|
Name |
Accession |
Description |
Interval |
E-value |
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-233 |
3.37e-155 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 430.07 E-value: 3.37e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAI 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENLAMGGFFADRHQYQQRIERVFTLFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 161 SLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVRSAYLGG 233
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLGG 237
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-233 |
2.62e-128 |
|
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: 361.99 E-value: 2.62e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAI 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENLAMGGFFA-DRHQYQQRIERVFTLFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYARrDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 160 PSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVRSAYLGG 233
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLGV 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-223 |
8.71e-114 |
|
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: 324.77 E-value: 8.71e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAIV 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEGRRVFSRMTVEENLAMGGFFADRHQYQQRIERVFTLFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPS 161
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540804698 162 LGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLAN 223
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-231 |
2.45e-71 |
|
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: 217.39 E-value: 2.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAIV 81
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEGRRVFSRMTVEENLAMGgFFADRHQYQQRIERVFTLFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPS 161
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTG-LAALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 162 LGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALlaNEAVRSAYL 231
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL--DEDKVRRYL 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-233 |
1.78e-62 |
|
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: 195.64 E-value: 1.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVA- 79
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIAr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 ---IVpegrRVFSRMTVEENLAMG--------------GFFADRHQYQQRIERVFTL--FPRLLERRSQRAGTMSGGEQQ 140
Cdd:COG0411 84 tfqNP----RLFPELTVLENVLVAaharlgrgllaallRLPRARREEREARERAEELleRVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 141 MLAIGRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAA 219
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
250
....*....|....
gi 1540804698 220 LLANEAVRSAYLGG 233
Cdd:COG0411 240 VRADPRVIEAYLGE 253
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-226 |
6.53e-58 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 183.41 E-value: 6.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVaiv 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 peGR-----RVFSRMTVEENLAMGG---------FFADRHQYQQRIERVFTL--FPRLLERRSQRAGTMSGGEQQMLAIG 145
Cdd:cd03219 78 --GRtfqipRLFPELTVLENVMVAAqartgsgllLARARREEREARERAEELleRVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 146 RALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEA 225
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
.
gi 1540804698 226 V 226
Cdd:cd03219 236 V 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-222 |
2.14e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 181.80 E-value: 2.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDItqWQTSRIMREAVAIV 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV--ARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEGRRVFSRMTVEENLA-MGGFF-ADRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:COG1131 79 PQEPALYPDLTVRENLRfFARLYgLPRKEARERIDELLELF-GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 160 PSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLA 222
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-224 |
5.24e-51 |
|
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: 165.80 E-value: 5.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwqTSRIMREAVAI 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK--EPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENLAmggFFA-----DRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLL 155
Cdd:COG4555 79 LPDERGLYDRLTVRENIR---YFAelyglFDEELKKRIEELIELL-GLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 156 LLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANE 224
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEI 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
11-232 |
2.83e-50 |
|
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: 163.48 E-value: 2.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 11 YGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAIVPEGRRVFSR 90
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 91 MTVEENL--AMGGFFADRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPII 168
Cdd:cd03218 90 LTVEENIlaVLEIRGLSKKEREEKLEELLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 169 IQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVRSAYLG 232
Cdd:cd03218 169 VQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
3.64e-46 |
|
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: 153.66 E-value: 3.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMReAVAI 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELAR-RIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENLAMGgffadRHQYQ-----------QRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALM 149
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALG-----RYPHLglfgrpsaedrEAVEEALERT-GLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 150 SQPKLLLLDEPSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVRS 228
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEE 233
|
..
gi 1540804698 229 AY 230
Cdd:COG1120 234 VY 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-211 |
7.38e-46 |
|
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: 150.24 E-value: 7.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDItqWQTSRIMREAVAIV 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI--KKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEGRRVFSRMTVEENLamggffadrhqyqqriervftlfprllerrsqragTMSGGEQQMLAIGRALMSQPKLLLLDEPS 161
Cdd:cd03230 79 PEEPSLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1540804698 162 LGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRV 211
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-210 |
1.25e-44 |
|
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: 148.38 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 3 SFNQVSAHY--GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWqTSRIMREAVAI 80
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKL-SLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 V---PEGRrvFSRMTVEENLAmggfFA------DRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQ 151
Cdd:cd03225 80 VfqnPDDQ--FFGPTVEEEVA----FGlenlglPEEEIEERVEEALELV-GLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 152 PKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGR 210
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-232 |
1.42e-44 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 149.02 E-value: 1.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAI 80
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENL--AMGGFFADRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLD 158
Cdd:COG1137 83 LPQEASIFRKLTVEDNIlaVLELRKLSKKEREERLEELLEEF-GITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 159 EPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVRSAYLG 232
Cdd:COG1137 162 EPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLG 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-224 |
1.70e-44 |
|
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: 148.63 E-value: 1.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHY-GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRImREAVAI 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL-RRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 V---PEgRRVFSrMTVEENLAMG----GFfaDRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPK 153
Cdd:COG1122 80 VfqnPD-DQLFA-PTVEEDVAFGpenlGL--PREEIRERVEEALELV-GLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 154 LLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANE 224
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
11-232 |
1.88e-44 |
|
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: 148.96 E-value: 1.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 11 YGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAIVPEGRRVFSR 90
Cdd:TIGR04406 11 YKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYLPQEASIFRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 91 MTVEENL-----AMGGFfaDRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLA 165
Cdd:TIGR04406 91 LTVEENImavleIRKDL--DRAEREERLEALLEEF-QISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540804698 166 PIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVRSAYLG 232
Cdd:TIGR04406 168 PIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLG 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-160 |
8.36e-43 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 141.63 E-value: 8.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwQTSRIMREAVAIVPEGRRVFSRMTVEEN 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD-DERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 97 LAMGG--FFADRHQYQQRIERVFTLFPR--LLERR-SQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:pfam00005 80 LRLGLllKGLSKREKDARAEEALEKLGLgdLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-230 |
4.66e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.92 E-value: 4.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwqtsriMREAVAI 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR------ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEgRRVFSR---MTVEENLAMG-----GFF-----ADRHQYQQRIERVftlfpRLLERRSQRAGTMSGGEQQMLAIGRA 147
Cdd:COG1121 80 VPQ-RAEVDWdfpITVRDVVLMGrygrrGLFrrpsrADREAVDEALERV-----GLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 148 LMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLeNGRVVLEDTGAALLANEAVR 227
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLS 232
|
...
gi 1540804698 228 SAY 230
Cdd:COG1121 233 RAY 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-212 |
4.76e-41 |
|
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: 139.19 E-value: 4.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSrimREAVAIV 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE---RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEGRRVFSRMTVEENLAMGGFFA--DRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRgvPKAEIRARVRELLELV-GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 160 PSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:cd03259 157 PLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-211 |
4.09e-40 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 137.24 E-value: 4.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYG----KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQW---QTSRIM 74
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 75 REAVAIVPEGRRVFSRMTVEENLAMGGFFAdRHQYQQRIERVFTLFPR--LLERRSQRAGTMSGGEQQMLAIGRALMSQP 152
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLA-GVPKKERRERAEELLERvgLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 153 KLLLLDEPSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNaNQALKLADRGYVLENGRV 211
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-232 |
4.65e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 137.94 E-value: 4.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVai 80
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGI-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 vpeGR-----RVFSRMTVEENL--AMGG-------FFADRHQYQ-QRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIG 145
Cdd:COG4674 88 ---GRkfqkpTVFEELTVFENLelALKGdrgvfasLFARLTAEErDRIEEVLETI-GLTDKADRLAGLLSHGQKQWLEIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 146 RALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEgMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEA 225
Cdd:COG4674 164 MLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGK-HSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQADPR 242
|
....*..
gi 1540804698 226 VRSAYLG 232
Cdd:COG4674 243 VIEVYLG 249
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-210 |
5.69e-40 |
|
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: 135.39 E-value: 5.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQ-WQTSRIMREAVAI 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDlEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENLAMGgffadrhqyqqriervftlfprllerrsqragtMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG---------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 161 SLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGR 210
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-212 |
3.33e-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: 135.00 E-value: 3.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 7 VSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCG-----EPRASEGSIVFQGQDITQWQTSRI-MREAVAI 80
Cdd:cd03260 6 LNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVDVLeLRRRVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFsRMTVEENLAMGgffaDRHQYQQRIERVFTLFPRLLER--------RSQRAGTMSGGEQQMLAIGRALMSQP 152
Cdd:cd03260 86 VFQKPNPF-PGSIYDNVAYG----LRLHGIKLKEELDERVEEALRKaalwdevkDRLHALGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 153 KLLLLDEPSLGLAPIIIQQIFDIIQQLREEgMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-212 |
4.39e-39 |
|
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: 134.20 E-value: 4.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 3 SFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwqtsriMREAVAIVP 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK------ERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 83 EgRRVFSR---MTVEENLAMG-----GFF-----ADRHQYQQRIERVftlfpRLLERRSQRAGTMSGGEQQMLAIGRALM 149
Cdd:cd03235 75 Q-RRSIDRdfpISVRDVVLMGlyghkGLFrrlskADKAKVDEALERV-----GLSELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 150 SQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRgYVLENGRVV 212
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVV 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-220 |
4.87e-39 |
|
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: 135.00 E-value: 4.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYG-KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRI--MREAV 78
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 79 AIVPEGRRVFSRMTVEENLaMGGFFADRHQYQ--------QRIERVFTLFPR--LLERRSQRAGTMSGGEQQMLAIGRAL 148
Cdd:cd03256 81 GMIFQQFNLIERLSVLENV-LSGRLGRRSTWRslfglfpkEEKQRALAALERvgLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 149 MSQPKLLLLDEPSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAAL 220
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-219 |
4.97e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 134.41 E-value: 4.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHY-GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRI--MREA 77
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 78 VAIVPEGRRVFSRMTVEENLA-----MGgffADRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQP 152
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVAlplrvTG---KSRKEIRRRVREVLDLV-GLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540804698 153 KLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAA 219
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-210 |
7.88e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 129.29 E-value: 7.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 3 SFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWqtsrimreavaivp 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKL-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 83 egrrvfsrmtveenlamggffaDRHQYQQRIERVFTLfprllerrsqragtmSGGEQQMLAIGRALMSQPKLLLLDEPSL 162
Cdd:cd00267 67 ----------------------PLEELRRRIGYVPQL---------------SGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1540804698 163 GLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGR 210
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-212 |
2.57e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 130.16 E-value: 2.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYG----KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQW---QTSRI 73
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLserELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 74 MREAVAIVPEGRRVFSRMTVEENLAMGGFFADRHqYQQRIERVFTLFPR--LLERRSQRAGTMSGGEQQMLAIGRALMSQ 151
Cdd:COG1136 84 RRRHIGFVFQFFNLLPELTALENVALPLLLAGVS-RKERRERARELLERvgLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 152 PKLLLLDEPS---------------LGLApiiiqqifdiiqqlREEGMTIFLVEQNANQAlKLADRGYVLENGRVV 212
Cdd:COG1136 163 PKLILADEPTgnldsktgeevlellRELN--------------RELGTTIVMVTHDPELA-ARADRVIRLRDGRIV 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-216 |
3.77e-37 |
|
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: 129.41 E-value: 3.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 11 YGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwqTSRIMREAVAIVPEGRRVFSR 90
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR--EPREVRRRIGIVFQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 91 MTVEENLAMGGFFAD--RHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPII 168
Cdd:cd03265 88 LTGWENLYIHARLYGvpGAERRERIDELLDFV-GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1540804698 169 IQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDT 216
Cdd:cd03265 167 RAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGT 215
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-218 |
4.90e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 130.59 E-value: 4.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGK-----IQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMR 75
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 76 EaVAivpegrRVF--------SRMTVEENLAM----GGFF--------ADRHQYQQRIERVftlfpRL-LERR-SQRAGT 133
Cdd:COG1101 81 Y-IG------RVFqdpmmgtaPSMTIEENLALayrrGKRRglrrgltkKRRELFRELLATL-----GLgLENRlDTKVGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 134 MSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
....*.
gi 1540804698 213 LEDTGA 218
Cdd:COG1101 229 LDVSGE 234
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-232 |
2.06e-36 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 128.57 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAI 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENLAMG-------GFFAD-------RHQYQQRIERVFTLFPR--LLERRSQRAGTMSGGEQQMLAI 144
Cdd:PRK11300 85 TFQHVRLFREMTVIENLLVAqhqqlktGLFSGllktpafRRAESEALDRAATWLERvgLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 145 GRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLAN 223
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 244
|
....*....
gi 1540804698 224 EAVRSAYLG 232
Cdd:PRK11300 245 PDVIKAYLG 253
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-230 |
2.60e-36 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 128.00 E-value: 2.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGK----IQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwQTSRIMRE 76
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR-RRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 77 AVAIV---PEGrrvfS---RMTVEENLAMGGFFADRHQYQQRIERVFT---LFPRLLERRSQragTMSGGEQQMLAIGRA 147
Cdd:COG1124 80 RVQMVfqdPYA----SlhpRHTVDRILAEPLRIHGLPDREERIAELLEqvgLPPSFLDRYPH---QLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 148 LMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLAneAV 226
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA--GP 230
|
....
gi 1540804698 227 RSAY 230
Cdd:COG1124 231 KHPY 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-212 |
2.70e-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: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITqwqtsrimreavAI 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT------------GL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRV---------FSRMTVEENLA----MGGFfaDRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRA 147
Cdd:COG3842 73 PPEKRNVgmvfqdyalFPHLTVAENVAfglrMRGV--PKAEIRARVAELLELV-GLEGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 148 LMSQPKLLLLDEPSLGL-APIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:COG3842 150 LAPEPRVLLLDEPLSALdAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-164 |
3.63e-36 |
|
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: 126.44 E-value: 3.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSriMREAVAI 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED--YRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENL----AMGGFFADRHQYQQRIERVftlfpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLL 156
Cdd:COG4133 80 LGHADGLKPELTVRENLrfwaALYGLRADREAIDEALEAV-----GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
....*...
gi 1540804698 157 LDEPSLGL 164
Cdd:COG4133 155 LDEPFTAL 162
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-212 |
1.65e-35 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 124.08 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 5 NQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQtSRIMREAVAIVPeg 84
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS-PKELARKIAYVP-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 85 rrvfsrmtveenlamggffadrhqyqQRIERVftlfpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGL 164
Cdd:cd03214 80 --------------------------QALELL-----GLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1540804698 165 APIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:cd03214 129 DIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-211 |
1.88e-35 |
|
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: 124.95 E-value: 1.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQ-WQTSRIMREAVAI 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENLAMGGFFADRHQYQQRIERVFTLFPR--LLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKvgLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 159 EPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRV 211
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-214 |
5.42e-35 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 123.48 E-value: 5.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITqwQTSRIMREAVAIV 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 pEGRRVFSRMTVEENLAMGGFFAD-RHQYQQRIERVFTlfprLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:cd03268 79 -EAPGFYPNLTARENLRLLARLLGiRKKRIDEVLDVVG----LKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 161 SLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLE 214
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
12-214 |
9.35e-35 |
|
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: 123.25 E-value: 9.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 12 GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwqTSRIMREAVAIVPEGRRVFSRM 91
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK--EPAEARRRLGFVSDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 92 TVEENLamgGFFAD-----RHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAP 166
Cdd:cd03266 94 TARENL---EYFAGlyglkGDELTARLEELADRL-GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1540804698 167 IIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLE 214
Cdd:cd03266 170 MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-211 |
2.87e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 121.85 E-value: 2.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRImREAVAIV 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW-RRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEgRRVFSRMTVEENLAMGGFFADRHQYQQRIERVFTLF---PRLLErrsQRAGTMSGGEQQMLAIGRALMSQPKLLLLD 158
Cdd:COG4619 80 PQ-EPALWGGTVRDNLPFPFQLRERKFDRERALELLERLglpPDILD---KPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 159 EPSLGLAPIIIQQIFDI-IQQLREEGMTIFLVEQNANQALKLADRGYVLENGRV 211
Cdd:COG4619 156 EPTSALDPENTRRVEELlREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-214 |
4.74e-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: 119.84 E-value: 4.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAIV 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 pegrrvfsrmtveenlamggffadrHQyqqriervftlfprllerrsqragtMSGGEQQMLAIGRALMSQPKLLLLDEPS 161
Cdd:cd03216 81 -------------------------YQ-------------------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 162 LGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLE 214
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
6.13e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 123.30 E-value: 6.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRI--Mreav 78
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIgyL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 79 aivPEGRRVFSRMTVEENLAmggFFA-----DRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPK 153
Cdd:COG4152 77 ---PEERGLYPKMKVGEQLV---YLArlkglSKAEAKRRADEWLERL-GLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 154 LLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDT 216
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGS 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-223 |
6.34e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 121.74 E-value: 6.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTS-RIMREAVA 79
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDeRLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSRMTVEENLAMGGFFADRHQYQQRIERVFTLFPR--LLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLL 157
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 158 DEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLAN 223
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-223 |
1.39e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 126.17 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHY-----GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRI-- 73
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 74 MREAVAIV---PEGrRVFSRMTVEENLAMGGFFADRHQYQQRIERVFT------LFPRLLERrsqRAGTMSGGEQQMLAI 144
Cdd:COG1123 340 LRRRVQMVfqdPYS-SLNPRMTVGDIIAEPLRLHGLLSRAERRERVAEllervgLPPDLADR---YPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 145 GRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLAN 223
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-202 |
2.97e-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: 119.28 E-value: 2.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHY-GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRI--MREA 77
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLplLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 78 VAIVPEGRRVFSRMTVEENLAM-----GgffADRHQYQQRIERVFTLFPrLLERRSQRAGTMSGGEQQMLAIGRALMSQP 152
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALplevrG---KKEREIQRRVGAALRQVG-LEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1540804698 153 KLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLveqnANQALKLADR 202
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIV----ATHDLSLVDR 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-227 |
1.45e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 123.20 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDItQWQTSRIMREA-VA 79
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRSPRDAQAAgIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSRMTVEENLAMG-----GFFADRHQYQQRIERVFTLF-----PRllerrsQRAGTMSGGEQQMLAIGRALM 149
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLGreprrGGLIDWRAMRRRARELLARLgldidPD------TPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540804698 150 SQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVR 227
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVR 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-228 |
1.52e-32 |
|
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: 117.99 E-value: 1.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTS--RIMREAVA 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSRMTVEENLAmggFFADRH----------QYQQRIERVftlfpRLLERRSQRAGTMSGGEQQMLAIGRALM 149
Cdd:cd03261 81 MLFQSGALFDSLTVFENVA---FPLREHtrlseeeireIVLEKLEAV-----GLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 150 SQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLA--NEAV 226
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAsdDPLV 232
|
..
gi 1540804698 227 RS 228
Cdd:cd03261 233 RQ 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-213 |
1.53e-32 |
|
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: 117.38 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRImreavAIV 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRI-----GYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEGRRVFSRMTVEENLAmggFFAD-----RHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLL 156
Cdd:cd03269 76 PEERGLYPKMKVIDQLV---YLAQlkglkKEEARRRIDEWLERL-ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1540804698 157 LDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVL 213
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-214 |
1.73e-32 |
|
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: 117.57 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYG----KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwqtsriMREA 77
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG------PGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 78 VAIVPEGRRVFSRMTVEENLAMgGFFADRHQYQQRIERVFTLFPR--LLERRSQRAGTMSGGEQQMLAIGRALMSQPKLL 155
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVAL-GLELQGVPKAEARERAEELLELvgLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540804698 156 LLDEPSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLEN--GRVVLE 214
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-230 |
1.76e-32 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 118.29 E-value: 1.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRI--MReav 78
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELarRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 79 AIVPEgrrvFSRM----TVEENLAMG--GFFADRHQYQQRIERVFTLF--PRLLERRSQragTMSGGEQQMLAIGRAL-- 148
Cdd:COG4559 78 AVLPQ----HSSLafpfTVEEVVALGraPHGSSAAQDRQIVREALALVglAHLAGRSYQ---TLSGGEQQRVQLARVLaq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 149 -----MSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLAN 223
Cdd:COG4559 151 lwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTD 230
|
....*..
