|
Name |
Accession |
Description |
Interval |
E-value |
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-232 |
3.41e-140 |
|
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: 391.50 E-value: 3.41e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAYV 81
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLLMGLSRFSARDaRAVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRS-RKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600055 162 EGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDMESEGVRGLVAI 232
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLAV 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-221 |
9.33e-119 |
|
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: 337.72 E-value: 9.33e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAY 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGL-SRFSARDARAVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAyARRDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 160 PTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDM 221
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRLNREG-VTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-224 |
1.58e-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: 326.31 E-value: 1.58e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAYV 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLLMGLSRFSARDARAVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 162 EGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDMESE 224
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEG-VTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-216 |
4.77e-58 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 183.73 E-value: 4.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTglRPHQRVRAGIAYV 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA--RDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLLM--GLSRFSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:COG1131 79 PQEPALYPDLTVRENLRFfaRLYGLPRKEARERIDELLELFG-LTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 160 PTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEG-KTVLLSTHYLEEAERLCDRVAIIDKGRIVADG 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-216 |
2.34e-56 |
|
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: 179.85 E-value: 2.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAY 80
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGL--------------SRFSARDARAVPDFIYEL--FPVLREMKQRRGGDLSGGQQQQLAI 144
Cdd:COG0411 84 TFQNPRLFPELTVLENVLVAAharlgrgllaallrLPRARREEREARERAEELleRVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 145 GRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-217 |
2.70e-56 |
|
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: 179.17 E-value: 2.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAYV 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLLMGLSR------FSARDARAVPDFIYELFPVLREMK-----QRRGGDLSGGQQQQLAIGRALAS 150
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQArtgsglLLARARREEREARERAEELLERVGladlaDRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 151 QPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQGR 217
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-216 |
3.03e-55 |
|
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: 176.59 E-value: 3.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPhqRVRAGIAY 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR--EARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMgLSRFSARDARAVPDFIYELFPV--LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILD 158
Cdd:COG4555 79 LPDERGLYDRLTVRENIRY-FAELYGLFDEELKKRIEELIELlgLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 159 EPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEG-KTVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-216 |
1.68e-54 |
|
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: 175.23 E-value: 1.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAgIAY 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMG-------LSRFSARDARAVPDfiyelfpVLR-----EMKQRRGGDLSGGQQQQLAIGRAL 148
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGryphlglFGRPSAEDREAVEE-------ALErtgleHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 149 ASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQG 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-227 |
7.29e-52 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 167.75 E-value: 7.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAY 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMG-----LSRFSARDARavpdfIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLL 155
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGgffaeRDQFQERIKW-----VYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 156 ILDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRD-MESEGVR 227
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQG-MTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAlLANEAVR 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-212 |
1.52e-49 |
|
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: 159.87 E-value: 1.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTglRPHQRVRAGIAYV 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK--KEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLlmglsrfsardaravpdfiyelfpvlremkqrrggDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:cd03230 79 PEEPSLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15600055 162 EGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEI 212
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEG-KTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
4.18e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 161.02 E-value: 4.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRsltglrPHQRVRAGIAY 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK------PPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREI---FPrLTVEENLLMGL-------SRFSARDARAVPDfiyelfpVLREM-----KQRRGGDLSGGQQQQLAIG 145
Cdd:COG1121 80 VPQRAEVdwdFP-ITVRDVVLMGRygrrglfRRPSRADREAVDE-------ALERVgledlADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 146 RALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEI 212
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREG-KTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-216 |
1.33e-48 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 159.39 E-value: 1.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPH-QRVRAGIA 79
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDiNKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 80 YVPQGREIFPRLTVEENLLMGL------SRFSARD-ARAVpdfiyeLFPV-LREMKQRRGGDLSGGQQQQLAIGRALASQ 151
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPikvkkmSKAEAEErAMEL------LERVgLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 152 PRLLILDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKEG-MTMVVVTHEMGFAREVADRVVFMDGGRIVEEG 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-212 |
1.54e-46 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 153.45 E-value: 1.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPH-QRVRAGIAY 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGLSRFSARDARAVPDFIYELFPV--LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKvgLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600055 159 EPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEI 212
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-216 |
9.33e-46 |
|
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: 151.52 E-value: 9.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAYV 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLLMGL--SRFSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLklRGVPKAEIRARVRELLELVG-LEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 160 PTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-216 |
2.64e-45 |
|
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: 150.38 E-value: 2.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 11 YGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRsltglrPHQRVRAGIAYVPQGREI--- 87
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK------PLEKERKRIGYVPQRRSIdrd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 88 FPrLTVEENLLMGL-------SRFSARDARAVpdfIYELFPV-LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:cd03235 83 FP-ISVRDVVLMGLyghkglfRRLSKADKAKV---DEALERVgLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 160 PTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARgEIVQQG 216
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRREG-MTILVVTHDLGLVLEYFDRVLLLNR-TVVASG 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-189 |
1.23e-44 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 149.41 E-value: 1.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAY 80
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGL--SRFSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILD 158
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAVLelRKLSKKEREERLEELLEEFG-ITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190
....*....|....*....|....*....|.
gi 15600055 159 EPTEGIQPSVIKEIGAVVRSLAARGdMAILL 189
Cdd:COG1137 162 EPFAGVDPIAVADIQKIIRHLKERG-IGVLI 191
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-188 |
1.65e-44 |
|
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: 148.01 E-value: 1.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHqrVRAGIAY 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED--YRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGLSRFSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEP 160
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVG-LAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180
....*....|....*....|....*...
gi 15600055 161 TEGIQPSVIKEIGAVVRSLAARGDMAIL 188
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-211 |
8.20e-44 |
|
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: 145.41 E-value: 8.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRP-HQRVRAGIAY 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGlsrfsardaravpdfiyelfpvlremkqrrggdLSGGQQQQLAIGRALASQPRLLILDEP 160
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG---------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15600055 161 TEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGE 211
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-220 |
1.20e-43 |
|
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: 153.52 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGS-----HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQR-- 73
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 74 VRAGIAYVPQG--REIFPRLTVEENLLMGLSRFSARDARAVPDFIYELfpvL------REMKQRRGGDLSGGQQQQLAIG 145
Cdd:COG1123 340 LRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAEL---LervglpPDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 146 RALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRD 220
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-229 |
4.93e-43 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 145.58 E-value: 4.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKL-HQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPH--QRVRAG 77
Cdd:COG3638 2 MLELRNLsKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRalRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 78 IAYVPQGREIFPRLTVEENLLMG-----------LSRFSARD-ARA--------VPDFIYelfpvlremkqRRGGDLSGG 137
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGrlgrtstwrslLGLFPPEDrERAlealervgLADKAY-----------QRADQLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 138 QQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGR 217
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGP 230
|
250
....*....|..
gi 15600055 218 GRDMESEGVRGL 229
Cdd:COG3638 231 PAELTDAVLREI 242
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-220 |
1.34e-42 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 143.63 E-value: 1.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKL-HQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIAY 80
Cdd:COG1122 1 IELENLsFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE-LRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQgreiFPRL-----TVEENLLMGLSRF--SARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPR 153
Cdd:COG1122 80 VFQ----NPDDqlfapTVEEDVAFGPENLglPREEIRERVEEALELVG-LEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 154 LLILDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRD 220
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-220 |
1.80e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 146.78 E-value: 1.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAY 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR---NVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGLS--RFSARDARA-VPDFIyELfpV-LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLI 156
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRmrGVPKAEIRArVAELL-EL--VgLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600055 157 LDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLV-----EqfydfAAELADQYLVMARGEIVQQGRGRD 220
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRRLQRELGITFIYVthdqeE-----ALALADRIAVMNDGRIEQVGTPEE 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-227 |
2.55e-42 |
|
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: 143.07 E-value: 2.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAYV 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLL-----MGLSRfSARDARAvpDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLI 156
Cdd:cd03218 81 PQEASIFRKLTVEENILavleiRGLSK-KEREEKL--EELLEEFH-ITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 157 LDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDM-ESEGVR 227
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRG-IGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIaANELVR 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-223 |
9.19e-42 |
|
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: 142.25 E-value: 9.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYG----GSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvRA 76
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF-RR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 77 GIAYVPQ-GREIF-PRLTVEENL-----LMGLSRFSARDARAVPDFiyELFPVLREmkqRRGGDLSGGQQQQLAIGRALA 149
Cdd:COG1124 80 RVQMVFQdPYASLhPRHTVDRILaeplrIHGLPDREERIAELLEQV--GLPPSFLD---RYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600055 150 SQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDMES 223
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-213 |
1.27e-41 |
|
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: 140.47 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 8 HQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLtglRPHQRVRAgIAYVPQ--GR 85
Cdd:cd03226 7 FSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKS-IGYVMQdvDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 86 EIFpRLTVEENLLMGLSRFSARDARAvpDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQ 165
Cdd:cd03226 83 QLF-TDSVREELLLGLKELDAGNEQA--ETVLKDLD-LYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600055 166 PSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIV 213
Cdd:cd03226 159 YKNMERVGELIRELAAQG-KAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-216 |
2.70e-41 |
|
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: 140.33 E-value: 2.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGS----HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQR--V 74
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkiR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 75 RAGIAYVPQ--GREIFPRLTVEENLLMGLSRF----SARDARAVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRAL 148
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHgklsKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 149 ASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-216 |
3.92e-41 |
|
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: 138.34 E-value: 3.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 3 QVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAgIAYVP 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 83 QGREifprltveenlLMGLSRFSARDARavpdfiyelfpvlremkqrrggDLSGGQQQQLAIGRALASQPRLLILDEPTE 162
Cdd:cd03214 80 QALE-----------LLGLAHLADRPFN----------------------ELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600055 163 GIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-216 |
2.53e-40 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 138.02 E-value: 2.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPH--QRVRAGIA 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 80 YVPQGREIFPRLTVEENLLMGLSRFSARDARAVPDFIYE-LFPV-LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLIL 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEkLEAVgLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600055 158 DEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-213 |
5.06e-40 |
|
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: 137.70 E-value: 5.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGS-HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPH--QRVRAGI 78
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 79 AYVPQGREIFPRLTVEENLLMG-----------LSRFSARD-ARAvpdfIYELFPV-LREMKQRRGGDLSGGQQQQLAIG 145
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrstwrslFGLFPKEEkQRA----LAALERVgLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 146 RALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIV 213
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
6.35e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 138.70 E-value: 6.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTglrphQRVRAGIAY 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-----PEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENL-----LMGLSRfsaRDARAVPDFIYELFpvlrEMKQRRG---GDLSGGQQQQLAIGRALASQP 152
Cdd:COG4152 76 LPEERGLYPKMKVGEQLvylarLKGLSK---AEAKRRADEWLERL----GLGDRANkkvEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600055 153 RLLILDEPTEGIQP---SVIKEigaVVRSLAARGdMAIL-------LVEqfydfaaELADQYLVMARGEIVQQG 216
Cdd:COG4152 149 ELLILDEPFSGLDPvnvELLKD---VIRELAAKG-TTVIfsshqmeLVE-------ELCDRIVIINKGRKVLSG 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-161 |
1.10e-39 |
|
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: 133.93 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGlRPHQRVRAGIAYVPQGREIFPRLTVEEN 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD-DERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 97 LLMG--LSRFSARDARAVPDFIYELFPVLREMKQR---RGGDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:pfam00005 80 LRLGllLKGLSKREKDARAEEALEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-221 |
1.48e-39 |
|
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: 142.35 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYY--GGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAR---EGQVAWEGRSLTGLRPHQRVR 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 76 AgIAYVPQGREI-FPRLTVEENLLMGLSRFSARDARAVPDFIYELFPV-LREMKQRRGGDLSGGQQQQLAIGRALASQPR 153
Cdd:COG1123 84 R-IGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVgLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 154 LLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDM 221
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-212 |
3.27e-39 |
|
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: 133.71 E-value: 3.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHqyygGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAY 80
Cdd:cd03215 4 VLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGRE---IFPRLTVEENLLMGLSrfsardaravpdfiyelfpvlremkqrrggdLSGGQQQQLAIGRALASQPRLLIL 157
Cdd:cd03215 80 VPEDRKregLVLDLSVAENIALSSL-------------------------------LSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 158 DEPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEI 212
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAG-KAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-216 |
9.12e-39 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 134.35 E-value: 9.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYG-GSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPH--QRVRAG 77
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 78 IAYVPQGREIFPRLTVEENLLMG-----------LSRFSARD-ARAvpdfIYELFPV-LREMKQRRGGDLSGGQQQQLAI 144
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGrlgykptwrslLGRFSEEDkERA----LSALERVgLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 145 GRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDG 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-211 |
2.05e-38 |
|
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: 132.59 E-value: 2.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 8 HQYYGGSH-ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvRAGIAYVPQgre 86
