEDMQTMFDLFPR-LKERRKQRAMTMSGGEQQMLAIAR 150
Cdd:TIGR02203 405 RRQ-VALVSQDVVLFND-TIANNIAygrTEQADraeIERALAAAYAQDFVDKLPLgLDTPIGENGVLLSGGQRQRLAIAR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLveqnAHH--ALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVI----AHRlsTIEKADRIVVMDDGRIVERGTHNELL 555
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-225 |
2.23e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 82.06 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFG--QPriRNGQILFSGEDISHKSTHYVasggiaqapegRRI- 91
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGilVP--TSGEVRVLGYVPFKRRKEFA-----------RRIg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 92 ---------FPDMTVEENL-LMGTI-PIGSQFAAEDMQTMFDLFpRLKERRKQRAMTMSGGeQQMLA-IARALMSRPKLL 159
Cdd:COG4586 99 vvfgqrsqlWWDLPAIDSFrLLKAIyRIPDAEYKKRLDELVELL-DLGELLDTPVRQLSLG-QRMRCeLAAALLHRPKIL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792998456 160 LLDEPSLGLAPIVVKQIFQTLSEL-ARSGMTIFL-------VEQnahhalkLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLtshdmddIEA-------LCDRVIVIDHGRIIYDGSLEELK 243
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-225 |
3.25e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.17 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSI-FGQPR--IRNGQILFSGEDISHKSTHYVaSGGIAQapegRRIF-PDMT 96
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPKgvKGSGSVLLNGMPIDAKEMRAI-SAYVQQ----DDLFiPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 97 VEENLL-MGTIPIGSQFAA-EDMQTMFDLFPRLKERRKQ--------RAMTMSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:TIGR00955 116 VREHLMfQAHLRMPRRVTKkEKRERVDEVLQALGLRKCAntrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 167 GLAPIVVKQIFQTLSELARSGMTIFL-VEQNAHHALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICtIHQPSSELFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-219 |
4.40e-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: 79.88 E-value: 4.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFG--QPrirngqilFSGEDISHKSTHYV--ASGGIAqapegrr 90
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiyPP--------DSGTVTVRGRVSSLlgLGGGFN------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 91 ifPDMTVEENL-LMGTIpigSQFAAEDMQTMFDL---FPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEpsl 166
Cdd:cd03220 97 --PELTGRENIyLNGRL---LGLSRKEIDEKIDEiieFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE--- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 167 GLApiVVKQIFQ-----TLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSG 219
Cdd:cd03220 169 VLA--VGDAAFQekcqrRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-231 |
5.11e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 80.44 E-value: 5.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS--GGIAQAPEGRriFPDMT 96
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRqvGMVFQNPDNQ--FVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 97 VEENLLMGTIPIGsqFAAEDMQtmfdlfPRLKERRKQRAMT---------MSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PRK13635 99 VQDDVAFGLENIG--VPREEMV------ERVDQALRQVGMEdflnrephrLSGGQKQRVAIAGVLALQPDIIILDEATSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 168 LAPIVVKQIFQTLSELAR-SGMTIFLVEQNAHHALKlSDRGYVMVNGQIRLSGSGEEL--LGNQEVR 231
Cdd:PRK13635 171 LDPRGRREVLETVRQLKEqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIfkSGHMLQE 236
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-223 |
5.17e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 5.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFG--QP---RI-RNGQI--LFSgedishksthyVASGgiaqap 86
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGilEPtsgRVeVNGRVsaLLE-----------LGAG------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 87 egrriF-PDMTVEEN-----LLMGtipigsqFAAEDMQTMFD---LFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPK 157
Cdd:COG1134 99 -----FhPELTGRENiylngRLLG-------LSRKEIDEKFDeivEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2792998456 158 LLLLDEpslGLApiVVKQIFQT-----LSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEE 223
Cdd:COG1134 167 ILLVDE---VLA--VGDAAFQKkclarIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-225 |
6.70e-18 |
|
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: 82.09 E-value: 6.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 20 ALKQVSLEVNKGETVALIGANGAGKSTL--LMSIFGQPRirNGQILFSGEDISHKSTHYVaSGGIAQAPEGRRIFpDMTV 97
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLakLLVGFFQAR--SGEILLNGFSLKDIDRHTL-RQFINYLPQEPYIF-SGSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 98 EENLLMGTIPIGSQ--------FAA-----EDMQTMFDlfPRLKERrkqrAMTMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:TIGR01193 565 LENLLLGAKENVSQdeiwaaceIAEikddiENMPLGYQ--TELSEE----GSSISGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2792998456 165 SLGLAPIVVKQIFQTLSELARSgmTIFLVeqnAHH--ALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNLQDK--TIIFV---AHRlsVAKQSDKIIVLDHGKIIEQGSHDELL 696
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-230 |
7.59e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 80.16 E-value: 7.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS--GGIAQAPEGrRIFpDMT 96
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkvGLVFQDPDD-QVF-SST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 97 VEENLLMGtiPIGSQFAAEDM----QTMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIV 172
Cdd:PRK13647 97 VWDDVAFG--PVNMGLDKDEVerrvEEALKAV-RMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 173 VKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIrLSGSGEELLGNQEV 230
Cdd:PRK13647 174 QETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRV-LAEGDKSLLTDEDI 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-215 |
8.75e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 79.73 E-value: 8.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSThyvasggiAQAPEGRR----IF-- 92
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR--------AQRKAFRRdiqmVFqd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 ------PDMTVEENL------LMGTIPIGSQFAAEDMQTMFDLFPRLKERRKQRamtMSGGEQQMLAIARALMSRPKLLL 160
Cdd:PRK10419 98 sisavnPRKTVREIIreplrhLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ---LSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 161 LDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVeqnAHHALKLSD----RGYVMVNGQI 215
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLF---ITHDLRLVErfcqRVMVMDNGQI 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-214 |
9.26e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.68 E-value: 9.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLL-------AFREVDVFYGVIQalkQVSLEVNKGETVALIGANGAGKSTLLMSIFG---QPRIR--NGQILFSGED 68
Cdd:PRK15134 1 MTQPLLaienlsvAFRQQQTVRTVVN---DVSLQIEAGETLALVGESGSGKSVTALSILRllpSPPVVypSGDIRFHGES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 69 ISHksthyvASGGIAQAPEGRR---IF--------PDMTVEENLL--------MGTIPIGSQfaaedmqtMFDLFPRLKE 129
Cdd:PRK15134 78 LLH------ASEQTLRGVRGNKiamIFqepmvslnPLHTLEKQLYevlslhrgMRREAARGE--------ILNCLDRVGI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 130 RRKQRAMT-----MSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKL 203
Cdd:PRK15134 144 RQAAKRLTdyphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKL 223
|
250
....*....|.
gi 2792998456 204 SDRGYVMVNGQ 214
Cdd:PRK15134 224 ADRVAVMQNGR 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-215 |
9.40e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 81.70 E-value: 9.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAQAPEGRR---IFPDMT 96
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEERRstgIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 97 VEENLLMGTI-----PIG---SQFAAEDMQTMFDLFpRLKERRKQRAM-TMSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PRK10982 343 IGFNSLISNIrnyknKVGlldNSRMKSDTQWVIDSM-RVKTPGHRTQIgSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2792998456 168 LAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-225 |
1.41e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.73 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 24 VSLEVNKGETVALIGANGAGKSTLLMSIFGQPRiRNGQILFSGEDISHKSTHYVASggiaqapegRRIF--------PDM 95
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELAR---------HRAYlsqqqsppFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 96 TVEENLLMGTIPIGSqfAAEDMQTMFDLFPRLKERRK-QRAMT-MSGGEQQMLAIARALM-------SRPKLLLLDEPSL 166
Cdd:COG4138 85 PVFQYLALHQPAGAS--SEAVEQLLAQLAEALGLEDKlSRPLTqLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2792998456 167 GLApiVVKQI--FQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:COG4138 163 SLD--VAQQAalDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-237 |
1.83e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.94 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLL------MSIFGQPRIRNGQILFSGEDISHKSTHYVAS--GGIAQAPEGrriF 92
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLkvlnrlIEIYDSKIKVDGKVLYFGKDIFQIDAIKLRKevGMVFQQPNP---F 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 PDMTVEENLLMGTIPIGSQFAAEDMQTMFD------LFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSl 166
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVEEclrkvgLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT- 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2792998456 167 GLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGN--QEVRKAYLGG 237
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSpkNELTEKYVIG 254
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
16-238 |
2.15e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 79.74 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 16 GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSthyvaSGGIAQApegRR----I 91
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALS-----ERELRAA---RRkigmI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 92 F------PDMTVEENLlmgtipigsqfaaedmqtmfdLFP-RL----KERRKQRAMTM-----------------SGGEQ 143
Cdd:COG1135 88 FqhfnllSSRTVAENV---------------------ALPlEIagvpKAEIRKRVAELlelvglsdkadaypsqlSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 144 QMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGE 222
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVL 226
|
250
....*....|....*...
gi 2792998456 223 ELLGN--QEVRKAYLGGV 238
Cdd:COG1135 227 DVFANpqSELTRRFLPTV 244
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
18-215 |
2.18e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 79.46 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 18 IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSthyvaSGGIAQApegRR----IFP 93
Cdd:PRK11153 18 IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALS-----EKELRKA---RRqigmIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DM------TVEENL-----LMGTIpigsqfAAEDMQTMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPKLLL 160
Cdd:PRK11153 90 HFnllssrTVFDNValpleLAGTP------KAEIKARVTELLELvgLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 161 LDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEqnahHAL----KLSDRGYVMVNGQI 215
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRElGLTIVLIT----HEMdvvkRICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-229 |
2.74e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 78.67 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS------GGIAQAPEGrRIF 92
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRpvrkriGMVFQFPES-QLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 PDmTVEENLLMGTIPIG---SQFAAEDMQTMFDL-FPRlkERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:PRK13646 100 ED-TVEREIIFGPKNFKmnlDEVKNYAHRLLMDLgFSR--DVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2792998456 169 APIVVKQIFQTLSELA-RSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQE 229
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-229 |
3.31e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 78.23 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGE--------DISHKsthyvaSGGIAQAPEGRriF 92
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwDIRHK------IGMVFQNPDNQ--F 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 PDMTVEENLLMGTIPIGsqFAAEDMQTMFDLFPRL------KERRKQRamtMSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:PRK13650 95 VGATVEDDVAFGLENKG--IPHEEMKERVNEALELvgmqdfKEREPAR---LSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792998456 167 GLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHaLKLSDRGYVMVNGQIRLSGSGEELLGNQE 229
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-190 |
3.41e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.17 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 9 REVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIShKSTHYVASGG-IAQAPE 87
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA-DARHRRAVCPrIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 88 --GRRIFPDMTVEENLlmgtipigsqfaaedmqtmfDLFPRL----KERRKQR-----------------AMTMSGGEQQ 144
Cdd:NF033858 84 glGKNLYPTLSVFENL--------------------DFFGRLfgqdAAERRRRidellratglapfadrpAGKLSGGMKQ 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2792998456 145 MLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSEL--ARSGMTI 190
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIraERPGMSV 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-220 |
3.67e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 80.44 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIshKSTHYVASGGIAQAPEGRRIFPDMTVEE 99
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 100 NLLMGTIPIGSQF--AAEDMQTMFDlFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIF 177
Cdd:TIGR01257 1023 HILFYAQLKGRSWeeAQLEMEAMLE-DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2792998456 178 QTLSELaRSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGS 220
Cdd:TIGR01257 1102 DLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-235 |
4.31e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.11 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS--GGIAQAPEGRriFPDMT 96
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKkiGIIFQNPDNQ--FIGAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 97 VEENLLMGTipIGSQFAAEDMQTMFDLFPR---LKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVV 173
Cdd:PRK13632 101 VEDDIAFGL--ENKKVPPKKMKDIIDDLAKkvgMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGK 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792998456 174 KQIFQTLSELARSGM-TIFLVEQNAHHALkLSDRGYVMVNGQIRLSGSGEELLGNQE-VRKAYL 235
Cdd:PRK13632 179 REIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEiLEKAKI 241
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-227 |
4.98e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 78.59 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 18 IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSThyvasggiAQAPEGRR----IFP 93
Cdd:PRK15079 34 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKD--------DEWRAVRSdiqmIFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DMTVEENLLMgTIpigSQFAAEDMQTMFDLFPRLKERRKQRAMTM----------------SGGEQQMLAIARALMSRPK 157
Cdd:PRK15079 106 DPLASLNPRM-TI---GEIIAEPLRTYHPKLSRQEVKDRVKAMMLkvgllpnlinryphefSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 158 LLLLDEPSLGLAPIVVKQIFQTLSELARS-GMT-IFLveqnAH------HalkLSDRGYVMVNGQIRLSGSGEELLGN 227
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVNLLQQLQREmGLSlIFI----AHdlavvkH---ISDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-230 |
5.52e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.13 E-value: 5.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKST-------LLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAQAPEgRRI 91
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTmiqltngLIISETGQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQFPE-YQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 92 FPDmTVEENLLMGTIPIGS--QFAAEDMQTMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PRK13645 104 FQE-TIEKDIAFGPVNLGEnkQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2792998456 170 PIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEV 230
Cdd:PRK13645 183 PKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-227 |
5.70e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.83 E-value: 5.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 4 PLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSI-----------FGQPRIRNGQILFSGEDISHK 72
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvsgyrYSGDVLLGGRSIFNYRDVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 73 STHYvasGGIAQAPEGrriFPdMTVEENLLMGT-----IPiGSQF--AAEDMQTMFDLFPRLKERRKQRAMTMSGGEQQM 145
Cdd:PRK14271 100 RRRV---GMLFQRPNP---FP-MSIMDNVLAGVrahklVP-RKEFrgVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 146 LAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSgMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLF 250
|
..