gi 1540804698 224 EAVRSAY 230
Cdd:COG4559 231 ELLERVY 237
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-212 |
2.42e-32 |
|
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: 117.22 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHY----GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTS--RIM 74
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 75 REAVAIVP-EGRRVFS-RMTVEENLAMGGFFADRHQYQQRIERVFTLFPRLLERRSQRAG----TMSGGEQQMLAIGRAL 148
Cdd:cd03257 81 RKEIQMVFqDPMSSLNpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNryphELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 149 MSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-223 |
2.60e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 117.40 E-value: 2.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTS-RIMREAVA 79
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDiNKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSRMTVEENLAMG-----GffADRHQYQQR----IERVftlfpRLLERRSQRAGTMSGGEQQMLAIGRALMS 150
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLApikvkK--MSKAEAEERamelLERV-----GLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 151 QPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLAN 223
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-232 |
4.61e-32 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 116.92 E-value: 4.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 5 NQVSAHYGKiQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAIVPEG 84
Cdd:PRK10895 8 NLAKAYKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 85 RRVFSRMTVEENLAMGGFFADRHQYQQRIERVFTLFPR--LLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSL 162
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEfhIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 163 GLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVRSAYLG 232
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG 236
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-166 |
8.83e-32 |
|
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: 115.37 E-value: 8.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 7 VSAHYGKIQALHQVSLTISQGeIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSriMREAVAIVPEGRR 86
Cdd:cd03264 6 LTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK--LRRRIGYLPQEFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 87 VFSRMTVEENLA----MGGfFADRHQyQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSL 162
Cdd:cd03264 83 VYPNFTVREFLDyiawLKG-IPSKEV-KARVDEVLELV-NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
....
gi 1540804698 163 GLAP 166
Cdd:cd03264 160 GLDP 163
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-210 |
1.15e-31 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 114.02 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYG--KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRImREAVA 79
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL-RKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSrMTVEENLamggffadrhqyqqriervftlfprllerrsqragtMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:cd03228 80 YVPQDPFLFS-GTIRENI------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 160 PSLGLAPIIIQQIFDIIQQLReEGMTIFLVEQNANqALKLADRGYVLENGR 210
Cdd:cd03228 123 ATSALDPETEALILEALRALA-KGKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-212 |
1.54e-31 |
|
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: 115.41 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSrimREAVAIV 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH---KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEGRRVFSRMTVEENLAMGGFFA--DRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKklPKAEIKERVAEALDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 160 PSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-223 |
1.63e-31 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 120.39 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHY--GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCG---EPRASEGSIVFQGQDITQWqTSRIMR 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLEL-SEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 76 EAVAIVP-EGRRVFSRMTVEENLAMG--GFFADRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQP 152
Cdd:COG1123 83 RRIGMVFqDPMTQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAV-GLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540804698 153 KLLLLDEPSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLAN 223
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-228 |
2.49e-31 |
|
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: 115.09 E-value: 2.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQ-ALHQVSLTISQGEIVTLIGANGAGKTTLLGTL--CGEPraSEGSIVFQGQDITQWQTSRiMREAV 78
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrLIEP--TSGEIFIDGEDIREQDPVE-LRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 79 AIVPEGRRVFSRMTVEENLA----MGGFfaDRHQYQQRIERVFTLF----PRLLERRSqraGTMSGGEQQMLAIGRALMS 150
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIAlvpkLLKW--PKEKIRERADELLALVgldpAEFADRYP---HELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 151 QPKLLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALL---ANEAV 226
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILrspANDFV 232
|
..
gi 1540804698 227 RS 228
Cdd:cd03295 233 AE 234
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-227 |
2.71e-31 |
|
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: 114.69 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDItqWQTSRIMREAVAi 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDI--TGLSEKELYELR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 vpegRRV---------FSRMTVEENLAmggFFADRHQ---YQQRIERV------------FTLFPRLLerrsqragtmSG 136
Cdd:COG1127 82 ----RRIgmlfqggalFDSLTVFENVA---FPLREHTdlsEAEIRELVleklelvglpgaADKMPSEL----------SG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 137 GEQQMLAIGRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVLED 215
Cdd:COG1127 145 GMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
250
....*....|....
gi 1540804698 216 TGAALLA--NEAVR 227
Cdd:COG1127 225 TPEELLAsdDPWVR 238
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-230 |
5.66e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.48 E-value: 5.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSR------IM 74
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElarrraVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 75 REAVAIvpegrrVFSrMTVEENLAMGgffadRHQYQQRIERVFTLFPRLLER--------RSQRagTMSGGEQQMLAIGR 146
Cdd:PRK13548 82 PQHSSL------SFP-FTVEEVVAMG-----RAPHGLSRAEDDALVAAALAQvdlahlagRDYP--QLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 147 ALM------SQPKLLLLDEPSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAA 219
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
250
....*....|.
gi 1540804698 220 LLANEAVRSAY 230
Cdd:PRK13548 228 VLTPETLRRVY 238
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-232 |
1.11e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 112.93 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKiQALHqVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITqwqtsrimreavAI 80
Cdd:COG3840 1 MLRLDDLTYRYGD-FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT------------AL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRV---------FSRMTVEENLAMGgfF--------ADRHQYQQRIERVftlfpRLLERRSQRAGTMSGGEQQMLA 143
Cdd:COG3840 67 PPAERPVsmlfqennlFPHLTVAQNIGLG--LrpglkltaEQRAQVEQALERV-----GLAGLLDRLPGQLSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 144 IGRALMSQPKLLLLDEP--SLGLApiiiqqifdiiqqLREE------------GMTIFLVEQNANQALKLADRGYVLENG 209
Cdd:COG3840 140 LARCLVRKRPILLLDEPfsALDPA-------------LRQEmldlvdelcrerGLTVLMVTHDPEDAARIADRVLLVADG 206
|
250 260
....*....|....*....|....*
gi 1540804698 210 RVVLEDTGAALLANE--AVRSAYLG 232
Cdd:COG3840 207 RIAADGPTAALLDGEppPALAAYLG 231
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-212 |
1.53e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 115.56 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRimREaVAI 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RN-IAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENLAMG----GFfaDRHQYQQRIERVFTLF--PRLLERrsqRAGTMSGGEQQMLAIGRALMSQPKL 154
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPlklrKV--PKAEIDRRVREAAELLglEDLLDR---KPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 155 LLLDEPSLGLAPiiiqqifdiiqQLREE------------GMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:COG3839 155 FLLDEPLSNLDA-----------KLRVEmraeikrlhrrlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-224 |
3.00e-30 |
|
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: 117.17 E-value: 3.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHY-GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRImREAVAI 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW-RRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSrMTVEENLAMGGFFADRHQYQQRIERV-----FTLFPRLLERR-SQRAGTMSGGEQQMLAIGRALMSQPKL 154
Cdd:COG4988 416 VPQNPYLFA-GTIRENLRLGRPDASDEELEAALEAAgldefVAALPDGLDTPlGEGGRGLSGGQAQRLALARALLRDAPL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 155 LLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANqaLKLADRGYVLENGRVVLEDTGAALLANE 224
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLAL--LAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-214 |
4.39e-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: 112.11 E-value: 4.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHY----GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMre 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGV-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 77 avaiVPEGRRVFSRMTVEENLAMG----GffADRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQP 152
Cdd:COG1116 85 ----VFQEPALLPWLTVLDNVALGlelrG--VPKAERRERARELLELV-GLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 153 KLLLLDEP---------------SLGLapiiiqqifdiiqqLREEGMTIFLVEQNANQALKLADRGYVLEN--GRVVLE 214
Cdd:COG1116 158 EVLLMDEPfgaldaltrerlqdeLLRL--------------WQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
17-212 |
5.56e-30 |
|
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: 111.27 E-value: 5.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWqtSRIMREaVAIVPEGRRVFSRMTVEEN 96
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL--PPEKRD-ISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 97 LAmggfFADRHQYQQRIE---RV-----FTLFPRLLERRsqrAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPII 168
Cdd:cd03299 92 IA----YGLKKRKVDKKEierKVleiaeMLGIDHLLNRK---PETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1540804698 169 IQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:cd03299 165 KEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-224 |
7.47e-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: 116.47 E-value: 7.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYG--KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTsRIMREAVA 79
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDP-ASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSRmTVEENLAMGGFFADrhqyQQRIERVFTL---------FPRLLERR-SQRAGTMSGGEQQMLAIGRALM 149
Cdd:COG2274 553 VVLQDVFLFSG-TIRENITLGDPDAT----DEEIIEAARLaglhdfieaLPMGYDTVvGEGGSNLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 150 SQPKLLLLDEPSLGLAPIIIQQIFDIIQQLReEGMTIFLVEQNAnQALKLADRGYVLENGRVVLEDTGAALLANE 224
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-222 |
9.58e-30 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 113.28 E-value: 9.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 20 VSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGqdiTQWQTSR------IMREAVAIVPEGRRVFSRMTV 93
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG---RTLFDSRkgiflpPEKRRIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 94 EENLAMGGFFADRHQYQQRIERVFTLF--PRLLERRSqraGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPIIIQQ 171
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFERVIELLgiGHLLGRLP---GRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1540804698 172 IFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLA 222
Cdd:TIGR02142 170 ILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-223 |
1.82e-29 |
|
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: 109.98 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVS----AHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTS--RIM 74
Cdd:cd03258 1 MIELKNVSkvfgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 75 REAVAIVPEGRRVFSRMTVEENLA----MGGffADRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMS 150
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAlpleIAG--VPKAEIEERVLELLELV-GLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 151 QPKLLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLAN 223
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-212 |
2.47e-29 |
|
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: 109.13 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQ--ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwQTSRIMREaVA 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQS-LG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSRMTVEENLAmggFFA-----DRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKL 154
Cdd:cd03263 79 YCPQFDALFDELTVREHLR---FYArlkglPKSEIKEEVELLLRVL-GLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540804698 155 LLLDEPSLGLAPIIIQQIFDIIQQLReEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-212 |
6.26e-29 |
|
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: 108.06 E-value: 6.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 4 FNQVSAHY--GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREaVAIV 81
Cdd:cd03245 5 FRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN-IGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEGRRVFSRmTVEENLAMGGFFADrhqyQQRIERVFTL---------FPRLLERR-SQRAGTMSGGEQQMLAIGRALMSQ 151
Cdd:cd03245 84 PQDVTLFYG-TLRDNITLGAPLAD----DERILRAAELagvtdfvnkHPNGLDLQiGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 152 PKLLLLDEPSLGLapiIIQQIFDIIQQLRE--EGMTIFLVEQNaNQALKLADRGYVLENGRVV 212
Cdd:cd03245 159 PPILLLDEPTSAM---DMNSEERLKERLRQllGDKTLIIITHR-PSLLDLVDRIIVMDSGRIV 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-212 |
1.03e-28 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 107.58 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKiQALHqVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITqwqTSRIMREAVAIV 81
Cdd:cd03298 1 VRLDKIRFSYGE-QPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT---AAPPADRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEGRRVFSRMTVEENLAMGGFFADRHQYQQRiERVFTLFPR--LLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:cd03298 76 FQENNLFAHLTVEQNVGLGLSPGLKLTAEDR-QAIEVALARvgLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 160 PSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-223 |
1.29e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 110.24 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDitqWQTSRIMREavaiv 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD---LFTNLPPRE----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 pegRRV---------FSRMTVEENLAMG--GFFADRHQYQQRIERVFTLFpRL--LERR--SQragtMSGGEQQMLAIGR 146
Cdd:COG1118 75 ---RRVgfvfqhyalFPHMTVAENIAFGlrVRPPSKAEIRARVEELLELV-QLegLADRypSQ----LSGGQRQRVALAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 147 ALMSQPKLLLLDEPsLG-----LAPiiiqqifdiiqQLREE---------GMTIFlVEQNANQALKLADRGYVLENGRVV 212
Cdd:COG1118 147 ALAVEPEVLLLDEP-FGaldakVRK-----------ELRRWlrrlhdelgGTTVF-VTHDQEEALELADRVVVMNQGRIE 213
|
250
....*....|.
gi 1540804698 213 LEDTGAALLAN 223
Cdd:COG1118 214 QVGTPDEVYDR 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-212 |
1.95e-28 |
|
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: 106.57 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 7 VSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRimREaVAIVPEGRR 86
Cdd:cd03301 6 VTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RD-IAMVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 87 VFSRMTVEENLAMGgfFADRHQYQQRIERVFTLFPRLL---ERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLG 163
Cdd:cd03301 83 LYPHMTVYDNIAFG--LKLRKVPKDEIDERVREVAELLqieHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1540804698 164 L-APIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:cd03301 161 LdAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-211 |
2.09e-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: 107.43 E-value: 2.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 7 VSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwqtSRIMREAVAIVPEGRR 86
Cdd:cd03296 8 VSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD---VPVQERNVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 87 VFSRMTVEENLAMG------GFFADRHQYQQRIERVFTLFpRL--LERR--SQragtMSGGEQQMLAIGRALMSQPKLLL 156
Cdd:cd03296 85 LFRHMTVFDNVAFGlrvkprSERPPEAEIRAKVHELLKLV-QLdwLADRypAQ----LSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 157 LDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRV 211
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-225 |
4.42e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 111.01 E-value: 4.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHY--GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRImREAVA 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL-RRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSrMTVEENLAMGGFFADRHQYQQRIERVftlfpRLLER-RSQRAG----------TMSGGEQQMLAIGRAL 148
Cdd:COG4987 413 VVPQRPHLFD-TTLRENLRLARPDATDEELWAALERV-----GLGDWlAALPDGldtwlgeggrRLSGGERRRLALARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 149 MSQPKLLLLDEPSLGLAPiiiQQIFDIIQQLRE--EGMTIFLVEQNAnQALKLADRGYVLENGRVVLEDTGAALLANEA 225
Cdd:COG4987 487 LRDAPILLLDEPTEGLDA---ATEQALLADLLEalAGRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-164 |
1.38e-27 |
|
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: 105.55 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGE-PRASEGSIVFQGQDITQWQTSRImREAVA 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWEL-RKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IV-PE-GRRVFSRMTVEEnLAMGGFFA--DRHQY-----QQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMS 150
Cdd:COG1119 82 LVsPAlQLRFPRDETVLD-VVLSGFFDsiGLYREptdeqRERARELLELL-GLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170
....*....|....
gi 1540804698 151 QPKLLLLDEPSLGL 164
Cdd:COG1119 160 DPELLILDEPTAGL 173
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-212 |
2.30e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 105.12 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCG----EPRAS-EGSIVFQGQDITQWQTSrimre 76
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndlIPGARvEGEILLDGEDIYDPDVD----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 77 avaiVPEGRR----VFSR-----MTVEENLAMG----GFfADRHQYQQRIERVFT---LFPRLLERRSQRAGTMSGGEQQ 140
Cdd:COG1117 87 ----VVELRRrvgmVFQKpnpfpKSIYDNVAYGlrlhGI-KSKSELDEIVEESLRkaaLWDEVKDRLKKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540804698 141 MLAIGRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEgMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-212 |
2.58e-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: 103.91 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 19 QVSLTISqGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGqdiTQWQTSRImreAVAIVPEGRRV---------FS 89
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG---TVLFDSRK---KINLPPQQRKIglvfqqyalFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 90 RMTVEENLAMGGFFADRHQYQQRIERVFTLF--PRLLERRSQragTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGL-AP 166
Cdd:cd03297 89 HLNVRENLAFGLKRKRNREDRISVDELLDLLglDHLLNRYPA---QLSGGEKQRVALARALAAQPELLLLDEPFSALdRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1540804698 167 IIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:cd03297 166 LRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-212 |
3.42e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 104.32 E-value: 3.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGT--LCGEPRASEGSIVFQGQDITQW---QTSRIMRE 76
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVlnLLETPDSGQLNIAGHQFDFSQKpseKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 77 AVAIVPEGRRVFSRMTVEENLAMGGFFADRHQYQQRIERVFTLFPRL-LERRSQR-AGTMSGGEQQMLAIGRALMSQPKL 154
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLrLTDKADRfPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540804698 155 LLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
3.51e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 105.66 E-value: 3.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwqTSRIMREAVAIV 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS--RARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEGRRVFSRMTVEENLAMGGFFADRHQYQQRiERVFTL--FPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAAR-ALVPPLleFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 160 PSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANE 224
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
19-229 |
3.54e-27 |
|
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: 106.72 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 19 QVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDitqWQTSRimrEAVAIVPEGRRV---------FS 89
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV---LQDSA---RGIFLPPHRRRIgyvfqearlFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 90 RMTVEENLAMGGFFADRHQYQQRIERVFTLF--PRLLERRsqrAGTMSGGEQQMLAIGRALMSQPKLLLLDEP--SLGLA 165
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERRISFDEVVELLgiGHLLDRR---PATLSGGERQRVAIGRALLSSPRLLLMDEPlaALDLA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 166 ------PiiiqqifdIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVRSA 229
Cdd:COG4148 168 rkaeilP--------YLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPL 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-212 |
4.45e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 103.94 E-value: 4.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGT--LCGEPRASEGSIV---FQGQDITQWQTSRIMRE 76
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVlnLLEMPRSGTLNIAgnhFDFSKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 77 AVAIVPEGRRVFSRMTVEENLAMGGFFADRHQYQQRIERVFTLFPRLleRRSQRAGT----MSGGEQQMLAIGRALMSQP 152
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERL--RLKPYADRfplhLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 153 KLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-212 |
5.33e-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: 102.72 E-value: 5.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 10 HYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQtsriMREAVAIVP-EGRRVF 88
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE----RRKSIGYVMqDVDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 89 SRMTVEENLAMGGffADRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPII 168
Cdd:cd03226 85 FTDSVREELLLGL--KELDAGNEQAETVLKDL-DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1540804698 169 IQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:cd03226 162 MERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-211 |
1.93e-26 |
|
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: 100.58 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 16 ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAIVPEGRR---VFSRMT 92
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPEDRKregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 93 VEENLAMggffadrhqyqqriervftlfPRLLerrsqragtmSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPIIIQQI 172
Cdd:cd03215 95 VAENIAL---------------------SSLL----------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEI 143
|
170 180 190
....*....|....*....|....*....|....*....