Cdd:cd03225 7 FSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL-RRKVGLVFQ--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 87 iFPR-----LTVEENLL-----MGLSRF--SARDARAVPDFIyelfpvLREMKQRRGGDLSGGQQQQLAIGRALASQPRL 154
Cdd:cd03225 83 -NPDdqffgPTVEEEVAfglenLGLPEEeiEERVEEALELVG------LEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 155 LILDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGE 211
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-216 |
6.91e-38 |
|
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: 132.03 E-value: 6.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQR--VRAGI 78
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyeLRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 79 AYVPQGREIFPRLTVEENLLMGL---SRFSARDARAVPDFIYELfpV-LREMKQRRGGDLSGGQQQQLAIGRALASQPRL 154
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLrehTDLSEAEIRELVLEKLEL--VgLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 155 LILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-212 |
8.41e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 130.71 E-value: 8.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIAYV 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE-WRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQgrEifPRL---TVEENLLMGlsrFSARDARAVPDFIYELFPVL---REMKQRRGGDLSGGQQQQLAIGRALASQPRLL 155
Cdd:COG4619 80 PQ--E--PALwggTVRDNLPFP---FQLRERKFDRERALELLERLglpPDILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600055 156 ILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLV----EQfydfAAELADQYLVMARGEI 212
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVshdpEQ----IERVADRVLTLEAGRL 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-221 |
1.55e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 136.69 E-value: 1.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAY 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMG--LSRFS-------ARDARAvpdfiyelfpVLREMK-----QRRGGDLSGGQQQQLAIGR 146
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGrePRRGGlidwramRRRARE----------LLARLGldidpDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 147 ALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDM 221
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQG-VAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-220 |
2.10e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 133.35 E-value: 2.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSL-TGLRPHQRvraGIAY 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRER---RVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGLS--RFSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILD 158
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRvrPPSKAEIRARVEELLELVQ-LEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 159 EPTEGIQPSVIKEIGAVVRSLAARGDMAILLV-----EqfydfAAELADQYLVMARGEIVQQGRGRD 220
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVthdqeE-----ALELADRVVVMNQGRIEQVGTPDE 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-213 |
2.60e-37 |
|
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: 127.93 E-value: 2.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAYV 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQgreifprltveenllmglsrfsardaravpdfiyelfpvlremkqrrggdLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:cd03216 81 YQ--------------------------------------------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600055 162 EGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIV 213
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-216 |
3.40e-37 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 129.41 E-value: 3.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYY----GGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGrsLTGLRPHQRVRA 76
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 77 GIAYVPQGREIFPRLTVEENL-----LMGLSRFSARDAravpdfIYELFPVL--REMKQRRGGDLSGGQQQQLAIGRALA 149
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLeyfagLYGLKGDELTAR------LEELADRLgmEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 150 SQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDmAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-231 |
7.74e-37 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 128.99 E-value: 7.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHiLRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAYV 81
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---DISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLLMGLsRFSARDARAVPDFIYELFPVL--REMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGL-KKRKVDKKEIERKVLEIAEMLgiDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600055 160 PTEG----IQPSVIKEIGAVVRSLaargDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDMESEGVRGLVA 231
Cdd:cd03299 156 PFSAldvrTKEKLREELKKIRKEF----GVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVA 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-216 |
1.46e-36 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 128.01 E-value: 1.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGS--HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHqrVRAGIA 79
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA--ARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 80 YVPQGREIFPRLTVEENLLM--GLSRFSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLIL 157
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFyaRLKGLPKSEIKEEVELLLRVLG-LTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600055 158 DEPTEGIQPSVIKEIGAVVrsLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLI--LEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-211 |
1.66e-36 |
|
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: 125.82 E-value: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 3 QVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIAYVP 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE-LRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 83 QgreifprltveenllmglsrfsardaravpdfiyelfpvlremkqrrggdLSGGQQQQLAIGRALASQPRLLILDEPTE 162
Cdd:cd00267 80 Q--------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600055 163 GIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGE 211
Cdd:cd00267 110 GLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
1.82e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 127.85 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGS----HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRV-- 74
Cdd:COG1136 4 LLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 75 -RAGIAYVPQGREIFPRLTVEENLLMGL--SRFSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQ 151
Cdd:COG1136 84 rRRHIGFVFQFFNLLPELTALENVALPLllAGVSRKERRERARELLERVG-LGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600055 152 PRLLILDEPT------EGiqpsviKEIGAVVRSLAARGDMAILLV--EQfydFAAELADQYLVMARGEIVQQGR 217
Cdd:COG1136 163 PKLILADEPTgnldskTG------EEVLELLRELNRELGTTIVMVthDP---ELAARADRVIRLRDGRIVSDER 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-226 |
3.69e-36 |
|
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: 130.62 E-value: 3.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 20 LSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTG------LRPHQRvraGIAYVPQGREIFPRLTV 93
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKR---RIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 94 EENLLMGLSRFSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIG 173
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFERVIELLG-IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600055 174 AVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDMESEGV 226
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-216 |
3.88e-36 |
|
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: 126.63 E-value: 3.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLrphqrVRAGIAYV 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA-----ARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENL-----LMGLSRfsaRDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLI 156
Cdd:cd03269 76 PEERGLYPKMKVIDQLvylaqLKGLKK---EEARRRIDEWLERLE-LSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 157 LDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAG-KTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-226 |
7.63e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.06 E-value: 7.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLhqyyGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAY 80
Cdd:COG1129 256 VLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VP-----QGreIFPRLTVEENLLMG-LSRFS-------ARDARAVPDFIyelfpvlREMK------QRRGGDLSGGQQQQ 141
Cdd:COG1129 332 VPedrkgEG--LVLDLSIRENITLAsLDRLSrgglldrRRERALAEEYI-------KRLRiktpspEQPVGNLSGGNQQK 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 142 LAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLV-----EqfydfAAELADQYLVMARGEIVQQG 216
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEG-KAVIVIsselpE-----LLGLSDRILVMREGRIVGEL 476
|
250
....*....|
gi 15600055 217 RGRDMESEGV 226
Cdd:COG1129 477 DREEATEEAI 486
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-216 |
8.14e-36 |
|
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: 125.79 E-value: 8.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAYV 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PqgrEIFPRLTVEENLLMGLSRFSARDARavpdfIYELFPV--LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:cd03268 81 P---GFYPNLTARENLRLLARLLGIRKKR-----IDEVLDVvgLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 160 PTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQG-ITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-216 |
1.89e-35 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 125.17 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLtgLRPHQRVRAGIAYV 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV--VREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLLM-----GLSRFSARD-ARAVPDFIyelfpVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLL 155
Cdd:cd03265 79 FQDLSVDDELTGWENLYIharlyGVPGAERRErIDELLDFV-----GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600055 156 ILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-160 |
3.01e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 125.59 E-value: 3.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYY----GGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHqrvra 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 77 gIAYVPQGREIFPRLTVEENLLMGL--SRFSARDARAVPDFIYELfpV-LREMKQRRGGDLSGGQQQQLAIGRALASQPR 153
Cdd:COG1116 82 -RGVVFQEPALLPWLTVLDNVALGLelRGVPKAERRERARELLEL--VgLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
....*..
gi 15600055 154 LLILDEP 160
Cdd:COG1116 159 VLLMDEP 165
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-225 |
5.72e-35 |
|
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: 130.26 E-value: 5.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLH-QYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvRAGIAY 80
Cdd:COG4988 337 IELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW-RRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPrLTVEENLLMGLSRFS-------ARDARAvPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPR 153
Cdd:COG4988 416 VPQNPYLFA-GTIRENLRLGRPDASdeeleaaLEAAGL-DEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 154 LLILDEPTEGIQPSVIKEIGAVVRSLaARGDMAILLVEQFYDfaAELADQYLVMARGEIVQQGRGRD-MESEG 225
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLAL--LAQADRILVLDDGRIVEQGTHEElLAKNG 563
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-216 |
1.10e-34 |
|
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: 122.79 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 20 LSFEAKvGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSL------TGLRPHQRvraGIAYVPQGREIFPRLTV 93
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkINLPPQQR---KIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 94 EENLLMGLSRFSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIG 173
Cdd:cd03297 93 RENLAFGLKRKRNREDRISVDELLDLLG-LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600055 174 AVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-216 |
1.23e-34 |
|
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: 126.37 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYygGSHILRgLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSL------TGLRPHQRv 74
Cdd:COG4148 2 MLEVDFRLRR--GGFTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargIFLPPHRR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 75 raGIAYVPQGREIFPRLTVEENLLMGLSRFSARDARAVPDFIYELF---PVLremkQRRGGDLSGGQQQQLAIGRALASQ 151
Cdd:COG4148 78 --RIGYVFQEARLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLgigHLL----DRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 152 PRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASG 216
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-216 |
1.25e-34 |
|
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: 123.06 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGL---VPAR--EGQVAWEGRSLTGLRPH-QRVR 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlIPGApdEGEVLLDGKDIYDLDVDvLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 76 AGIAYVPQGREIFPrLTVEENLLMGLSRFSARDARAVPDFIYElfpVLR------EMKQR-RGGDLSGGQQQQLAIGRAL 148
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEE---ALRkaalwdEVKDRlHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 149 ASQPRLLILDEPTEGIQPSVIKEIGAVVRSLaaRGDMAILLV----EQfydfAAELADQYLVMARGEIVQQG 216
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVthnmQQ----AARVADRTAFLLNGRLVEFG 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-216 |
1.93e-34 |
|
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: 122.30 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGeVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRphQRVRAGIAYV 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP--QKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENL--LMGLSRFSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:cd03264 78 PQEFGVYPNFTVREFLdyIAWLKGIPSKEVKARVDEVLELVN-LGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600055 160 PTEGIQP-------SVIKEIGAvvrslaargDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03264 157 PTAGLDPeerirfrNLLSELGE---------DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-217 |
2.96e-34 |
|
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: 129.18 E-value: 2.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 11 YGGSH--ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIAYVPQGREIF 88
Cdd:COG2274 483 YPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS-LRRQIGVVLQDVFLF 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 89 PRlTVEENLLMGLSRFS-------ARDArAVPDFIYELfP-----VLREmkqrRGGDLSGGQQQQLAIGRALASQPRLLI 156
Cdd:COG2274 562 SG-TIRENITLGDPDATdeeiieaARLA-GLHDFIEAL-PmgydtVVGE----GGSNLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600055 157 LDEPTEGIQPSVIKEIGAVVRSLAArgDMAILLVeqfydfA-----AELADQYLVMARGEIVQQGR 217
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLLK--GRTVIII------AhrlstIRLADRIIVLDKGRIVEDGT 692
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-216 |
3.31e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.19 E-value: 3.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAY 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR---NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGL--SRFSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILD 158
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLklRKVPKAEIDRRVREAAELLG-LEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 159 EPTEGIQP----SVIKEIGAVVRSLaargDMAILLV--EQfydfaAE---LADQYLVMARGEIVQQG 216
Cdd:COG3839 159 EPLSNLDAklrvEMRAEIKRLHRRL----GTTTIYVthDQ-----VEamtLADRIAVMNDGRIQQVG 216
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-212 |
3.43e-34 |
|
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: 121.83 E-value: 3.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGG----SHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRV--- 74
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 75 RAGIAYVPQGREIFPRLTVEENLLMGLsRFSARDARAVPDFIYELFPV--LREMKQRRGGDLSGGQQQQLAIGRALASQP 152
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPL-LLAGVPKKERRERAEELLERvgLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 153 RLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLV---EQFydfaAELADQYLVMARGEI 212
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVthdPEL----AEYADRIIELRDGKI 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-217 |
9.58e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 121.02 E-value: 9.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGsHILRgLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAY 80
Cdd:COG3840 1 MLRLDDLTYRYGD-FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER---PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGLS---RFSARDARAVPDFIYELfpVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLIL 157
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLGLRpglKLTAEQRAQVEQALERV--GLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 158 DEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGR 217
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGP 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-216 |
1.08e-33 |
|
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: 121.29 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAYV 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLLMGLsRFSARDARAVPDFIYELFPVLREMKQ------RRGGDLSGGQQQQLAIGRALASQPRLL 155
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGL-RVKPRSERPPEAEIRAKVHELLKLVQldwladRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600055 156 ILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVG 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-220 |
1.21e-33 |
|
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: 120.76 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGS----HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRV-- 74
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 75 RAGIAYVPQGREIFPRLTVEENL-----LMGLSRfSARDARavpdfIYELFPV--LREMKQRRGGDLSGGQQQQLAIGRA 147
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENValpleIAGVPK-AEIEER-----VLELLELvgLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 148 LASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRD 220
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-160 |
1.25e-33 |
|
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: 120.27 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGS----HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHqrvrag 77
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 78 IAYVPQGREIFPRLTVEENLLMGLS--RFSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLL 155
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLElqGVPKAEARERAEELLELVG-LSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
....*
gi 15600055 156 ILDEP 160
Cdd:cd03293 154 LLDEP 158
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-216 |
1.40e-33 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 123.61 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAYV 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKR---DYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLLMGLS--RFSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKnrGMGRAEVAERVAELLDLVG-LPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 160 PTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVG 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
1.66e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 122.22 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIayV 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV--V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLLMgLSRF---SARDARAVPDFIYElFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILD 158
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLV-FGRYfglSAAAARALVPPLLE-FAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 159 EPTEGIQPSVIKEIGAVVRSLAARGDmAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDM-ESE 224
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALiESE 229
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-221 |
2.54e-33 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 120.68 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLT-------GLRPH-- 71
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgELVPAdr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 72 ---QRVRAGIAYVPQGREIFPRLTVEENLL------MGLSRFSARD-ARAVpdfiyeLFPV-LREMKQRRGGDLSGGQQQ 140
Cdd:COG4598 88 rqlQRIRTRLGMVFQSFNLWSHMTVLENVIeapvhvLGRPKAEAIErAEAL------LAKVgLADKRDAYPAHLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 141 QLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRD 220
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEG-RTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAE 240
|
.