gi 2792998456 226 GN 227
Cdd:PRK14271 251 SS 252
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
8-235 |
5.92e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.95 E-value: 5.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 8 FREVDVFYGV-----IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDI----SHKSTHYVA 78
Cdd:PRK13641 5 FENVDYIYSPgtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKKLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 79 S--GGIAQAPEGRrIFPDmTVEENLLMGTIPIG-SQFAAEDMQTMFDLFPRLKERRKQRA-MTMSGGEQQMLAIARALMS 154
Cdd:PRK13641 85 KkvSLVFQFPEAQ-LFEN-TVLKDVEFGPKNFGfSEDEAKEKALKWLKKVGLSEDLISKSpFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 155 RPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQE-VRKA 233
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwLKKH 242
|
..
gi 2792998456 234 YL 235
Cdd:PRK13641 243 YL 244
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-230 |
6.25e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.35 E-value: 6.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 18 IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQI----LFSGEDIS-HKSTHYVASGGIAQAPEGRRI- 91
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNnHELITNPYSKKIKNFKELRRRv 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 92 -----FPDM-----TVEENLLMGTIPIG------SQFAAEDMQTMfdlfpRLKERRKQRA-MTMSGGEQQMLAIARALMS 154
Cdd:PRK13631 119 smvfqFPEYqlfkdTIEKDIMFGPVALGvkkseaKKLAKFYLNKM-----GLDDSYLERSpFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 155 RPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEV 230
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-225 |
1.14e-16 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 78.25 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISH-------KSTHYVAsggiaQAPEgrrIFP 93
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwdreelgRHIGYLP-----QDVE---LFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DmTVEENL-LMGTIPIGSQFAAEDMQTMFDLFPRLKE----RRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:COG4618 420 G-TIAENIaRFGDADPEKVVAAAKLAGVHEMILRLPDgydtRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 169 APIVVKQIFQTLSELARSGMTIFLVeqnAH--HALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:COG4618 499 DDEGEAALAAAIRALKARGATVVVI---THrpSLLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-224 |
1.33e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 76.98 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIS-HKSTHYVAS-----GGIAQAPEgRRIFP 93
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKPlrkkvGIVFQFPE-HQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DmTVEENLLMGTIPIG--SQFAAEDMQTMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:PRK13634 101 E-TVEKDICFGPMNFGvsEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2792998456 172 VVKQIFQTLSELAR-SGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:PRK13634 180 GRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-215 |
1.41e-16 |
|
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: 74.56 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIS--HKSTHYVASGGIAQapegrrifpdmtvE 98
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwDPNELGDHVGYLPQ-------------D 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 99 ENLLMGTIpigsqfaAEDMqtmfdlfprlkerrkqramtMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQ 178
Cdd:cd03246 85 DELFSGSI-------AENI--------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ 137
|
170 180 190
....*....|....*....|....*....|....*....
gi 2792998456 179 TLSELARSGMTIFLVeqnAHH--ALKLSDRGYVMVNGQI 215
Cdd:cd03246 138 AIAALKAAGATRIVI---AHRpeTLASADRILVLEDGRV 173
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-201 |
1.44e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.96 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGedisHKSTHYVAsggiaQAPEGRRIFPd 94
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVP-----QRSEVPDSLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 MTVEENLLMGTIP-IGS--QFAAEDMQTMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:NF040873 72 LTVRDLVAMGRWArRGLwrRLTRDDRAAVDDALERvgLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|..
gi 2792998456 170 PIVVKQIFQTLSELARSGMTIFLVEQNAHHAL 201
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVVVTHDLELVR 183
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-238 |
1.53e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.70 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFG-----QPRIRNGQILFSGEDiSHKSTHYVAS--GGIAQAPEGRrI 91
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSSTS-KQKEIKPVRKkvGVVFQFPESQ-L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 92 FPDmTVEENLLMGTIPIG-SQFAAEDMQT-MFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PRK13643 98 FEE-TVLKDVAFGPQNFGiPKEKAEKIAAeKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 170 PIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEVRKAYLGGV 238
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHELGV 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-226 |
1.79e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.92 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 3 EPLLAFREVDVFY-----GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILF-----------SG 66
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 67 EDISHKSTHYVasgGIAQAPEGrrIFPDMTVEENLlmgTIPIGSQFAAE--DMQTMFDLFPRLKERRKQRAM------TM 138
Cdd:TIGR03269 357 PDGRGRAKRYI---GILHQEYD--LYPHRTVLDNL---TEAIGLELPDElaRMKAVITLKMVGFDEEKAEEIldkypdEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 139 SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI----VVKQIFQTLSELarsGMTIFLVEQNAHHALKLSDRGYVMVNGQ 214
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPItkvdVTHSILKAREEM---EQTFIIVSHDMDFVLDVCDRAALMRDGK 505
|
250
....*....|..
gi 2792998456 215 IRLSGSGEELLG 226
Cdd:TIGR03269 506 IVKIGDPEEIVE 517
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-217 |
2.00e-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: 75.45 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIaqapegrrifpd 94
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGV------------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 MTVEENLLMGTIPIGSQFAAedMQTMFDLFP-RLKERR-------------KQRAMTMSGGEQQMLAIARALMSRPKLLL 160
Cdd:cd03267 99 VFGQKTQLWWDLPVIDSFYL--LAAIYDLPPaRFKKRLdelselldleellDTPVRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 161 LDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRgyVMVNGQIRL 217
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARR--VLVIDKGRL 232
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-224 |
2.88e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 76.30 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFY----GVIQALKQVSLEVNKGETVALIGANGAGKSTL---LMSIFGQPRIRNGQILFSGEDISHKS 73
Cdd:PRK09473 8 QADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTafaLMGLLAANGRIGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 74 THYVASggiAQAPEGRRIFPD--------MTVEENL---LMGTIPIGSQFAAEDMQTMFDLFpRLKERRKQraMTM---- 138
Cdd:PRK09473 88 EKELNK---LRAEQISMIFQDpmtslnpyMRVGEQLmevLMLHKGMSKAEAFEESVRMLDAV-KMPEARKR--MKMyphe 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 139 -SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIR 216
Cdd:PRK09473 162 fSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTM 241
|
....*...
gi 2792998456 217 LSGSGEEL 224
Cdd:PRK09473 242 EYGNARDV 249
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-219 |
3.89e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.96 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSthyvasg 80
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRD------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 gIAQAPEGRRIFPDMT----VEENLLMGTIP-------IGS--------------QFAAEDMQTM------FDLFPRlke 129
Cdd:PRK11701 75 -LYALSEAERRRLLRTewgfVHQHPRDGLRMqvsaggnIGErlmavgarhygdirATAGDWLERVeidaarIDDLPT--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 130 rrkqramTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGY 208
Cdd:PRK11701 151 -------TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLL 223
|
250
....*....|.
gi 2792998456 209 VMVNGQIRLSG 219
Cdd:PRK11701 224 VMKQGRVVESG 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-164 |
3.97e-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: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 4 PLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLmsifgqpRIRNGQI-LFSGE-DISHKsthyVASGG 81
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLL-------KLLAGELePDSGTvKLGET----VKIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 82 IAQapEGRRIFPDMTVEENLlmgtipigSQfAAEDMQTM--------FdLFPRlkERRKQRAMTMSGGEQQMLAIARALM 153
Cdd:COG0488 383 FDQ--HQEELDPDKTVLDEL--------RD-GAPGGTEQevrgylgrF-LFSG--DDAFKPVGVLSGGEKARLALAKLLL 448
|
170
....*....|.