gi 1540804698 173 FDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRV 211
Cdd:cd03215 144 YRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-219 |
1.93e-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: 102.13 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHY----GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQW---QTSRI 73
Cdd:COG4181 8 IIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 74 MREAVAIVPEGRRVFSRMTVEENLAMGGFFADRHQYQQR----IERVftlfpRLLERRSQRAGTMSGGEQQMLAIGRALM 149
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARaralLERV-----GLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 150 SQPKLLLLDEPSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKlADRGYVLENGRVVLEDTGAA 219
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-223 |
2.20e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.88 E-value: 2.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAI 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENLAMG-----GFFADRHQYQQRIERV-----FTLFPRllerrsQRAGTMSGGEQQMLAIGRALMS 150
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGleptkGGRLDRKAARARIRELserygLDVDPD------AKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540804698 151 QPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV----LEDTGAALLAN 223
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVgtvdTAETSEEELAE 235
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-211 |
3.86e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 103.87 E-value: 3.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwqtsrimreavaIV 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH------------VP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEGRRV---------FSRMTVEENLAmggfFADRHQY--QQRIE-RVF-TLFPRLLERRSQRAGT-MSGGEQQMLAIGRA 147
Cdd:PRK09452 83 AENRHVntvfqsyalFPHMTVFENVA----FGLRMQKtpAAEITpRVMeALRMVQLEEFAQRKPHqLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 148 LMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRV 211
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-211 |
7.07e-26 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 100.17 E-value: 7.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 4 FNQVSAHY-GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRI--MREAVAI 80
Cdd:cd03292 3 FINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpyLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENLAmggfFADR---HQYQQRIERVFTLFPRL-LERRSQR-AGTMSGGEQQMLAIGRALMSQPKLL 155
Cdd:cd03292 83 VFQDFRLLPDRNVYENVA----FALEvtgVPPREIRKRVPAALELVgLSHKHRAlPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 156 LLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRV 211
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-223 |
1.01e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 104.48 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHY-GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRImREAVAI 80
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL-RRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRmTVEENLAMGGFFADRHQYQQ-----RIERVFTLFPRLLERR-SQRAGTMSGGEQQMLAIGRALMSQPKL 154
Cdd:COG1132 419 VPQDTFLFSG-TIRENIRYGRPDATDEEVEEaakaaQAHEFIEALPDGYDTVvGERGVNLSGGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 155 LLLDEPSLGLAPIIIQQIFDIIQQLReEGMTIFLVeqnanqA-----LKLADRGYVLENGRVVLEDTGAALLAN 223
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLM-KGRTTIVI------AhrlstIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-224 |
1.69e-25 |
|
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: 98.75 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEP--RASEGSIVFQGQDITQwqtsrimreava 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITD------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 ivpegrrvfsrMTVEENLAMGGFFAdrHQYQQRIERVFTLFprLLerRSQRAGtMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:cd03217 69 -----------LPPEERARLGIFLA--FQYPPEIPGVKNAD--FL--RYVNEG-FSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 160 PSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKL-ADRGYVLENGRVVLEdtGAALLANE 224
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKS--GDKELALE 194
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-221 |
2.60e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.45 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwqTSRIMREAVAIV 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA--RARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEGRRVFSRMTVEENLAMGGFFADRHQyqQRIERVFTL---FPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLD 158
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFGMST--REIEAVIPSlleFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 159 EPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALL 221
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-212 |
4.75e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.41 E-value: 4.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 16 ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAIVPEGRR---VFSRMT 92
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAYIPEDRLgrgLVPDMS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 93 VEENLAMGgffadrHQYQQRIERVFTLFPRLLERRSQR---------------AGTMSGGEQQMLAIGRALMSQPKLLLL 157
Cdd:COG3845 353 VAENLILG------RYRRPPFSRGGFLDRKAIRAFAEElieefdvrtpgpdtpARSLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 158 DEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:COG3845 427 AQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-212 |
5.91e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 100.15 E-value: 5.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHY----GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTS--RIM 74
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 75 REAVAIVPEGRRVFSRMTVEENLAM-----GgffADRhqyQQRIERVFTLFPR--LLERRSQRAGTMSGGEQQMLAIGRA 147
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALpleiaG---VPK---AEIRKRVAELLELvgLSDKADAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 148 LMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
7.47e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.91 E-value: 7.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGK-IQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVA 79
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IV---PEGRrvFSRMTVEENLAMG--GFFADRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKL 154
Cdd:PRK13644 81 IVfqnPETQ--FVGRTVEEDLAFGpeNLCLPPIEIRKRVDRALAEI-GLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540804698 155 LLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQaLKLADRGYVLENGRVVLEDTGAALLANEAVRsaYLG 232
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ--TLG 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-222 |
1.41e-24 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 96.91 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 4 FNQVSAHY-GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRiMREAVAIVP 82
Cdd:cd03254 5 FENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS-LRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 83 EGRRVFSRmTVEENLAMGGFFADRHQYQQRIERV-FTLFPRLLER-----RSQRAGTMSGGEQQMLAIGRALMSQPKLLL 156
Cdd:cd03254 84 QDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAgAHDFIMKLPNgydtvLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 157 LDEPSLGLAPIIIQQIFDIIQQLReEGMTIFLVEQNANqALKLADRGYVLENGRVVLEDTGAALLA 222
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-212 |
2.31e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.14 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQ---WQTS-RIMRE 76
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvppYQRPiNMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 77 AVAIVPEgrrvfsrMTVEENLAMgGFFADR---HQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPK 153
Cdd:PRK11607 99 SYALFPH-------MTVEQNIAF-GLKQDKlpkAEIASRVNEMLGLV-HMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 154 LLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-209 |
4.03e-24 |
|
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: 96.00 E-value: 4.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRImreavaIVPEGRRVFSRMTVEEN 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM------VVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 97 --LAMGGFFADRHQYQQR--IERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGL-APIIIQQ 171
Cdd:TIGR01184 75 iaLAVDRVLPDLSKSERRaiVEEHIALV-GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALdALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1540804698 172 IFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENG 209
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-232 |
9.18e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.03 E-value: 9.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYgkiQALH-QVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITqwqTSRIMREAVA 79
Cdd:PRK10771 1 MLKLTDITWLY---HHLPmRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT---TTPPSRRPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSRMTVEENLAMG---GF---FADRHQYQQRIERVF--TLFPRLlerrsqrAGTMSGGEQQMLAIGRALMSQ 151
Cdd:PRK10771 75 MLFQENNLFSHLTVAQNIGLGlnpGLklnAAQREKLHAIARQMGieDLLARL-------PGQLSGGQRQRVALARCLVRE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 152 PKLLLLDEPSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVRSAY 230
Cdd:PRK10771 148 QPILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASAL 227
|
..
gi 1540804698 231 LG 232
Cdd:PRK10771 228 LG 229
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-202 |
1.73e-23 |
|
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: 93.45 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 7 VSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQD---ITQWQTSRIMREAVAIVPE 83
Cdd:TIGR03608 4 ISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQEtppLNSKKASKFRREKLGYLFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 84 GRRVFSRMTVEENLAMGGFFADRHQYQQRIERVFTL-FPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSL 162
Cdd:TIGR03608 84 NFALIENETVEENLDLGLKYKKLSKKEKREKKKEALeKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1540804698 163 GLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQAlKLADR 202
Cdd:TIGR03608 164 SLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADR 202
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-211 |
2.17e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 96.31 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 5 NQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDItqwqtSRI-MRE-AVAIVP 82
Cdd:PRK10851 6 ANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-----SRLhARDrKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 83 EGRRVFSRMTVEENLAMGGFFADRHQ------YQQRIERVFTL--FPRLLERR-SQragtMSGGEQQMLAIGRALMSQPK 153
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTVLPRRErpnaaaIKAKVTQLLEMvqLAHLADRYpAQ----LSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 154 LLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRV 211
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-230 |
3.26e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREaVAI 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENLAMGgffadRHQYQQRIERVFTLFPRLLERRSQRAG----------TMSGGEQQMLAIGRALMS 150
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMG-----RTPHRSRFDTWTETDRAAVERAMERTGvaqfadrpvtSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 151 QPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVRSAY 230
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAF 236
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-216 |
3.30e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.07 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTL--CGE--PRAS-EGSIVFQGQDITQWQTSRI-M 74
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDlnPEVTiTGSIVYNGHNIYSPRTDTVdL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 75 REAVAIVPEGRRVFSrMTVEENLAMGGFFA---DRHQYQQRIERVF---TLFPRLLERRSQRAGTMSGGEQQMLAIGRAL 148
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGLRLKgikDKQVLDEAVEKSLkgaSIWDEVKDRLHDSALGLSGGQQQRVCIARVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 149 MSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEgMTIFLVEQNANQALKLADR-GYVLENGRVVLEDT 216
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRtGFFLDGDLIEYNDT 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-164 |
3.64e-23 |
|
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: 96.97 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHY-GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWqTSRIMREAVAI 80
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA-DADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRmTVEENLAMGGFFADRHQYQQRIERVFTL-----FPRLLERRSQRAGTM-SGGEQQMLAIGRALMSQPKL 154
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARPDASDAEIREALERAGLDefvaaLPQGLDTPIGEGGAGlSGGQAQRLALARAFLRDAPL 479
|
170
....*....|
gi 1540804698 155 LLLDEPSLGL 164
Cdd:TIGR02857 480 LLLDEPTAHL 489
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-226 |
1.63e-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: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGK--IQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLcgePR---ASEGSIVFQGQDITQWQTSRiMRE 76
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI---PRfydVDSGRILIDGHDVRDYTLAS-LRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 77 AVAIVPEGRRVFSRmTVEENLAMGGFFADRHQY---------QQRIERvftlFPRLLERR-SQRAGTMSGGEQQMLAIGR 146
Cdd:cd03251 77 QIGLVSQDVFLFND-TVAENIAYGRPGATREEVeeaaraanaHEFIME----LPEGYDTViGERGVKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 147 ALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLrEEGMTIFLVEQNANqALKLADRGYVLENGRVVLEDTGAALLANEAV 226
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELLAQGGV 229
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-216 |
2.46e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 91.61 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWqTSRIMREAVAI 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML-SSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENLAMG--------GFFA--DRHQYQQRIERVftlfpRLLERRSQRAGTMSGGEQQMLAIGRALMS 150
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGrspwlslwGRLSaeDNARVNQAMEQT-----RINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 151 QPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDT 216
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-160 |
2.47e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 91.85 E-value: 2.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGK----IQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwqtsrimre 76
Cdd:COG4525 3 MLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 77 avaivPEGRR--VFSR------MTVEENLAMGGFFA--DRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGR 146
Cdd:COG4525 74 -----PGADRgvVFQKdallpwLNVLDNVAFGLRLRgvPKAERRARAEELLALV-GLADFARRRIWQLSGGMRQRVGIAR 147
|
170
....*....|....
gi 1540804698 147 ALMSQPKLLLLDEP 160
Cdd:COG4525 148 ALAADPRFLLMDEP 161
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-160 |
2.99e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 90.23 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCG--EPRAS-EGSIVFQGQDITqwqtsrimrea 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtlSPAFSaSGEVLLNGRRLT----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 78 vAIVPEGRRV---------FSRMTVEENLAMGgfFADRHQYQQRIERVFTLFPRL-LERRSQRA-GTMSGGEQQMLAIGR 146
Cdd:COG4136 70 -ALPAEQRRIgilfqddllFPHLSVGENLAFA--LPPTIGRAQRRARVEQALEEAgLAGFADRDpATLSGGQRARVALLR 146
|
170
....*....|....
gi 1540804698 147 ALMSQPKLLLLDEP 160
Cdd:COG4136 147 ALLAEPRALLLDEP 160
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-212 |
3.73e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 91.13 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 11 YGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGT------LCGEPRAsEGSIVFQGQDITQWQTSRiMREAVAIVPEG 84
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlieLYPEARV-SGEVYLDGQDIFKMDVIE-LRRRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 85 RRVFSRMTVEENLAMG----GFFADRHQYQQRIERVF---TLFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLL 157
Cdd:PRK14247 91 PNPIPNLSIFENVALGlklnRLVKSKKELQERVRWALekaQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 158 DEPSLGLAPIIIQQIFDIIQQLREEgMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-220 |
4.98e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.54 E-value: 4.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 16 ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAIVPEGRR---VFSRMT 92
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAYVPEDRKgegLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 93 VEENLAMG-------GFFADRHQYQQRIERVFTLF----PRLlerrSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPS 161
Cdd:COG1129 347 IRENITLAsldrlsrGGLLDRRRERALAEEYIKRLriktPSP----EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 162 LG---------------LApiiiqqifdiiqqlrEEGMTIFLV-----EqnanqALKLADRGYVLENGRVVLEDTGAAL 220
Cdd:COG1129 423 RGidvgakaeiyrlireLA---------------AEGKAVIVIsselpE-----LLGLSDRILVMREGRIVGELDREEA 481
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-212 |
5.92e-22 |
|
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: 93.35 E-value: 5.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCG-EPRAS-EGSIVFQGQDITQWQTSRIMREAV 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvYPHGTwDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 79 AIVPEGRRVFSRMTVEENLAMGGFF---ADRHQYQQRIERVFTLFPRL---LERRSQRAGTMSGGEQQMLAIGRALMSQP 152
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEItlpGGRMAYNAMYLRAKNLLRELqldADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 153 KLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-216 |
6.44e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 91.26 E-value: 6.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 16 ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTS-RIMREAVAIV---PEgRRVFSRm 91
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlSDIRKKVGLVfqyPE-YQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 92 TVEENLAMG----GFFADrhQYQQRIERVFTLFPRLLERRSQRAG-TMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAP 166
Cdd:PRK13637 100 TIEKDIAFGpinlGLSEE--EIENRVKRAMNIVGLDYEDYKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 167 IIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVLEDT 216
Cdd:PRK13637 178 KGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-214 |
7.08e-22 |
|
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: 88.52 E-value: 7.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYG--KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSriMREAVA 79
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA--LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSrMTVEENLAmggffadrhqyqqriervftlfprlleRRsqragtMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:cd03247 79 VLNQRPYLFD-TTLRNNLG---------------------------RR------FSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 160 PSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQnaNQALKLADRGYVLENGRVVLE 214
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLKDKTLIWITHH--LTGIEHMDKILFLENGKIIMQ 177
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-228 |
1.87e-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: 89.63 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 5 NQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCG--EPraSEGSIVFQGQDITQW---QTSRIMREAVA 79
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRliEP--TSGKVLIDGQDIAAMsrkELRELRRKKIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSRMTVEENLAMGGFFA--DRHQYQQRIERVFTLFPrLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLL 157
Cdd:cd03294 106 MVFQSFALLPHRTVLENVAFGLEVQgvPRAEREERAAEALELVG-LEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 158 DEPSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALL---ANEAVRS 228
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILtnpANDYVRE 259
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
15-231 |
4.00e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 88.98 E-value: 4.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 15 QALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRI-MREAVAIV---PEGrRVFSR 90
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLeVRKTVGIVfqnPDD-QLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 91 mTVEENLAMG----GFFADRHQyqqriERVFTLFPRL-LERRSQRA-GTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGL 164
Cdd:PRK13639 95 -TVEEDVAFGplnlGLSKEEVE-----KRVKEALKAVgMEGFENKPpHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540804698 165 APIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLAN-EAVRSAYL 231
Cdd:PRK13639 169 DPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDiETIRKANL 236
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-161 |
4.07e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.62 E-value: 4.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVS-AHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRI--MREA 77
Cdd:PRK10908 1 MIRFEHVSkAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 78 VAIVPEGRRVFSRMTVEENLAMGGFFADRHQYQQRiERVFTLFPR--LLERRSQRAGTMSGGEQQMLAIGRALMSQPKLL 155
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIR-RRVSAALDKvgLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
....*.
gi 1540804698 156 LLDEPS 161
Cdd:PRK10908 160 LADEPT 165
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-212 |
4.37e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAI 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENLAMGgffadRH-----------QYQQRIERVFTLFPRLLERRS--QRAGTMSGGEQQMLAIGRA 147
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIG-----RHltkkvcgvniiDWREMRVRAAMMLLRVGLKVDldEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 148 LMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-201 |
5.31e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 88.30 E-value: 5.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 7 VSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLL------GTLCGEPRAsEGSIVFQGQDITQWQTSRI-MREAVA 79
Cdd:PRK14243 16 LNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlNDLIPGFRV-EGKVTFHGKNLYAPDVDPVeVRRRIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSRmTVEENLAMG----GFFADRHQYQQRIERVFTLFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLL 155
Cdd:PRK14243 95 MVFQKPNPFPK-SIYDNIAYGarinGYKGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1540804698 156 LLDEPSLGLAPIIIQQIFDIIQQLREEgMTIFLVEQNANQALKLAD 201
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-230 |
5.93e-21 |
|
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: 87.70 E-value: 5.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEP--RASEGSIVFQGQDITQWQTSRIMREAVA 79
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPsyEVTSGTILFKGQDLLELEPDERARAGLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 I-------VP------------EGRRvfsRMTVEENLAMGGFfadRHQYQQRIERVftLFPRLLERRSQRAGtMSGGEQQ 140
Cdd:TIGR01978 81 LafqypeeIPgvsnleflrsalNARR---SARGEEPLDLLDF---EKLLKEKLALL--DMDEEFLNRSVNEG-FSGGEKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 141 MLAIGRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNaNQALKL--ADRGYVLENGRVVLEdtGA 218
Cdd:TIGR01978 152 RNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHY-QRLLNYikPDYVHVLLDGRIVKS--GD 228
|
250
....*....|..
gi 1540804698 219 ALLANEAVRSAY 230
Cdd:TIGR01978 229 VELAKELEAKGY 240
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-166 |
7.12e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 90.57 E-value: 7.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 7 VSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDItqwqTSRIMREAV----AIVP 82
Cdd:NF033858 7 VSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM----ADARHRRAVcpriAYMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 83 E--GRRVFSRMTVEENLAmggFFA-----DRHQYQQRIERVFT---LFPrLLERrsqRAGTMSGGEQQMLAIGRALMSQP 152
Cdd:NF033858 83 QglGKNLYPTLSVFENLD---FFGrlfgqDAAERRRRIDELLRatgLAP-FADR---PAGKLSGGMKQKLGLCCALIHDP 155
|
170
....*....|....
gi 1540804698 153 KLLLLDEPSLGLAP 166
Cdd:NF033858 156 DLLILDEPTTGVDP 169
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-160 |
1.05e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.12 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 4 FNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQG--------QDITQWQTSRIMR 75
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 76 EAVAIVPEGRRVFSRM-TVEENLAMGGFFADR-------------HQYQQRIERVFT-L-FPRllERRSQRAGTMSGGEQ 139
Cdd:COG0488 81 TVLDGDAELRALEAELeELEAKLAEPDEDLERlaelqeefealggWEAEARAEEILSgLgFPE--EDLDRPVSELSGGWR 158
|
170 180
....*....|....*....|.