gi 15600055 221 M 221
Cdd:COG4598 241 V 241
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-216 |
2.50e-32 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 117.78 E-value: 2.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCL--MG-LVPAR--EGQVAWEGRSLTGLRPH-QRVR 75
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrMNdLVPGVriEGKVLFDGQDIYDKKIDvVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 76 AGIAYVPQGREIFPrLTVEENLLMGLSRFSARDaRAVPDFIYE-------LFPVLREMKQRRGGDLSGGQQQQLAIGRAL 148
Cdd:TIGR00972 82 RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKD-KKELDEIVEeslkkaaLWDEVKDRLHDSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 149 ASQPRLLILDEPTEGIQPSVIKEIGAVVRSLaaRGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPIATGKIEELIQEL--KKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYG 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-213 |
2.58e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 122.44 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAY 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGLS-----RFSARDARAvpdfiyelfpVLREMKQRRG---------GDLSGGQQQQLAIGR 146
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGLEptkggRLDRKAARA----------RIRELSERYGldvdpdakvEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 147 ALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLV-----EqfydfAAELADQYLVMARGEIV 213
Cdd:COG3845 155 ALYRGARILILDEPTAVLTPQEADELFEILRRLAAEG-KSIIFIthklrE-----VMAIADRVTVLRRGKVV 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
11-231 |
3.30e-32 |
|
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: 116.95 E-value: 3.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 11 YGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAYVPQGREIFPR 90
Cdd:cd03300 10 YGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---PVNTVFQNYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 91 LTVEENLLMGLS--RFSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSV 168
Cdd:cd03300 87 LTVFENIAFGLRlkKLPKAEIKERVAEALDLVQ-LEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 169 IKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDMESEGVRGLVA 231
Cdd:cd03300 166 RKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVA 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-216 |
1.15e-31 |
|
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: 115.04 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAYV 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLLMGLsRFSARDARAVPDFIYELFPVLR--EMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGL-KLRKVPKDEIDERVREVAELLQieHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 160 PTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-224 |
2.14e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 117.62 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 11 YGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIayVPQGREIFPR 90
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGV--VPQFDNLDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 91 LTVEENLLM--GLSRFSARDARAVPDFIYElFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSV 168
Cdd:PRK13536 129 FTVRENLLVfgRYFGMSTREIEAVIPSLLE-FARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600055 169 IKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDMESE 224
Cdd:PRK13536 208 RHLIWERLRSLLARG-KTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-221 |
8.58e-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: 113.55 E-value: 8.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 9 QYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPhQRVRAGIAYVPQGREIF 88
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP-VELRRKIGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 89 PRLTVEENL-----LMGLSRfSARDARAvpdfiYELFPVLR----EMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:cd03295 88 PHMTVEENIalvpkLLKWPK-EKIRERA-----DELLALVGldpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 160 PTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDM 221
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-216 |
9.93e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 113.57 E-value: 9.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSL-----TGLRPHQRVRA 76
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 77 GIAYVPQGREIFPRLTVEENLL------MGLSRFSARDaRAVpdfiyELFPVLR--EMKQRRGGDLSGGQQQQLAIGRAL 148
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIeapckvLGLSKEQARE-KAM-----KLLARLRltDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 149 ASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAIlLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQV-IVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-216 |
3.01e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.11 E-value: 3.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQR-VRAGIA 79
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 80 YVPQGREIFPRLTVEENLLMG------LSRFSARD-ARAVpdfiyeLFPV-LREMKQRRGGDLSGGQQQQLAIGRALASQ 151
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGplrvrgASKEEAEKqAREL------LAKVgLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 152 PRLLILDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-216 |
1.00e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 110.87 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSL-----TGLRPHQRVRA 76
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 77 GIAYVPQGREIFPRLTVEENLL------MGLSRFSARdARAVpdfiyELFPVLR--EMKQRRGGDLSGGQQQQLAIGRAL 148
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIeapcrvLGLSKDQAL-ARAE-----KLLERLRlkPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 149 ASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAETG-ITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-217 |
1.04e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 111.24 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAY 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGLSR---------------FSARDARAVPDFIYELFPV-LREMKQRRGGDLSGGQQQQLAI 144
Cdd:PRK11300 85 TFQHVRLFREMTVIENLLVAQHQqlktglfsgllktpaFRRAESEALDRAATWLERVgLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 145 GRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGR 217
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-216 |
1.61e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 110.63 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAgIAY 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR-RAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREI-FPrLTVEENLLMGLS--RFSARDARAVPDFIYELFPVLrEMKQRRGGDLSGGQQQQLAIGRALA------SQ 151
Cdd:PRK13548 81 LPQHSSLsFP-FTVEEVVAMGRAphGLSRAEDDALVAAALAQVDLA-HLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 152 PRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-216 |
1.72e-29 |
|
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: 112.07 E-value: 1.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYY----GGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAR---EGQVAWEGRSLTGLRPHQ- 72
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 73 -RVRAG-IAYVPQgrEIF----PRLTVEENLLMGLSRF-----SARDARAV----------PDFIYELFPvlremkqrrg 131
Cdd:COG0444 81 rKIRGReIQMIFQ--DPMtslnPVMTVGDQIAEPLRIHgglskAEARERAIellervglpdPERRLDRYP---------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 132 GDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQfyDFA--AELADQYLVMAR 209
Cdd:COG0444 149 HELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITH--DLGvvAEIADRVAVMYA 226
|
....*..
gi 15600055 210 GEIVQQG 216
Cdd:COG0444 227 GRIVEEG 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-216 |
2.07e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 110.44 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPH---------- 71
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 72 --QRVRAGIAYVPQGREIFPRLTVEENLL------MGLSRFSARDaRAVpdFIYELFPVLREMKQRRGGDLSGGQQQQLA 143
Cdd:PRK10619 86 qlRLLRTRLTMVFQHFNLWSHMTVLENVMeapiqvLGLSKQEARE-RAV--KYLAKVGIDERAQGKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 144 IGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFyDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM-GFARHVSSHVIFLHQGKIEEEG 234
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
10-217 |
2.79e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 114.49 E-value: 2.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 10 YYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIAYVPQGREIFP 89
Cdd:COG1132 349 YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES-LRRQIGVVPQDTFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 90 RlTVEENLLMGLSRFS-------ARDARAVpDFIYELfP-----VLREmkqrRGGDLSGGQQQQLAIGRALASQPRLLIL 157
Cdd:COG1132 428 G-TIRENIRYGRPDATdeeveeaAKAAQAH-EFIEAL-PdgydtVVGE----RGVNLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 158 DEPTEGIQPSVIKEIGAVVRSLAArgDMAILLVeqfydfA-----AELADQYLVMARGEIVQQGR 217
Cdd:COG1132 501 DEATSALDTETEALIQEALERLMK--GRTTIVI------AhrlstIRNADRILVLDDGRIVEQGT 557
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-216 |
3.25e-29 |
|
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: 108.02 E-value: 3.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLV--PAREGQVAWEGRSltglRPHQRVRAGIAYVPQGREIFPRLTV 93
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGRP----LDKRSFRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 94 EENLlmglsRFSArdaravpdfiyelfpvlrEMKQrrggdLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIG 173
Cdd:cd03213 100 RETL-----MFAA------------------KLRG-----LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600055 174 AVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03213 152 SLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-188 |
3.65e-29 |
|
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: 108.21 E-value: 3.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 12 GGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrvRAGIAYVPQGREIFPRL 91
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP--HENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 92 TVEENLlmglsRFSARDARAVPDFIYELFPV--LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVI 169
Cdd:TIGR01189 89 SALENL-----HFWAAIHGGAQRTIEDALAAvgLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170
....*....|....*....
gi 15600055 170 KEIGAVVRSLAARGDMAIL 188
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLL 182
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-172 |
3.93e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 108.60 E-value: 3.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSH-ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQ--RVRAG 77
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 78 IAYVPQGREIFPRLTVEENL-----LMGLSRfsARDARAVPDfIYELfpV-LREMKQRRGGDLSGGQQQQLAIGRALASQ 151
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENValplrVTGKSR--KEIRRRVRE-VLDL--VgLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180
....*....|....*....|.
gi 15600055 152 PRLLILDEPTEGIQPSVIKEI 172
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEI 176
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-216 |
4.29e-29 |
|
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: 108.90 E-value: 4.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVP---AREGQVAWEGRSLtglRPHQrVRAGIAYVPQGREIFPRLT 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPR---KPDQ-FQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 93 VEENLL-MGLSRFSARDARAVPDFIYElFPVLREMKQRRGGD-----LSGGQQQQLAIGRALASQPRLLILDEPTEGIQP 166
Cdd:cd03234 98 VRETLTyTAILRLPRKSSDAIRKKRVE-DVLLRDLALTRIGGnlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600055 167 SVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-217 |
5.65e-29 |
|
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: 113.71 E-value: 5.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSH--ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIA 79
Cdd:COG4987 334 LELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD-LRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 80 YVPQGREIFpRLTVEENLLMGLSRFSARDARAV------PDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPR 153
Cdd:COG4987 413 VVPQRPHLF-DTTLRENLRLARPDATDEELWAAlervglGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAP 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 154 LLILDEPTEGIQPSVIKEIGAVVRSLAArgDMAILLV---EQfydfAAELADQYLVMARGEIVQQGR 217
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLIthrLA----GLERMDRILVLEDGRIVEQGT 552
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
10-216 |
8.35e-29 |
|
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: 108.08 E-value: 8.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 10 YYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLrPHQRVRAGIAYVPQGREIFP 89
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 90 RlTVEENLLMGlsRFSARD------ARAV--PDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:cd03254 91 G-TIMENIRLG--RPNATDeevieaAKEAgaHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 162 EGIQPSVIKEIGAVVRSLaARGDMAILLveqfydfAAEL-----ADQYLVMARGEIVQQG 216
Cdd:cd03254 168 SNIDTETEKLIQEALEKL-MKGRTSIII-------AHRLstiknADKILVLDDGKIIEEG 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-221 |
2.37e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 107.53 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRP--HQ-----R 73
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsQQkglirQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 74 VRAGIAYVPQGREIFPRLTVEENLLMG--LSRFSARDArAVPDFIYELFPVLREMKQ----RRggdLSGGQQQQLAIGRA 147
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGpvIVKGEPKEE-ATARARELLAKVGLAGKEtsypRR---LSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 148 LASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAA-RGDMAILLVEQfyDFAAELADQYLVMARGEIVQQGRGRDM 221
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEM--SFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-211 |
2.89e-28 |
|
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: 105.16 E-value: 2.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 11 YGGSH--ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIAYVPQGREIF 88
Cdd:cd03228 10 YPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES-LRKNIAYVPQDPFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 89 PRlTVEENLLmglsrfsardaravpdfiyelfpvlremkqrrggdlSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSV 168
Cdd:cd03228 89 SG-TIRENIL------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600055 169 IKEIGAVVRSLaaRGDMAILLVeqfydfA-----AELADQYLVMARGE 211
Cdd:cd03228 132 EALILEALRAL--AKGKTVIVI------AhrlstIRDADRIIVLDDGR 171
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-213 |
2.97e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.27 E-value: 2.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLH-QYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAY 80
Cdd:COG3845 258 LEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VP---QGREIFPRLTVEENLLMG------LSRFSARDARAVPDFiyelfpvLREMKQR---RGGD-------LSGGQQQQ 141
Cdd:COG3845 338 IPedrLGRGLVPDMSVAENLILGryrrppFSRGGFLDRKAIRAF-------AEELIEEfdvRTPGpdtparsLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 142 LAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIV 213
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAG-AAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-221 |
1.18e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 105.36 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAYV 81
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLLMGLS---RFSARDARAVPDFIYELFPVlREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILD 158
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQirdDLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 159 EPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDM 221
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSG-LGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-188 |
1.57e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 104.19 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPhqrvRAGIAY 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV----AEACHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMgLSRFSARDARAVPDFI--YELFPVLremkQRRGGDLSGGQQQQLAIGRALASQPRLLILD 158
Cdd:PRK13539 78 LGHRNAMKPALTVAENLEF-WAAFLGGEELDIAAALeaVGLAPLA----HLPFGYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|
gi 15600055 159 EPTEGIQPSVIKEIGAVVRSLAARGDMAIL 188
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLAQGGIVIA 182
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-216 |
2.56e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 107.23 E-value: 2.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAY 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQR---PINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGLSRfsARDARA-VPDFIYELFPV--LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLIL 157
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGLKQ--DKLPKAeIASRVNEMLGLvhMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600055 158 DEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-216 |
3.59e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 106.32 E-value: 3.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLrpHQRVRAgIAYV 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRK-VGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLLMGLSRFSARDaRAVPDFIYELFPVLREMKQ------RRGGDLSGGQQQQLAIGRALASQPRLL 155
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGLTVLPRRE-RPNAAAIKAKVTQLLEMVQlahladRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600055 156 ILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
8-207 |
6.38e-27 |
|
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: 107.76 E-value: 6.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 8 HQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvRAGIAYVPQGREI 87
Cdd:TIGR02857 329 VAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RDQIAWVPQHPFL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 88 FPRlTVEENLLMGLSRFSARDARAVPDFIY--ELFPVLREMKQRRGGD----LSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:TIGR02857 408 FAG-TIAENIRLARPDASDAEIREALERAGldEFVAALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600055 162 EGIQPSVIKEIGAVVRSLAARgdmAILLVEQFYDFAAELADQYLVM 207
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQG---RTVLLVTHRLALAALADRIVVL 529
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-221 |
8.38e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.45 E-value: 8.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 11 YGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLV-----PAREGQVAWEGRSLTGLrPHQRVRAGIAYVPQGR 85
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKM-DVIELRRRVQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 86 EIFPRLTVEENLLMG--LSRF--SARDARAVPDFIYELFPVLREMKQRRG---GDLSGGQQQQLAIGRALASQPRLLILD 158
Cdd:PRK14247 92 NPIPNLSIFENVALGlkLNRLvkSKKELQERVRWALEKAQLWDEVKDRLDapaGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 159 EPTEGIQPSVIKEIGAVVRSLaaRGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDM 221
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-221 |
8.51e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 103.58 E-value: 8.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCL--MG-LVP-AR-EGQVAWEGRSLtgLRPHQ---R 73
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNdLIPgARvEGEILLDGEDI--YDPDVdvvE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 74 VRAGIAYVPQGREIFPrLTVEENLLMGLSRFSARDaRAVPDFIYELfpVLR------EMKQR---RGGDLSGGQQQQLAI 144
Cdd:COG1117 90 LRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKS-KSELDEIVEE--SLRkaalwdEVKDRlkkSALGLSGGQQQRLCI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 145 GRALASQPRLLILDEPTEGIQP---SVIKEigaVVRSLaaRGDMAILLV----EQfydfAAELADQYLVMARGEIVQQGR 217
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALDPistAKIEE---LILEL--KKDYTIVIVthnmQQ----AARVSDYTAFFYLGELVEFGP 236
|
....