gi 2792998456 154 SRPKLLLLDEP 164
Cdd:COG0488 449 SPPNVLLLDEP 459
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
16-227 |
4.48e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 76.23 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 16 GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDI---SHKSTHYVASGGIAQAPEGRRIF 92
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakiSDAELREVRRKKIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 PDMTVEENLLMGtIPIGSQFAAEDMQTMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAP 170
Cdd:PRK10070 119 PHMTVLDNTAFG-MELAGINAEERREKALDALRQvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 171 IVVKQIFQTLSEL-ARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGN 227
Cdd:PRK10070 198 LIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-204 |
4.69e-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: 73.93 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYvaSGGIAQA 85
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP--HENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 86 PEGRRIFPDMTVEENLlmgtipigsQFAAEDMQ----TMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPKLL 159
Cdd:TIGR01189 79 GHLPGLKPELSALENL---------HFWAAIHGgaqrTIEDALAAvgLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2792998456 160 LLDEPSLGLAPIVVKQIFQTLSE-LARSGMTIFlveqNAHHALKLS 204
Cdd:TIGR01189 150 ILDEPTTALDKAGVALLAGLLRAhLARGGIVLL----TTHQDLGLV 191
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-210 |
5.87e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 74.51 E-value: 5.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 4 PLLAFREVDVFYGV----IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHksthyvas 79
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 80 ggiaqaPEGRR--------IFPDMTVEENL-----LMGTIPIGSQFAAEDMQTMFDLfprlKERRKQRAMTMSGGEQQML 146
Cdd:COG4525 74 ------PGADRgvvfqkdaLLPWLNVLDNVafglrLRGVPKAERRARAEELLALVGL----ADFARRRIWQLSGGMRQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2792998456 147 AIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSEL-ARSGMTIFLVEQNAHHALKLSDRGYVM 210
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-200 |
7.84e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.92 E-value: 7.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 16 GVIQALKQVSLEVNKGETVALIGANGAGKSTlLMSIFG---QPriRNGQILFSGEDISHKSTHYVAS------GGIAQAp 86
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKST-LMNILGcldKP--TSGTYRVAGQDVATLDADALAQlrrehfGFIFQR- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 87 egRRIFPDMTVEENLLMGTIPIGSQfAAEDMQTMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:PRK10535 95 --YHLLSHLTAAQNVEVPAVYAGLE-RKQRLLRAQELLQRlgLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 2792998456 165 SLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHA 200
Cdd:PRK10535 172 TGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVA 207
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-225 |
1.01e-15 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 73.67 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGV--IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS--GG 81
Cdd:cd03252 1 ITFEHVRFRYKPdgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRqvGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 82 IAQApegrRIFPDMTVEENLLMG--TIPIGSQFAAEDMQTMFDLFPRLKERRKQ----RAMTMSGGEQQMLAIARALMSR 155
Cdd:cd03252 81 VLQE----NVLFNRSIRDNIALAdpGMSMERVIEAAKLAGAHDFISELPEGYDTivgeQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2792998456 156 PKLLLLDEPSLGLAPIVVKQIFQTLSELArSGMTIFLVeqnAHH--ALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIII---AHRlsTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-225 |
1.31e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 74.56 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 4 PLLAFR----EVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQP----RIRNGQILFSGEDISHKSth 75
Cdd:COG4170 2 PLLDIRnltiEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLS-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 76 yvasggiaqaPEGRR---------IF--------PDMTVEENLlMGTIPiGSQFAAEDMQtmfdlfpRLKERRKQ----- 133
Cdd:COG4170 80 ----------PRERRkiigreiamIFqepsscldPSAKIGDQL-IEAIP-SWTFKGKWWQ-------RFKWRKKRaiell 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 134 ---------RAMT-----MSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELAR-SGMTIFLVEQNAH 198
Cdd:COG4170 141 hrvgikdhkDIMNsypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLE 220
|
250 260
....*....|....*....|....*..
gi 2792998456 199 HALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:COG4170 221 SISQWADTITVLYCGQTVESGPTEQIL 247
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-233 |
1.48e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 75.14 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKST--LLMSIFGQPRirNGQILFSGEDISHKSTHYVAS--GGIAQAPegrrIFPD 94
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTvaALLQNLYQPT--GGQVLLDGVPLVQYDHHYLHRqvALVGQEP----VLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 MTVEENLLMG-------TIPIGSQFA-AEDMQTMF--DLFPRLKERRKQramtMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:TIGR00958 569 GSVRENIAYGltdtpdeEIMAAAKAAnAHDFIMEFpnGYDTEVGEKGSQ----LSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2792998456 165 SLGLaPIVVKQIFQTLSELArsGMTIFLVE------QNAHHALklsdrgyVMVNGQIRLSGSGEELLGNQEVRKA 233
Cdd:TIGR00958 645 TSAL-DAECEQLLQESRSRA--SRTVLLIAhrlstvERADQIL-------VLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-225 |
1.74e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 75.00 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 5 LLAFREVDVFY-GVIQALKQVSLEVNKGETVALIGANGAGKST---LLMSIFgQPriRNGQILFSGEDIShksthyvasg 80
Cdd:PRK13657 334 AVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTlinLLQRVF-DP--QSGRILIDGTDIR---------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 GIAQAPEGRRI---FPDM-----TVEENLLMGTiPIGSQ----FAAEDMQTMfDLFPR----LKERRKQRAMTMSGGEQQ 144
Cdd:PRK13657 401 TVTRASLRRNIavvFQDAglfnrSIEDNIRVGR-PDATDeemrAAAERAQAH-DFIERkpdgYDTVVGERGRQLSGGERQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 145 MLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELaRSGMTIFLVeqnAHhalKLS-----DRGYVMVNGQIRLSG 219
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFII---AH---RLStvrnaDRILVFDNGRVVESG 551
|
....*.
gi 2792998456 220 SGEELL 225
Cdd:PRK13657 552 SFDELV 557
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-230 |
1.79e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.63 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS------GGIAQAPEGRrIFp 93
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKqirkkvGLVFQFPESQ-LF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DMTVEENLLMGTIPIG-SQFAAEDM-QTMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:PRK13649 100 EETVLKDVAFGPQNFGvSQEEAEALaREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 172 VVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLgnQEV 230
Cdd:PRK13649 180 GRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF--QDV 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-217 |
1.88e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.17 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILfsgedishksthyVASGGIAQA 85
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-------------AGTAPLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 86 PEG-------RRIFPDMTVEENLLMGtipIGSQFAAEDMQTMFDLfpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKL 158
Cdd:PRK11247 80 REDtrlmfqdARLLPWKKVIDNVGLG---LKGQWRDAALQALAAV--GLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2792998456 159 LLLDEPsLG----LAPIVVKQIFQTLSElaRSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRL 217
Cdd:PRK11247 155 LLLDEP-LGaldaLTRIEMQDLIESLWQ--QHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGL 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-203 |
1.95e-15 |
|
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: 72.50 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTL--LMSIFGQPRirNGQILFSGEDIS---HKSTHYVASGgIAQAPegrrIFP 93
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVvaLLENFYQPQ--GGQVLLDGKPISqyeHKYLHSKVSL-VGQEP----VLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DMTVEENLL--MGTIPIGSQFAAEDMQTMFDLFPRLK----ERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:cd03248 101 ARSLQDNIAygLQSCSFECVKEAAQKAHAHSFISELAsgydTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2792998456 168 LAPIVVKQIFQTLSELARSgMTIFLVE------QNAHHALKL 203
Cdd:cd03248 181 LDAESEQQVQQALYDWPER-RTVLVIAhrlstvERADQILVL 221
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-215 |
1.96e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.83 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRN--GQILFSGEDISHKSTHYVASGGIAQAPEGRR----IF 92
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNisGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKgyglNL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 PDmTVEENLLMGTIPIGSQF----------AAEDMqtmfdlfpRLKERRK-----QRAMTMSGGEQQMLAIARALMSRPK 157
Cdd:NF040905 354 ID-DIKRNITLANLGKVSRRgvideneeikVAEEY--------RKKMNIKtpsvfQKVGNLSGGNQQKVVLSKWLFTDPD 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2792998456 158 LLLLDEPSLGlapIVV--K-QIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:NF040905 425 VLILDEPTRG---IDVgaKyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-208 |
2.17e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 71.90 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGIAQAPEGrrIFPDMTVEEN 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSG--INPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 101 LLMGTIPIGSQFAAEDMQTMFDL-----FPrlkerrkqrAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQ 175
Cdd:PRK13540 95 CLYDIHFSPGAVGITELCRLFSLehlidYP---------CGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180 190
....*....|....*....|....*....|...
gi 2792998456 176 IFQTLSELARSGMTIFLveqNAHHALKLSDRGY 208
Cdd:PRK13540 166 IITKIQEHRAKGGAVLL---TSHQDLPLNKADY 195
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-207 |
4.07e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.07 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 2 NEPLLAFREVDVF---YGVIqaLKQVSLEVNKGETVALIGANGAGKSTLLMSI-----FGQPRIR---NGQILFsgedIS 70
Cdd:COG4178 359 EDGALALEDLTLRtpdGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpYGSGRIArpaGARVLF----LP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 71 HKSthYVASGGIAQA---PEGRRIFPDMTVEENLLMGTIPigsqfaaedmqtmfDLFPRLKERRkQRAMTMSGGEQQMLA 147
Cdd:COG4178 433 QRP--YLPLGTLREAllyPATAEAFSDAELREALEAVGLG--------------HLAERLDEEA-DWDQVLSLGEQQRLA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 148 IARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSElARSGMTIFLV----EQNAHHA--LKLSDRG 207
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVghrsTLAAFHDrvLELTGDG 560
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-228 |
4.30e-15 |
|
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: 74.18 E-value: 4.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 17 VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEdishksthyvasggIAQAPEGRRIFPDmT 96
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMPG-T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 97 VEENLLMGT----IPIGSQFAAEDMQTMFDLFP-RLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:TIGR01271 503 IKDNIIFGLsydeYRYTSVIKACQLEEDIALFPeKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 172 VVKQIFQT-LSELARSGMTIFLVEQNAHhaLKLSDRGYVMVNGQIRLSGSGEELLGNQ 228
Cdd:TIGR01271 583 TEKEIFEScLCKLMSNKTRILVTSKLEH--LKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-234 |
6.25e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.60 E-value: 6.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQP--RIRNGQILFSGEDISHKSTHYVA 78
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 79 SGGI---AQAP----------------EGRRIFPDMTVEENLLMGTIpIGSQFAAEDMQTMFdLFPRLKErrkqramTMS 139
Cdd:CHL00131 83 HLGIflaFQYPieipgvsnadflrlayNSKRKFQGLPELDPLEFLEI-INEKLKLVGMDPSF-LSRNVNE-------GFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 140 GGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVeqnAHHALKLS----DRGYVMVNGQI 215
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILI---THYQRLLDyikpDYVHVMQNGKI 230
|
250
....*....|....*....
gi 2792998456 216 RLSGSGEelLGNQEVRKAY 234
Cdd:CHL00131 231 IKTGDAE--LAKELEKKGY 247
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-225 |
1.02e-14 |
|
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: 72.93 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYV-ASGGIaqAPEGRRIFPDmTV 97
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLrAAIGI--VPQDTVLFND-TI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 98 EENLLMGTiPIGSQ---FAAEDMQTMFDLFPRLKE----RRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAP 170
Cdd:COG5265 449 AYNIAYGR-PDASEeevEAAARAAQIHDFIESLPDgydtRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 171 IVVKQIFQTLSELARSGMTIFLveqnAHhalKLS-----DRGYVMVNGQIRLSGSGEELL 225
Cdd:COG5265 528 RTERAIQAALREVARGRTTLVI----AH---RLStivdaDEILVLEAGRIVERGTHAELL 580
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-215 |
1.59e-14 |
|
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: 69.60 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 18 IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIR---NGQILFSGEDIshKSTHYVASGGIAQAPEGRRIFPD 94
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY--KEFAEKYPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 MTVEENLlmgtipigsQFAAedmqtmfdlfpRLKERRKQRAmtMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVK 174
Cdd:cd03233 98 LTVRETL---------DFAL-----------RCKGNEFVRG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2792998456 175 QIFQTLSELAR-SGMTIFL-VEQNAHHALKLSDRGYVMVNGQI 215
Cdd:cd03233 156 EILKCIRTMADvLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-216 |
3.73e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.04 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 17 VIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS------GGIAQApegRR 90
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlrakhvGFVFQS---FM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 91 IFPDMTVEEN-----LLMGTIPIGSQFAAEDMQTMFDLFPRLKERRKQramtMSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:PRK10584 99 LIPTLNALENvelpaLLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ----LSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2792998456 166 LGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKlSDRGYVMVNGQIR 216
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAAR-CDRRLRLVNGQLQ 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-234 |
4.32e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.63 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS--GGIAQapegRRIF 92
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARriGLLAQ----NATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 P-DMTVEENLLMGTIPigsqfaaedMQTMFDLFPRLKERRKQRAM--------------TMSGGEQQMLAIARALMSRPK 157
Cdd:PRK10253 93 PgDITVQELVARGRYP---------HQPLFTRWRKEDEEAVTKAMqatgithladqsvdTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 158 LLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEVRKAY 234
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-225 |
4.79e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 70.22 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 4 PLLAFREVDVFY----GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQP----RIRNGQILFSGEDISHKST- 74
Cdd:PRK15093 2 PLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 75 -------HYVASggIAQAPEGRrIFPDMTVEENLlMGTIPiGSQFAAEDMQTM-------FDLFPRLKERRKQRAM---- 136
Cdd:PRK15093 82 errklvgHNVSM--IFQEPQSC-LDPSERVGRQL-MQNIP-GWTYKGRWWQRFgwrkrraIELLHRVGIKDHKDAMrsfp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 137 -TMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELAR-SGMTIFLVEQNAHHALKLSDRGYVMVNGQ 214
Cdd:PRK15093 157 yELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
250
....*....|.