gi 1540804698 140 QMLAIGRALMSQPKLLLLDEP 160
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEP 179
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-224 |
1.19e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 89.88 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHY--GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRiMREAVA 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA-LRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSRmTVEENLAMGGFFADRHQYQQRIERVFtlFPRLLErrsQRAG----------TMSGGEQQMLAIGRALM 149
Cdd:PRK11160 418 VVSQRVHLFSA-TLRDNLLLAAPNASDEALIEVLQQVG--LEKLLE---DDKGlnawlgeggrQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540804698 150 SQPKLLLLDEPSLGLAPiiiQQIFDIIQQLRE--EGMTIFLVEQNANqALKLADRGYVLENGRVVLEDTGAALLANE 224
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDA---ETERQILELLAEhaQNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQELLAQQ 564
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-230 |
1.46e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 87.15 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREaVAIVPEGRRVFSRMTVEEN 96
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 97 LAMG--------GFF--ADRHQYQQRIERVfTLFP---RLLErrsqragTMSGGEQQMLAIGRALMSQPKLLLLDEPSLG 163
Cdd:PRK10575 106 VAIGrypwhgalGRFgaADREKVEEAISLV-GLKPlahRLVD-------SLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540804698 164 LAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVRSAY 230
Cdd:PRK10575 178 LDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-223 |
1.70e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.95 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTS---------- 71
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 72 --RIMREAVAIVPEGRRVFSRMTVEENLAMGGFFADRHQYQQRIER-VFTLFPRLLERRSQRA--GTMSGGEQQMLAIGR 146
Cdd:PRK10619 86 qlRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERaVKYLAKVGIDERAQGKypVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540804698 147 ALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLAN 223
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
13-162 |
2.17e-20 |
|
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: 85.95 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 13 KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQ----DITQWQTSRIM---REAVAIVPEGR 85
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPREILalrRRTIGYVSQFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 86 RVFSRMT----VEENL-AMGgffADRHQYQQRIERVFTLFpRLLERRSQRA-GTMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:COG4778 103 RVIPRVSaldvVAEPLlERG---VDREEARARARELLARL-NLPERLWDLPpATFSGGEQQRVNIARGFIADPPLLLLDE 178
|
....*
gi 1540804698 160 P--SL 162
Cdd:COG4778 179 PtaSL 183
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-212 |
2.46e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.81 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDItQWQTSRIMREA-VAI 80
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-RFASTTAALAAgVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 -------VPEgrrvfsrMTVEENLAMGGF-----FADRHQYQQRIErvftlfpRLLER------RSQRAGTMSGGEQQML 142
Cdd:PRK11288 84 iyqelhlVPE-------MTVAENLYLGQLphkggIVNRRLLNYEAR-------EQLEHlgvdidPDTPLKYLSIGQRQMV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 143 AIGRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYV 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
15-229 |
2.53e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 86.71 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 15 QALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwQTSRIMREAVAIV---PEGrRVFSrM 91
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA-ENEKWVRSKVGLVfqdPDD-QVFS-S 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 92 TVEENLAMG--GFFADRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPIII 169
Cdd:PRK13647 96 TVWDDVAFGpvNMGLDKDEVERRVEEALKAV-RMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 170 QQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDtGAALLANEAVRSA 229
Cdd:PRK13647 175 ETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDEDIVEQ 233
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-211 |
2.90e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 88.52 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAIVPEGRR---VFSRMTV 93
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 94 EENLAM--------GGFFADRHQYQQRIERVFTLFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLA 165
Cdd:PRK10762 348 KENMSLtalryfsrAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1540804698 166 PIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRV 211
Cdd:PRK10762 428 VGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-211 |
4.00e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.83 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 6 QVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCG---EPRASEGSIVFQGQDIT-QWQTSRIMREAVA-- 79
Cdd:PRK09984 9 KLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitGDKSAGSHIELLGRTVQrEGRLARDIRKSRAnt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 -IVPEGRRVFSRMTVEENLAMGGFFAD-------RHQYQQRIERVFTLFPR--LLERRSQRAGTMSGGEQQMLAIGRALM 149
Cdd:PRK09984 89 gYIFQQFNLVNRLSVLENVLIGALGSTpfwrtcfSWFTREQKQRALQALTRvgMVHFAHQRVSTLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 150 SQPKLLLLDEPSLGLAPIIIQQIFDIIQQLRE-EGMTIFLVEQNANQALKLADRGYVLENGRV 211
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-230 |
4.12e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 85.52 E-value: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREaVAI 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKR-LAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENLAMGGF--------FADRHQYQQRIERvFTLFP---RLLErrsqragTMSGGEQQMLAIGRALM 149
Cdd:COG4604 80 LRQENHINSRLTVRELVAFGRFpyskgrltAEDREIIDEAIAY-LDLEDladRYLD-------ELSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 150 SQPKLLLLDEP--------SLGLapiiiqqifdiIQQLR----EEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTG 217
Cdd:COG4604 152 QDTDYVLLDEPlnnldmkhSVQM-----------MKLLRrladELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTP 220
|
250
....*....|...
gi 1540804698 218 AALLANEAVRSAY 230
Cdd:COG4604 221 EEIITPEVLSDIY 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-216 |
4.59e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 86.78 E-value: 4.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHY----GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTS--RIM 74
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 75 REAVAIVPEGRRVFSRMTVEENLAMGGFFADRHqyQQRIE-RVFTLFPR--LLERRSQRAGTMSGGEQQMLAIGRALMSQ 151
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTP--KAEIKaRVTELLELvgLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 152 PKLLLLDEPSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDT 216
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
15-223 |
4.63e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 85.57 E-value: 4.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 15 QALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSI------VFQGQDITQWQTS-RIMREAVAIVPEGRRV 87
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLSQQKGLiRQLRQHVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 88 FSRMTVEENLAMGGFFADRHQYQQRIERVFTLFPR--LLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLA 165
Cdd:PRK11264 97 FPHRTVLENIIEGPVIVKGEPKEEATARARELLAKvgLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540804698 166 PIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLAN 223
Cdd:PRK11264 177 PELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-216 |
5.33e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.01 E-value: 5.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 12 GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwQTSRIMREAVAIVPEG--RRVFS 89
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-ENIREVRKFVGLVFQNpdDQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 90 RmTVEENLAMG--GFFADRHQYQQRIERVFTLFPrLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPI 167
Cdd:PRK13652 94 P-TVEQDIAFGpiNLGLDEETVAHRVSSALHMLG-LEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1540804698 168 IIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVLEDT 216
Cdd:PRK13652 172 GVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGT 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-215 |
5.53e-20 |
|
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: 84.89 E-value: 5.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 11 YGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDitqwqtSRIMREAVAIVPEgrrvfsr 90
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV------SSLLGLGGGFNPE------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 91 MTVEENLAMGGFF--ADRHQYQQRIERVFTlFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEpslGLA--- 165
Cdd:cd03220 99 LTGRENIYLNGRLlgLSRKEIDEKIDEIIE-FSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE---VLAvgd 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1540804698 166 PIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLED 215
Cdd:cd03220 175 AAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
6.06e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.67 E-value: 6.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGK-IQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDItQWQTSRIM--REA 77
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMklRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 78 VAIV---PEgRRVFSrMTVEENLAMG--GFFADRHQYQQRIERVftlfprlLER------RSQRAGTMSGGEQQMLAIGR 146
Cdd:PRK13636 84 VGMVfqdPD-NQLFS-ASVYQDVSFGavNLKLPEDEVRKRVDNA-------LKRtgiehlKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 147 ALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLAN-E 224
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEkE 234
|
....*..
gi 1540804698 225 AVRSAYL 231
Cdd:PRK13636 235 MLRKVNL 241
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-227 |
9.35e-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: 84.86 E-value: 9.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHY---------GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTS 71
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 72 --RIMREAVAIVPEG--RRVFSRMTVEENLAMGGFFADRHQYQQRIERVFTLFpRLLERRS----QRAGTMSGGEQQMLA 143
Cdd:TIGR02769 82 qrRAFRRDVQLVFQDspSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELL-DMVGLRSedadKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 144 IGRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFL-VEQNANQALKLADRGYVLENGRVVLEDTGAALL- 221
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLfITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLs 240
|
....*..
gi 1540804698 222 -ANEAVR 227
Cdd:TIGR02769 241 fKHPAGR 247
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-210 |
1.15e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.91 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 11 YGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCG-EPRAS-EGSIVFQGQDItQWQTSR--------IMREAVAI 80
Cdd:PRK13549 15 FGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYPHGTyEGEIIFEGEEL-QASNIRdteragiaIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEgrrvfsrMTVEENLAMG-----GFFADRHQYQQRIERvftlfprLLERRS------QRAGTMSGGEQQMLAIGRALM 149
Cdd:PRK13549 94 VKE-------LSVLENIFLGneitpGGIMDYDAMYLRAQK-------LLAQLKldinpaTPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 150 SQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGR 210
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-201 |
1.63e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.32 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 5 NQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLC------GEPRAsEGSIVFQGQDITQWQTS-RIMREA 77
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVRV-EGRVEFFNQNIYERRVNlNRLRRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 78 VAIVPEGRRVFSrMTVEENLAMGGFFADRH---QYQQRIERVFT---LFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQ 151
Cdd:PRK14258 90 VSMVHPKPNLFP-MSVYDNVAYGVKIVGWRpklEIDDIVESALKdadLWDEIKHKIHKSALDLSGGQQQRLCIARALAVK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1540804698 152 PKLLLLDEPSLGLAPIIIQQIFD--IIQQLREEgMTIFLVEQNANQALKLAD 201
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESliQSLRLRSE-LTMVIVSHNLHQVSRLSD 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-212 |
2.50e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 83.74 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 10 HYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTL-----CGEPRASEGSIVFQGQDITQWQTSRI-MREAVAIVPE 83
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIeVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 84 GRRVFSRMTVEENLAMG----GFFADRHQYQQRIE---RVFTLFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLL 156
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGvklnGLVKSKKELDERVEwalKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 157 LDEPSLGLAPIIIQQIFDIIQQLREEgMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-212 |
3.02e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 83.15 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 11 YGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGqdITQWQTSRIMREAVAIVpegrrVFSR 90
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRKKFLRRIGVV-----FGQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 91 MTVEENL-AMGGFFADRH-------QYQQRIERVFTLFP--RLLErrsQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:cd03267 104 TQLWWDLpVIDSFYLLAAiydlppaRFKKRLDELSELLDleELLD---TPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 161 SLGL-APIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:cd03267 181 TIGLdVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-213 |
3.32e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 83.64 E-value: 3.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 16 ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTS---RIMREAVAIV---PEGRrVFS 89
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdiKQIRKKVGLVfqfPESQ-LFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 90 RmTVEENLAMG--GFFADRHQYQQRIERVFTLFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPI 167
Cdd:PRK13649 101 E-TVLKDVAFGpqNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1540804698 168 IIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVL 213
Cdd:PRK13649 180 GRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVL 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-160 |
3.34e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.77 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 7 VSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwqtSRIMREAVAIVPEGRR 86
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQQRDICMVFQSYA 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 87 VFSRMTVEEN----LAMGGffADRHQYQQRIERVFTLFPrlLERRSQR-AGTMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:PRK11432 89 LFPHMSLGENvgygLKMLG--VPKEERKQRVKEALELVD--LAGFEDRyVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-212 |
4.09e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.55 E-value: 4.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 12 GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQW---QTSRIMREAVAIVPEGRRVF 88
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREHFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 89 SRMTVEENLAMGGFFADRHQyQQRIERVFTLFPR--LLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAP 166
Cdd:PRK10535 99 SHLTAAQNVEVPAVYAGLER-KQRLLRAQELLQRlgLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1540804698 167 IIIQQIFDIIQQLREEGMTIFLVEQNANQALKlADRGYVLENGRVV 212
Cdd:PRK10535 178 HSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-230 |
6.79e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.72 E-value: 6.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 20 VSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAIVPEGRRVfSRMTVEENLAM 99
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQS-SGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 100 G---------GFFADRHQYQQRIERVFTLFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPIIIQ 170
Cdd:PRK15439 361 NvcalthnrrGFWIKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 171 QIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVRSAY 230
Cdd:PRK15439 441 DIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRLAF 500
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
17-211 |
7.98e-19 |
|
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: 80.34 E-value: 7.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRImREAVAIVPEGRRVFSRmTVEEN 96
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL-GDHVGYLPQDDELFSG-SIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 97 LamggffadrhqyqqriervftlfprllerrsqragtMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPIIIQQIFDII 176
Cdd:cd03246 96 I------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....*
gi 1540804698 177 QQLREEGMTIFLVEQNANqALKLADRGYVLENGRV 211
Cdd:cd03246 140 AALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-213 |
1.49e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAI 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENLAMGgfFADRHQYQQRIERVFTLFPRLLERRSQrAGTMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFG--LPKRQASMQKMKQLLAALGCQLDLDSS-AGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 161 SLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVL 213
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIAL 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-222 |
1.73e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 81.75 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGK-----IQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDI---TQWQTSRI 73
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 74 MREAVAIV---PEGRrVFSRmTVEENLAMG--GFFADRHQYQqriERVFTL-----FPRllERRSQRAGTMSGGEQQMLA 143
Cdd:PRK13646 83 VRKRIGMVfqfPESQ-LFED-TVEREIIFGpkNFKMNLDEVK---NYAHRLlmdlgFSR--DVMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 144 IGRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLR-EEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLA 222
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-214 |
1.87e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.26 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQT-SRIMREAVAI 80
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREdTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRrvfsrmtVEENLAMGGFFADRHQYQQRIERVftlfpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:PRK11247 93 LPWKK-------VIDNVGLGLKGQWRDAALQALAAV-----GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 161 SLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVVLE 214
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-160 |
2.04e-18 |
|
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: 82.02 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHY----GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCG---EPRASEGSIVFQGQDITQwQTSRI 73
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLK-LSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 74 MREA----VAIV---------PegrrvfsRMTVEENLAMG---GFFADRHQYQQRIERVFTL--FPRLLERRSQRAGTMS 135
Cdd:COG0444 80 LRKIrgreIQMIfqdpmtslnP-------VMTVGDQIAEPlriHGGLSKAEARERAIELLERvgLPDPERRLDRYPHELS 152
|
170 180
....*....|....*....|....*
gi 1540804698 136 GGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEP 177
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-216 |
2.56e-18 |
|
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: 83.52 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 16 ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDItqwQTS-RIMREAVAIVPEGRRVFSRMTVE 94
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI---ETNlDAVRQSLGMCPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 95 ENLAMGGFFADRHQYQQRIERVFTLFPR-LLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPIIIQQIF 173
Cdd:TIGR01257 1022 EHILFYAQLKGRSWEEAQLEMEAMLEDTgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1540804698 174 DIIQQLReEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDT 216
Cdd:TIGR01257 1102 DLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-160 |
2.78e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 2.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFqGQDITqwqtsrimreaVAI 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-----------IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVF-SRMTVEENLAMGGFFADRHQYQQRIERvFtLFPRllERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:COG0488 383 FDQHQEELdPDKTVLDELRDGAPGGTEQEVRGYLGR-F-LFSG--DDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
.
gi 1540804698 160 P 160
Cdd:COG0488 459 P 459
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-160 |
2.95e-18 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 82.81 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 12 GKIQALHQVSLTISQGEIVTLIGANGAGKTTL----LGTLcgeprASEGSIVFQGQDITQWQTS--RIMREAVAIV---P 82
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRRalRPLRRRMQVVfqdP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 83 egrrvFS----RMTVEENLAMG-GFFADRHQYQQRIERVFtlfpRLLERRSQRAGTM-------SGGEQQMLAIGRALMS 150
Cdd:COG4172 372 -----FGslspRMTVGQIIAEGlRVHGPGLSAAERRARVA----EALEEVGLDPAARhryphefSGGQRQRIAIARALIL 442
|
170
....*....|
gi 1540804698 151 QPKLLLLDEP 160
Cdd:COG4172 443 EPKLLVLDEP 452
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-222 |
3.00e-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: 82.87 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYG-KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSrIMREAVAI 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRH-TLRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRmTVEENLAMGgffADRHQYQQRIERVFTL---------FPRLLERR-SQRAGTMSGGEQQMLAIGRALMS 150
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLLG---AKENVSQDEIWAACEIaeikddienMPLGYQTElSEEGSSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540804698 151 QPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEgmTIFLVEQNANQAlKLADRGYVLENGRVVLEDTGAALLA 222
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLD 697
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-212 |
3.77e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 80.36 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQD--------ITQWQTSR 72
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlyaLSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 73 IMREAVAIVPEGRRVFSRMTV-------EENLAMGgffaDRH---------QYQQRIERVftlfprlLERRSQRAGTMSG 136
Cdd:PRK11701 86 LLRTEWGFVHQHPRDGLRMQVsaggnigERLMAVG----ARHygdiratagDWLERVEID-------AARIDDLPTTFSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540804698 137 GEQQMLAIGRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-212 |
4.92e-18 |
|
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: 78.75 E-value: 4.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCG--EPRASEGSIVFQGQDITQWQTSRIMreavAIVPEGRRVFSRMTVE 94
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKII----GYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 95 ENLamggffadrhQYQQRIERVftlfprllerrsqragtmSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPIIIQQIFD 174
Cdd:cd03213 101 ETL----------MFAAKLRGL------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1540804698 175 IIQQLREEGMT-IFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:cd03213 153 LLRRLADTGRTiICSIHQPSSEIFELFDKLLLLSQGRVI 191
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-211 |
5.58e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 81.61 E-value: 5.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 7 VSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRimrEAVAIVPEGRR 86
Cdd:PRK11000 9 VTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE---RGVGMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 87 VFSRMTVEENLAMGGFFA--DRHQYQQRIERVFTLF--PRLLERRSQragTMSGGEQQMLAIGRALMSQPKLLLLDEPSL 162
Cdd:PRK11000 86 LYPHLSVAENMSFGLKLAgaKKEEINQRVNQVAEVLqlAHLLDRKPK---ALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1540804698 163 GLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRV 211
Cdd:PRK11000 163 NLDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-160 |
5.84e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 81.43 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHY-GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwqtsrimREA-- 77
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE-------LEPad 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 78 --VAIVPEGRRVFSRMTVEENLAMG----GFfaDRHQYQQRIE---RVFTLFPrLLERRSQRagtMSGGEQQMLAIGRAL 148
Cdd:PRK11650 76 rdIAMVFQNYALYPHMSVRENMAYGlkirGM--PKAEIEERVAeaaRILELEP-LLDRKPRE---LSGGQRQRVAMGRAI 149
|
170
....*....|..
gi 1540804698 149 MSQPKLLLLDEP 160
Cdd:PRK11650 150 VREPAVFLFDEP 161
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-212 |
7.62e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 79.71 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTL------CGEPRASEGSIVFQGQDITQWQTSRiMREAVAIVPEGRRVFSR 90
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlieiYDSKIKVDGKVLYFGKDIFQIDAIK-LRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 91 MTVEENLAM---GGFFADRHQYQQRIE---RVFTLFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGL 164
Cdd:PRK14246 105 LSIYDNIAYplkSHGIKEKREIKKIVEeclRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1540804698 165 APIIIQQIFDIIQQLREEgMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:PRK14246 185 DIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-212 |
1.17e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.16 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 4 FNQVSAHY-GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLcgePRA---SEGSIVFQGQDITQwQTSRIMREAVA 79
Cdd:PRK13657 337 FDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL---QRVfdpQSGRILIDGTDIRT-VTRASLRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSRmTVEENLAMGGFFADRHQYQQRIERVFTLfpRLLERRSQRAGTM--------SGGEQQMLAIGRALMSQ 151
Cdd:PRK13657 413 VVFQDAGLFNR-SIEDNIRVGRPDATDEEMRAAAERAQAH--DFIERKPDGYDTVvgergrqlSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 152 PKLLLLDEPSLGLAPIIIQQIFDIIQQLReEGMTIFLVeqnanqALKL-----ADRGYVLENGRVV 212
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELM-KGRTTFII------AHRLstvrnADRILVFDNGRVV 548
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-202 |
1.62e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.32 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHY--GKIQA--LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTS---RI 73
Cdd:PRK11629 5 LLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 74 MREAVAIVPEGRRVFSRMTVEENLAM----GGffADRHQYQQRIERVFTLFPrlLERRSQ-RAGTMSGGEQQMLAIGRAL 148
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMplliGK--KKPAEINSRALEMLAAVG--LEHRANhRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 149 MSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVeqnANQALKLADR 202
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLV---VTHDLQLAKR 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-222 |
2.35e-17 |
|
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: 78.04 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYG-KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQW-QTSriMREAVA 79
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtLDS--LRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSRmTVEENLAMGGFFA-DRHQY----QQRIERVFTLFP-----RLLERrsqraGTM-SGGEQQMLAIGRAL 148
Cdd:cd03253 79 VVPQDTVLFND-TIGYNIRYGRPDAtDEEVIeaakAAQIHDKIMRFPdgydtIVGER-----GLKlSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 149 MSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLveqnanqALKL-----ADRGYVLENGRVVLEDTGAALLA 222
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVI-------AHRLstivnADKIIVLKDGRIVERGTHEELLA 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-226 |
2.70e-17 |
|
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: 77.58 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 4 FNQVSAHY---GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLcgePR---ASEGSIVFQGQDITQwQTSRIMREA 77
Cdd:cd03249 3 FKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL---ERfydPTSGEILLDGVDIRD-LNLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 78 VAIVPEGRRVFSrMTVEENLAMGGFFADRHQYQQ-----RIERVFTLFPRLLERR-SQRAGTMSGGEQQMLAIGRALMSQ 151
Cdd:cd03249 79 IGLVSQEPVLFD-GTIAENIRYGKPDATDEEVEEaakkaNIHDFIMSLPDGYDTLvGERGSQLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 152 PKLLLLDEPSLGLAPIIIQQIFDIIQQLReEGMTIFLVEQNANqALKLADRGYVLENGRVVLEDTGAALLANEAV 226
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELMAQKGV 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-212 |
2.90e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.97 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 4 FNQVSAHYgkIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDI-TQWQTSRIMREAVAIV- 81
Cdd:PRK13651 12 FNKKLPTE--LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEkNKKKTKEKEKVLEKLVi 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 --PEGRRVFSRMTVEENLAMGGFFADRHQYQQRIERVFTLFPRLL----ERRSQRAGTM------------------SGG 137
Cdd:PRK13651 90 qkTRFKKIKKIKEIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMgvskEEAKKRAAKYielvgldesylqrspfelSGG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 138 EQQMLAIGRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-166 |
2.92e-17 |
|
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: 80.10 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHY-GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRImREAVAI 80
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV-RRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSrMTVEENLAMGGFFADRHQYQQRIERVFTLfpRLLERRSQRAGT--------MSGGEQQMLAIGRALMSQP 152
Cdd:TIGR02868 414 CAQDAHLFD-TTVRENLRLARPDATDEELWAALERVGLA--DWLRALPDGLDTvlgeggarLSGGERQRLALARALLADA 490
|
170
....*....|....