gi 15600055 218 GRDM 221
Cdd:COG1117 237 TEQI 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-161 |
1.13e-26 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 102.51 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGS----HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGL--RPHQRV 74
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdeDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 75 RAG-IAYVPQGREIFPRLTVEENLLMGLSRFSARDARAVPdfiyelfpvlREMKQRRG---------GDLSGGQQQQLAI 144
Cdd:COG4181 88 RARhVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARA----------RALLERVGlghrldhypAQLSGGEQQRVAL 157
|
170
....*....|....*..
gi 15600055 145 GRALASQPRLLILDEPT 161
Cdd:COG4181 158 ARAFATEPAILFADEPT 174
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-212 |
1.19e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 106.94 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 21 SFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAR-EGQVAWEGRSLTGLRPHQRVRAGIAYVPQGRE---IFPRLTVEEN 96
Cdd:PRK13549 282 SFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKrdgIVPVMGVGKN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 97 L-LMGLSRFSARdarAVPDFIYELFPVLREMKQRRG---------GDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQP 166
Cdd:PRK13549 362 ItLAALDRFTGG---SRIDDAAELKTILESIQRLKVktaspelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600055 167 SVIKEIGAVVRSLAARGdMAILLVeqfydfAAEL------ADQYLVMARGEI 212
Cdd:PRK13549 439 GAKYEIYKLINQLVQQG-VAIIVI------SSELpevlglSDRVLVMHEGKL 483
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-224 |
1.64e-26 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 104.11 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 32 LLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAYVPQGREIFPRLTVEENLLMGLSRFSARDARA 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLR---HINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 112 VPDFIYELFPV-LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLV 190
Cdd:TIGR01187 78 KPRVLEALRLVqLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFV 157
|
170 180 190
....*....|....*....|....*....|....
gi 15600055 191 EQFYDFAAELADQYLVMARGEIVQQGRGRDMESE 224
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-217 |
2.45e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 104.00 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGS----HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQ--RV 74
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 75 RAGIAYVPQGREIFPRLTVEENL-----LMGLSRfSARDARavpdfIYELFPV--LREMKQRRGGDLSGGQQQQLAIGRA 147
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENValpleIAGVPK-AEIRKR-----VAELLELvgLSDKADAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 148 LASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGR 217
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGP 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-220 |
3.66e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 105.52 E-value: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAY 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGLSRfSARDARAVPDFIYELFPVLR-EMKqrrGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPK-RQASMQKMKQLLAALGCQLDlDSS---AGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600055 160 PTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRD 220
Cdd:PRK15439 167 PTASLTPAETERLFSRIRELLAQG-VGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-225 |
1.16e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.25 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 27 GEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTG------LRPhQRVRAGIAYVPQGREIFPRlTVEENLLMG 100
Cdd:PRK13634 33 GSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknkkLKP-LRKKVGIVFQFPEHQLFEE-TVEKDICFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 101 LSRF--SARDARAVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRS 178
Cdd:PRK13634 111 PMNFgvSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15600055 179 LAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDMESEG 225
Cdd:PRK13634 191 LHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-221 |
1.34e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 103.98 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 18 RGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAYVPQGRE---IFPRLTVE 94
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQssgLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 95 ENL------LMGLSRFSARDARAVPDFIYELFPVLREMKQRRGGdLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSV 168
Cdd:PRK15439 360 WNVcalthnRRGFWIKPARENAVLERYRRALNIKFNHAEQAART-LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600055 169 IKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDM 221
Cdd:PRK15439 439 RNDIYQLIRSIAAQN-VAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-216 |
2.03e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 98.82 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPhQRVRAGIAYVPQGREIFPRlTVEEN 96
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP-ADLRRNIGYVPQDVTLFYG-TLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 97 LLMGLSrfSARDAR--------AVPDFI------YELfpvlreMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTE 162
Cdd:cd03245 98 ITLGAP--LADDERilraaelaGVTDFVnkhpngLDL------QIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600055 163 GIQPSVIKEIGAVVRSLAarGDMAILLVEQFYDFaAELADQYLVMARGEIVQQG 216
Cdd:cd03245 170 AMDMNSEERLKERLRQLL--GDKTLIIITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-212 |
2.49e-25 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 103.16 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAYVPQGRE---IFPRLTV 93
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 94 EENL-LMGLSRFS--------ARDARAVPDFIyELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGI 164
Cdd:PRK10762 348 KENMsLTALRYFSraggslkhADEQQAVSDFI-RLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600055 165 QPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEI 212
Cdd:PRK10762 427 DVGAKKEIYQLINQFKAEG-LSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-216 |
4.84e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.93 E-value: 4.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAgIAY 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGLS-------RFSARDARAVPDFIYELFpvLREMKQRRGGDLSGGQQQQLAIGRALASQPR 153
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSpwlslwgRLSAEDNARVNQAMEQTR--INHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 154 LLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVeqfYDF--AAELADQYLVMARGEIVQQG 216
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVL---HDLnqASRYCDHLVVLANGHVMAQG 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-221 |
7.11e-25 |
|
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: 102.13 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYG-GSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIAY 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT-LRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRlTVEENLLMGLSRFSARDA--RAVPdfIYELFPVLREMKQ-------RRGGDLSGGQQQQLAIGRALASQ 151
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLLGAKENVSQDEiwAACE--IAEIKDDIENMPLgyqtelsEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 152 PRLLILDEPTEGIQPSVIKEIgavVRSLAARGDMAILLVEQFYDFaAELADQYLVMARGEIVQQGRGRDM 221
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKI---VNNLLNLQDKTIIFVAHRLSV-AKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-220 |
7.72e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.41 E-value: 7.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 7 LHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAYVPQGRE 86
Cdd:PRK09452 20 ISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR---HVNTVFQSYA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 87 IFPRLTVEENLLMGLsRFSARDARAVPDFIYE-LFPV-LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGI 164
Cdd:PRK09452 97 LFPHMTVFENVAFGL-RMQKTPAAEITPRVMEaLRMVqLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600055 165 QPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRD 220
Cdd:PRK09452 176 DYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-216 |
9.55e-25 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 97.18 E-value: 9.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAkvGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAYV 81
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFAQ--GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR---PVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLLMGLS---RFSARDARAVPDFIYELFpvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILD 158
Cdd:cd03298 76 FQENNLFAHLTVEQNVGLGLSpglKLTAEDRQAIEVALARVG--LAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 159 EPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-216 |
1.59e-24 |
|
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: 100.91 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPArEGQVAWEGRSLTGLRPHQ--RVRAGIAYVpqgreiF------ 88
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRAlrPLRRRMQVV------Fqdpfgs 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 89 --PRLTVE----ENLL---MGLSRfSARDARAVPdfiyelfpVLRE------MKQRRGGDLSGGQQQQLAIGRALASQPR 153
Cdd:COG4172 375 lsPRMTVGqiiaEGLRvhgPGLSA-AERRARVAE--------ALEEvgldpaARHRYPHEFSGGQRQRIAIARALILEPK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 154 LLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEqfYDFA--AELADQYLVMARGEIVQQG 216
Cdd:COG4172 446 LLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFIS--HDLAvvRALAHRVMVMKDGKVVEQG 508
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-161 |
1.63e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWegrsltglrpHQRVRagIAY 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL----------GETVK--IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIF-PRLTVEENLLMGLSRFSARDARAV-PDFiyeLFPvlREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILD 158
Cdd:COG0488 383 FDQHQEELdPDKTVLDELRDGAPGGTEQEVRGYlGRF---LFS--GDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLD 457
|
...
gi 15600055 159 EPT 161
Cdd:COG0488 458 EPT 460
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-190 |
2.75e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.03 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCL--MGLVPAR---EGQVAWEGRSLTGLRPH-QRVR 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEvrvEGRVEFFNQNIYERRVNlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 76 AGIAYVPQGREIFPrLTVEENLLMGLSRFSARDARAVPDFI------YELFPVLREMKQRRGGDLSGGQQQQLAIGRALA 149
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVesalkdADLWDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15600055 150 SQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLV 190
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIV 207
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-225 |
2.91e-24 |
|
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: 96.40 E-value: 2.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 13 GSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPhQRVRAGIAYVPQGREIFPRlT 92
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP-AWLRRQVGVVLQENVLFNR-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 93 VEENLLMGLSRFSARDARAVP------DFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQP 166
Cdd:cd03252 92 IRDNIALADPGMSMERVIEAAklagahDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600055 167 SVIKEIGAVVRSLAArGDMAILLVEQFYdfAAELADQYLVMARGEIVQQGRGRDMESEG 225
Cdd:cd03252 172 ESEHAIMRNMHDICA-GRTVIIIAHRLS--TVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-212 |
3.12e-24 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 99.90 E-value: 3.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 20 LSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAR-EGQVAWEGRSLTGLRPHQRVRAGIAYVPQGRE---IFPRLTVEE 95
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 96 NL-LMGLSRFSARdarAVPDFIYELFPVLREMKQRRG---------GDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQ 165
Cdd:TIGR02633 359 NItLSVLKSFCFK---MRIDAAAELQIIGSAIQRLKVktaspflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15600055 166 PSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEI 212
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEG-VAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-216 |
4.11e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.80 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 5 DKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQ-RVRAGIAYVPQ 83
Cdd:PRK13652 8 DLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvRKFVGLVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 84 GREIFPRlTVEENLLMGLSRFSArDARAVPDFIYELFPVL--REMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:PRK13652 88 DDQIFSP-TVEQDIAFGPINLGL-DEETVAHRVSSALHMLglEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 162 EGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYG 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-216 |
4.15e-24 |
|
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: 96.31 E-value: 4.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 10 YYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQ-VAWEGRSLTG-----LRPHqrvragIAYV-P 82
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGedvweLRKR------IGLVsP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 83 Q-GREIFPRLTVEENLLMGL-------SRFSARDARAVPDFIYELfpVLREMKQRRGGDLSGGQQQQLAIGRALASQPRL 154
Cdd:COG1119 86 AlQLRFPRDETVLDVVLSGFfdsiglyREPTDEQRERARELLELL--GLAHLADRPFGTLSQGEQRRVLIARALVKDPEL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 155 LILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:COG1119 164 LILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG 225
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-215 |
4.56e-24 |
|
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: 96.41 E-value: 4.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQR--VRAGIAYVPQG--REIFPRL 91
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRraFRRDVQLVFQDspSAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 92 TVEENL---LMGLSRFSARDARAVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSV 168
Cdd:TIGR02769 106 TVRQIIgepLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15600055 169 IKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQ 215
Cdd:TIGR02769 186 QAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-216 |
6.27e-24 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 96.37 E-value: 6.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQR--VRAGIAYVPQgreiFPR---- 90
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLkdLRKKVGLVFQ----FPEhqlf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 91 -LTVEENLLMGLSRF--SARDARAVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPS 167
Cdd:TIGR04521 97 eETVYKDIAFGPKNLglSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600055 168 VIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:TIGR04521 177 GRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDG 225
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-216 |
6.97e-24 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 96.70 E-value: 6.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHI-LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIA 79
Cdd:COG1125 1 MIEFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE-LRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 80 YVPQGREIFPRLTVEEN-----LLMGLSRfSARDARAvpdfiYELFPVL----REMKQRRGGDLSGGQQQQLAIGRALAS 150
Cdd:COG1125 80 YVIQQIGLFPHMTVAENiatvpRLLGWDK-ERIRARV-----DELLELVgldpEEYRDRYPHELSGGQQQRVGVARALAA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600055 151 QPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:COG1125 154 DPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYD 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-226 |
7.88e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.41 E-value: 7.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRpHQRVRAGIAYVPQGREIFPRlTVEE 95
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD-HHYLHRQVALVGQEPVLFSG-SVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 96 NLLMGLSRFSARDARAVP------DFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQpsvi 169
Cdd:TIGR00958 574 NIAYGLTDTPDEEIMAAAkaanahDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD---- 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 170 KEIGAVVRSLAARGDMAILLVEQFYDfAAELADQYLVMARGEIVQQGRGRD-MESEGV 226
Cdd:TIGR00958 650 AECEQLLQESRSRASRTVLLIAHRLS-TVERADQILVLKKGSVVEMGTHKQlMEDQGC 706
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-224 |
8.55e-24 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 98.74 E-value: 8.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVP--AREGQVAWEGRSLTGLRPHQRVRAGI 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 79 AYVPQGREIFPRLTVEENLLMGLSRFSARDARAVPDFIYELFPVLREMK------QRRGGDLSGGQQQQLAIGRALASQP 152
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQldadnvTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 153 RLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAeLADQYLVMARGEIVQQGRGRDMESE 224
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKA-VCDTICVIRDGQHVATKDMSTMSED 231
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-218 |
9.13e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 94.54 E-value: 9.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 27 GEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAYVPQGREIFPRLTVEENLLMGLS---R 103
Cdd:TIGR01277 24 GEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQR---PVSMLFQENNLFAHLTVRQNIGLGLHpglK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 104 FSARDARAVPDFIYELFpvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARG 183
Cdd:TIGR01277 101 LNAEQQEKVVDAAQQVG--IADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSER 178
|
170 180 190
....*....|....*....|....*....|....*
gi 15600055 184 DMAILLVEQFYDFAAELADQYLVMARGEIVQQGRG 218
Cdd:TIGR01277 179 QRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-221 |
1.79e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.84 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCL--MG-LVP--AREGQVAWEGRSLTGLRPHQ-RV 74
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNdLNPevTITGSIVYNGHNIYSPRTDTvDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 75 RAGIAYVPQGREIFPrLTVEENLLMGLsRFSARDARAVPDFIYEL----FPVLREMKQR---RGGDLSGGQQQQLAIGRA 147
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGL-RLKGIKDKQVLDEAVEKslkgASIWDEVKDRlhdSALGLSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600055 148 LASQPRLLILDEPTEGIQPSVIKEIGAVVRSLaaRGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDM 221
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
9-216 |
1.86e-23 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 98.01 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 9 QYYG-GSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIAYVPQGrei 87
Cdd:TIGR03375 472 AYPGqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAD-LRRNIGYVPQD--- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 88 fPRL---TVEENLLMGlsRFSARDA---RAVpdfiyELFPVLREMKQ----------RRGGDLSGGQQQQLAIGRALASQ 151
Cdd:TIGR03375 548 -PRLfygTLRDNIALG--APYADDEeilRAA-----ELAGVTEFVRRhpdgldmqigERGRSLSGGQRQAVALARALLRD 619
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 152 PRLLILDEPTEGIQPSVIKEIGAVVRSLAArgDMAILLVEQFYDFaAELADQYLVMARGEIVQQG 216
Cdd:TIGR03375 620 PPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSL-LDLVDRIIVMDNGRIVADG 681
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-192 |
2.63e-23 |
|
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: 92.94 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPhqRVRAGIAYV 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD--SIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLlmglsRFSARD--ARAVPDFIYELfpVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:cd03231 79 GHAPGIKTTLSVLENL-----RFWHADhsDEQVEEALARV--GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|...