gi 2792998456 215 IRLSGSGEELL 225
Cdd:PRK15093 237 TVETAPSKELV 247
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-224 |
5.85e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.06 E-value: 5.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 8 FREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSThyvASGGIAQAPE 87
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP---AERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 88 GRRIFPDMTVEENLLMGTIPIGS---------QFAAEDMQtmfdlFPRLKERRKQramTMSGGEQQMLAIARALMSRPKL 158
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAGAkkeeinqrvNQVAEVLQ-----LAHLLDRKPK---ALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 159 LLLDEPSLGLAPIVVKQIFQTLSEL-ARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-236 |
6.10e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVasggIAQAPEGRRI---FPdMT 96
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL----VAYVPQSEEVdwsFP-VL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 97 VEENLLMGT---IPIGSQFAAEDMQTMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPI 171
Cdd:PRK15056 97 VEDVVMMGRyghMGWLRRAKKRDRQIVTAALARvdMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2792998456 172 VVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGyVMVNGQIRLSGSGEELLGNQEVRKAYLG 236
Cdd:PRK15056 177 TEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFTAENLELAFSG 240
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-224 |
6.41e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.26 E-value: 6.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFG----QPRIR-NGQILfSGEDISHKSTHYVASGGIAQAPEGrrifp 93
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyQGSLKiNGIEL-RELDPESWRKHLSWVGQNPQLPHG----- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 dmTVEENLLMGTIPIG-SQFAAEDMQTMFDLF-PRLKE----RRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PRK11174 438 --TLRDNVLLGNPDASdEQLQQALENAWVSEFlPLLPQgldtPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 168 LAPIVVKQIFQTLSELARSGMTIFLVEQNAhhALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:PRK11174 516 LDAHSEQLVMQALNAASRRQTTLMVTHQLE--DLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-208 |
1.77e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 66.75 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSG------EDISHKSTHYVasgGIAQAPEGRrifpd 94
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldfqRDSIARGLLYL---GHAPGIKTT----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 MTVEENLLMGTiPIGSQFAAEDMQTMFDLfpRLKERRKqrAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVK 174
Cdd:cd03231 88 LSVLENLRFWH-ADHSDEQVEEALARVGL--NGFEDRP--VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180 190
....*....|....*....|....*....|....*
gi 2792998456 175 QIFQTL-SELARSGMTIFlveqNAHHALKLSDRGY 208
Cdd:cd03231 163 RFAEAMaGHCARGGMVVL----TTHQDLGLSEAGA 193
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
15-224 |
2.93e-13 |
|
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: 68.29 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRN--GQIL----------------FSGEDIS---HKS 73
Cdd:TIGR03269 10 FDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPtsGRIIyhvalcekcgyverpsKVGEPCPvcgGTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 74 THYVASGGIAQAPEGRRI--------------FPDMTVEENLLMGTIPIGSQfAAEDMQTMFDLFP--RLKERRKQRAMT 137
Cdd:TIGR03269 90 EPEEVDFWNLSDKLRRRIrkriaimlqrtfalYGDDTVLDNVLEALEEIGYE-GKEAVGRAVDLIEmvQLSHRITHIARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 138 MSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELAR-SGMTIFLVEQNAHHALKLSDRGYVMVNGQIR 216
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKaSGISMVLTSHWPEVIEDLSDKAIWLENGEIK 248
|
....*...
gi 2792998456 217 LSGSGEEL 224
Cdd:TIGR03269 249 EEGTPDEV 256
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-165 |
3.45e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 64.78 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILF-SGEDISHksthyvasggIAQ 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgSTVKIGY----------FEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 85 apegrrifpdmtveenllmgtipigsqfaaedmqtmfdlfprlkerrkqramtMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:cd03221 71 -----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
.
gi 2792998456 165 S 165
Cdd:cd03221 98 T 98
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-225 |
4.00e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 66.65 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 9 REVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISH--------------KST 74
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtpsrelakrlailrQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 75 HYVAsggiaqapegrRIfpdmTVEEnLLmgtipigsqfaaedmqtMFDLFP----RLKERRKQ---RAM----------- 136
Cdd:COG4604 85 HINS-----------RL----TVRE-LV-----------------AFGRFPyskgRLTAEDREiidEAIayldledladr 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 137 ---TMSGGEQQMLAIARALMSRPKLLLLDEP--SLGLAPIVvkQIFQTLSELAR-SGMTIFLVEQNAHHALKLSDRGYVM 210
Cdd:COG4604 132 yldELSGGQRQRAFIAMVLAQDTDYVLLDEPlnNLDMKHSV--QMMKLLRRLADeLGKTVVIVLHDINFASCYADHIVAM 209
|
250
....*....|....*
gi 2792998456 211 VNGQIRLSGSGEELL 225
Cdd:COG4604 210 KDGRVVAQGTPEEII 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-234 |
4.96e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.49 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 24 VSLEVNKGETVALIGANGAGKSTLLMSIFGQPRiRNGQILFSGEDISHKSTHYVA--SGGIAQApegRRIFPDMTVEENL 101
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELArhRAYLSQQ---QTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 102 LM----GTIPIGSQFAAEDMQTMFDLFPRLkERRKQramTMSGGEQQ-------MLAIARALMSRPKLLLLDEPSLGLAP 170
Cdd:PRK03695 91 TLhqpdKTRTEAVASALNEVAEALGLDDKL-GRSVN---QLSGGEWQrvrlaavVLQVWPDINPAGQLLLLDEPMNSLDV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792998456 171 IVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEVRKAY 234
Cdd:PRK03695 167 AQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-229 |
6.29e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 66.66 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 18 IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS--GGIAQAPEGRriFPDM 95
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRkiGMVFQNPDNQ--FVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 96 TVEENLLMGTIPIGsqFAAEDMQTMFD---LFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIV 172
Cdd:PRK13642 98 TVEDDVAFGMENQG--IPREEMIKRVDealLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 173 VKQIFQTLSELA-RSGMTIFLVEQNAHHALKlSDRGYVMVNGQIRLSGSGEELLGNQE 229
Cdd:PRK13642 176 RQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-190 |
6.54e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.28 E-value: 6.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISH----KSTHYVasggiaqapeGRRIF--PD 94
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpdvaEACHYL----------GHRNAmkPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 MTVEENL-----LMGTIPIGSQFAAEDMQtMFDLFPRlkerrkqRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PRK13539 88 LTVAENLefwaaFLGGEELDIAAALEAVG-LAPLAHL-------PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|..
gi 2792998456 170 PIVVKQIFQTLSE-LARSGMTI 190
Cdd:PRK13539 160 AAAVALFAELIRAhLAQGGIVI 181
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-224 |
9.01e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 67.35 E-value: 9.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDI------SHKSTHYVAS-GGIAQAPEGR--- 89
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltnisdVHQNMGYCPQfDAIDDLLTGRehl 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 90 ------RIFPDMTVEENLLMGTIPIGSQFAAEDMqtmfdlfprlkerrkqrAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:TIGR01257 2034 ylyarlRGVPAEEIEKVANWSIQSLGLSLYADRL-----------------AGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2792998456 164 PSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
16-164 |
9.65e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.41 E-value: 9.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 16 GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSThyvASGGIAQAPEGRRIFPDM 95
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP---ADRDIAMVFQNYALYPHM 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 96 TVEENLLMG---------TIPIGSQFAAedmqTMFDLFPRLKerRKQRAmtMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:PRK11650 92 SVRENMAYGlkirgmpkaEIEERVAEAA----RILELEPLLD--RKPRE--LSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-225 |
1.04e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 65.42 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASgGIAQA 85
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR-RLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 86 PEGRRIFPDMTVEENLLMGTIPIGS---QFAAED----MQTMFDLfpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKL 158
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSPWLSlwgRLSAEDnarvNQAMEQT--RINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 159 LLLDEPS--LGLAPIVvkQIFQTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:PRK11231 160 VLLDEPTtyLDINHQV--ELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-211 |
1.39e-12 |
|
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: 65.12 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 27 EVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKsthyvasggiaqaPEgrRIFPD--MTVEEnLLMG 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYK-------------PQ--YIKADyeGTVRD-LLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 105 TIP---IGSQFAAEDMQTMfdlfpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGL---APIVVKQIFQ 178
Cdd:cd03237 85 ITKdfyTHPYFKTEIAKPL-----QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLdveQRLMASKVIR 159
|
170 180 190
....*....|....*....|....*....|...
gi 2792998456 179 TLSELARSgmTIFLVEQNAHHALKLSDRgyVMV 211
Cdd:cd03237 160 RFAENNEK--TAFVVEHDIIMIDYLADR--LIV 188
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-228 |
1.76e-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: 65.26 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEdishksthyvasggIAQAPEGRRIFPDmTVEEN 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 101 LLMGT----IPIGSQFAAEDMQTMFDLFP-RLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQ 175
Cdd:cd03291 118 IIFGVsydeYRYKSVVKACQLEEDITKFPeKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2792998456 176 IFQTLSELARSGMTIFLVEQNAHHaLKLSDRGYVMVNGQIRLSGSGEELLGNQ 228
Cdd:cd03291 198 IFESCVCKLMANKTRILVTSKMEH-LKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-227 |
2.04e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.30 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGqilfsgedishksTHYVASGGIAQAPEGRRIFpDMTVEEN 100
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD-------------ASVVIRGTVAYVPQVSWIF-NATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 101 LLMGtipigSQFAAE---------DMQTMFDLFP--RLKERrKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PLN03130 699 ILFG-----SPFDPEryeraidvtALQHDLDLLPggDLTEI-GERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 170 PIVVKQIFQTLSELARSGMTIFLVeQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGN 227
Cdd:PLN03130 773 AHVGRQVFDKCIKDELRGKTRVLV-TNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-232 |
2.09e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.21 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKST---LLMSIFGQPRIRNGQILFSGEDISHKSTH 75
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 76 YVAS--GGIAQAPEGRriFPDMTVEENLLMGTipIGSQFAAEDMQTMF-DLFPR--LKERRKQRAMTMSGGEQQMLAIAR 150
Cdd:PRK13640 81 DIREkvGIVFQNPDNQ--FVGATVGDDVAFGL--ENRAVPRPEMIKIVrDVLADvgMLDYIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELAR-SGMTIFLVEQNAHHAlKLSDRGYVMVNGQIRLSGSGEELLGNQE 229
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
...