gi 1540804698 153 KLLLLDEPSLGLAP 166
Cdd:TIGR02868 491 PILLLDEPTEHLDA 504
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-231 |
3.25e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.13 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRI-MREAVA 79
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLaLRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IV---PEGRRVFSRMTVEENLAMGGFFADRHQYQQRIERVFTLFPRLlERRSQRAGTMSGGEQQMLAIGRALMSQPKLLL 156
Cdd:PRK13638 81 TVfqdPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQ-HFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 157 LDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLE-DTGAALLANEAVRSAYL 231
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHgAPGEVFACTEAMEQAGL 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-227 |
8.08e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.99 E-value: 8.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 19 QVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQ---DITQwqtsrimreAVAIVPEGRRV-------- 87
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEK---------GICLPPEKRRIgyvfqdar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 88 -FSRMTVEENLAMGGFFADRHQYQQ-----RIERVFTLFPrllerrsqraGTMSGGEQQMLAIGRALMSQPKLLLLDEP- 160
Cdd:PRK11144 87 lFPHYKVRGNLRYGMAKSMVAQFDKivallGIEPLLDRYP----------GSLSGGEKQRVAIGRALLTAPELLLMDEPl 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540804698 161 -SLGLaPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVR 227
Cdd:PRK11144 157 aSLDL-PRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-212 |
9.24e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 9.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTL-CGEPRASE--GSIVFQGQDITQWQtsriMREAVAIVPEGRRVFSRMTV 93
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPKGVKgsGSVLLNGMPIDAKE----MRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 94 EENLA-MGGFFADRHQYQ-QRIERVFTLFPRLLERRSQ--------RAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLG 163
Cdd:TIGR00955 117 REHLMfQAHLRMPRRVTKkEKRERVDEVLQALGLRKCAntrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1540804698 164 LAPIIIQQIFDIIQQLREEGMTIFL-VEQNANQALKLADRGYVLENGRVV 212
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGKTIICtIHQPSSELFELFDKIILMAEGRVA 246
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-189 |
9.39e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 75.35 E-value: 9.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 11 YGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVfqgqditqwqtsRIMREAVAIVPEGRRVFSR 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------------RAGGARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 91 M--TVEENLAMGGF----------FADRHQYQQRIERVftlfpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLD 158
Cdd:NF040873 70 LplTVRDLVAMGRWarrglwrrltRDDRAAVDDALERV-----GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190
....*....|....*....|....*....|.
gi 1540804698 159 EPSLGLAPIIIQQIFDIIQQLREEGMTIFLV 189
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARGATVVVV 175
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-216 |
1.68e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.21 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 15 QALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQ---WQtsriMREAVAIV---PEGRRVF 88
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetvWD----VRRQVGMVfqnPDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 89 SrmTVEENLAMG----GFfaDRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGL 164
Cdd:PRK13635 97 A--TVQDDVAFGleniGV--PREEMVERVDQALRQV-GMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 165 APIIIQQIFDIIQQLREEGM-TIFLVEQNANQALKlADRGYVLENGRVVLEDT 216
Cdd:PRK13635 172 DPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGT 223
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-161 |
1.73e-16 |
|
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: 75.22 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHY--GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRImREAVA 79
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL-RSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSRmTVEENLAMGGFFADRHQYQ-----QRIERVFTLFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKL 154
Cdd:cd03244 82 IIPQDPVLFSG-TIRSNLDPFGEYSDEELWQalervGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
....*..
gi 1540804698 155 LLLDEPS 161
Cdd:cd03244 161 LVLDEAT 167
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-231 |
2.11e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.02 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 15 QALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwQTS----RIMREAVAIV---PEGRrV 87
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITP-ETGnknlKKLRKKVSLVfqfPEAQ-L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 88 FSRmTVEENLAMG----GFFAD--RHQYQQRIERVfTLFPRLLERRSQRagtMSGGEQQMLAIGRALMSQPKLLLLDEPS 161
Cdd:PRK13641 99 FEN-TVLKDVEFGpknfGFSEDeaKEKALKWLKKV-GLSEDLISKSPFE---LSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 162 LGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLAN-EAVRSAYL 231
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDkEWLKKHYL 244
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
2.24e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.94 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQA--LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwQTSRIMREAV 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD-DNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 79 AIV---PEGRRVFSrmTVEENLAMG--GFFADRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPK 153
Cdd:PRK13648 86 GIVfqnPDNQFVGS--IVKYDVAFGleNHAVPYDEMHRRVSEALKQV-DMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 154 LLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKlADRGYVLENGRVVLEDT 216
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGT 225
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-212 |
2.59e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 77.08 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 7 VSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAIVPEGRR 86
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 87 VFSRMTVEENLAMG-----GFFADRHQYQQRIERVFTLFPRLLERRsQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPS 161
Cdd:PRK10982 84 LVLQRSVMDNMWLGryptkGMFVDQDKMYRDTKAIFDELDIDIDPR-AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 162 LGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
19-227 |
3.06e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.57 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 19 QVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRI--MREAVAIVPEGRRVFSRMTVEEN 96
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 97 LAmggfFADRHQYQQRIERVFTLFPRLLERRSQRAGT------MSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPIIIQ 170
Cdd:PRK11831 105 VA----YPLREHTQLPAPLLHSTVMMKLEAVGLRGAAklmpseLSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540804698 171 QIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVR 227
Cdd:PRK11831 181 VLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR 238
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-233 |
3.17e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.52 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKiQALHQVSLTISQGEIVTLIGANGAGKTTLLGTL------CGEPRASeGSIVFQGQDITQWQTSRIM 74
Cdd:PRK14271 22 MAAVNLTLGFAGK-TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkVSGYRYS-GDVLLGGRSIFNYRDVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 75 REAVAIVPEGRRVFSrMTVEENLAMG---GFFADRHQY----QQRIERVfTLFPRLLERRSQRAGTMSGGEQQMLAIGRA 147
Cdd:PRK14271 100 RRRVGMLFQRPNPFP-MSIMDNVLAGvraHKLVPRKEFrgvaQARLTEV-GLWDAVKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 148 LMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEgMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLAN--EA 225
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSpkHA 256
|
....*...
gi 1540804698 226 VRSAYLGG 233
Cdd:PRK14271 257 ETARYVAG 264
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
12-160 |
3.22e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 75.92 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 12 GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCG--EPraSEGSIVFQGQDITQWQTS--RIMREAVAIV---Peg 84
Cdd:COG4608 29 GVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRleEP--TSGEILFDGQDITGLSGRelRPLRRRMQMVfqdP-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 85 rrvFS----RMTVEENLAMG----GFfADRHQYQQRIERvftlfprLLERRSQRAGTM-------SGGEQQMLAIGRALM 149
Cdd:COG4608 105 ---YAslnpRMTVGDIIAEPlrihGL-ASKAERRERVAE-------LLELVGLRPEHAdryphefSGGQRQRIGIARALA 173
|
170
....*....|.
gi 1540804698 150 SQPKLLLLDEP 160
Cdd:COG4608 174 LNPKLIVCDEP 184
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
3.36e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 75.41 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYG--KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwQTSRIMREAV 78
Cdd:PRK13632 7 MIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK-ENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 79 AIV---PEGRrvFSRMTVEENLAMG--GFFADRHQYQQRIERVFTL--FPRLLERRSQragTMSGGEQQMLAIGRALMSQ 151
Cdd:PRK13632 86 GIIfqnPDNQ--FIGATVEDDIAFGleNKKVPPKKMKDIIDDLAKKvgMEDYLDKEPQ---NLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 152 PKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGM-TIFLVEQNANQALkLADRGYVLENGRVVLEDTGAALLANEAV 226
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-212 |
3.90e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 76.75 E-value: 3.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 14 IQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCG-EPRAS-EGSIVFQGQdITQWQTSR--------IMREAVAIVPE 83
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvYPHGSyEGEILFDGE-VCRFKDIRdsealgivIIHQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 84 grrvfsrMTVEENLAMG-----GFFADRHQYQQR----IERVftlfpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKL 154
Cdd:NF040905 93 -------LSIAENIFLGnerakRGVIDWNETNRRarelLAKV-----GLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540804698 155 LLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-160 |
3.96e-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: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRimREAVAIV 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP--HENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEGRRVFSRMTVEENLAmggFFADRHQYQQRieRVFTLFPRL-LERRSQR-AGTMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:TIGR01189 79 GHLPGLKPELSALENLH---FWAAIHGGAQR--TIEDALAAVgLTGFEDLpAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
.
gi 1540804698 160 P 160
Cdd:TIGR01189 154 P 154
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-209 |
4.12e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.30 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 16 ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwqtsRIMREAVAIVPEGRRV-FSRMTVE 94
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNLVAYVPQSEEVdWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 95 ENLAMGGFFA-----------DRHQYQQRIERVftlfpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLG 163
Cdd:PRK15056 98 EDVVMMGRYGhmgwlrrakkrDRQIVTAALARV-----DMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 164 LAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLAD-----RGYVLENG 209
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDytvmvKGTVLASG 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-211 |
4.51e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 76.40 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 13 KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGE-PRASEGSIVFQGQDITQWQTSRIMREAVAIVPEGRR---VF 88
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 89 SRMTVEENLAMGGFfaDRHQYQQRIERVFTL--FPRLLERRSQRA-------GTMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:TIGR02633 352 PILGVGKNITLSVL--KSFCFKMRIDAAAELqiIGSAIQRLKVKTaspflpiGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1540804698 160 PSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRV 211
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-230 |
4.65e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.02 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 5 NQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREaVAIVPEG 84
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 85 RRVFSRMTVEENLAMGGFfadRHQ-----YQQRIERVFTLFPR---LLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLL 156
Cdd:PRK10253 90 ATTPGDITVQELVARGRY---PHQplftrWRKEDEEAVTKAMQatgITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 157 LDEPSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVRSAY 230
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-213 |
4.72e-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: 76.33 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHY--GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMReAVA 79
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR-HIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSRmTVEENLA-MGGF----------FADRHQ--------YQQRIervftlfprllerrSQRAGTMSGGEQQ 140
Cdd:COG4618 410 YLPQDVELFDG-TIAENIArFGDAdpekvvaaakLAGVHEmilrlpdgYDTRI--------------GEGGARLSGGQRQ 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 141 MLAIGRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANqALKLADRGYVLENGRVVL 213
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQA 546
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-212 |
5.16e-16 |
|
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: 74.23 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 15 QALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPR---ASEGSIVFQGQDITQWQtsriMREAVAIVPEGRRVFSRM 91
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQ----FQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 92 TVEENLAMGGFFADRHQYQQRIERVFTLFPRLLERRSQRAGTM-----SGGEQQMLAIGRALMSQPKLLLLDEPSLGLAP 166
Cdd:cd03234 97 TVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNlvkgiSGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1540804698 167 IIIQQIFDIIQQLREEGMTIFL-VEQNANQALKLADRGYVLENGRVV 212
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-164 |
9.04e-16 |
|
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: 72.91 E-value: 9.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSriMREAVAIVPEGRRVFSRMTVEEN 96
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS--IARGLLYLGHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540804698 97 LAmggFFADRHQYQQRIERVFTLFPRLLERRSqrAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGL 164
Cdd:cd03231 94 LR---FWHADHSDEQVEEALARVGLNGFEDRP--VAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-231 |
1.04e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.59 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 5 NQVSAHYGKIQalhQVSLTISQGEIVTLIGANGAGKTTLLGTLCG-EPRASeGSIVFQGQDITQWQTSRIMREAVAIVPE 83
Cdd:PRK09700 270 NVTSRDRKKVR---DISFSVCRGEILGFAGLVGSGRTELMNCLFGvDKRAG-GEIRLNGKDISPRSPLDAVKKGMAYITE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 84 GRR---VFSRMTVEENLAM------GGF-----FADRHQYQQRIERVFTLFPRLLERRSQRAGTMSGGEQQMLAIGRALM 149
Cdd:PRK09700 346 SRRdngFFPNFSIAQNMAIsrslkdGGYkgamgLFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 150 SQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVRSA 229
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIMAW 505
|
..
gi 1540804698 230 YL 231
Cdd:PRK09700 506 AL 507
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-216 |
1.08e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 74.29 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 16 ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFqGQDITQWQTS----RIMREAVAIV---PEgRRVF 88
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKnkklKPLRKKVGIVfqfPE-HQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 89 SRmTVEENLAMG--GFFADRHQYQQRIERVFTLF---PRLLERRSQRagtMSGGEQQMLAIGRALMSQPKLLLLDEPSLG 163
Cdd:PRK13634 100 EE-TVEKDICFGpmNFGVSEEDAKQKAREMIELVglpEELLARSPFE---LSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 164 LAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDT 216
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGT 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-212 |
1.15e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.27 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 4 FNQVSAHYGK-----IQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQG----QDITQWQTSRIM 74
Cdd:PRK13645 9 LDNVSYTYAKktpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 75 REAVAIV---PEgRRVFSRmTVEENLAMG--GFFADRHQYQQRIERVFTL--FPRLLERRSqrAGTMSGGEQQMLAIGRA 147
Cdd:PRK13645 89 RKEIGLVfqfPE-YQLFQE-TIEKDIAFGpvNLGENKQEAYKKVPELLKLvqLPEDYVKRS--PFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 148 LMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-164 |
2.08e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.21 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITqwqtsrIMREAVAI 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID------DPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVF--SRMTVEENLAmggFFAD-RHQYQQRIERVFTLF--PRLLERRsqrAGTMSGGEQQMLAIGRALMSQPKLL 155
Cdd:PRK13539 76 HYLGHRNAmkPALTVAENLE---FWAAfLGGEELDIAAALEAVglAPLAHLP---FGYLSAGQKRRVALARLLVSNRPIW 149
|
....*....
gi 1540804698 156 LLDEPSLGL 164
Cdd:PRK13539 150 ILDEPTAAL 158
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-160 |
2.54e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.81 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRimreavAI 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER------GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENLAMGGFFA--DRHQYQQRIERVFTLFPrLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLD 158
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLAgvEKMQRLEIAHQMLKKVG-LEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
..
gi 1540804698 159 EP 160
Cdd:PRK11248 154 EP 155
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-159 |
2.59e-15 |
|
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: 71.67 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGK--IQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRiMREAVA 79
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED-LRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSRmTVEENLAMGGFFADrhqyqqriERVFTLFprlleRRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:cd03369 86 IIPQDPTLFSG-TIRSNLDPFDEYSD--------EEIYGAL-----RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-230 |
2.86e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.57 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 20 VSLTISQGEIVTLIGANGAGKTTLLGTLCGEpRASEGSIVFQGQDITQWQTSRIMReavaivpegRRVFSRMTVEENLAM 99
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELAR---------HRAYLSQQQSPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 100 GGF-FADRHQYQQ-RIERVFTLFPRLLER------RSQRAGTMSGGEQQ-------MLAIGRALMSQPKLLLLDEPSLGL 164
Cdd:COG4138 85 PVFqYLALHQPAGaSSEAVEQLLAQLAEAlgledkLSRPLTQLSGGEWQrvrlaavLLQVWPTINPEGQLLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 165 APIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVRSAY 230
Cdd:COG4138 165 DVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVF 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-216 |
2.96e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 72.91 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHY--GKIQALHQVSLTISQGEIVTLIGANGAGKTT---LLGTLCGEPRASEGSIVFQGQDITQwQTSRIMRE 76
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTA-KTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 77 AVAIV---PEGRrvFSRMTVEENLAMG--GFFADRHQYQQRIERVFTLFPRLLERRSQRAgTMSGGEQQMLAIGRALMSQ 151
Cdd:PRK13640 85 KVGIVfqnPDNQ--FVGATVGDDVAFGleNRAVPRPEMIKIVRDVLADVGMLDYIDSEPA-NLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 152 PKLLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQAlKLADRGYVLENGRVVLEDT 216
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGS 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-231 |
3.27e-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: 72.13 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYG--KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwQTSRIMREAVA 79
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAL-ADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSRmTVEENLAMGGFFADRHQ--YQQRIERVFTLFPRLLERRSQ----RAGTMSGGEQQMLAIGRALMSQPK 153
Cdd:cd03252 80 VVLQENVLFNR-SIRDNIALADPGMSMERviEAAKLAGAHDFISELPEGYDTivgeQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540804698 154 LLLLDEPSLGLAPIIIQQIFDIIQQLReEGMTIFLVEQNANqALKLADRGYVLENGRVVLEDTGAALLANEAvRSAYL 231
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAENG-LYAYL 233
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-164 |
3.28e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.11 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 7 VSAHYGKiQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEpRASEGSIVFQGQ-----DITQWqtsrimREAVAIV 81
Cdd:PRK11174 357 ILSPDGK-TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIelrelDPESW------RKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 ------PEGrrvfsrmTVEENLAMGGFFADRHQYQQRIERVFTL-FPRLLERR-----SQRAGTMSGGEQQMLAIGRALM 149
Cdd:PRK11174 429 gqnpqlPHG-------TLRDNVLLGNPDASDEQLQQALENAWVSeFLPLLPQGldtpiGDQAAGLSVGQAQRLALARALL 501
|
170
....*....|....*
gi 1540804698 150 SQPKLLLLDEPSLGL 164
Cdd:PRK11174 502 QPCQLLLLDEPTASL 516
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-231 |
3.30e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.41 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHY---------GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTS 71
Cdd:PRK10419 3 LLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 72 --RIMREAVAIVPEGR--RVFSRMTVEENLA------MGGFFADRHQYQQRIERVFTLFPRLLERRSQRagtMSGGEQQM 141
Cdd:PRK10419 83 qrKAFRRDIQMVFQDSisAVNPRKTVREIIReplrhlLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ---LSGGQLQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 142 LAIGRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFL-VEQNANQALKLADRGYVLENGRVVLEDTGAAL 220
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLfITHDLRLVERFCQRVMVMDNGQIVETQPVGDK 239
|
250
....*....|....*.