gi 15600055 160 PTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQ 192
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-213 |
3.68e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 94.00 E-value: 3.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYG-GS----HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVR 75
Cdd:COG1101 1 MLELKNLSKTFNpGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 76 agiaYVpqGReIF--------PRLTVEENLLMGLSR-----FSARDARAVPDFIYELFPVLR-----EMKQRRgGDLSGG 137
Cdd:COG1101 81 ----YI--GR-VFqdpmmgtaPSMTIEENLALAYRRgkrrgLRRGLTKKRRELFRELLATLGlglenRLDTKV-GLLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 138 QQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLV----EQfydfAAELADQYLVMARGEIV 213
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVthnmEQ----ALDYGNRLIMMHEGRII 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-226 |
8.30e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.01 E-value: 8.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAY 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGlsRFSARDARAVPDFIYelfpvlREMKQRRG----------------GDLSGGQQQQLAI 144
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIG--RHLTKKVCGVNIIDW------REMRVRAAmmllrvglkvdldekvANLSISHKQMLEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 145 GRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDmAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDMESE 224
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
..
gi 15600055 225 GV 226
Cdd:PRK09700 236 DI 237
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-188 |
9.45e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 91.40 E-value: 9.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRP---------- 70
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeyhqdllylg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 71 HQrvrAGIAyvpqgreifPRLTVEENLlmglsRFSARDARAVPDFiyELFPVLREMKQRRGGD-----LSGGQQQQLAIG 145
Cdd:PRK13538 81 HQ---PGIK---------TELTALENL-----RFYQRLHGPGDDE--ALWEALAQVGLAGFEDvpvrqLSAGQQRRVALA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600055 146 RALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAIL 188
Cdd:PRK13538 142 RLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVIL 184
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
9.57e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.37 E-value: 9.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYG-GSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRP---HQRVRA 76
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 77 GIAYVPQGREIFPRlTVEENLLMGLS--RFSARDARAVPDFIYELFPVlREMKQRRGGDLSGGQQQQLAIGRALASQPRL 154
Cdd:PRK13636 85 GMVFQDPDNQLFSA-SVYQDVSFGAVnlKLPEDEVRKRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600055 155 LILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDM--ESEGVRG 228
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVfaEKEMLRK 238
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-183 |
1.06e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.14 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 11 YGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVawegrsltglrpHQRVRAGIAYVPQGREI--- 87
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGARVAYVPQRSEVpds 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 88 FPrLTVEENLLMG-------LSRFSARDARAVPDFIYELfpVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEP 160
Cdd:NF040873 70 LP-LTVRDLVAMGrwarrglWRRLTRDDRAAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180
....*....|....*....|...
gi 15600055 161 TEGIQPSVIKEIGAVVRSLAARG 183
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARG 169
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-214 |
1.13e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.83 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKL-HQYYGGS--------HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPH 71
Cdd:PRK10419 3 LLNVSGLsHHYAHGGlsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 72 QR--VRAGIAYVPQGR--EIFPRLTVEENL------LMGLSRfSARDARAvpDFIYELFPVLREMKQRRGGDLSGGQQQQ 141
Cdd:PRK10419 83 QRkaFRRDIQMVFQDSisAVNPRKTVREIIreplrhLLSLDK-AERLARA--SEMLRAVDLDDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 142 LAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQ 214
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-224 |
1.17e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 95.62 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 18 RGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAYVPQGRE---IFPRLTVE 94
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 95 ENL-------------LMGLsrFSARDARAVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:PRK09700 360 QNMaisrslkdggykgAMGL--FHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 162 EGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDMESE 224
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDG-KVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSE 499
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
10-172 |
1.34e-22 |
|
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: 95.51 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 10 YYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLrPHQRVRAGIAYVPQGREIFP 89
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSL-DQDEVRRRVSVCAQDAHLFD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 90 RlTVEENLLMGLSRFSARDARAV------PDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEG 163
Cdd:TIGR02868 423 T-TVRENLRLARPDATDEELWAAlervglADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
....*....
gi 15600055 164 IQPSVIKEI 172
Cdd:TIGR02868 502 LDAETADEL 510
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-219 |
1.34e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 92.21 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVP----AR-EGQVAWEGRSLTGLRPHQ-RVR 75
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeARvEGEVRLFGRNIYSPDVDPiEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 76 AGIAYVPQGREIFPRLTVEENLLMGLSRFSARDARAVPDFIYELF----PVLREMKQR---RGGDLSGGQQQQLAIGRAL 148
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWAlkkaALWDEVKDRlndYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600055 149 ASQPRLLILDEPTEGIQPSVIKEIGAVVRSLaaRGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGR 219
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTR 233
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-220 |
1.56e-22 |
|
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: 92.32 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLrPHQRVRA----GIAYVPQGREIFPRLT 92
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAM-SRKELRElrrkKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 93 VEENLLMGLS----RFSARDARAvpdfIYELFPV-LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPS 167
Cdd:cd03294 119 VLENVAFGLEvqgvPRAEREERA----AEALELVgLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600055 168 VIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRD 220
Cdd:cd03294 195 IRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEE 247
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-216 |
1.97e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.91 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRS-----LTGLRPHQR-- 73
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLYALSEAERrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 74 -VRAGIAYVPQGreifPRltveENLLMGLS-------RFSARDARAVPDFIYELFPVLR--EMKQRRGGDL----SGGQQ 139
Cdd:PRK11701 86 lLRTEWGFVHQH----PR----DGLRMQVSaggnigeRLMAVGARHYGDIRATAGDWLErvEIDAARIDDLpttfSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 140 QQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-216 |
2.69e-22 |
|
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: 90.28 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAR--EGQVAWEGRSLTGLRPHQRVRAGIA 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 80 YVPQGREIFPRLTVEenllmglsrfsardaravpDFiyelfpvLREMkqrrGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:cd03217 81 LAFQYPPEIPGVKNA-------------------DF-------LRYV----NEGFSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 160 PTEGIQPSVIKEIGAVVRSLAARGdMAILLV---EQFYDFAAelADQYLVMARGEIVQQG 216
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREEG-KSVLIIthyQRLLDYIK--PDRVHVLYDGRIVKSG 187
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-218 |
2.91e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.73 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 14 SHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPA---REGQVAWEGRSLTglRPHQRVRAgiAYVPQGREIFPR 90
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID--AKEMRAIS--AYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 91 LTVEENLL----MGLSRFSARDAR--AVPDFIYELfpVLREMKQRRGGD------LSGGQQQQLAIGRALASQPRLLILD 158
Cdd:TIGR00955 114 LTVREHLMfqahLRMPRRVTKKEKreRVDEVLQAL--GLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 159 EPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRG 218
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSP 251
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-160 |
5.37e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.85 E-value: 5.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAR---EGQVAWEGRSLTGLRPHQRvraG 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQR---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 78 IAYVPQGREIFPRLTVEENLLMGLSRFSARDARAvpDFIYElfpVLRE-----MKQRRGGDLSGGQQQQLAIGRALASQP 152
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFALPPTIGRAQRR--ARVEQ---ALEEaglagFADRDPATLSGGQRARVALLRALLAEP 152
|
....*...
gi 15600055 153 RLLILDEP 160
Cdd:COG4136 153 RALLLDEP 160
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-216 |
6.47e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 93.37 E-value: 6.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 20 LSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAReGQVAWEGRSLTGLRPHQRvRAGIAYVPQGreifPRL---TVEEN 96
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESW-RKHLSWVGQN----PQLphgTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 97 LLMGlsRFSARDARA--------VPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSV 168
Cdd:PRK11174 443 VLLG--NPDASDEQLqqalenawVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600055 169 IKeigAVVRSL--AARGDMAILLVEQFYDFAAelADQYLVMARGEIVQQG 216
Cdd:PRK11174 521 EQ---LVMQALnaASRRQTTLMVTHQLEDLAQ--WDQIWVMQDGQIVQQG 565
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
13-226 |
6.50e-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: 89.98 E-value: 6.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 13 GSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIAYVPQGREIFPRlT 92
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS-LRRQIGLVSQDVFLFND-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 93 VEENLLMGLS-------RFSARDARAVpDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQ 165
Cdd:cd03251 92 VAENIAYGRPgatreevEEAARAANAH-EFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 166 PSVIKEIGAVVRSLAA-RGDMAIllveqfydfAAEL-----ADQYLVMARGEIVQQGRGRD-MESEGV 226
Cdd:cd03251 171 TESERLVQAALERLMKnRTTFVI---------AHRLstienADRIVVLEDGKIVERGTHEElLAQGGV 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-217 |
6.64e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.62 E-value: 6.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 15 HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAReGQVAWEGRSLTGLRPHQR--VRAGIAYVPQ--GREIFPR 90
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLlpVRHRIQVVFQdpNSSLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 91 LTVEENLLMGLS----RFSA--RDARaVPDFIYE--LFPVLRemkQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTE 162
Cdd:PRK15134 379 LNVLQIIEEGLRvhqpTLSAaqREQQ-VIAVMEEvgLDPETR---HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 163 GIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGR 217
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-220 |
6.89e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 91.26 E-value: 6.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLR---PHQRVRAGIAYVPQGREIFPRlTV 93
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklSDIRKKVGLVFQYPEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 94 EENLLMGLSRFSARDARaVPDFIYELFPVL----REMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVI 169
Cdd:PRK13637 102 EKDIAFGPINLGLSEEE-IENRVKRAMNIVgldyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15600055 170 KEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRD 220
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-216 |
8.91e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 89.74 E-value: 8.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLvPARE---GQVAWEGRSLTGLRPHQRVRAGI 78
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH-PKYEvtsGSILLDGEDILELSPDERARAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 79 AYVPQGREIFPRLTVEeNLL---MGLSRFSARDARAVPDFIYELFPVLrEMKQ---RRG--GDLSGGQQQQLAIGRALAS 150
Cdd:COG0396 80 FLAFQYPVEIPGVSVS-NFLrtaLNARRGEELSAREFLKLLKEKMKEL-GLDEdflDRYvnEGFSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600055 151 QPRLLILDEPTEGIQPSVIKEIGAVVRSLAARgDMAILLV---EQFYDFAAelADQYLVMARGEIVQQG 216
Cdd:COG0396 158 EPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIIthyQRILDYIK--PDFVHVLVDGRIVKSG 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-183 |
9.73e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 92.68 E-value: 9.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 11 YGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVP--AREGQVAWEGRSLT--GLRPHQRvrAGIAYVPQGRE 86
Cdd:PRK13549 15 FGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQasNIRDTER--AGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 87 IFPRLTVEENLLMG--LSRFSARDARAVPDFIYELfpvLREMK-----QRRGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:PRK13549 93 LVKELSVLENIFLGneITPGGIMDYDAMYLRAQKL---LAQLKldinpATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180
....*....|....*....|....