gi 2792998456 230 VRK 232
Cdd:PRK13640 236 MLK 238
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-164 |
2.15e-12 |
|
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: 64.27 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 18 IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS---GGIAQAPEGRRIFpD 94
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSrnrYSVAYAAQKPWLL-N 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 95 MTVEENLLMGTiPIGSQ-----FAAEDMQTMFDLFPRLKERR-KQRAMTMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:cd03290 93 ATVEENITFGS-PFNKQrykavTDACSLQPDIDLLPFGDQTEiGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-224 |
2.25e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.72 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 24 VSLEVNKGETVALIGANGAGKSTLLMSIFG--QPRIR--NGQILFSGEDISHKSTHYVASGGIAQAPEGR----RIFPDM 95
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGilPAGVRqtAGRVLLDGKPVAPCALRGRKIATIMQNPRSAfnplHTMHTH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 96 TVEENLLMGTIPIGSQFAA-------EDMQTMFDLFPrlkerrkqraMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:PRK10418 102 ARETCLALGKPADDATLTAaleavglENAARVLKLYP----------FEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 169 APIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:PRK10418 172 DVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-164 |
2.32e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.37 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGV----------IQALKQVSLEVNKGETVALIGANGAGKSTL--LMSIFGQPRirNGQILFSGED 68
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVkrglfkperlVKALDGVSFTLERGKTLAVVGESGCGKSTLarLLTMIETPT--GGELYYQGQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 69 ISHKSTHYVAS-----GGIAQAPEGRrIFPDMTV----EENLLMGTipigSQFAAEDMQTMFDLFPR--LKERRKQRAMT 137
Cdd:PRK11308 79 LLKADPEAQKLlrqkiQIVFQNPYGS-LNPRKKVgqilEEPLLINT----SLSAAERREKALAMMAKvgLRPEHYDRYPH 153
|
170 180
....*....|....*....|....*...
gi 2792998456 138 M-SGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:PRK11308 154 MfSGGQRQRIAIARALMLDPDVVVADEP 181
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-164 |
2.43e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.58 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 14 FYGViQALKQVSLEVNKGETVALIGANGAGKSTlLMSI------FGQpriRNGQILFSGEDISHKSTHYVASGGIAQAPE 87
Cdd:NF040905 11 FPGV-KALDDVNLSVREGEIHALCGENGAGKST-LMKVlsgvypHGS---YEGEILFDGEVCRFKDIRDSEALGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 88 GRRIFPDMTVEENLLMGTIPigSQFAAEDMQTMF----DLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLL 161
Cdd:NF040905 86 ELALIPYLSIAENIFLGNER--AKRGVIDWNETNrrarELLAKvgLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
...
gi 2792998456 162 DEP 164
Cdd:NF040905 164 DEP 166
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-200 |
2.44e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.81 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 2 NEPLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFG-QPR-IRNGQILF-----SGEDISHKST 74
Cdd:PRK10938 257 NEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQgYSNDLTLFgrrrgSGETIWDIKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 75 H--YVASggiaQAPEGRRIfpDMTVEENLLMGTI-PIGSQFAAEDMQTM-----FDLFPRLKERRKQRAMTMSGGEQQML 146
Cdd:PRK10938 337 HigYVSS----SLHLDYRV--STSVRNVILSGFFdSIGIYQAVSDRQQKlaqqwLDILGIDKRTADAPFHSLSWGQQRLA 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 147 AIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMT--IFLveqnAHHA 200
Cdd:PRK10938 411 LIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqlLFV----SHHA 462
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-163 |
2.55e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.96 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNE--PLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKS--THY 76
Cdd:PRK10247 1 MQEnsPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpeIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 77 VASGGIAQAPEgrrIFPDmTVEENLLMgtiPIGSQFAAEDMQTMFDLFPRL---KERRKQRAMTMSGGEQQMLAIARALM 153
Cdd:PRK10247 81 QQVSYCAQTPT---LFGD-TVYDNLIF---PWQIRNQQPDPAIFLDDLERFalpDTILTKNIAELSGGEKQRISLIRNLQ 153
|
170
....*....|
gi 2792998456 154 SRPKLLLLDE 163
Cdd:PRK10247 154 FMPKVLLLDE 163
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-207 |
6.02e-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: 61.79 E-value: 6.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSI-----FGQPRI---RNGQILFsgedishksthyvasggIAQAPegrrIF 92
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALaglwpWGSGRIgmpEGEDLLF-----------------LPQRP----YL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 PDMTVEENLLmgtipigsqfaaedmqtmfdlFPRLKErrkqramtMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIV 172
Cdd:cd03223 76 PLGTLREQLI---------------------YPWDDV--------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2792998456 173 VKQIFQTLSELarsGMTIFLV------EQNAHHALKLSDRG 207
Cdd:cd03223 127 EDRLYQLLKEL---GITVISVghrpslWKFHDRVLDLDGEG 164
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-225 |
7.05e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.27 E-value: 7.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 18 IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYvasggiaQAPEGRRIFPDMTV 97
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-------RSQRIRMIFQDPST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 98 EENLLMGTipigSQFAAEDMQTMFDLFPRLKERRKQRAMTMSG---------------GEQQMLAIARALMSRPKLLLLD 162
Cdd:PRK15112 99 SLNPRQRI----SQILDFPLRLNTDLEPEQREKQIIETLRQVGllpdhasyyphmlapGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792998456 163 EPSLGLAPIVVKQIFQTLSEL-ARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
3.84e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 61.31 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYGVIQA--LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVA 78
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 79 S--GGIAQAPEGRriFPDMTVEENLLMG----TIPigsqfaAEDM-----QTMFDLfpRLKERRKQRAMTMSGGEQQMLA 147
Cdd:PRK13648 83 KhiGIVFQNPDNQ--FVGSIVKYDVAFGlenhAVP------YDEMhrrvsEALKQV--DMLERADYEPNALSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 148 IARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSEL-ARSGMTIFLVEQNAHHALKlSDRGYVMVNGQIRLSGSGEELLG 226
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
...
gi 2792998456 227 NQE 229
Cdd:PRK13648 232 HAE 234
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-224 |
6.90e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.91 E-value: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLMSIFG----QPRIRNGQILFSGED---ISHKSTHYVASGGIAQapegrrI 91
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlidyPGRVMAEKLEFNGQDlqrISEKERRNLVGAEVAM------I 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 92 FPD-MTVeenlLMGTIPIGSQFaaedMQTMFDLFPRLKERRKQRAM--------------------TMSGGEQQMLAIAR 150
Cdd:PRK11022 95 FQDpMTS----LNPCYTVGFQI----MEAIKVHQGGNKKTRRQRAIdllnqvgipdpasrldvyphQLSGGMSQRVMIAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 151 ALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELAR-SGMTIF-------LVEQNAHHALklsdrgyVMVNGQIRLSGSGE 222
Cdd:PRK11022 167 AIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVlithdlaLVAEAAHKII-------VMYAGQVVETGKAH 239
|
..
gi 2792998456 223 EL 224
Cdd:PRK11022 240 DI 241
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
15-204 |
7.62e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.10 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSthyvASGGIAQAPEGrrIFPD 94
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AERGVVFQNEG--LLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 MTVEENLLMGTIPIG-----SQFAAEDMQTMFDLfprlKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PRK11248 85 RNVQDNVAFGLQLAGvekmqRLEIAHQMLKKVGL----EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 2792998456 170 PIVVKQIFQTLSEL-ARSGMTIFLVEQNAHHALKLS 204
Cdd:PRK11248 161 AFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMA 196
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-234 |
7.71e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.61 E-value: 7.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQ---------PRIRnGQILFSGEDISHKSTHYVASGGIAQAPEGRRI 91
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggaprgARVT-GDVTLNGEPLAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 92 FPdMTVEENLLMGTIPIGSQFAAEDMQTMfDLFPRLKERRKQRAM------TMSGGEQQMLAIARAL---------MSRP 156
Cdd:PRK13547 96 FA-FSAREIVLLGRYPHARRAGALTHRDG-EIAWQALALAGATALvgrdvtTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 157 KLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEVRKAY 234
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCY 252
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-195 |
7.95e-11 |
|
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: 61.46 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFgqpRIRN--GQILFSGedISHKS----THYVASGGIAQapegrRIFpd 94
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL---RLLSteGEIQIDG--VSWNSvtlqTWRKAFGVIPQ-----KVF-- 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 95 mtveenLLMGTIPIG----SQFAAED---------MQTMFDLFP-RLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLL 160
Cdd:TIGR01271 1303 ------IFSGTFRKNldpyEQWSDEEiwkvaeevgLKSVIEQFPdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190
....*....|....*....|....*....|....*
gi 2792998456 161 LDEPSLGLAPIVVKQIFQTLSElARSGMTIFLVEQ 195
Cdd:TIGR01271 1377 LDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEH 1410
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-208 |
8.19e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.43 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 25 SLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIS------HKSTHYV--ASGgiaqapegrrIFPDMT 96
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdeyHQDLLYLghQPG----------IKTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 97 VEENLlmgtipigsQFAAE-----DMQTMFDLFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:PRK13538 91 ALENL---------RFYQRlhgpgDDEALWEALAQvgLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2792998456 170 PIVVKQIFQTLSE-LARSGMTIFlveqNAHHALKLSDRGY 208
Cdd:PRK13538 162 KQGVARLEALLAQhAEQGGMVIL----TTHQDLPVASDKV 197
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
5-215 |
9.67e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 9.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 5 LLAFREVDVFygviQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQP----RIRNGQILFSGEDISHKSTHYvaSG 80
Cdd:TIGR00956 65 LKKFRDTKTF----DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGITPEEIKKHY--RG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 GIAQAPEGRRIFPDMTVEENLlmgtipigsQFAA--EDMQTMFDLFPRLKERRKQRAMTM-------------------- 138
Cdd:TIGR00956 139 DVVYNAETDVHFPHLTVGETL---------DFAArcKTPQNRPDGVSREEYAKHIADVYMatyglshtrntkvgndfvrg 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 139 -SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELAR-SGMTIFL-VEQNAHHALKLSDRGYVMVNGQI 215
Cdd:TIGR00956 210 vSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVaIYQCSQDAYELFDKVIVLYEGYQ 289
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-164 |
1.09e-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: 60.72 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLmsifgqpRIRNG-QILFSGEDISHKSthyVASGGIAQAPEgrrIFPDMTVEE 99
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLL-------RIMAGvDKDFNGEARPQPG---IKVGYLPQEPQ---LDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 100 NLLMGTIP----------IGSQFAAED--MQTMFDLFPRLKE-----------RRKQRAM-------------TMSGGEQ 143
Cdd:TIGR03719 88 NVEEGVAEikdaldrfneISAKYAEPDadFDKLAAEQAELQEiidaadawdldSQLEIAMdalrcppwdadvtKLSGGER 167
|
170 180
....*....|....*....|.