gi 1540804698 221 L-----ANEAVRSAYL 231
Cdd:PRK10419 240 LtfsspAGRVLQNAVL 255
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-222 |
3.37e-15 |
|
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: 73.98 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYG--KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLcgePR---ASEGSIVFQGQDITQWqTSRIMRE 76
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLI---PRfyePDSGQILLDGHDLADY-TLASLRR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 77 AVAIVPEGRRVFSRmTVEENLAmggfFADRHQY-QQRIERVFTL---------FPRLLERR-SQRAGTMSGGEQQMLAIG 145
Cdd:TIGR02203 407 QVALVSQDVVLFND-TIANNIA----YGRTEQAdRAEIERALAAayaqdfvdkLPLGLDTPiGENGVLLSGGQRQRLAIA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540804698 146 RALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTifLVEQNANQALKLADRGYVLENGRVVLEDTGAALLA 222
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT--LVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLA 556
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-216 |
4.43e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.43 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 16 ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAIV---PEGRRVFSrmT 92
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVfqnPDNQIVAT--I 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 93 VEENLAMG----GFFAD--RHQYQQRIERVftlfpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAP 166
Cdd:PRK13633 103 VEEDVAFGpenlGIPPEeiRERVDESLKKV-----GMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 167 IIIQQIFDIIQQL-REEGMTIFLVEQNANQALKlADRGYVLENGRVVLEDT 216
Cdd:PRK13633 178 SGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGT 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-232 |
4.72e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.14 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTS---RIMREAV 78
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrEVRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 79 AIVPEGRRVFSRMTVEENLAMGGFFADRHQYQQRIERVFTLFPRLLERRSQ-RAGTMSGGEQQMLAIGRALMSQPKLLLL 157
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHsYPDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 158 DEPSLGLAPIIIQQIFDIIQQLR-EEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALL---ANEAVRSAYLG 232
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILnnpANDYVRTFFRG 267
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-214 |
4.96e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.41 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 20 VSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAIVPEGRR---VFSRMTVEEN 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 97 LAM--------GGFFADRHQYQQRIERvftlFPRLLE----RRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGL 164
Cdd:PRK11288 352 INIsarrhhlrAGCLINNRWEAENADR----FIRSLNiktpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1540804698 165 APIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLE 214
Cdd:PRK11288 428 DVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
14-220 |
7.33e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 7.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 14 IQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDIT-------QWQTSRIMREAVAIVPEgrr 86
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssQEAGIGIIHQELNLIPQ--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 87 vfsrMTVEENLAMGGFFADRH---QYQQRIERVFTLFPRL-LERRSQR-AGTMSGGEQQMLAIGRALMSQPKLLLLDEPS 161
Cdd:PRK10762 94 ----LTIAENIFLGREFVNRFgriDWKKMYAEADKLLARLnLRFSSDKlVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 162 LGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAAL 220
Cdd:PRK10762 170 DALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-212 |
7.59e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 72.07 E-value: 7.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYG-----KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIvfQGQDITQWQTSRI-- 73
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV--TVGDIVVSSTSKQke 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 74 ---MREAVAIV---PEGRrVFSRmTVEENLAMG--GFFADRHQYQQRIERVFTLFPRLLERRSQRAGTMSGGEQQMLAIG 145
Cdd:PRK13643 79 ikpVRKKVGVVfqfPESQ-LFEE-TVLKDVAFGpqNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540804698 146 RALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-231 |
1.07e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.88 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 4 FNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCG--EPraSEGSIVFQGqditqwqtsRI--MRE-AV 78
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGilEP--TSGRVEVNG---------RVsaLLElGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 79 AIVPEgrrvfsrMTVEEN-----LAMGgffADRHQYQQRIERV--FTlfpRLLERRSQRAGTMSGGEQQMLAIGRALMSQ 151
Cdd:COG1134 98 GFHPE-------LTGRENiylngRLLG---LSRKEIDEKFDEIveFA---ELGDFIDQPVKTYSSGMRARLAFAVATAVD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 152 PKLLLLDEpslGLA---PIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTgaallANEAVRs 228
Cdd:COG1134 165 PDILLVDE---VLAvgdAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD-----PEEVIA- 235
|
...
gi 1540804698 229 AYL 231
Cdd:COG1134 236 AYE 238
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-211 |
1.12e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.27 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 13 KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGE-PRASEGSIVFQGQDITQWQTSRIMREAVAIVPEGRR---VF 88
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKrdgIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 89 SRMTVEEN--LAMGGFFADR---------HQYQQRIER--VFTLFPRLlerrsqRAGTMSGGEQQMLAIGRALMSQPKLL 155
Cdd:PRK13549 354 PVMGVGKNitLAALDRFTGGsriddaaelKTILESIQRlkVKTASPEL------AIARLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 156 LLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRV 211
Cdd:PRK13549 428 ILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-160 |
2.31e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.06 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 18 HQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwqtsriMRE-----------AVAIVPEgrr 86
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR------QRDeyhqdllylghQPGIKTE--- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 87 vfsrMTVEENLAmggFFADRHQYQQRiERVFTLFPR--LLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:PRK13538 89 ----LTALENLR---FYQRLHGPGDD-EALWEALAQvgLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
17-224 |
3.35e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 69.33 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEP--RASEGSIVFQGQDITQwqtsrimreavaivpegrrvfsrMTVE 94
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILE-----------------------LSPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 95 ENLAMGGFFAdrHQYQQRIE--RVFTL-----------------FPRLLERRSQRAG------------TMSGGEQ---- 139
Cdd:COG0396 73 ERARAGIFLA--FQYPVEIPgvSVSNFlrtalnarrgeelsareFLKLLKEKMKELGldedfldryvneGFSGGEKkrne 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 140 --QMLAIgralmsQPKLLLLDEP------------SLGLApiiiqqifdiiqQLREEGMTIFLVEQNaNQALKL--ADRG 203
Cdd:COG0396 151 ilQMLLL------EPKLAILDETdsgldidalrivAEGVN------------KLRSPDRGILIITHY-QRILDYikPDFV 211
|
250 260
....*....|....*....|.
gi 1540804698 204 YVLENGRVVleDTGAALLANE 224
Cdd:COG0396 212 HVLVDGRIV--KSGGKELALE 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-211 |
4.45e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.53 E-value: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 16 ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAIVPEGRR---VFSRMT 92
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEERRstgIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 93 VEENlamgGFFADRHQYQQRIervftlfpRLLERR------------------SQRA--GTMSGGEQQMLAIGRALMSQP 152
Cdd:PRK10982 343 IGFN----SLISNIRNYKNKV--------GLLDNSrmksdtqwvidsmrvktpGHRTqiGSLSGGNQQKVIIGRWLLTQP 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 153 KLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRV 211
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-164 |
5.68e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAI 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEEnlamggffADRHQYQQRIERVftlfpRLLERRSQRagtMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:PRK09544 84 LTVNRFLRLRPGTKK--------EDILPALKRVQAG-----HLIDAPMQK---LSGGETQRVLLARALLNRPQLLVLDEP 147
|
....
gi 1540804698 161 SLGL 164
Cdd:PRK09544 148 TQGV 151
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-161 |
6.12e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 66.70 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIvfqgqditqwqtsrimreavaIV 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------------------TW 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEGRRVfsrmtveenlamgGFFAdrhQyqqriervftlfprllerrsqragtMSGGEQQMLAIGRALMSQPKLLLLDEPS 161
Cdd:cd03221 60 GSTVKI-------------GYFE---Q-------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-212 |
7.97e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 7.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 20 VSLTISQGEIVTLIGANGAGKTTLLGTLCGEpRASEGSIVFQGQDITQWQTSRIMREAVAIVPEGRRVFSrMTVEENLAM 99
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFA-MPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 100 ggffadrHQYQQ-RIERVFTLFPRLLER--------RSqrAGTMSGGEQQ-------MLAIGRALMSQPKLLLLDEPSLG 163
Cdd:PRK03695 93 -------HQPDKtRTEAVASALNEVAEAlglddklgRS--VNQLSGGEWQrvrlaavVLQVWPDINPAGQLLLLDEPMNS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1540804698 164 LAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:PRK03695 164 LDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-161 |
9.32e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.88 E-value: 9.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYG----KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQW---QTSRI 73
Cdd:PRK10584 6 IVEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 74 MREAVAIVPEGRRVFSRMTVEENLAMGGFF---ADRHQYQQRIERVFTLfpRLLERRSQRAGTMSGGEQQMLAIGRALMS 150
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPALLrgeSSRQSRNGAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170
....*....|.
gi 1540804698 151 QPKLLLLDEPS 161
Cdd:PRK10584 164 RPDVLFADEPT 174
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-223 |
9.49e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.96 E-value: 9.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 11 YGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSI--------------------VFqGQ------D 64
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrvlgyvpfkrrkefarrigvVF-GQrsqlwwD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 65 ITQWQTSRIMReavAI--VPEGRrvfsrmtveenlamggffadrhqYQQRIERVFTLFpRLLERRSQRAGTMSGGeQQML 142
Cdd:COG4586 111 LPAIDSFRLLK---AIyrIPDAE-----------------------YKKRLDELVELL-DLGELLDTPVRQLSLG-QRMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 143 A-IGRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQL-REEGMTIFL-------VEQnanqalkLADRGYVLENGRVVL 213
Cdd:COG4586 163 CeLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLtshdmddIEA-------LCDRVIVIDHGRIIY 235
|
250
....*....|
gi 1540804698 214 EDTGAALLAN 223
Cdd:COG4586 236 DGSLEELKER 245
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-210 |
9.55e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 67.49 E-value: 9.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 16 ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQditqwqtsrimreaVAIVPEGRRVFSrMTVEE 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------------IAYVSQEPWIQN-GTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 96 NLAMGGFFadrhqYQQRIERV---------FTLFPRLLERR-SQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLA 165
Cdd:cd03250 85 NILFGKPF-----DEERYEKVikacalepdLEILPDGDLTEiGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1540804698 166 PiiIQQIFDIIQQLREEGM---TIFLVEQNAnQALKLADRGYVLENGR 210
Cdd:cd03250 160 A--HVGRHIFENCILGLLLnnkTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-204 |
9.78e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.28 E-value: 9.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSriMREAVAI 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCT--YQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRMTVEENLAMGGFFADRHQYQQRIERVFTL-----FPrllerrsqrAGTMSGGEQQMLAIGRALMSQPKLL 155
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLehlidYP---------CGLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1540804698 156 LLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLveqNANQALKLADRGY 204
Cdd:PRK13540 150 LLDEPLVALDELSLLTIITKIQEHRAKGGAVLL---TSHQDLPLNKADY 195
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-229 |
1.05e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 69.75 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 4 FNQVSAHY---GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREaVAI 80
Cdd:TIGR00958 481 FQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ-VAL 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRmTVEENLAMGGFFADRHQYQQRIERVF-----TLFPRLLERRSQRAGT-MSGGEQQMLAIGRALMSQPKL 154
Cdd:TIGR00958 560 VGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANahdfiMEFPNGYDTEVGEKGSqLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 155 LLLDEPSLGLAPIIIQQIFDIIQQlreEGMTIFLVEQNANQALKlADRGYVLENGRVVLEDTGAALLANEAVRSA 229
Cdd:TIGR00958 639 LILDEATSALDAECEQLLQESRSR---ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
13-160 |
1.62e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.58 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 13 KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDIT-----QWQTSR-----IMREAVA-IV 81
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmkddEWRAVRsdiqmIFQDPLAsLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PegrrvfsRMTVEENLA--MGGFFADRHQyQQRIERVFT------LFPRLLERRSQRagtMSGGEQQMLAIGRALMSQPK 153
Cdd:PRK15079 113 P-------RMTIGEIIAepLRTYHPKLSR-QEVKDRVKAmmlkvgLLPNLINRYPHE---FSGGQCQRIGIARALILEPK 181
|
....*..
gi 1540804698 154 LLLLDEP 160
Cdd:PRK15079 182 LIICDEP 188
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
14-222 |
1.92e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.81 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 14 IQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAIVPEGRRVFSRMTV 93
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 94 EENLAMG--GFFADRHQYQQRIERVFtLFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPIIIQQ 171
Cdd:PRK13642 100 EDDVAFGmeNQGIPREEMIKRVDEAL-LAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1540804698 172 IFDIIQQLREE-GMTIFLVEQNANQALKlADRGYVLENGRVVLEDTGAALLA 222
Cdd:PRK13642 179 IMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-161 |
1.98e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.68 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 23 TISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFqgqDITqwqtsrimreaVAIVPEGRRVFSRMTVEENLAMGGF 102
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---ELK-----------ISYKPQYIKPDYDGTVEDLLRSITD 426
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 103 FADRHQYQQRIERVFTLfPRLLERrsqRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPS 161
Cdd:PRK13409 427 DLGSSYYKSEIIKPLQL-ERLLDK---NVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
10-214 |
2.59e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.22 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 10 HYGKIQALHQVSLTISQGEIVTLIGANGAG--KTTLLGTLCGePRASEGSIVFQgqdiTQWQTSRIMREAVAI---VPEG 84
Cdd:NF000106 22 HFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G-PDAGRRPWRF*----TWCANRRALRRTIG*hrpVR*G 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 85 RRvfSRMTVEENLAMGGFFAD--RHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSL 162
Cdd:NF000106 97 RR--ESFSGRENLYMIGR*LDlsRKDARARADELLERF-SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1540804698 163 GLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLE 214
Cdd:NF000106 174 GLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-217 |
2.78e-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: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 7 VSAHY-----GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQ-GQDITQWQTSRIM-----R 75
Cdd:TIGR03269 285 VSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPDgrgraK 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 76 EAVAIVPEGRRVFSRMTVEENL--AMGGFFADRHQyqqRIERVFTLFPRLLERRSQRA------GTMSGGEQQMLAIGRA 147
Cdd:TIGR03269 365 RYIGILHQEYDLYPHRTVLDNLteAIGLELPDELA---RMKAVITLKMVGFDEEKAEEildkypDELSEGERHRVALAQV 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 148 LMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVleDTG 217
Cdd:TIGR03269 442 LIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIV--KIG 510
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-211 |
3.61e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.06 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQ---ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQ---WQtsriM 74
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenvWD----I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 75 REAVAIV---PEGRrvFSRMTVEENLAMG----GFfaDRHQYQQRIERVFTLFPrLLERRSQRAGTMSGGEQQMLAIGRA 147
Cdd:PRK13650 80 RHKIGMVfqnPDNQ--FVGATVEDDVAFGlenkGI--PHEEMKERVNEALELVG-MQDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 148 LMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQaLKLADRGYVLENGRV 211
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQV 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-159 |
5.63e-13 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 65.96 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 15 QALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQtSRIMREAVAIVPEGRRVFSRmTVE 94
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE-HKYLHSKVSLVGQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540804698 95 ENLAMG------------GFFADRHQYQQRIERVFTlfprllERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:cd03248 106 DNIAYGlqscsfecvkeaAQKAHAHSFISELASGYD------TEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDE 176
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-230 |
1.02e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.62 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRAS--------EGSIVFQGQDITQWQTSRIMREAVAIVPEGRRVF 88
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 89 SrMTVEENLAMGGF-FADRHQYQQRIERvfTLFPRLLERRSQRA------GTMSGGEQQMLAIGRAL---------MSQP 152
Cdd:PRK13547 97 A-FSAREIVLLGRYpHARRAGALTHRDG--EIAWQALALAGATAlvgrdvTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 153 KLLLLDEPSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLANEAVRSAY 230
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCY 252
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-224 |
1.18e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.92 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRImREAVAIVPEGRRVFSRmTVEEN 96
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL-RRVLSIIPQSPVLFSG-TVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 97 LAMGGFFADRHQYQ----QRIERVFTLFPRLLERRSQRAG-TMSGGEQQMLAIGRALMSQPKLLLLDEPSlglAPIIIQQ 171
Cdd:PLN03232 1330 IDPFSEHNDADLWEalerAHIKDVIDRNPFGLDAEVSEGGeNFSVGQRQLLSLARALLRRSKILVLDEAT---ASVDVRT 1406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 172 IFDIIQQLREE--GMTIFLVEQNANQALKlADRGYVLENGRVVLEDTGAALLANE 224
Cdd:PLN03232 1407 DSLIQRTIREEfkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-159 |
1.36e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 66.20 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHY-GK-IQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRiMREAVA 79
Cdd:PRK11176 342 IEFRNVTFTYpGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLAS-LRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSRmTVEENLAmggfFADRHQY-QQRIERVFTL-----FPRLLERR-----SQRAGTMSGGEQQMLAIGRAL 148
Cdd:PRK11176 421 LVSQNVHLFND-TIANNIA----YARTEQYsREQIEEAARMayamdFINKMDNGldtviGENGVLLSGGQRQRIAIARAL 495
|
170
....*....|.
gi 1540804698 149 MSQPKLLLLDE 159
Cdd:PRK11176 496 LRDSPILILDE 506
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-159 |
1.56e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 66.38 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHY-GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQW-QTSriMREAVA 79
Cdd:COG5265 358 VRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVtQAS--LRAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 80 IVPEGRRVFSrMTVEENLAMGGFFADRHQYQQRIERVFTLfpRLLERRSQRAGTM--------SGGEQQMLAIGRALMSQ 151
Cdd:COG5265 436 IVPQDTVLFN-DTIAYNIAYGRPDASEEEVEAAARAAQIH--DFIESLPDGYDTRvgerglklSGGEKQRVAIARTLLKN 512
|
....*...
gi 1540804698 152 PKLLLLDE 159
Cdd:COG5265 513 PPILIFDE 520
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-226 |
1.69e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 65.64 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 4 FNQVSAHygKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSI----VFQGQDITQWQ------TSRI 73
Cdd:PRK13631 31 FDEKQEN--ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHElitnpySKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 74 -----MREAVAIV---PEgRRVFsRMTVEENLAMGGFFADRHQYQQRIERVFTLF-----PRLLERRSQRagtMSGGEQQ 140
Cdd:PRK13631 109 knfkeLRRRVSMVfqfPE-YQLF-KDTIEKDIMFGPVALGVKKSEAKKLAKFYLNkmgldDSYLERSPFG---LSGGQKR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 141 MLAIGRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAAL 220
Cdd:PRK13631 184 RVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEI 263
|
....*.
gi 1540804698 221 LANEAV 226
Cdd:PRK13631 264 FTDQHI 269
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-159 |
3.05e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.58 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRiMREAVAI 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI-YRQQVSY 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 81 VPEGRRVFSRmTVEENLAMGGFFADRHQYQQRIERVFTLFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-216 |
3.62e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.21 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 7 VSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCG--EPRASEGSIV------------------------- 59
Cdd:TIGR03269 6 LTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIyhvalcekcgyverpskvgepcpvc 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 60 ---FQGQDITQWQTS----RIMREAVAIVPEgrRVFS---RMTVEEN----LAMGGFFADRHQYQ--QRIERVftlfpRL 123
Cdd:TIGR03269 86 ggtLEPEEVDFWNLSdklrRRIRKRIAIMLQ--RTFAlygDDTVLDNvleaLEEIGYEGKEAVGRavDLIEMV-----QL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 124 LERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPIIIQQI-FDIIQQLREEGMTIFLVEQNANQALKLADR 202
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVhNALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250
....*....|....