gi 15600055 160 PTEGIQPSVIKEIGAVVRSLAARG 183
Cdd:PRK13549 170 PTASLTESETAVLLDIIRDLKAHG 193
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-216 |
1.06e-21 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 92.83 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLH----QYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAR----EGQVAWEGRSLTGLRPHQ 72
Cdd:COG4172 6 LLSVEDLSvafgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 73 --RVRagiayvpqGREI---F--------PRLTVE----ENLL--MGLSRFSARdARAVpdfiyELfpvLREMK----QR 129
Cdd:COG4172 86 lrRIR--------GNRIamiFqepmtslnPLHTIGkqiaEVLRlhRGLSGAAAR-ARAL-----EL---LERVGipdpER 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 130 RGGD----LSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEqfYDFA--AELADQ 203
Cdd:COG4172 149 RLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLIT--HDLGvvRRFADR 226
|
250
....*....|...
gi 15600055 204 YLVMARGEIVQQG 216
Cdd:COG4172 227 VAVMRQGEIVEQG 239
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-226 |
1.14e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.45 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLT-GLRPHQRVRAGIA 79
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDySKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 80 YVPQG--REIFpRLTVEENLLMGLSRFSARD---ARAVPDFIyeLFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRL 154
Cdd:PRK13638 81 TVFQDpeQQIF-YTDIDSDIAFSLRNLGVPEaeiTRRVDEAL--TLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600055 155 LILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFyDFAAELADQYLVMARGEIVQQG-------RGRDMESEGV 226
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDI-DLIYEISDAVYVLRQGQILTHGapgevfaCTEAMEQAGL 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-160 |
1.26e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 89.92 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGS----HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVra 76
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 77 giayVPQGREIFPRLTVEENL-----LMGLSRfSARDARAVpdfiYELFPV-LREMKQRRGGDLSGGQQQQLAIGRALAS 150
Cdd:COG4525 81 ----VFQKDALLPWLNVLDNVafglrLRGVPK-AERRARAE----ELLALVgLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170
....*....|
gi 15600055 151 QPRLLILDEP 160
Cdd:COG4525 152 DPRFLLMDEP 161
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-161 |
1.62e-21 |
|
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: 88.68 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 14 SHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTgLRPHQRVRAGIAYVPQGREIFPRlTV 93
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600055 94 EENLLMGLSRFS------ARDARAVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:cd03248 105 QDNIAYGLQSCSfecvkeAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-217 |
1.85e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 89.37 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAgIAY 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKR-LAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEEnlLMGLSRF-------SARDARAVPDFIYELfpVLREMKQRRGGDLSGGQQQQLAIGRALASQPR 153
Cdd:COG4604 80 LRQENHINSRLTVRE--LVAFGRFpyskgrlTAEDREIIDEAIAYL--DLEDLADRYLDELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 154 LLILDEPTEG--IQPSVikEIGAVVRSLAARGDMAILLVeqFYD--FAAELADQYLVMARGEIVQQGR 217
Cdd:COG4604 156 YVLLDEPLNNldMKHSV--QMMKLLRRLADELGKTVVIV--LHDinFASCYADHIVAMKDGRVVAQGT 219
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-216 |
2.22e-21 |
|
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: 92.12 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSH--ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAgIA 79
Cdd:COG4618 331 LSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH-IG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 80 YVPQGREIFPRlTVEENLlmglSRFSARDARAVpdfiyelfpV-------LREMKQR-----------RGGDLSGGQQQQ 141
Cdd:COG4618 410 YLPQDVELFDG-TIAENI----ARFGDADPEKV---------VaaaklagVHEMILRlpdgydtrigeGGARLSGGQRQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 142 LAIGRALASQPRLLILDEP-----TEGIQpsvikEIGAVVRSLAARG--------DMAILlveqfydfaaELADQYLVMA 208
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPnsnldDEGEA-----ALAAAIRALKARGatvvvithRPSLL----------AAVDKLLVLR 540
|
....*...
gi 15600055 209 RGEIVQQG 216
Cdd:COG4618 541 DGRVQAFG 548
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-161 |
2.36e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.66 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 4 VDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGrsltGLRphqrvragIAYVPQ 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----GLR--------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 84 GREIFPRLTVEENLLMGLSRFSARDAR--------AVPDFIYELFPVLREMKQRRGG----------------------- 132
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELRALEAEleeleaklAEPDEDLERLAELQEEFEALGGweaearaeeilsglgfpeedldr 148
|
170 180 190
....*....|....*....|....*....|..
gi 15600055 133 ---DLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:COG0488 149 pvsELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
11-221 |
3.27e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.16 E-value: 3.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 11 YGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAYVPQGREIFPR 90
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR---DICMVFQSYALFPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 91 LTVEENLLMGLS---------RFSARDARAVPDfiyelfpvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:PRK11432 93 MSLGENVGYGLKmlgvpkeerKQRVKEALELVD--------LAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 162 EGIQPSVIKEIGAVVRSLAARGDMAILLV--EQFYDFAaeLADQYLVMARGEIVQQGRGRDM 221
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVthDQSEAFA--VSDTVIVMNKGKIMQIGSPQEL 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
29-217 |
3.79e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.93 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 29 VTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSL------TGLRPHQRvraGIAYVPQGREIFPRLTVEENLLMGLS 102
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaekgICLPPEKR---RIGYVFQDARLFPHYKVRGNLRYGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 103 RFSardaRAVPDFIYELF---PVLRemkqRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSL 179
Cdd:PRK11144 103 KSM----VAQFDKIVALLgiePLLD----RYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600055 180 AARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGR 217
Cdd:PRK11144 175 AREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-224 |
3.82e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.99 E-value: 3.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQV------------AWEGRSLTGL---RPHQRVRAGI--- 78
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtsdeenLWDIRNKAGMvfqNPDNQIVATIvee 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 79 --AYVPQGREIFP---RLTVEENLlmglsrfsardaRAVPDFIYELF-PVLremkqrrggdLSGGQQQQLAIGRALASQP 152
Cdd:PRK13633 106 dvAFGPENLGIPPeeiRERVDESL------------KKVGMYEYRRHaPHL----------LSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 153 RLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAElADQYLVMARGEIVQQGRGRDMESE 224
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
10-216 |
4.09e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.79 E-value: 4.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 10 YYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVawegrSLTGLRPHQRVRAG-IAYVPQGREI- 87
Cdd:PRK15056 16 WRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQALQKNlVAYVPQSEEVd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 88 --FPRLtVEENLLMG-------LSRFSARDARAVPDFIYELfpVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILD 158
Cdd:PRK15056 91 wsFPVL-VEDVVMMGryghmgwLRRAKKRDRQIVTAALARV--DMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 159 EPTEGIQPSVIKEIGAVVRSLAARGDmAILLVEQFYDFAAELADqYLVMARGEIVQQG 216
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCD-YTVMVKGTVLASG 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1-183 |
4.15e-21 |
|
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: 87.46 E-value: 4.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKlhQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLR----PHQRVRA 76
Cdd:cd03292 3 FINVTK--TYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraiPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 77 GIAYvpQGREIFPRLTVEENLLMGL--SRFSARDARA-VPDFIYELfpVLREMKQRRGGDLSGGQQQQLAIGRALASQPR 153
Cdd:cd03292 81 GVVF--QDFRLLPDRNVYENVAFALevTGVPPREIRKrVPAALELV--GLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190
....*....|....*....|....*....|
gi 15600055 154 LLILDEPTEGIQPSVIKEIGAVVRSLAARG 183
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAG 186
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-213 |
4.27e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.13 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 21 SFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAYVPQGRE---IFPRLTVEENL 97
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKaegIIPVHSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 98 LMGLSRFSAR---------DARAVPDFIYELfpvlrEMKQRRG----GDLSGGQQQQLAIGRALASQPRLLILDEPTEGI 164
Cdd:PRK11288 353 NISARRHHLRagclinnrwEAENADRFIRSL-----NIKTPSReqliMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 165 QPSVIKEIGAVVRSLAARGdMAILLVeqfydfAAEL------ADQYLVMARGEIV 213
Cdd:PRK11288 428 DVGAKHEIYNVIYELAAQG-VAVLFV------SSDLpevlgvADRIVVMREGRIA 475
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
9.04e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 87.74 E-value: 9.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSH--ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLR-PHQRVRAG 77
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 78 IAYV-PQGReiFPRLTVEENLLMGLS--RFSARDaraVPDFIYELFPV--LREMKQRRGGDLSGGQQQQLAIGRALASQP 152
Cdd:PRK13632 87 IIFQnPDNQ--FIGATVEDDIAFGLEnkKVPPKK---MKDIIDDLAKKvgMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 153 RLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDfAAELADQYLVMARGEIVQQGR 217
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMD-EAILADKVIVFSEGKLIAQGK 225
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-216 |
9.33e-21 |
|
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: 86.16 E-value: 9.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAR---EGQVAWEGrsLTGLRPHQRVRAGIAYVPQGREIFPRLT 92
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG--IPYKEFAEKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 93 VEENLlmglsRFSARdARAvPDFIyelfpvlremkqrRGgdLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEI 172
Cdd:cd03233 100 VRETL-----DFALR-CKG-NEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600055 173 GAVVRSLA-ARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03233 158 LKCIRTMAdVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-160 |
1.16e-20 |
|
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: 85.98 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRsltglrphqrvragIAYVPQGREIFPRlTVEE 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------------IAYVSQEPWIQNG-TIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 96 NLLMGlSRFSARDARAV-------PDFiyELFPvlremkqrrGGD----------LSGGQQQQLAIGRALASQPRLLILD 158
Cdd:cd03250 85 NILFG-KPFDEERYEKVikacalePDL--EILP---------DGDlteigekginLSGGQKQRISLARAVYSDADIYLLD 152
|
..