gi 2792998456 144 QMLAIARALMSRPKLLLLDEP 164
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEP 188
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-225 |
1.16e-10 |
|
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: 61.11 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGqilfsgedishkstHYVASGGIAQAPEGRRIFPDmTVEEN 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG--------------HVHMKGSVAYVPQQAWIQND-SLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 101 LLMGTiPIGSQFAAEDMQTMfDLFPRLK-----ERRK--QRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVV 173
Cdd:TIGR00957 719 ILFGK-ALNEKYYQQVLEAC-ALLPDLEilpsgDRTEigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2792998456 174 KQIFQTL--SELARSGMTIFLVEQNAHHaLKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:TIGR00957 797 KHIFEHVigPEGVLKNKTRILVTHGISY-LPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-234 |
1.28e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.80 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASgGIAQAPEGRRIFPDMTVEEN 100
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR-KVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 101 LLMGTIP----IGsQFAAEDMQ------TMFDLFP---RLKErrkqramTMSGGEQQMLAIARALMSRPKLLLLDEPS-- 165
Cdd:PRK10575 106 VAIGRYPwhgaLG-RFGAADREkveeaiSLVGLKPlahRLVD-------SLSGGERQRAWIAMLVAQDSRCLLLDEPTsa 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 166 LGLAPIV-VKQIFQTLSElaRSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEVRKAY 234
Cdd:PRK10575 178 LDIAHQVdVLALVHRLSQ--ERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
15-215 |
1.60e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.13 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 15 YGVIQALKQVSLEVNKGETVALIGANGAG--KSTLLMSIFGQPRIRNGQILFSGedISHKSTHYVASGGIAQAPEGRRif 92
Cdd:NF000106 23 FGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TW--CANRRALRRTIG*HRPVR*GRR-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 PDMTVEENLLMgtIPIGSQFAAEDMQTMFD-LFPR--LKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLA 169
Cdd:NF000106 99 ESFSGRENLYM--IGR*LDLSRKDARARADeLLERfsLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2792998456 170 PIVVKQIFQTLSELARSGMTIFLVEQ------NAHHALKLSDRGYVMVNGQI 215
Cdd:NF000106 177 PRTRNEVWDEVRSMVRDGATVLLTTQymeeaeQLAHELTVIDRGRVIADGKV 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-183 |
1.64e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.10 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 3 EPLLAFREVDVFYGVIQ-----------ALKQVSLEVNKGETVALIGANGAGKST----LLMSIFGQprirnGQILFSGE 67
Cdd:PRK15134 273 SPLLDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 68 DISHKSTHyvasggiAQAPEGRRI---FPDMTVEENLLMGTIpigsQFAAEDMQTMF-DLFPRLKERRKQRAMT------ 137
Cdd:PRK15134 348 PLHNLNRR-------QLLPVRHRIqvvFQDPNSSLNPRLNVL----QIIEEGLRVHQpTLSAAQREQQVIAVMEevgldp 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2792998456 138 ---------MSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSEL 183
Cdd:PRK15134 417 etrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSL 471
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-168 |
2.20e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.97 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 4 PLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQIlfsgedishKSTHYVASGGIA 83
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 84 QAPEGRRIFPdMTVEENLLMGTipiGSQFAaedmqtmfDLFPRLKerRKQRA-------MTMSGGEQQMLAIARALMSRP 156
Cdd:PRK09544 74 QKLYLDTTLP-LTVNRFLRLRP---GTKKE--------DILPALK--RVQAGhlidapmQKLSGGETQRVLLARALLNRP 139
|
170
....*....|..
gi 2792998456 157 KLLLLDEPSLGL 168
Cdd:PRK09544 140 QLLVLDEPTQGV 151
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-223 |
2.55e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.89 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 31 GETVALIGANGAGKSTLLMSIFGQPRIRN--GQILFSGEDISH---KSTHYVASGGIaqapegrrIFPDMTVEENLLMGT 105
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKqilKRTGFVTQDDI--------LYPHLTVRETLVFCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 106 IPIGSQFAAEDMQTMF--DLFPRLKERRKQRAMT-------MSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQI 176
Cdd:PLN03211 166 LLRLPKSLTKQEKILVaeSVISELGLTKCENTIIgnsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2792998456 177 FQTLSELARSGMTIFL-VEQNAHHALKLSDRGYVMVNGQIRLSGSGEE 223
Cdd:PLN03211 246 VLTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-165 |
2.60e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 27 EVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSgEDISHKsthyvasggiaqaPEGRRIFPDMTVEENLLMGTI 106
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYK-------------PQYIKPDYDGTVEDLLRSITD 426
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 107 PIGSQFAAEDMQTMFDLfPRLKERRkqrAMTMSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:PRK13409 427 DLGSSYYKSEIIKPLQL-ERLLDKN---VKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-225 |
3.09e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 58.71 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLmSIFGQPRIRNGQILFSGedishksthyvASGGIAQAPEGRRIFPDMTVEEN 100
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLL-SAFLRLLNTEGDIQIDG-----------VSWNSVPLQKWRKAFGVIPQKVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 101 LLMGTI-----PIGsQFAAED---------MQTMFDLFP-RLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:cd03289 88 IFSGTFrknldPYG-KWSDEEiwkvaeevgLKSVIEQFPgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 166 LGLAPIVVKQIFQTLSElARSGMTIFLVEQNAHHALKlSDRGYVMVNGQIRLSGSGEELL 225
Cdd:cd03289 167 AHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLL 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-228 |
3.80e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.60 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 5 LLAFREVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDishksthyVASGGI 82
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD--------VAKFGL 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 83 AQAPEGRRIFPDMTVeenLLMGTIPIG-SQFAAEDMQTMFDLFPR--LKE--RRKQRAM---------TMSGGEQQMLAI 148
Cdd:PLN03232 1306 TDLRRVLSIIPQSPV---LFSGTVRFNiDPFSEHNDADLWEALERahIKDviDRNPFGLdaevseggeNFSVGQRQLLSL 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 149 ARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSgMTIFLVEQNAHHALKlSDRGYVMVNGQIRLSGSGEELLGNQ 228
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS-CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-193 |
4.10e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.87 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 25 SLEVNKGETVALIGANGAGKSTLLMSIFGQprirngQILFSGEDISHKSTHYVASGGIAQ---APEGRRIFPDM------ 95
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGE------LPLLSGERQSQFSHITRLSFEQLQklvSDEWQRNNTDMlspged 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 96 ----TVEENLLMGTI-PIGSQFAAEDMQTMfDLFPRlkerrkqRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAP 170
Cdd:PRK10938 97 dtgrTTAEIIQDEVKdPARCEQLAQQFGIT-ALLDR-------RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180
....*....|....*....|...
gi 2792998456 171 IVVKQIFQTLSELARSGMTIFLV 193
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITLVLV 191
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-232 |
4.38e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.22 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFYGVIQ-ALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIShksthyvasggiAQ 84
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT------------AE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 85 APEGRR-----IFPDMTVEENLLmgtipiGSQFAAEDMQTMFDLFPRLKERRKQR-------AMTMSGGEQQMLAIARAL 152
Cdd:PRK10522 391 QPEDYRklfsaVFTDFHLFDQLL------GPEGKPANPALVEKWLERLKMAHKLEledgrisNLKLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 153 MSRPKLLLLDEPSLGLAPiVVKQIF--QTLSELARSGMTIFLVEQNAHHaLKLSDRGYVMVNGQIR-LSGSGEELLGNQE 229
Cdd:PRK10522 465 AEERDILLLDEWAADQDP-HFRREFyqVLLPLLQEMGKTIFAISHDDHY-FIHADRLLEMRNGQLSeLTGEERDAASRDA 542
|
...
gi 2792998456 230 VRK 232
Cdd:PRK10522 543 VAR 545
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-163 |
5.00e-10 |
|
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: 59.19 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 8 FREVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASgGIAQA 85
Cdd:TIGR00957 1287 FRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF-KITII 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 86 PEGRRIFPDmtveeNLLMGTIPIGsQFAAEDMQTMFDL---------FP-RLKERRKQRAMTMSGGEQQMLAIARALMSR 155
Cdd:TIGR00957 1366 PQDPVLFSG-----SLRMNLDPFS-QYSDEEVWWALELahlktfvsaLPdKLDHECAEGGENLSVGQRQLVCLARALLRK 1439
|
....*...
gi 2792998456 156 PKLLLLDE 163
Cdd:TIGR00957 1440 TKILVLDE 1447
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-224 |
7.49e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.33 E-value: 7.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 18 IQALKQVSLEVNKGETVALIGANGAGKSTL---LMSIFGQP-----------RIRNGQILFSGEdISHKSTHYVASGGIA 83
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTalaLMRLLEQAgglvqcdkmllRRRSRQVIELSE-QSAAQMRHVRGADMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 84 QapegrrIFPD-MTVeenlLMGTIPIGSQFAAE--------------DMQTMFDL--FPRLKERRKQRAMTMSGGEQQML 146
Cdd:PRK10261 108 M------IFQEpMTS----LNPVFTVGEQIAESirlhqgasreeamvEAKRMLDQvrIPEAQTILSRYPHQLSGGMRQRV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 147 AIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEEL 224
Cdd:PRK10261 178 MIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
10-190 |
1.56e-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: 55.71 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 10 EVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLmSIFGQPR---IRNGQILFSGEDIS---HKSTHYVASGGIa 83
Cdd:cd03232 12 TVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLL-DVLAGRKtagVITGEILINGRPLDknfQRSTGYVEQQDV- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 84 qapegrrIFPDMTVEENLLmgtipigsqFAAedmqtmfdlfprlkerrKQRAMTMSggEQQMLAIARALMSRPKLLLLDE 163
Cdd:cd03232 90 -------HSPNLTVREALR---------FSA-----------------LLRGLSVE--QRKRLTIGVELAAKPSILFLDE 134
|
170 180
....*....|....*....|....*..
gi 2792998456 164 PSLGLAPIVVKQIFQTLSELARSGMTI 190
Cdd:cd03232 135 PTSGLDSQAAYNIVRFLKKLADSGQAI 161
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-225 |
1.86e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 57.34 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTL--LMSIFGQprIRNGQILFSGEDIShkstHYVASG- 80
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYD--IDEGEILLDGHDLR----DYTLASl 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 --GIAQAPEGRRIFPDmTVEENLlmgtipigsQFAAEDMQTMFDLfprlkERRKQRAMTM-------------------- 138
Cdd:PRK11176 416 rnQVALVSQNVHLFND-TIANNI---------AYARTEQYSREQI-----EEAARMAYAMdfinkmdngldtvigengvl 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 139 -SGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELA--RSGMTIflveqnAHH--ALKLSDRGYVMVNG 213
Cdd:PRK11176 481 lSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQknRTSLVI------AHRlsTIEKADEILVVEDG 554
|
250
....*....|..
gi 2792998456 214 QIRLSGSGEELL 225
Cdd:PRK11176 555 EIVERGTHAELL 566
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-164 |
1.90e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQIlfsgedisHKSTHYvasgGIAQAPEGRRIF-PDMTVEE 99
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI--------HCGTKL----EVAYFDQHRAELdPEKTVMD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 100 NLLMG--TIPIGSQ----------FaaedmqtmfdLFPrlkerrKQRAMT----MSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:PRK11147 403 NLAEGkqEVMVNGRprhvlgylqdF----------LFH------PKRAMTpvkaLSGGERNRLLLARLFLKPSNLLILDE 466
|
.
gi 2792998456 164 P 164
Cdd:PRK11147 467 P 467
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
14-196 |
2.21e-09 |
|
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: 55.02 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 14 FYGVIQ-ALKQVSLEVNKGETVALIGANGAGKSTLLMSIFgqprirngqilfsgedishksthyvASGGIAQAPEGRRIF 92
Cdd:cd03238 3 VSGANVhNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL-------------------------YASGKARLISFLPKF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 PDMTveenllmgTIPIGSqfaaedMQTMFDL---FPRLKerrkQRAMTMSGGEQQMLAIARALMSRPK--LLLLDEPSLG 167
Cdd:cd03238 58 SRNK--------LIFIDQ------LQFLIDVglgYLTLG----QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180
....*....|....*....|....*....