gi 1540804698 203 GYVLENGRVVLEDT 216
Cdd:TIGR03269 239 AIWLENGEIKEEGT 252
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-159 |
4.91e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 64.73 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 16 ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRiMREAVAIVPEGRRVFSRmTVEE 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS-WRSRLAVVSQTPFLFSD-TVAN 407
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 96 NLAMGGFFADrhqyQQRIERVFTL---------FPRLLERRSQRAGTM-SGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:PRK10789 408 NIALGRPDAT----QQEIEHVARLasvhddilrLPQGYDTEVGERGVMlSGGQKQRISIARALLLNAEILILDD 477
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-222 |
6.49e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.27 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDIT-------------Q 67
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITrlsfeqlqklvsdE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 68 WQtsrimREAVAIVPEGRRVFSRMTVEenlamggFFADRHQYQQRIERVFTLF--PRLLERRSQRagtMSGGEQQMLAIG 145
Cdd:PRK10938 83 WQ-----RNNTDMLSPGEDDTGRTTAE-------IIQDEVKDPARCEQLAQQFgiTALLDRRFKY---LSTGETRKTLLC 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540804698 146 RALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLA 222
Cdd:PRK10938 148 QALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-224 |
9.67e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.99 E-value: 9.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTsRIMREAVAIVPEGRRVFSRmTVEEN 96
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGL-MDLRKVLGIIPQAPVLFSG-TVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 97 LAMGGFFADRHQYQQrIER-----VFTLFPRLLERRSQRAG-TMSGGEQQMLAIGRALMSQPKLLLLDEPSlglAPIIIQ 170
Cdd:PLN03130 1333 LDPFNEHNDADLWES-LERahlkdVIRRNSLGLDAEVSEAGeNFSVGQRQLLSLARALLRRSKILVLDEAT---AAVDVR 1408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 171 QIFDIIQQLREE--GMTIFLVEQNANQALKlADRGYVLENGRVVLEDTGAALLANE 224
Cdd:PLN03130 1409 TDALIQKTIREEfkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-161 |
2.32e-11 |
|
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: 62.88 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 23 TISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIvfqgqditqwqtsrIMREAVAIVPEGRRVFSRMTVEENL--AMG 100
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------------DEDLKISYKPQYISPDYDGTVEEFLrsANT 427
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 101 GFFaDRHQYQQRIERVFTLfPRLLERRsqrAGTMSGGEQQMLAIGRALMSQPKLLLLDEPS 161
Cdd:COG1245 428 DDF-GSSYYKTEIIKPLGL-EKLLDKN---VKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-166 |
2.38e-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: 63.01 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCgEPRASEGSIVFQGqdiTQWQ--TSRIMREAVAIVPEGRRVFSRmTVE 94
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDG---VSWNsvTLQTWRKAFGVIPQKVFIFSG-TFR 1309
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540804698 95 ENLAMGGFFADRHQYQQRIE----RVFTLFPRLLERRSQRAG-TMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAP 166
Cdd:TIGR01271 1310 KNLDPYEQWSDEEIWKVAEEvglkSVIEQFPDKLDFVLVDGGyVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-209 |
2.55e-11 |
|
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: 63.11 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQ--ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSriMREAV 78
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD--VHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 79 AIVPEGRRVFSRMTVEENLAMggFFADRHQYQQRIERV---------FTLFPRLLerrsqrAGTMSGGEQQMLAIGRALM 149
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHLYL--YARLRGVPAEEIEKVanwsiqslgLSLYADRL------AGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 150 SQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENG 209
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-164 |
2.62e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.42 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 15 QALHQVSLTISQGEIVTLIGANGAGKTT----LLGTLcgeprASEGSIVFQGQDITQWQTSRIM--REAVAIV---PEGR 85
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLpvRHRIQVVfqdPNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 86 ---RVFSRMTVEENLAMGGFFADRHQYQQRIERVFTLFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSL 162
Cdd:PRK15134 375 lnpRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
..
gi 1540804698 163 GL 164
Cdd:PRK15134 455 SL 456
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
14-160 |
2.95e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.90 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 14 IQALHQVSLTISQGEIVTLIGANGAGKTTL--LGTLCGEPraSEGSIVFQGQDITQW--QTSRIMREAVAIV---PEG-- 84
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLarLLTMIETP--TGGELYYQGQDLLKAdpEAQKLLRQKIQIVfqnPYGsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 85 ---RRVFSrmTVEENLAMGGFFADrhqyQQRIERVFTLFPR--LLERRSQRAGTM-SGGEQQMLAIGRALMSQPKLLLLD 158
Cdd:PRK11308 106 nprKKVGQ--ILEEPLLINTSLSA----AERREKALAMMAKvgLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVAD 179
|
..
gi 1540804698 159 EP 160
Cdd:PRK11308 180 EP 181
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-222 |
3.01e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.42 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 15 QALHQVSLTISQGEIVTLIGANGAGKT----TLLGTLCGEPRA-SEGSIVFQGQDI--TQWQTSRIMR--EAVAIVPEGR 85
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLlhASEQTLRGVRgnKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 86 RVFSRM-TVEENLA--------MGGFfADRHQYQQRIERVFTLFPRllERRSQRAGTMSGGEQQMLAIGRALMSQPKLLL 156
Cdd:PRK15134 103 VSLNPLhTLEKQLYevlslhrgMRRE-AARGEILNCLDRVGIRQAA--KRLTDYPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540804698 157 LDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLA 222
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFS 246
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-223 |
5.88e-11 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 61.62 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 12 GKIQALHQVSLTISQGEIVTLIGANGAGKT----TLLGTLCGEPRASEGSIVFQGQDITQWqTSRIMReavAIvpEGRR- 86
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGL-SERELR---RI--RGNRi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 87 --VFSR--------MTVEENLA------MGgffADRHQYQQRIERvftlfprLLER-----RSQRAGT----MSGGEQQ- 140
Cdd:COG4172 95 amIFQEpmtslnplHTIGKQIAevlrlhRG---LSGAAARARALE-------LLERvgipdPERRLDAyphqLSGGQRQr 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 141 -MLAIgrALMSQPKLLLLDEPS-----------LGLapiiiqqifdiiqqL----REEGMTIFLVEQNANQALKLADRGY 204
Cdd:COG4172 165 vMIAM--ALANEPDLLIADEPTtaldvtvqaqiLDL--------------LkdlqRELGMALLLITHDLGVVRRFADRVA 228
|
250
....*....|....*....
gi 1540804698 205 VLENGRVVLEDTGAALLAN 223
Cdd:COG4172 229 VMRQGEIVEQGPTAELFAA 247
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-160 |
9.41e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 9.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGE-PRASEGSIVFQGqditqwqtsrimreAVAIVPEGRRVFSrMTVEE 95
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGElSHAETSSVVIRG--------------SVAYVPQVSWIFN-ATVRE 697
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 96 NLAMGGFFaDRHQYQQRIERV-----FTLFP-RLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:PLN03232 698 NILFGSDF-ESERYWRAIDVTalqhdLDLLPgRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-212 |
1.16e-10 |
|
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: 58.81 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 13 KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCG--EPRAS-EGSIVFQGQDITqwQTSRIMREAVAIVPEGRRVFS 89
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtEGNVSvEGDIHYNGIPYK--EFAEKYPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 90 RMTVEENLAmggfFADRHQYQQRIeRVFtlfprllerrsqragtmSGGEQQMLAIGRALMSQPKLLLLDEPSLGL-APII 168
Cdd:cd03233 97 TLTVRETLD----FALRCKGNEFV-RGI-----------------SGGERKRVSIAEALVSRASVLCWDNSTRGLdSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1540804698 169 IQQIFDIIQQLREEGMTIFL-VEQNANQALKLADRGYVLENGRVV 212
Cdd:cd03233 155 LEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-222 |
2.34e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 59.73 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQ-ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWqTSRIMREAVAI 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL-SHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VPEGRRVFSRmTVEENLAMGGFFADRHQYQ-----QRIERVFTLFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLL 155
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTLGRDISEEQVWQaletvQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540804698 156 LLDEPSLGLAPIIIQQIFDIIQQLREEgmTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLA 222
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLA 563
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-159 |
3.36e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.44 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDitqwqtsRIM-------------REAVAiVPE 83
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-------RVLflpqrpylplgtlREALL-YPA 450
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540804698 84 GRRVFSRMTVEENLAMGGF--FADRHQYQQRIERVFtlfprllerrsqragtmSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:COG4178 451 TAEAFSDAELREALEAVGLghLAERLDEEADWDQVL-----------------SLGEQQRLAFARLLLHKPDWLFLDE 511
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
17-166 |
3.51e-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: 58.33 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCgEPRASEGSIVFQGqdiTQWQTSRIM--REAVAIVPEGRRVFSRmTVE 94
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDG---VSWNSVPLQkwRKAFGVIPQKVFIFSG-TFR 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540804698 95 ENLAMGGFFADRHQYQQRIE----RVFTLFPRLLERRSQRAG-TMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAP 166
Cdd:cd03289 95 KNLDPYGKWSDEEIWKVAEEvglkSVIEQFPGQLDFVLVDGGcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 171
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
2-160 |
4.52e-10 |
|
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: 58.33 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIqaLHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREavaiv 81
Cdd:cd03291 40 LFFSNLCLVGAPV--LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPG----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 pegrrvfsrmTVEENLAMGGFFaDRHQYQQ-----RIERVFTLFPRLLERRSQRAG-TMSGGEQQMLAIGRALMSQPKLL 155
Cdd:cd03291 113 ----------TIKENIIFGVSY-DEYRYKSvvkacQLEEDITKFPEKDNTVLGEGGiTLSGGQRARISLARAVYKDADLY 181
|
....*
gi 1540804698 156 LLDEP 160
Cdd:cd03291 182 LLDSP 186
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-203 |
6.91e-10 |
|
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: 56.01 E-value: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGeprasegsivfqgqdITQWQTSRImreavaIVPEGRRVFsrmtveen 96
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG---------------LWPWGSGRI------GMPEGEDLL-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 97 lamggfFADRHQYqqriervftlFPR--LlerRSQRA----GTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPiiiQ 170
Cdd:cd03223 68 ------FLPQRPY----------LPLgtL---REQLIypwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE---E 125
|
170 180 190
....*....|....*....|....*....|....*....
gi 1540804698 171 QIFDIIQQLREEGMTIFLV------EQNANQALKLADRG 203
Cdd:cd03223 126 SEDRLYQLLKELGITVISVghrpslWKFHDRVLDLDGEG 164
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-212 |
7.07e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 57.99 E-value: 7.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 12 GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEP----RASEGSIVFQGQDITQW---QTSRIMREAVAIV--- 81
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLsprERRKIIGREIAMIfqe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEG-----RRVFSRMtvEENL---AMGGFFADRHQyqQRIERVFTLFPRLLERRSQR-----AGTMSGGEQQMLAIGRAL 148
Cdd:COG4170 98 PSScldpsAKIGDQL--IEAIpswTFKGKWWQRFK--WRKKRAIELLHRVGIKDHKDimnsyPHELTEGECQKVMIAMAI 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 149 MSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLRE-EGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-160 |
1.01e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQgQDITqwqTSRIMREAVAI 80
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLI---VARLQQDPPRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 VpEGrRVFSrmTVEENLA-MGGFFADRHQYQQRI-----ERVFTLFPRL-----------LERRSQ------------RA 131
Cdd:PRK11147 79 V-EG-TVYD--FVAEGIEeQAEYLKRYHDISHLVetdpsEKNLNELAKLqeqldhhnlwqLENRINevlaqlgldpdaAL 154
|
170 180
....*....|....*....|....*....
gi 1540804698 132 GTMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEP 183
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-230 |
1.59e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.19 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRAS--EGSIVFQGQDITQwqtsrimreav 78
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILD----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 79 aivpegrrvfsrMTVEENLAMGGFFA---------------------DRHQYQQRIE--------------RVFTLFPRL 123
Cdd:CHL00131 76 ------------LEPEERAHLGIFLAfqypieipgvsnadflrlaynSKRKFQGLPEldplefleiineklKLVGMDPSF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 124 LERRSQRAgtMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVE--QNANQALKlAD 201
Cdd:CHL00131 144 LSRNVNEG--FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILIThyQRLLDYIK-PD 220
|
250 260
....*....|....*....|....*....
gi 1540804698 202 RGYVLENGRVVLedTGAALLANEAVRSAY 230
Cdd:CHL00131 221 YVHVMQNGKIIK--TGDAELAKELEKKGY 247
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-160 |
1.73e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.61 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIqaLHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREavaiv 81
Cdd:TIGR01271 429 LFFSNFSLYVTPV--LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPG----- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 pegrrvfsrmTVEENLAMGGFFaDRHQYQQ-----RIERVFTLFPRLLERRSQRAG-TMSGGEQQMLAIGRALMSQPKLL 155
Cdd:TIGR01271 502 ----------TIKDNIIFGLSY-DEYRYTSvikacQLEEDIALFPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADLY 570
|
....*
gi 1540804698 156 LLDEP 160
Cdd:TIGR01271 571 LLDSP 575
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
71-233 |
1.78e-09 |
|
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: 57.33 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 71 SRIMREAVAIVPEGRRV--FSRMTVEENLAmggFFADRHQYQQR-----------IERVFTL----FPRL-LERRsqrAG 132
Cdd:TIGR00630 414 TRLKPEALAVTVGGKSIadVSELSIREAHE---FFNQLTLTPEEkkiaeevlkeiRERLGFLidvgLDYLsLSRA---AG 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 133 TMSGGEQQMLA----IGRALMSQpkLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNaNQALKLADR------ 202
Cdd:TIGR00630 488 TLSGGEAQRIRlatqIGSGLTGV--LYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTIRAADYvidigp 564
|
170 180 190
....*....|....*....|....*....|..
gi 1540804698 203 GYVLENGRVVLEDTGAALLAN-EAVRSAYLGG 233
Cdd:TIGR00630 565 GAGEHGGEVVASGTPEEILANpDSLTGQYLSG 596
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-159 |
2.66e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.88 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQaLHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQditqwQTSRIMREAVAI 80
Cdd:PRK13541 1 MLSLHQLQFNIEQKN-LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNC-----NINNIAKPYCTY 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 81 VPEGRRVFSRMTVEENLAmggFFADRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:PRK13541 75 IGHNLGLKLEMTVFENLK---FWSEIYNSAETLYAAIHYF-KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-124 |
3.86e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 55.96 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 20 VSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwqtsrimreavaivpegrrvfsrmtveenlam 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA-------------------------------- 398
|
90 100
....*....|....*....|....*...
gi 1540804698 100 ggffADRHQYQQRIERVFT---LFPRLL 124
Cdd:COG4615 399 ----DNREAYRQLFSAVFSdfhLFDRLL 422
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-160 |
5.31e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.90 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGE-PRASEGSIVFQGqditqwqtsrimreAVAIVPEGRRVFSrMTVEE 95
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGElPPRSDASVVIRG--------------TVAYVPQVSWIFN-ATVRD 697
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 96 NLAMGGFFaDRHQYQQRIE-----RVFTLFP-RLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:PLN03130 698 NILFGSPF-DPERYERAIDvtalqHDLDLLPgGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-161 |
6.29e-09 |
|
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: 54.72 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 23 TISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVfqgqditqwqtsrIMREAVAIVPEGRRVFSRMTVEENLA--MG 100
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIE-------------IELDTVSYKPQYIKADYEGTVRDLLSsiTK 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 101 GFFADrHQYQQRIERVFTLfPRLLERrsqRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPS 161
Cdd:cd03237 88 DFYTH-PYFKTEIAKPLQI-EQILDR---EVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-161 |
8.47e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQW---QTSRIMREA 77
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWvnqETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 78 VAIVPEGRRVFSRMTVEENLAM----GGFFADRHQYQQRIErVFTLFPR---LL-------ERRSQRAGTMSGGEQQMLA 143
Cdd:PRK10636 81 LEYVIDGDREYRQLEAQLHDANerndGHAIATIHGKLDAID-AWTIRSRaasLLhglgfsnEQLERPVSDFSGGWRMRLN 159
|
170
....*....|....*...
gi 1540804698 144 IGRALMSQPKLLLLDEPS 161
Cdd:PRK10636 160 LAQALICRSDLLLLDEPT 177
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-160 |
1.02e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.95 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGqditqwqtsrimreAVAIVPEGRRVfSRMTVEEN 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------------SVAYVPQQAWI-QNDSLREN 718
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540804698 97 LAMGGFFADRHqYQQRIERVfTLFPRLLERRS-------QRAGTMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:TIGR00957 719 ILFGKALNEKY-YQQVLEAC-ALLPDLEILPSgdrteigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
17-222 |
1.04e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.89 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRAS--EGSIVFQGQDITQwqtsRIMREaVAIVPEGRRVFSRMTVE 94
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK----QILKR-TGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 95 ENLAMGGFFadrhqyqqRIERVFTLFPRLLERRSQRAGT-----------------MSGGEQQMLAIGRALMSQPKLLLL 157
Cdd:PLN03211 159 ETLVFCSLL--------RLPKSLTKQEKILVAESVISELgltkcentiignsfirgISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540804698 158 DEPSLGLAPIIIQQIFDIIQQLREEGMTIFL-VEQNANQALKLADRGYVLENGRVVLEDTGAALLA 222
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-212 |
2.08e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.16 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 18 HQVSLTISQGEIVTLIGANGAGKT----TLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMREAVAIVPegRRVFS---- 89
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQNP--RSAFNplht 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 90 -RMTVEENLAMGGFFADRHQYQQRIE--------RVFTLFPRllerrsqragTMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:PRK10418 98 mHTHARETCLALGKPADDATLTAALEavglenaaRVLKLYPF----------EMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 161 SLGL-APIIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:PRK10418 168 TTDLdVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-159 |
2.09e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.82 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQ-ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQwqtsrimreavai 80
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA------------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 vpegrrvfsrmtveenlamggffADRHQYQQRIERVFT---LFPRLLERRSQRAGT------------------------ 133
Cdd:PRK10522 390 -----------------------EQPEDYRKLFSAVFTdfhLFDQLLGPEGKPANPalvekwlerlkmahkleledgris 446
|
170 180
....*....|....*....|....*....
gi 1540804698 134 ---MSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:PRK10522 447 nlkLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-159 |
2.61e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.80 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRiMREAVAIVPEGRRVFSRmTVEEN 96
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD-LRFKITIIPQDPVLFSG-SLRMN 1379
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540804698 97 LAMGGFFADRHQYQ----QRIERVFTLFPRLLERRSQRAG-TMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:TIGR00957 1380 LDPFSQYSDEEVWWalelAHLKTFVSALPDKLDHECAEGGeNLSVGQRQLVCLARALLRKTKILVLDE 1447
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-160 |
3.70e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 51.95 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 14 IQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQ---WQTSRIMREAVAIVPEGRRVFSr 90
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEpsfEATRSRNRYSVAYAAQKPWLLN- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540804698 91 MTVEENLAMGGFFaDRHQYQQRIERVfTLFPR--LLERRSQ-----RAGTMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:cd03290 93 ATVEENITFGSPF-NKQRYKAVTDAC-SLQPDidLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-161 |
4.44e-08 |
|
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: 53.02 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVF----------QGQDI-----T 66
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklayvdQSRDAldpnkT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 67 QWQTsrIMREAVAIVPEGRRVFSRmtveenlAMGGFFADRHQYQQriervftlfprllerrsQRAGTMSGGEQQMLAIGR 146
Cdd:TIGR03719 403 VWEE--ISGGLDIIKLGKREIPSR-------AYVGRFNFKGSDQQ-----------------KKVGQLSGGERNRVHLAK 456
|
170
....*....|....*
gi 1540804698 147 ALMSQPKLLLLDEPS 161
Cdd:TIGR03719 457 TLKSGGNVLLLDEPT 471
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-231 |
8.93e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.14 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 133 TMSGGEQQMLAIGRALMSQPK--LLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNaNQALKLADR------GY 204
Cdd:PRK00635 476 TLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRiidigpGA 554
|
90 100
....*....|....*....|....*...
gi 1540804698 205 VLENGRVVLEDTGAALLAN-EAVRSAYL 231
Cdd:PRK00635 555 GIFGGEVLFNGSPREFLAKsDSLTAKYL 582
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-164 |
1.37e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.56 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFN--QVSAHYGKIqaLHQVSLTISQGEIVTLIGANGAGKTTLLGTLCG--EPRASEGSIVFQGQDITQWQTSRIMRE 76
Cdd:PRK09580 1 MLSIKdlHVSVEDKAI--LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLELSPEDRAGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 77 A--------VAIVPEGRRVFSRMTVEENLAMGGFFA-DRHQYQQRIERVFTLF--PRLLERRSQRAGtMSGGEQQMLAIG 145
Cdd:PRK09580 79 GifmafqypVEIPGVSNQFFLQTALNAVRSYRGQEPlDRFDFQDLMEEKIALLkmPEDLLTRSVNVG-FSGGEKKRNDIL 157
|
170
....*....|....*....