gi 15600055 159 EP 160
Cdd:cd03250 153 DP 154
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-224 |
1.18e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.87 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYG-----GSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQ--- 72
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 73 --RVRAGIAYVPQGREIFPRlTVEENLLMGLSRF--SARDARAVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRAL 148
Cdd:PRK13643 81 pvRKKVGVVFQFPESQLFEE-TVLKDVAFGPQNFgiPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600055 149 ASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDmAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDMESE 224
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
9-212 |
1.24e-20 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 85.35 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 9 QYYGGSH-ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvRAGIAYVPQGREI 87
Cdd:cd03246 9 RYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL-GDHVGYLPQDDEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 88 FPRlTVEENLlmglsrfsardaravpdfiyelfpvlremkqrrggdLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPS 167
Cdd:cd03246 88 FSG-SIAENI------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600055 168 VIKEIGAVVRSLAARGDMAILLVEQfyDFAAELADQYLVMARGEI 212
Cdd:cd03246 131 GERALNQAIAALKAAGATRIVIAHR--PETLASADRILVLEDGRV 173
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-220 |
1.33e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.13 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAgIAY 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMG----LSRFSARDA--RAVPDFIYELFPVLReMKQRRGGDLSGGQQQQLAIGRALASQPRL 154
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGrtphRSRFDTWTEtdRAAVERAMERTGVAQ-FADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600055 155 LILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFyDFAAELADQYLVMARGEIVQQGRGRD 220
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDL-DLAARYCDELVLLADGRVRAAGPPAD 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-221 |
1.45e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.02 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLT-GLRPHQ----RVR 75
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfGKDIFQidaiKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 76 AGIAYVPQGREIFPRLTVEENLLMGLSRFSARDARAVPDFIYE------LFPVLREMKQRRGGDLSGGQQQQLAIGRALA 149
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEEclrkvgLWKEVYDRLNSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 150 SQPRLLILDEPTEGIQPSVIKEIGAVVRSLaaRGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDM 221
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-216 |
1.53e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.56 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYggSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAY 80
Cdd:PRK10771 1 MLKLTDITWLY--HHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRR---PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGLS---RFSARDARAVPDFIYELFpvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLIL 157
Cdd:PRK10771 76 LFQENNLFSHLTVAQNIGLGLNpglKLNAAQREKLHAIARQMG--IEDLLARLPGQLSGGQRQRVALARCLVREQPILLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600055 158 DEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK10771 154 DEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDG 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-210 |
1.91e-20 |
|
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: 85.98 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVragiayVPQGREIFPRLTVEEN 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV------VFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 97 LLMGLSR----FSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEI 172
Cdd:TIGR01184 75 IALAVDRvlpdLSKSERRAIVEEHIALVG-LTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600055 173 GAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARG 210
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-216 |
2.38e-20 |
|
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: 85.62 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIAYVPQGREIFPRlTVEE 95
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHD-LRSRISIIPQDPVLFSG-TIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 96 NLlMGLSRFS------ARDARAVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVI 169
Cdd:cd03244 97 NL-DPFGEYSdeelwqALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15600055 170 KEIGAVVRSlaARGDMAILLV----EQFYDFaaelaDQYLVMARGEIVQQG 216
Cdd:cd03244 176 ALIQKTIRE--AFKDCTVLTIahrlDTIIDS-----DRILVLDKGRVVEFD 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-221 |
2.58e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 86.72 E-value: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQ---RVRAGIAYVPQGRE--IFPRl 91
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikQIRKKVGLVFQFPEsqLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 92 TVEENLLMGLSRF--SARDARAVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVI 169
Cdd:PRK13649 102 TVLKDVAFGPQNFgvSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600055 170 KEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDM 221
Cdd:PRK13649 182 KELMTLFKKLHQSG-MTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-230 |
3.99e-20 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 85.28 E-value: 3.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIAYVPQGREIFPRlTVEE 95
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRW-LRSQIGLVSQEPVLFDG-TIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 96 NLLMGlsRFSARDARAVP--------DFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPS 167
Cdd:cd03249 96 NIRYG--KPDATDEEVEEaakkanihDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600055 168 VIKEI-GAVVRslAARGDMAILLveqfydfAAEL-----ADQYLVMARGEIVQQGRGRD-MESEGV-RGLV 230
Cdd:cd03249 174 SEKLVqEALDR--AMKGRTTIVI-------AHRLstirnADLIAVLQNGQVVEQGTHDElMAQKGVyAKLV 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-217 |
4.78e-20 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 84.97 E-value: 4.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 9 QYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIAYVPQGREIF 88
Cdd:cd03253 9 AYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS-LRRAIGVVPQDTVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 89 PRlTVEENLLMGlsRFSARD------ARA--VPDFIyELFP-----VLREmkqrRGGDLSGGQQQQLAIGRALASQPRLL 155
Cdd:cd03253 88 ND-TIGYNIRYG--RPDATDeevieaAKAaqIHDKI-MRFPdgydtIVGE----RGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 156 ILDEPTEGIQPSVIKEIGAVVRSLAArGDMAILLveqfydfAAEL-----ADQYLVMARGEIVQQGR 217
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSK-GRTTIVI-------AHRLstivnADKIIVLKDGRIVERGT 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-216 |
9.37e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.91 E-value: 9.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 19 GLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQR--VRAGIAYVPQG--REIFPRLTVE 94
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWraVRSDIQMIFQDplASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 95 ENLLMGLSRFSARDARA-VPDFIYELFP---VLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIK 170
Cdd:PRK15079 119 EIIAEPLRTYHPKLSRQeVKDRVKAMMLkvgLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600055 171 EIGAVVRSLAArgDMAILLVEQFYDFAA--ELADQYLVMARGEIVQQG 216
Cdd:PRK15079 199 QVVNLLQQLQR--EMGLSLIFIAHDLAVvkHISDRVLVMYLGHAVELG 244
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-216 |
1.15e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.79 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYY-GGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGlRPHQRVRAGIAY 80
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA-ENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQ--GREIFPrLTVEENLL-----MGLSRFS----ARDA-RAVPdfiyelfpvLREMKQRRGGDLSGGQQQQLAIGRAL 148
Cdd:PRK13647 84 VFQdpDDQVFS-STVWDDVAfgpvnMGLDKDEverrVEEAlKAVR---------MWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 149 ASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDmAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-161 |
1.16e-19 |
|
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: 81.73 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWegrsltglrpHQRVRagIAYV 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW----------GSTVK--IGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQgreifprltveenllmglsrfsardaravpdfiyelfpvlremkqrrggdLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:cd03221 69 EQ--------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-217 |
1.34e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 85.62 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGS----HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQ--RV 74
Cdd:PRK11153 1 MIELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 75 RAGIAYVPQGREIFPRLTVEENL-----LMGLSRfSARDARavpdfIYELFPV--LREMKQRRGGDLSGGQQQQLAIGRA 147
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNValpleLAGTPK-AEIKAR-----VTELLELvgLSDKADRYPAQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 148 LASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGR 217
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-221 |
1.45e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 84.49 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAR--------EGQVAWEGRSLTGLRPHQ 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 73 RVRAGIAYVPQGREIFPrLTVEENLLMGlsRFSarDARAVPDFIYELFPVLREMKQRRGGD---------LSGGQQQQLA 143
Cdd:PRK13547 81 LARLRAVLPQAAQPAFA-FSAREIVLLG--RYP--HARRAGALTHRDGEIAWQALALAGATalvgrdvttLSGGELARVQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 144 IGRALA---------SQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQ 214
Cdd:PRK13547 156 FARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVA 235
|
....*..
gi 15600055 215 QGRGRDM 221
Cdd:PRK13547 236 HGAPADV 242
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
1.53e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 84.36 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLH-QYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEG-------RSLTGLRphQ 72
Cdd:PRK13639 1 ILETRDLKySYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkKSLLEVR--K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 73 RVraGIAYVPQGREIFPRlTVEEN-----LLMGLSRFS----ARDA-RAVPDFIYELFPvlremkqrrGGDLSGGQQQQL 142
Cdd:PRK13639 79 TV--GIVFQNPDDQLFAP-TVEEDvafgpLNLGLSKEEvekrVKEAlKAVGMEGFENKP---------PHHLSGGQKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 143 AIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDM- 221
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVf 225
|
....*...
gi 15600055 222 -ESEGVRG 228
Cdd:PRK13639 226 sDIETIRK 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-161 |
1.66e-19 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 85.17 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 19 GLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQ--RVRAGIAYV---PQGrEIFPRLTV 93
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrPLRRRMQMVfqdPYA-SLNPRMTV 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600055 94 EENLLMGLSRFSARDARAVPDFIYELFPV--LR-EMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:COG4608 115 GDIIAEPLRIHGLASKAERRERVAELLELvgLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-160 |
2.04e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.47 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 11 YGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAYVPQGREIFPR 90
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER---GVGMVFQSYALYPH 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600055 91 LTVEENLLMGLSRFSA----RDAR--AVPDfIYELFPVLremkQRRGGDLSGGQQQQLAIGRALASQPRLLILDEP 160
Cdd:PRK11000 90 LSVAENMSFGLKLAGAkkeeINQRvnQVAE-VLQLAHLL----DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-221 |
4.60e-19 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 85.09 E-value: 4.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAgIAYVPQGREIFPRlTVEE 95
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH-IGYLPQDVELFPG-TVAE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 96 NLlmglSRFsarDARAVPDFIYELFPV--LREMKQR-----------RGGDLSGGQQQQLAIGRALASQPRLLILDEP-- 160
Cdd:TIGR01842 411 NI----ARF---GENADPEKIIEAAKLagVHELILRlpdgydtvigpGGATLSGGQRQRIALARALYGDPKLVVLDEPns 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600055 161 ---TEGIQpSVIKEIGAvvrsLAARGDMAILLVEQFYdfAAELADQYLVMARGEIVQQGRGRDM 221
Cdd:TIGR01842 484 nldEEGEQ-ALANAIKA----LKARGITVVVITHRPS--LLGCVDKILVLQDGRIARFGERDEV 540
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-160 |
5.26e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.83 E-value: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVragiay 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGLS---------RFSARDARAVPDfiyelfpvLREMKQRRGGDLSGGQQQQLAIGRALASQ 151
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQlagvekmqrLEIAHQMLKKVG--------LEGAEKRYIWQLSGGQRQRVGIARALAAN 146
|
....*....
gi 15600055 152 PRLLILDEP 160
Cdd:PRK11248 147 PQLLLLDEP 155
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-217 |
7.19e-19 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 81.30 E-value: 7.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLrPHQRVRAGIAYVPQGREIFPRlTVEE 95
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI-PLEDLRSSLTIIPQDPTLFSG-TIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 96 NLlmglSRFSARDARavpdfiyELFPVLRemkQRRGGD-LSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGA 174
Cdd:cd03369 101 NL----DPFDEYSDE-------EIYGALR---VSEGGLnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600055 175 VVRSLAARGDMAILL--VEQFYDFaaelaDQYLVMARGEIVQQGR 217
Cdd:cd03369 167 TIREEFTNSTILTIAhrLRTIIDY-----DKILVMDAGEVKEYDH 206
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
9-232 |
9.28e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.49 E-value: 9.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 9 QYYG-GSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTglrPH--QRVRAGIAYVPQGR 85
Cdd:PRK13648 16 QYQSdASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT---DDnfEKLRKHIGIVFQNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 86 E-IFPRLTVEENLLMGLSRFSA---RDARAVPDFIYELfpvlrEMKQRRGGD---LSGGQQQQLAIGRALASQPRLLILD 158
Cdd:PRK13648 93 DnQFVGSIVKYDVAFGLENHAVpydEMHRRVSEALKQV-----DMLERADYEpnaLSGGQKQRVAIAGVLALNPSVIILD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600055 159 EPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAElADQYLVMARGEIVQQGRGRDMESEGvRGLVAI 232
Cdd:PRK13648 168 EATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHA-EELTRI 239
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-216 |
9.36e-19 |
|
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: 80.43 E-value: 9.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGS--HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRphQRVRAGIA 79
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE--KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 80 YVPQGREIFPRlTVEENLlmglsrfsardaravpdfiyelfpvlremkqrrGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:cd03247 79 VLNQRPYLFDT-TLRNNL---------------------------------GRRFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 160 PTEGIQPSVIKEIGAVVRSLAArgDMAILLVEQFYDfAAELADQYLVMARGEIVQQG 216
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-216 |
1.02e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.45 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRP-HQRVRAGIAYVPQGREiFPRLTVEE 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVFQNPDNQ-FVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 96 NLLMGLSRFSARDARAVPDFIYELFPV-LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGA 174
Cdd:PRK13642 102 DVAFGMENQGIPREEMIKRVDEALLAVnMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15600055 175 VVRSLAARGDMAILLVEQFYDFAAElADQYLVMARGEIVQQG 216
Cdd:PRK13642 182 VIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEA 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
13-216 |
1.83e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.37 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 13 GSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAgIAYVPQGREIFPRLT 92
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 93 VEENLLMG-------LSRFSARDARAVPDFIyeLFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQ 165
Cdd:PRK10575 102 VRELVAIGrypwhgaLGRFGAADREKVEEAI--SLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600055 166 PSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADqYLVMAR-GEIVQQG 216
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCD-YLVALRgGEMIAQG 230
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
32-216 |
1.88e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 83.61 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 32 LLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRpHQRVRAGIAYVPQ---------------GREIfprltVEEN 96
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAMVQQdpvvladtflanvtlGRDI-----SEEQ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 97 LLMGLSRFS-ARDARAVPDFIYELfpvLREmkqrRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKeigAV 175
Cdd:PRK10790 446 VWQALETVQlAELARSLPDGLYTP---LGE----QGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ---AI 515
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600055 176 VRSLAARGDMAILLVeqfydFAAEL-----ADQYLVMARGEIVQQG 216
Cdd:PRK10790 516 QQALAAVREHTTLVV-----IAHRLstiveADTILVLHRGQAVEQG 556
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-216 |
1.95e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 81.60 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIAYVPQGRE-IFPRLTVEE 95
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD-VRRQVGMVFQNPDnQFVGATVQD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 96 NLLMGLsrfsarDARAVP--DFIYELFPVLREMK-----QRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSV 168
Cdd:PRK13635 102 DVAFGL------ENIGVPreEMVERVDQALRQVGmedflNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600055 169 IKEIGAVVRSLAARGDMAILLVEQFYDFAAElADQYLVMARGEIVQQG 216
Cdd:PRK13635 176 RREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-216 |
2.06e-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: 83.91 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 28 EVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSL-TGLrphQRVRAGIAYVPQGREIFPRLTVEENLLMglsrFSA 106
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNL---DAVRQSLGMCPQHNILFHHLTVAEHILF----YAQ 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 107 RDARAVPDFIYELFPVLREM-----KQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVrsLAA 181
Cdd:TIGR01257 1030 LKGRSWEEAQLEMEAMLEDTglhhkRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKY 1107
|
170 180 190
....*....|....*....|....*....|....*
gi 15600055 182 RGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:TIGR01257 1108 RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-215 |
2.42e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.63 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYG----GSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGL----RPHQ 72
Cdd:PRK11629 5 LLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 73 RVRAgIAYVPQGREIFPRLTVEENLLMGLSRFSARDARAVPDFIYELFPV-LREMKQRRGGDLSGGQQQQLAIGRALASQ 151
Cdd:PRK11629 85 RNQK-LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVgLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600055 152 PRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQyLVMARGEIVQQ 215
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ-LEMRDGRLTAE 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-216 |
3.94e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.91 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 11 YGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPA-----REGQVAWEGRSLTGLRPHQRVRAGIAYVPQGR 85
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 86 EIFPrLTVEENLLMGLSRFS---ARDARAVPDFIYELFPVLREMKQRRGGD---LSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRAHKlvpRKEFRGVAQARLTEVGLWDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 160 PTEGIQPSVIKEIGAVVRSLAARgdMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEG 244
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-227 |
5.11e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 80.59 E-value: 5.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTG------LRPhqrVRAGIAYVPQgreiFPR 90
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRP---VRKRIGMVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 91 L-----TVEENLLMGLSRFSArDARAVPDFIYEL-----FPvlREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEP 160
Cdd:PRK13646 96 SqlfedTVEREIIFGPKNFKM-NLDEVKNYAHRLlmdlgFS--RDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 161 TEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDMESEGVR 227
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-161 |
7.20e-18 |
|
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: 79.02 E-value: 7.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYY-----GGSHI--LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMG---------LVPAREGQVawegrS 64
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnylpdsgsiLVRHDGGWV-----D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 65 LTGLRPHQ--RVRAG-IAYVPQGREIFPRLT----VEENLL-MGLSRFSARD-ARA------VPDFIYELFPvlremkqr 129
Cdd:COG4778 79 LAQASPREilALRRRtIGYVSQFLRVIPRVSaldvVAEPLLeRGVDREEARArAREllarlnLPERLWDLPP-------- 150
|
170 180 190
....*....|....*....|....*....|..