gi 2792998456 168 LAPIVVKQIFQTLSELARSGMTIFLVEQN 196
Cdd:cd03238 120 LHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-165 |
3.61e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.33 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 27 EVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQIlFSGEDISHKsthyvasggiaqaPEGRRIFPDMTVEEnLLMGTI 106
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-DEDLKISYK-------------PQYISPDYDGTVEE-FLRSAN 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2792998456 107 PI---GSQFAAEDMQTMfdlfpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:COG1245 427 TDdfgSSYYKTEIIKPL-----GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-193 |
4.07e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.96 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIShksthyvasggiaqapegrrIFPDMTVEEN 100
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ--------------------FGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 101 LLM-GTIPIGSQFAAE----DMQTMFDLFPRLKERRKQRAMtmsggeqqmlaIARALMSRPKLLLLDEPSLGLAPIVVKQ 175
Cdd:COG2401 106 IGRkGDFKDAVELLNAvglsDAVLWLRRFKELSTGQKFRFR-----------LALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170
....*....|....*...
gi 2792998456 176 IFQTLSELARSGMTIFLV 193
Cdd:COG2401 175 VARNLQKLARRAGITLVV 192
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-225 |
4.64e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.87 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISH------KSTHYVASggiaQAPegrRIFP 93
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqldswRSRLAVVS----QTP---FLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DmTVEENLLMGTiPIGSQFAAED---MQTMFDLFPRLKERRK----QRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSL 166
Cdd:PRK10789 403 D-TVANNIALGR-PDATQQEIEHvarLASVHDDILRLPQGYDtevgERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2792998456 167 GLAPIVVKQIFQTLSELaRSGMTIFLveqNAHH--ALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:PRK10789 481 AVDGRTEHQILHNLRQW-GEGRTVII---SAHRlsALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-229 |
5.63e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.90 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIShksthyvaSGGIAQAPEGRRIFPDMTVeen 100
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS--------KFGLMDLRKVLGIIPQAPV--- 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 101 LLMGTI-----PIGSQFAAEdmqtMFDLFPR--LKE--RRKQRAM---------TMSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:PLN03130 1324 LFSGTVrfnldPFNEHNDAD----LWESLERahLKDviRRNSLGLdaevseageNFSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2792998456 163 EPSlglAPIVVKQ---IFQTLSELARS-GMTIFlveqnAH--HALKLSDRGYVMVNGQIRLSGSGEELLGNQE 229
Cdd:PLN03130 1400 EAT---AAVDVRTdalIQKTIREEFKScTMLII-----AHrlNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-163 |
8.64e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.11 E-value: 8.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKStHYVASGGIAQAPEgrrifpDMTVEEN 100
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAMVQQ------DPVVLAD 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 101 LLMGTIPIGSQFA-------------AEDMQTMFD-LFPRLKERrkqrAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:PRK10790 430 TFLANVTLGRDISeeqvwqaletvqlAELARSLPDgLYTPLGEQ----GNNLSVGQKQLLALARVLVQTPQILILDE 502
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
6-229 |
9.23e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.56 E-value: 9.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 6 LAFREVDVFY--GVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDIshksthyvASGGIA 83
Cdd:PTZ00243 1309 LVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI--------GAYGLR 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 84 qapEGRRIFPDMTVEENLLMGTIPIG----SQFAAEDMQTMFDLFPrLKERRKQRA-----------MTMSGGEQQMLAI 148
Cdd:PTZ00243 1381 ---ELRRQFSMIPQDPVLFDGTVRQNvdpfLEASSAEVWAALELVG-LRERVASESegidsrvleggSNYSVGQRQLMCM 1456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 149 ARALMSR-PKLLLLDEPSLGLAPIVVKQIFQTLselaRSGMTIFLVEQNAH--HALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:PTZ00243 1457 ARALLKKgSGFILMDEATANIDPALDRQIQATV----MSAFSAYTVITIAHrlHTVAQYDKIIVMDHGAVAEMGSPRELV 1532
|
....
gi 2792998456 226 GNQE 229
Cdd:PTZ00243 1533 MNRQ 1536
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-164 |
9.72e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 9.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGE------------DISHKSTHYVAsGGIAQAPEG 88
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivarlqqdpprNVEGTVYDFVA-EGIEEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 89 RRIFPDMTV-------EENL-----LMGTIpigsqfaaeDMQTMFDLFPRLKERRKQRAMT-------MSGGEQQMLAIA 149
Cdd:PRK11147 98 LKRYHDISHlvetdpsEKNLnelakLQEQL---------DHHNLWQLENRINEVLAQLGLDpdaalssLSGGWLRKAALG 168
|
170
....*....|....*
gi 2792998456 150 RALMSRPKLLLLDEP 164
Cdd:PRK11147 169 RALVSNPDVLLLDEP 183
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-215 |
1.04e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 18 IQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS-----GGIAQAP----EG 88
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAlrrdiQFIFQDPyaslDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 89 RRIFPDMTVEENLLMGTIPigSQFAAEDMQTMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGLLP--GKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2792998456 169 APIVVKQIFQTLSELARS-GMTIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-225 |
1.34e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILfsgedishksthyvASGGIAQAPEGRRIFpDMTVEEN 100
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--------------AERSIAYVPQQAWIM-NATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 101 LLMgtipigsqFAAEDMQTMFD-------------LFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PTZ00243 741 ILF--------FDEEDAARLADavrvsqleadlaqLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 168 LAPIVVKQIFQTLSELARSGMTIFLVEQNAhHALKLSDRGYVMVNGQIRLSGSGEELL 225
Cdd:PTZ00243 813 LDAHVGERVVEECFLGALAGKTRVLATHQV-HVVPRADYVVALGDGRVEFSGSSADFM 869
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
59-235 |
1.71e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 59 NGQILFSGEDISHKSTHYVAS--GGIAQAPegrrIFPDMTVEENLLMGT-------IPIGSQFAAEDmQTMFDLFPRLKE 129
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDLRNlfSIVSQEP----MLFNMSIYENIKFGKedatredVKRACKFAAID-EFIESLPNKYDT 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 130 RRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELA-RSGMTIFLVeqnAHH--ALKLSDR 206
Cdd:PTZ00265 1351 NVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITI---AHRiaSIKRSDK 1427
|
170 180 190
....*....|....*....|....*....|....*
gi 2792998456 207 GYVMVNGQ-----IRLSGSGEELLGNQE-VRKAYL 235
Cdd:PTZ00265 1428 IVVFNNPDrtgsfVQAHGTHEELLSVQDgVYKKYV 1462
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
94-224 |
2.76e-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: 53.86 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DMTVEENL-LMGTIPIGSQFaaedMQTMFDL---FPRLKerrkQRAMTMSGGEQQMLAIARALMSR---PKLLLLDEPSL 166
Cdd:TIGR00630 790 DMTVEEAYeFFEAVPSISRK----LQTLCDVglgYIRLG----QPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTT 861
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 167 GLAPIVVKQIFQTLSELARSGMTIFLVEQN------AHHALKL----SDRGyvmvnGQIRLSGSGEEL 224
Cdd:TIGR00630 862 GLHFDDIKKLLEVLQRLVDKGNTVVVIEHNldviktADYIIDLgpegGDGG-----GTVVASGTPEEV 924
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-164 |
6.63e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 19 QALKQVSLEVNKGETVALIGANGAGKSTLLmsifgqpRIRNGqiL---FSGEdishksthYVASGGI-----AQAPEgrr 90
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLL-------RIMAG--VdkeFEGE--------ARPAPGIkvgylPQEPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 91 IFPDMTVEENLLMGTIP----------IGSQFAAE--DMQTMFDLFPRLKE-----------RRKQRAM----------- 136
Cdd:PRK11819 81 LDPEKTVRENVEEGVAEvkaaldrfneIYAAYAEPdaDFDALAAEQGELQEiidaadawdldSQLEIAMdalrcppwdak 160
|
170 180 190
....*....|....*....|....*....|
gi 2792998456 137 --TMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:PRK11819 161 vtKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-164 |
1.69e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQIlfsgedishKSTHYVASGGIAQAPEGRriFP-DMTVEE 99
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV---------KWSENANIGYYAQDHAYD--FEnDLTLFD 403
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 100 NLlmgtipigSQFAAE--DMQTMFDLFPRL---KERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEP 164
Cdd:PRK15064 404 WM--------SQWRQEgdDEQAVRGTLGRLlfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-227 |
1.94e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.37 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 133 QRAM-TMSGGEQQMLAIARALMSRPK--LLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNaHHALKLSDR--- 206
Cdd:PRK00635 471 ERALaTLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRiid 549
|
90 100
....*....|....*....|....
gi 2792998456 207 ---GYVMVNGQIRLSGSGEELLGN 227
Cdd:PRK00635 550 igpGAGIFGGEVLFNGSPREFLAK 573
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-225 |
2.05e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.37 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 137 TMSGGEQQMLAIARALMS---RPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAhHALKLSDrgYVM--- 210
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVAD--YVLelg 885
|
90 100
....*....|....*....|
gi 2792998456 211 -----VNGQIRLSGSGEELL 225
Cdd:PRK00635 886 peggnLGGYLLASCSPEELI 905
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
21-194 |
2.50e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 49.95 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLM-SIF--GQPRIRNGQILFSGEDISHKSTHYVASggiaqaPEGrrIFPDMTV 97
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFdTIYaeGQRRYVESLSAYARQFLGQMDKPDVDS------IEG--LSPAIAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 98 EENLL-------MGTIpigsqfaaedmQTMFD----LFPR--LKERRKQ-------------RAMTMSGGEQQMLAIARA 151
Cdd:cd03270 83 DQKTTsrnprstVGTV-----------TEIYDylrlLFARvgIRERLGFlvdvglgyltlsrSAPTLSGGEAQRIRLATQ 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2792998456 152 LMSRPK--LLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVE 194
Cdd:cd03270 152 IGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVE 196
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
94-198 |
9.88e-07 |
|
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: 48.38 E-value: 9.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DMTVEEnllmgtipigsqfAAEdmqtMFDLFPRLKERRK-------------QRAMTMSGGEQQMLAIARALMSR---PK 157
Cdd:cd03271 130 DMTVEE-------------ALE----FFENIPKIARKLQtlcdvglgyiklgQPATTLSGGEAQRIKLAKELSKRstgKT 192
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2792998456 158 LLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAH 198
Cdd:cd03271 193 LYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLD 233
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
21-229 |
1.48e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 47.98 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVAS--GGIAQAP---EGRRIF--- 92
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSrlSIILQDPilfSGSIRFnld 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 93 PDMTVEENLLMGTIPIGSqfaaedMQTMFDLFP-RLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLaPI 171
Cdd:cd03288 117 PECKCTDDRLWEALEIAQ------LKNMVKSLPgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI-DM 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2792998456 172 VVKQIFQTLSELARSGMTIFLVEQNAHHALKlSDRGYVMVNGQIRLSGSGEELLGNQE 229
Cdd:cd03288 190 ATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQED 246
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-163 |
1.55e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 38 GANGAGKSTLLMSIFGQPRIRNGQILFSGEDISHKSTHYVASGGiaqapEGRRIFPDMTVEENLLMGTIPIGSqfaAEDM 117
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG-----HNLGLKLEMTVFENLKFWSEIYNS---AETL 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2792998456 118 QTMFDLFpRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDE 163
Cdd:PRK13541 105 YAAIHYF-KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-234 |
2.28e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.09 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQP--RIRNGQILFSGEDISHKSTHYVASGGIAQAPEGRRIFPDMTvE 98
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYPVEIPGVS-N 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 99 ENLLMGTIPIGSQFAAEDMQTMFDLFPRLKERRKQRAMT-----------MSGGEQQMLAIARALMSRPKLLLLDEPSLG 167
Cdd:PRK09580 96 QFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPedlltrsvnvgFSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792998456 168 LAPIVVKQIFQTLSELaRSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGNQEVRKAY 234
Cdd:PRK09580 176 LDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQGY 241
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-215 |
2.39e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 34 VALIGANGAGKSTLLMSIFGQPRIRNGQILFSGE-DISHKSTHYVASGGIAQAP--EGRRIFPDmtVEENLL---MGTIP 107
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvRMAVFSQHHVDGLDLSSNPllYMMRCFPG--VPEQKLrahLGSFG 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 108 IGSQFAaedMQTMFdlfprlkerrkqramTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSeLARSG 187
Cdd:PLN03073 616 VTGNLA---LQPMY---------------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV-LFQGG 676
|
170 180
....*....|....*....|....*...