gi 1540804698 146 RALMSQPKLLLLDEPSLGL 164
Cdd:PRK09580 158 QMAVLEPELCILDESDSGL 176
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-166 |
1.92e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 11 YGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGE-PRASEGSIVFQGQ---------DITQ---WQTSRIMREa 77
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhPQGYSNDLTLFGRrrgsgetiwDIKKhigYVSSSLHLD- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 78 vaivpegRRVFSRMtveENLAMGGFFADRHQYQQRIERVFTLFPRLLERRSQRAGT-------MSGGEQQMLAIGRALMS 150
Cdd:PRK10938 349 -------YRVSTSV---RNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKRTadapfhsLSWGQQRLALIVRALVK 418
|
170
....*....|....*.
gi 1540804698 151 QPKLLLLDEPSLGLAP 166
Cdd:PRK10938 419 HPTLLILDEPLQGLDP 434
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-212 |
2.01e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.57 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 12 GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEP----RASEGSIVFQGQDITQW-----------QTSRIMRE 76
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLsprerrklvghNVSMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 77 AVAIVPEGRRVfSRMTVEenlAMGGFFADRHQYQQ---RIERVFTLFPRLLERRSQRAG-----TMSGGEQQMLAIGRAL 148
Cdd:PRK15093 98 PQSCLDPSERV-GRQLMQ---NIPGWTYKGRWWQRfgwRKRRAIELLHRVGIKDHKDAMrsfpyELTEGECQKVMIAIAL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 149 MSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLRE-EGMTIFLVEQNANQALKLADRGYVLENGRVV 212
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-160 |
2.70e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 21 SLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSI-VFQGQDITQWQTSRimreaVAIVPEgrrvfsrMTVEENLAM 99
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhCGTKLEVAYFDQHR-----AELDPE-------KTVMDNLAE 406
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 100 G-------GffADRH--QYQQRIervftLFPrllerrSQRAGT----MSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:PRK11147 407 GkqevmvnG--RPRHvlGYLQDF-----LFH------PKRAMTpvkaLSGGERNRLLLARLFLKPSNLLILDEP 467
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
2-202 |
4.19e-07 |
|
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: 48.47 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 2 LSFNQVSAHygkiqALHQVSLTISQGEIVTLIGANGAGKTTLlgtlcgeprasegsiVFQGqditqwqtsrIMREAVAIV 81
Cdd:cd03238 1 LTVSGANVH-----NLQNLDVSIPLNVLVVVTGVSGSGKSTL---------------VNEG----------LYASGKARL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEGRRVFSRMTVeenlamggFFADrhQYQQRIERVFTLFPrlLErrsQRAGTMSGGEQQMLAIGRALMSQPK--LLLLDE 159
Cdd:cd03238 51 ISFLPKFSRNKL--------IFID--QLQFLIDVGLGYLT--LG---QKLSTLSGGELQRVKLASELFSEPPgtLFILDE 115
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1540804698 160 PSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNaNQALKLADR 202
Cdd:cd03238 116 PSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADW 157
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-160 |
4.30e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.93 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 3 SFNQVS-AHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCG-------EPRASEG-SIVFQGQDiTQWQTSRI 73
Cdd:TIGR03719 6 TMNRVSkVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdkdfngEARPQPGiKVGYLPQE-PQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 74 MREAV-AIVPEGRRVFSRMTvEENLAMGGFFADrhqYQQRIERVFTLFPRL-------LERRSQRA-------------G 132
Cdd:TIGR03719 85 VRENVeEGVAEIKDALDRFN-EISAKYAEPDAD---FDKLAAEQAELQEIIdaadawdLDSQLEIAmdalrcppwdadvT 160
|
170 180
....*....|....*....|....*...
gi 1540804698 133 TMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEP 188
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
14-222 |
4.34e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.40 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 14 IQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDIT----QWQTSRI----MREAVAIVPEGR 85
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySYRSQRIrmifQDPSTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 86 ---------RVFSRMTVEE-------NLAMGGFFADRHQYqqriervftlFPRLLerrsqragtmSGGEQQMLAIGRALM 149
Cdd:PRK15112 106 isqildfplRLNTDLEPEQrekqiieTLRQVGLLPDHASY----------YPHML----------APGQKQRLGLARALI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 150 SQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREE-GMTIFLVEQNANQALKLADRGYVLENGRVVLEDTGAALLA 222
Cdd:PRK15112 166 LRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
16-222 |
4.42e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 16 ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQ-----DITqwqtSRimreavaivpegRRV--- 87
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvdagDIA----TR------------RRVgym 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 88 ---FS---RMTVEENLAMGG--FFADRHQYQQRIERVFTLFpRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:NF033858 345 sqaFSlygELTVRQNLELHArlFHLPAAEIAARVAEMLERF-DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 160 PSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKlADRGYVLENGRVVLEDTGAALLA 222
Cdd:NF033858 424 PTSGVDPVARDMFWRLLIELsREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVA 486
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
54-164 |
4.63e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 54 SEGSIVFQGQDITQWQTsRIMREAVAIVPEGRRVFSrMTVEENLAMGGFFADRhqyqQRIERV--FTLFPRLLERRSQRA 131
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNL-KDLRNLFSIVSQEPMLFN-MSIYENIKFGKEDATR----EDVKRAckFAAIDEFIESLPNKY 1348
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1540804698 132 GT--------MSGGEQQMLAIGRALMSQPKLLLLDEPSLGL 164
Cdd:PTZ00265 1349 DTnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSL 1389
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-160 |
4.89e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 7 VSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIvfqgqditQWQtsrimreavaivpegrr 86
Cdd:PRK15064 325 LTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWS----------------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 87 vfsrmtveENlAMGGFFADRHQYQqrIERVFTLFP--------------------RLL---ERRSQRAGTMSGGEQQMLA 143
Cdd:PRK15064 380 --------EN-ANIGYYAQDHAYD--FENDLTLFDwmsqwrqegddeqavrgtlgRLLfsqDDIKKSVKVLSGGEKGRML 448
|
170
....*....|....*..
gi 1540804698 144 IGRALMSQPKLLLLDEP 160
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEP 465
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
10-211 |
5.33e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.89 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 10 HYgkiqALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGqditqwqtsrimreAVAIVPEGRRVFS 89
Cdd:PRK13545 37 HY----ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--------------SAALIAISSGLNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 90 RMTVEENLAMGGFFA--DRHQYQQRIERVFTlFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEP-SLGlAP 166
Cdd:PRK13545 99 QLTGIENIELKGLMMglTKEKIKEIIPEIIE-FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAlSVG-DQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1540804698 167 IIIQQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRV 211
Cdd:PRK13545 177 TFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-163 |
7.71e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 15 QALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEP--RASEGSIVFQGQDITQWQTSRIMREAVAIVPEGRRVF---- 88
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYglnl 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 89 ----SRMTVEENL---AMGGFFADRHQYqqrieRVFTLFPRLLERRS----QRAGTMSGGEQQMLAIGRALMSQPKLLLL 157
Cdd:NF040905 354 iddiKRNITLANLgkvSRRGVIDENEEI-----KVAEEYRKKMNIKTpsvfQKVGNLSGGNQQKVVLSKWLFTDPDVLIL 428
|
....*.
gi 1540804698 158 DEPSLG 163
Cdd:NF040905 429 DEPTRG 434
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-230 |
8.13e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.97 E-value: 8.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGK----IQALHQVSLTISQGEIVTLIGANGAGKT----TLLGTLCGEPRASEGSIVFQGQD---ITQWQ 69
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDlqrISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 70 TSRIMREAVAIVPE------------GRRVFSRMTVEEnlamGGFFADRHQyqqRIERVFTL--FPRLLERRSQRAGTMS 135
Cdd:PRK11022 83 RRNLVGAEVAMIFQdpmtslnpcytvGFQIMEAIKVHQ----GGNKKTRRQ---RAIDLLNQvgIPDPASRLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 136 GGEQQMLAIGRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQL-REEGMTIFLVEQNANQALKLADRGYVLENGRVVle 214
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVV-- 233
|
250
....*....|....*.
gi 1540804698 215 DTGAALLANEAVRSAY 230
Cdd:PRK11022 234 ETGKAHDIFRAPRHPY 249
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
128-202 |
1.93e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.25 E-value: 1.93e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540804698 128 SQRAGTMSGGEQQMLA----IGRALMSQpkLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNaNQALKLADR 202
Cdd:cd03270 132 SRSAPTLSGGEAQRIRlatqIGSGLTGV--LYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADH 207
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-209 |
2.18e-06 |
|
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: 46.47 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 12 GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRAS--EGSIVFQGQDITQWQTSRImreavAIVPEGRRVFS 89
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNFQRST-----GYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 90 RMTVEENLamggffadrhqyqqriervftLFPRLLerrsqRAgtMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPIII 169
Cdd:cd03232 93 NLTVREAL---------------------RFSALL-----RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1540804698 170 QQIFDIIQQLREEGMTIFL-VEQNANQALKLADRGYVLENG 209
Cdd:cd03232 145 YNIVRFLKKLADSGQAILCtIHQPSASIFEKFDRLLLLKRG 185
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-161 |
2.43e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 21 SLTISQGEIVTLIGANGAGKTTLLGTLC-----GEPRASEGSIVFQ---GQDITQWQT--------SRIMREAVAIVPEG 84
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGIPKNCQILHVEQevvGDDTTALQCvlntdierTQLLEEEAQLVAQQ 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 85 RRV-FSRMTVEENLAMGGFfADRHQYQQRIERVFTLFPRL-------------------LERRSQRAGTMSGGEQQMLAI 144
Cdd:PLN03073 277 RELeFETETGKGKGANKDG-VDKDAVSQRLEEIYKRLELIdaytaearaasilaglsftPEMQVKATKTFSGGWRMRIAL 355
|
170
....*....|....*..
gi 1540804698 145 GRALMSQPKLLLLDEPS 161
Cdd:PLN03073 356 ARALFIEPDLLLLDEPT 372
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-161 |
2.81e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 1 MLSFNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIvfqgqditqwqtsrimreavai 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---------------------- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 81 vpegrrvfsrmtveeNLAMG---GFFAdRHQY------QQRIERVFTLFPRLLERR---------------SQRAGTMSG 136
Cdd:PRK10636 370 ---------------GLAKGiklGYFA-QHQLeflradESPLQHLARLAPQELEQKlrdylggfgfqgdkvTEETRRFSG 433
|
170 180
....*....|....*....|....*
gi 1540804698 137 GEQQMLAIGRALMSQPKLLLLDEPS 161
Cdd:PRK10636 434 GEKARLVLALIVWQRPNLLLLDEPT 458
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-159 |
2.86e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.49 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 20 VSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMrEAVAivpegrRVFSRMTVEENLAM 99
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLI-DAIG------RKGDFKDAVELLNA 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 100 GGfFADrhqyqqrierVFTLFPRLLErrsqragtMSGGEQQMLAIGRALMSQPKLLLLDE 159
Cdd:COG2401 122 VG-LSD----------AVLWLRRFKE--------LSTGQKFRFRLALLLAERPKLLVIDE 162
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-161 |
3.97e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 4 FNQVSAHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSI----------VFQGQDI-----TQW 68
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIkigetvklayVDQSRDAldpnkTVW 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 69 qtsrimrEAVA-----IVPEGRRVFSRMTVeenlamgGFFADRHQYQQriervftlfprllerrsQRAGTMSGGEQQMLA 143
Cdd:PRK11819 407 -------EEISggldiIKVGNREIPSRAYV-------GRFNFKGGDQQ-----------------KKVGVLSGGERNRLH 455
|
170
....*....|....*...
gi 1540804698 144 IGRALMSQPKLLLLDEPS 161
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPT 473
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-160 |
9.12e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.31 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 17 LHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIvfqgqditqWQTSRImreavAIVPEGRRVFSrMTVEEN 96
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAERSI-----AYVPQQAWIMN-ATVRGN 740
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540804698 97 LAmggFF----ADRHQYQQRI---ERVFTLFPRLLERRSQRAG-TMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:PTZ00243 741 IL---FFdeedAARLADAVRVsqlEADLAQLGGGLETEIGEKGvNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-164 |
9.63e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 13 KIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEP----RASEGSIVFQGqdITQWQTSRIMREAVAIVPEGRRVF 88
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDG--ITPEEIKKHYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 89 SRMTVEENLAmggfFADRHQY-QQRIERVftlfPRLLERRSQRAGTM---------------------SGGEQQMLAIGR 146
Cdd:TIGR00956 151 PHLTVGETLD----FAARCKTpQNRPDGV----SREEYAKHIADVYMatyglshtrntkvgndfvrgvSGGERKRVSIAE 222
|
170
....*....|....*...
gi 1540804698 147 ALMSQPKLLLLDEPSLGL 164
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGL 240
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-164 |
4.97e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 43.56 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 12 GKIQALHQVSLTISQGEIVTLIGANGAGKT----TLLGTLCGEPRASeGSIVFQGQDI---TQWQTSRIMREAVAIVpeg 84
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIG-GSATFNGREIlnlPEKELNKLRAEQISMI--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 85 rrvFSR--------MTVEENLA--------MGGFFADRhqyqqriERVFTL----FPRLLERRSQRAGTMSGGEQQMLAI 144
Cdd:PRK09473 103 ---FQDpmtslnpyMRVGEQLMevlmlhkgMSKAEAFE-------ESVRMLdavkMPEARKRMKMYPHEFSGGMRQRVMI 172
|
170 180
....*....|....*....|
gi 1540804698 145 GRALMSQPKLLLLDEPSLGL 164
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTAL 192
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-166 |
7.88e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.53 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 24 ISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDITQWQTSRIMrEAVAIVPEGRRVFSRMtveENLAMGGFF 103
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFM-AYLGHLPGLKADLSTL---ENLHFLCGL 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 104 ADRHQyQQRIERVFTLFPrLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAP 166
Cdd:PRK13543 110 HGRRA-KQMPGSALAIVG-LAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-160 |
1.03e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 3 SFNQVS-AHYGKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQgQDITqwqtsrimreaVAIV 81
Cdd:PRK11819 8 TMNRVSkVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGIK-----------VGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 82 PEGRRVFSRMTVEENLAMGgfFADRHQYQQRIERVFTLFP--------------RL-----------LERRSQRA----- 131
Cdd:PRK11819 76 PQEPQLDPEKTVRENVEEG--VAEVKAALDRFNEIYAAYAepdadfdalaaeqgELqeiidaadawdLDSQLEIAmdalr 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1540804698 132 --------GTMSGGEQQMLAIGRALMSQPKLLLLDEP 160
Cdd:PRK11819 154 cppwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-211 |
1.36e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.11 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 16 ALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQditqwqtsrimreaVAIVPEGRRVFSRMTVEE 95
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--------------VSVIAISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 96 N-----LAMGgffADRHQYQQRIERVFTlFPRLLERRSQRAGTMSGGEQQMLAIGRALMSQPKLLLLDEP-SLGlAPIII 169
Cdd:PRK13546 105 NiefkmLCMG---FKRKEIKAMTPKIIE-FSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSVG-DQTFA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1540804698 170 QQIFDIIQQLREEGMTIFLVEQNANQALKLADRGYVLENGRV 211
Cdd:PRK13546 180 QKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-209 |
2.06e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 133 TMSGGEQQMLAIGRALMS---QPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANqALKLADrgYVLENG 209
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMH-VVKVAD--YVLELG 885
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
12-164 |
2.38e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 12 GKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGepRASEGSIvfqgqditqwqTSRIMreavaIV--PEGRRVFS 89
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVI-----------TGGDR-----LVngRPLDSSFQ 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 90 R--------------MTVEENLAMGGFF--------ADRHQYqqrIERVFtlfpRLLERRSQR---AGTMSGG---EQ-Q 140
Cdd:TIGR00956 836 RsigyvqqqdlhlptSTVRESLRFSAYLrqpksvskSEKMEY---VEEVI----KLLEMESYAdavVGVPGEGlnvEQrK 908
|
170 180
....*....|....*....|....*
gi 1540804698 141 MLAIGRALMSQPKLLL-LDEPSLGL 164
Cdd:TIGR00956 909 RLTIGVELVAKPKLLLfLDEPTSGL 933
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-207 |
2.45e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 40.63 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 24 ISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSivfqgqdiTQWQTSRImreavAIVPegrrvfsrmtveenlamggff 103
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN--------DEWDGITP-----VYKP--------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 104 adrhqyqQRIErvftlfprllerrsqragtMSGGEQQMLAIGRALMSQPKLLLLDEPSLGLAPIIIQQIFDIIQQLREEG 183
Cdd:cd03222 68 -------QYID-------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
170 180
....*....|....*....|....*
gi 1540804698 184 M-TIFLVEQNANQALKLADRGYVLE 207
Cdd:cd03222 122 KkTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
7-58 |
3.13e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.07 E-value: 3.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1540804698 7 VSAHYGK-IQALHQVsltISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSI 58
Cdd:PRK01889 177 VSALDGEgLDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-159 |
5.01e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.61 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 4 FNQVSAhygKIQALHQVSLTISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGSIVFQGQDI-----TQWQTSR-----I 73
Cdd:PRK10261 330 LNRVTR---EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspGKLQALRrdiqfI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 74 MREAVAIVPEGRRV-FSRMtveENLAMGGFF---ADRHQYQQRIERVfTLFPrllERRSQRAGTMSGGEQQMLAIGRALM 149
Cdd:PRK10261 407 FQDPYASLDPRQTVgDSIM---EPLRVHGLLpgkAAAARVAWLLERV-GLLP---EHAWRYPHEFSGGQRQRICIARALA 479
|
170
....*....|
gi 1540804698 150 SQPKLLLLDE 159
Cdd:PRK10261 480 LNPKVIIADE 489
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
131-164 |
5.92e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.78 E-value: 5.92e-04
10 20 30
....*....|....*....|....*....|....
gi 1540804698 131 AGTMSGGEQQMLAIGRALMSQPKLLLLDEPSLGL 164
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
72-209 |
1.97e-03 |
|
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: 38.84 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 72 RIMREAVAIVPEGRRVFS--RMTVEENLAmggFFADRHQYQQRIErvfTLFPRLLE--RRSQRAGTMSGGEQQMLAIGRA 147
Cdd:TIGR00630 770 RYNRETLEVKYKGKNIADvlDMTVEEAYE---FFEAVPSISRKLQ---TLCDVGLGyiRLGQPATTLSGGEAQRIKLAKE 843
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540804698 148 LMSQ---PKLLLLDEPSLGLAPIIIQQIFDIIQQLREEGMTIFLVEQNANqALKLADrgYVLENG 209
Cdd:TIGR00630 844 LSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLD-VIKTAD--YIIDLG 905
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-98 |
2.31e-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: 2.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540804698 26 QGEIVTLIGANGAGKTTLLGTLCGE-PRASEGSIVFQGQDITQWQTSRIMREAVAIVPEGRRVFSRMTVEENLA 98
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARElGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALA 74
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-161 |
4.41e-03 |
|
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: 37.84 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 23 TISQGEIVTLIGANGAGKTTLLGTLCGEPRASEGsivfqgqditqwqtsRIMREavaivPEGRRVFSRMTVEEnlaMGGF 102
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLG---------------DYDEE-----PSWDEVLKRFRGTE---LQDY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540804698 103 FAD----------RHQYQQRIERVFTLFPR-LLERRSQRA-------------------GTMSGGEQQMLAIGRALMSQP 152
Cdd:COG1245 152 FKKlangeikvahKPQYVDLIPKVFKGTVReLLEKVDERGkldelaeklglenildrdiSELSGGELQRVAIAAALLRDA 231
|
....*....
gi 1540804698 153 KLLLLDEPS 161
Cdd:COG1245 232 DFYFFDEPS 240
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-44 |
9.04e-03 |
|
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: 36.52 E-value: 9.04e-03
10 20
....*....|....*....|....*...
gi 1540804698 17 LHQVSLTISQGeIVTLIGANGAGKTTLL 44
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSIL 40
|
|
| |