gi 2792998456 188 mtIFLVEQNAHHALKLSDRGYVMVNGQI 215
Cdd:PLN03073 677 --VLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-237 |
4.30e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.32 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 134 RAMTMSGGEQQMLAIARALMSRPK--LLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNaHHALKLSDR----- 206
Cdd:TIGR00630 485 AAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTIRAADYvidig 563
|
90 100 110
....*....|....*....|....*....|...
gi 2792998456 207 -GYVMVNGQIRLSGSGEELLGNQE-VRKAYLGG 237
Cdd:TIGR00630 564 pGAGEHGGEVVASGTPEEILANPDsLTGQYLSG 596
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-165 |
4.33e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 46.85 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 24 VSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFsGEDishksthyVASGGIAQAPEGrrIFPDMTVEEN--- 100
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GET--------VKLAYVDQSRDA--LDPNKTVWEEisg 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 101 ----LLMGTIPIGSQ-------FAAEDMQtmfdlfprlkerrkQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:TIGR03719 410 gldiIKLGKREIPSRayvgrfnFKGSDQQ--------------KKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-192 |
8.63e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 20 ALKQVSLEVNKGETVALIGANGAGKST-------LL------MSIFGQPrirngqilfsgedishksthyVASGGIAQAp 86
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLpasegeAWLFGQP---------------------VDAGDIATR- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 87 egRRI---------FPDMTVEENLLMGT----IPiGSQFAA--EDMQTMFDLfprlKERRKQRAMTMSGGEQQMLAIARA 151
Cdd:NF033858 339 --RRVgymsqafslYGELTVRQNLELHArlfhLP-AAEIAArvAEMLERFDL----ADVADALPDSLPLGIRQRLSLAVA 411
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2792998456 152 LMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARS-GMTIFL 192
Cdd:NF033858 412 VIHKPELLILDEPTSGVDPVARDMFWRLLIELSREdGVTIFI 453
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-227 |
1.63e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.27 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 20 ALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQIlfsgeDISHKSTHYVASGGIAQAPEGRRifpdmTVE- 98
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAISSGLNGQLTGIE-----NIEl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 99 ENLLMGtipIGSQFAAEDMQTMFDlFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEP-SLGlAPIVVKQIF 177
Cdd:PRK13545 109 KGLMMG---LTKEKIKEIIPEIIE-FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAlSVG-DQTFTKKCL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2792998456 178 QTLSELARSGMTIFLVEQNAHHALKLSDRGYVMVNGQIRLSGSGEELLGN 227
Cdd:PRK13545 184 DKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-165 |
2.42e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 4 PLLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQI-LFSGEDISHKSTHYVASggi 82
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEF--- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 83 aqapegrrifpdMTVEENLLMGTIPIGSQFAAEDMQTMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLD 162
Cdd:PRK10636 388 ------------LRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
...
gi 2792998456 163 EPS 165
Cdd:PRK10636 456 EPT 458
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
18-62 |
2.55e-05 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 44.54 E-value: 2.55e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2792998456 18 IQALKQVsleVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQI 62
Cdd:PRK01889 185 LDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-192 |
2.80e-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: 44.22 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 21 LKQVSLEVNKGETVaLIGANGAGKSTLLMSI---FGQPRIRNgqilFSGEDISHKS--------------------THYV 77
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALrllLGPSSSRK----FDEEDFYLGDdpdlpeieieltfgsllsrlLRLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 78 ASGGIAQAPEG---------RRIFPDMT--VEENL--LMGTIPIGSQFAAEDMQTMFDLF-PRLKERRKQRAMTMSGGEQ 143
Cdd:COG3593 89 LKEEDKEELEEaleelneelKEALKALNelLSEYLkeLLDGLDLELELSLDELEDLLKSLsLRIEDGKELPLDRLGSGFQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2792998456 144 QMLAIA--RALM-----SRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFL 192
Cdd:COG3593 169 RLILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVII 224
|
|
| 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 2792998456 135 AMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGL 168
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-209 |
3.79e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.86 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 27 EVNKGETVALIGANGAGKSTLLmsifgqpRIRNGQILFSGEDIShksthyvasggiaqapegrrifpdmtveenllmgti 106
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAV-------KILAGQLIPNGDNDE------------------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 107 pigsqfaaedmqtmfdlFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGL---APIVVKQIFQTLSEL 183
Cdd:cd03222 58 -----------------WDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLdieQRLNAARAIRRLSEE 120
|
170 180
....*....|....*....|....*.
gi 2792998456 184 ARSgmTIFLVEQNAHHALKLSDRGYV 209
Cdd:cd03222 121 GKK--TALVVEHDLAVLDYLSDRIHV 144
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
94-196 |
5.03e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DMTVEEnllmgtipigsqfAAEdmqtMFDLFPRLKERRK-------------QRAMTMSGGEQQMLAIARALMSRPK--- 157
Cdd:COG0178 787 DMTVEE-------------ALE----FFENIPKIARKLQtlqdvglgyiklgQPATTLSGGEAQRVKLASELSKRSTgkt 849
|
90 100 110
....*....|....*....|....*....|....*....
gi 2792998456 158 LLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQN 196
Cdd:COG0178 850 LYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHN 888
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-195 |
5.46e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 40.89 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 17 VIQALkqvSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGqilfsgedishksTHYVASGG----IAQAPE-GRR- 90
Cdd:TIGR00954 467 LIESL---SFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG-------------RLTKPAKGklfyVPQRPYmTLGt 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 91 -----IFPDmTVEENLLMGtipigsqFAAEDMQTMFD---LFPRLKERRKQRAM-----TMSGGEQQMLAIARALMSRPK 157
Cdd:TIGR00954 531 lrdqiIYPD-SSEDMKRRG-------LSDKDLEQILDnvqLTHILEREGGWSAVqdwmdVLSGGEKQRIAMARLFYHKPQ 602
|
170 180 190
....*....|....*....|....*....|....*...
gi 2792998456 158 LLLLDEPSLGLAPIVVKQIFQTLSELarsGMTIFLVEQ 195
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRLCREF---GITLFSVSH 637
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
129-165 |
6.11e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 6.11e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2792998456 129 ERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPS 165
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPT 372
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
94-196 |
6.50e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 94 DMTVEEnllmgtipigsqfAAEdmqtMFDLFPRLKERRK-------------QRAMTMSGGEQQMLAIARALMSRPK--- 157
Cdd:PRK00349 791 DMTVEE-------------ALE----FFEAIPKIARKLQtlvdvglgyiklgQPATTLSGGEAQRVKLAKELSKRSTgkt 853
|
90 100 110
....*....|....*....|....*....|....*....
gi 2792998456 158 LLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQN 196
Cdd:PRK00349 854 LYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHN 892
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-194 |
7.76e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 40.15 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 30 KGETVALIGANGAGKSTLLmSI--------FGQP-----------------------RIRNGQIlfsgeDISHKSTHyva 78
Cdd:COG1245 98 KGKVTGILGPNGIGKSTAL-KIlsgelkpnLGDYdeepswdevlkrfrgtelqdyfkKLANGEI-----KVAHKPQY--- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 79 sggIAQAPegrRIFpDMTVEEnLLMGTIPIGsqfAAEDMQTMFDLFPRLKerrkQRAMTMSGGEQQMLAIARALMSRPKL 158
Cdd:COG1245 169 ---VDLIP---KVF-KGTVRE-LLEKVDERG---KLDELAEKLGLENILD----RDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2792998456 159 LLLDEPSLGLapivvkQIFQ------TLSELARSGMTIFLVE 194
Cdd:COG1245 234 YFFDEPSSYL------DIYQrlnvarLIRELAEEGKYVLVVE 269
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-165 |
9.08e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.15 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 5 LLAFREVDVFYGVIQALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGE-----------DISHKS 73
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqetpALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 74 THYVASGGiaqaPEGRRIFPDMTV--EENLLMGTIPIGSQFAAEDMQTMFDLFPRL-------KERRKQRAMTMSGGEQQ 144
Cdd:PRK10636 81 LEYVIDGD----REYRQLEAQLHDanERNDGHAIATIHGKLDAIDAWTIRSRAASLlhglgfsNEQLERPVSDFSGGWRM 156
|
170 180
....*....|....*....|.
gi 2792998456 145 MLAIARALMSRPKLLLLDEPS 165
Cdd:PRK10636 157 RLNLAQALICRSDLLLLDEPT 177
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-188 |
2.55e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.35 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 30 KGETVALIGANGAGKSTLLMSIFGQ-PRIRNGQILFSGEDISHKsthyvasggiaqapegrrifpdmtveenllmgtipi 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARElGPPGGGVIYIDGEDILEE------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 109 gsqfaaedmqtmfDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLLLLDEPSLGLAPIVVKQIFQTLSELARSGM 188
Cdd:smart00382 45 -------------VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLL 111
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-238 |
6.68e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 133 QRAMTMSGGEQQMLAIARALMSRPK---LLLLDEPSLGLAPIVVKQIFQTLSELARSGMTIFLVEQNAhHALKLSD---- 205
Cdd:PRK00635 1695 QNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDP-ALLKQADylie 1773
|
90 100 110
....*....|....*....|....*....|....*.
gi 2792998456 206 --RGYVMVNGQIRLSGSGEEL-LGNQEVRKAYLGGV 238
Cdd:PRK00635 1774 mgPGSGKTGGKILFSGPPKDIsASKDSLLKTYMCNL 1809
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-196 |
7.33e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 36.72 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 1 MNEPLLAFREVDVFYgviqALKQVSLEVNKGETVALIGANGAGKSTLLMSIFGQPRIRNGQILFSGEdishksthyVASG 80
Cdd:PRK13546 24 MKDALIPKHKNKTFF----ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE---------VSVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792998456 81 GIAQAPEGRrifpdMTVEENLLMGTIPIG-SQFAAEDMQTMFDLFPRLKERRKQRAMTMSGGEQQMLAIARALMSRPKLL 159
Cdd:PRK13546 91 AISAGLSGQ-----LTGIENIEFKMLCMGfKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDIL 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 2792998456 160 LLDEP-SLGLAPIVVKQIfQTLSELARSGMTIFLVEQN 196
Cdd:PRK13546 166 VIDEAlSVGDQTFAQKCL-DKIYEFKEQNKTIFFVSHN 202
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
18-70 |
8.90e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 35.93 E-value: 8.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2792998456 18 IQALKQVSLEVNKGETVaLIGANGAGKSTLLMSI----FGQPRI--RNGQILFSGEDIS 70
Cdd:pfam13476 6 FRSFRDQTIDFSKGLTL-ITGPNGSGKTTILDAIklalYGKTSRlkRKSGGGFVKGDIR 63
|
|
| |