gi 15600055 130 rgGDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:COG4778 151 --ATFSGGEQQRVNIARGFIADPPLLLLDEPT 180
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-221 |
8.43e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.84 E-value: 8.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMG-LVP--AREGQVAWEGRSLTGLRPHQ-RVRAGIAYV-PQGReiFPR 90
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPddNPNSKITVDGITLTAKTVWDiREKVGIVFQnPDNQ--FVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 91 LTVEENLLMGLsrfsarDARAVPDfiYELFPVLREMKQRRG---------GDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:PRK13640 100 ATVGDDVAFGL------ENRAVPR--PEMIKIVRDVLADVGmldyidsepANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 162 EGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDfAAELADQYLVMARGEIVQQGRGRDM 221
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-166 |
1.05e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.32 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 3 QVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGlvpAR---EGQVAWEGRSLTGLRPHQRVRAGIA 79
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG---ARkiqQGRVEVLGGDMADARHRRAVCPRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 80 YVPQG--REIFPRLTVEENL-----LMGLSRfSARDARavpdfIYEL--------FPvlremkQRRGGDLSGGQQQQLAI 144
Cdd:NF033858 80 YMPQGlgKNLYPTLSVFENLdffgrLFGQDA-AERRRR-----IDELlratglapFA------DRPAGKLSGGMKQKLGL 147
|
170 180
....*....|....*....|..
gi 15600055 145 GRALASQPRLLILDEPTEGIQP 166
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDP 169
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-224 |
1.31e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.29 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLV---PAREGQVAWEGRSLTG----LRPHQR 73
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQRegrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 74 VRAGIAYVPQGREIFPRLTVEENLLMG-----------LSRFS-ARDARAvpdfIYELFPV-LREMKQRRGGDLSGGQQQ 140
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIGalgstpfwrtcFSWFTrEQKQRA----LQALTRVgMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 141 QLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRD 220
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
....
gi 15600055 221 MESE 224
Cdd:PRK09984 240 FDNE 243
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-212 |
1.32e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 78.95 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVawegrsLTGLRPHQRVRAGIAYV 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLLMGLS---RFSARDA-RAVPdfiyelfpvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLIL 157
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGLKgqwRDAALQAlAAVG---------LADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 158 DEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEI 212
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-216 |
1.69e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 80.62 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 19 GLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAW----EGRSLTGLRPHQRVRAG--IAYVPQGREIFPRLT 92
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGRGRAKryIGILHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 93 VEENLLMGLSrFSARDARAVPDFIYELFPV------LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQP 166
Cdd:TIGR03269 382 VLDNLTEAIG-LELPDELARMKAVITLKMVgfdeekAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDP 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600055 167 svIKEIGAVVRSLAARGDM--AILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:TIGR03269 461 --ITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-216 |
2.59e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.25 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYY--GGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLrPHQRVRAGIA 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY-SEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 80 YVPQGREIFPRlTVEENLLMGLSrfSARDARavpdfiyelfpvLREMKQRRG---------------GD----LSGGQQQ 140
Cdd:PRK11160 418 VVSQRVHLFSA-TLRDNLLLAAP--NASDEA------------LIEVLQQVGleklleddkglnawlGEggrqLSGGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 141 QLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAArgDMAILLV-------EQFydfaaelaDQYLVMARGEIV 213
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMIthrltglEQF--------DRICVMDNGQII 552
|
...
gi 15600055 214 QQG 216
Cdd:PRK11160 553 EQG 555
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-212 |
4.15e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.85 E-value: 4.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 14 SHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIAYVPQGRE-IFPRLT 92
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-IRHKIGMVFQNPDnQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 93 VEENLLMGLSR--FSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIK 170
Cdd:PRK13650 99 VEDDVAFGLENkgIPHEEMKERVNEALELVG-MQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15600055 171 EIGAVVRSLAARGDMAILLVEQFYDFAAeLADQYLVMARGEI 212
Cdd:PRK13650 178 ELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-190 |
4.50e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.57 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAYVPQGREIFPRLTVEEN 96
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 97 LLMGL--SRFSARDARAVpdfIYELFPVLREM-----KQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVI 169
Cdd:PRK11288 100 LYLGQlpHKGGIVNRRLL---NYEAREQLEHLgvdidPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREI 176
|
170 180
....*....|....*....|.
gi 15600055 170 KEIGAVVRSLAARGdMAILLV 190
Cdd:PRK11288 177 EQLFRVIRELRAEG-RVILYV 196
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-216 |
5.09e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.35 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWE--------GRSLTGLRPHQR-------VRAGIAY 80
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkkNNHELITNPYSKkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQgreiFP-----RLTVEENLLMGLSRF--SARDARAVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPR 153
Cdd:PRK13631 121 VFQ----FPeyqlfKDTIEKDIMFGPVALgvKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 154 LLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFyDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTM-EHVLEVADEVIVMDKGKILKTG 258
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
9-160 |
5.19e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 78.73 E-value: 5.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 9 QYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRvraGIAYVPQGREIF 88
Cdd:PRK11650 12 SYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR---DIAMVFQNYALY 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600055 89 PRLTVEENLLMGL-------SRFSARDARAVPdfIYELFPVLremkQRRGGDLSGGQQQQLAIGRALASQPRLLILDEP 160
Cdd:PRK11650 89 PHMSVRENMAYGLkirgmpkAEIEERVAEAAR--ILELEPLL----DRKPRELSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
16-225 |
7.84e-17 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 79.02 E-value: 7.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIAYVPQGREIFPRlTVEE 95
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAW-LRRQMGVVLQENVLFSR-SIRD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 96 NLlmGLSRFSARDARAVP--------DFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPS 167
Cdd:TIGR01846 550 NI--ALCNPGAPFEHVIHaaklagahDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYE 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 168 VIKEIGAVVRSLaARGDMAILLVEQFYdfAAELADQYLVMARGEIVQQGRGRDMESEG 225
Cdd:TIGR01846 628 SEALIMRNMREI-CRGRTVIIIAHRLS--TVRACDRIIVLEKGQIAESGRHEELLALQ 682
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-224 |
9.69e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.95 E-value: 9.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKL-HQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIA 79
Cdd:PRK13644 1 MIRLENVsYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 80 YVPQGREI-FPRLTVEENLLMGLSRF-------SARDARAVPDFiyelfpVLREMKQRRGGDLSGGQQQQLAIGRALASQ 151
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLAFGPENLclppieiRKRVDRALAEI------GLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 152 PRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAelADQYLVMARGEIVQQGRGRDMESE 224
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD--ADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
16-161 |
1.03e-16 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 75.91 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRV---RAGIAYVPQGREIFPRLT 92
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIilrRELIGYIFQSFNLIPHLS 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600055 93 VEENLLMGLS-RFSARDAR-AVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:NF038007 100 IFDNVALPLKyRGVAKKERiERVNQVLNLFG-IDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPT 169
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-202 |
1.09e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 76.74 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRC---LMGLVP-AR-EGQVAWEGRSL--TGLRPHQrV 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPgFRvEGKVTFHGKNLyaPDVDPVE-V 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 75 RAGIAYVPQGREIFPRlTVEENLLMG------------LSRFSARDAravpdfiyELFPVLREMKQRRGGDLSGGQQQQL 142
Cdd:PRK14243 90 RRRIGMVFQKPNPFPK-SIYDNIAYGaringykgdmdeLVERSLRQA--------ALWDEVKDKLKQSGLSLSGGQQQRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 143 AIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARgdMAILLVEQFYDFAAELAD 202
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSD 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-216 |
1.26e-16 |
|
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: 75.65 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 15 HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGR--SLTGLrphqrvRAGIAyvpqgreifPRLT 92
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsSLLGL------GGGFN---------PELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 93 VEEN-----LLMGLSRfsaRDARAVPDFIYElFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPT----EG 163
Cdd:cd03220 101 GRENiylngRLLGLSR---KEIDEKIDEIIE-FSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLavgdAA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600055 164 IQPSVIKEIgavvRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03220 177 FQEKCQRRL----RELLKQG-KTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
11-226 |
1.67e-16 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 77.83 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 11 YGGSHI--LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRpHQRVRAGIAYVPQGREIF 88
Cdd:TIGR02203 340 YPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT-LASLRRQVALVSQDVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 89 PRlTVEENLLMGLS--------RFSARDARAVpDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEP 160
Cdd:TIGR02203 419 ND-TIANNIAYGRTeqadraeiERALAAAYAQ-DFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEA 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 161 TEGIQPSVIKEIGAVVRSLaARGDMAILLVEQFYdfAAELADQYLVMARGEIVQQGRGRD-MESEGV 226
Cdd:TIGR02203 497 TSALDNESERLVQAALERL-MQGRTTLVIAHRLS--TIEKADRIVVMDDGRIVERGTHNElLARNGL 560
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-190 |
3.30e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 74.75 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPhQRVRAGIAY 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRlTVEENLLMG-LSRFSARDARAVPDFIyELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIFPwQIRNQQPDPAIFLDDL-ERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190
....*....|....*....|....*....|.
gi 15600055 160 PTEGIQPSVIKEIGAVVRSLAARGDMAILLV 190
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWV 194
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-216 |
4.45e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 76.38 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGL--VPAREGQVAW-----------EGRSLTG- 67
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyvERPSKVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 68 --------LRPHQ------------RVRAGIAYVPQGR-EIFPRLTVEENLLMGLSR--FSARDA--RAVpDFIYELFPV 122
Cdd:TIGR03269 81 pcpvcggtLEPEEvdfwnlsdklrrRIRKRIAIMLQRTfALYGDDTVLDNVLEALEEigYEGKEAvgRAV-DLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 123 LREMKQRRggDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELAD 202
Cdd:TIGR03269 160 HRITHIAR--DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250
....*....|....
gi 15600055 203 QYLVMARGEIVQQG 216
Cdd:TIGR03269 238 KAIWLENGEIKEEG 251
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-212 |
5.08e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 76.31 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAYVPQGRE---IFPRLTV 93
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEERRstgIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 94 EENLL----------MGLsrFSARDARAVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEG 163
Cdd:PRK10982 344 GFNSLisnirnyknkVGL--LDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600055 164 IQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAeLADQYLVMARGEI 212
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLG-ITDRILVMSNGLV 469
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-216 |
5.49e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.04 E-value: 5.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRS----LTGLRPHQRVRAGIAYVPQgreiFPRL- 91
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAipanLKKIKEVKRLRKEIGLVFQ----FPEYq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 92 ----TVEENLLMGLSRFSARDARA---VPDFIyELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGI 164
Cdd:PRK13645 103 lfqeTIEKDIAFGPVNLGENKQEAykkVPELL-KLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600055 165 QPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
25-210 |
8.92e-16 |
|
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: 72.66 E-value: 8.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 25 KVGEVTCLLGRNGVGKTTLLRCL-----MGLVparEGQVawegrSLTGLRPHQRVRAGIAYVPQGREIFPRLTVEENLlm 99
Cdd:cd03232 31 KPGTLTALMGESGAGKTTLLDVLagrktAGVI---TGEI-----LINGRPLDKNFQRSTGYVEQQDVHSPNLTVREAL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 100 glsRFSArdaravpdfiyelfpVLRemkqrrggDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSL 179
Cdd:cd03232 101 ---RFSA---------------LLR--------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15600055 180 AARGdMAIL---------LVEQFydfaaelaDQYLVMARG 210
Cdd:cd03232 155 ADSG-QAILctihqpsasIFEKF--------DRLLLLKRG 185
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-183 |
9.01e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 9.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAY 80
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMG---LSRFSARDARAVPDFIYELFPVL--REMKQRRGGDLSGGQQQQLAIGRALASQPRLL 155
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLGrefVNRFGRIDWKKMYAEADKLLARLnlRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180
....*....|....*....|....*...
gi 15600055 156 ILDEPTEGIQPSVIKEIGAVVRSLAARG 183
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIRELKSQG 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-216 |
1.10e-15 |
|
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: 73.52 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVawegrSLTGLRPHQR---VRAGIAYV-PQGREIFPRLT 92
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-----RVAGLVPWKRrkkFLRRIGVVfGQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 93 VEE--NLLMGLSRFSARDARAVPDFIYELFPVLREMKQ--RRggdLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSV 168
Cdd:cd03267 112 VIDsfYLLAAIYDLPPARFKKRLDELSELLDLEELLDTpvRQ---LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600055 169 IKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:cd03267 189 QENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-209 |
1.25e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGrsltGLRphqrvragIAY 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----KLR--------IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFPRLTVEENLLMGLsRFSARDAravpdfiyELFPVLREMK-----QRRGGDLSGGQQQQLAIGRALASQPRLL 155
Cdd:PRK09544 72 VPQKLYLDTTLPLTVNRFLRL-RPGTKKE--------DILPALKRVQaghliDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 156 ILDEPTEGI----QPSVIKEIGAVVRSLaargDMAILLVEQfydfaaelaDQYLVMAR 209
Cdd:PRK09544 143 VLDEPTQGVdvngQVALYDLIDQLRREL----DCAVLMVSH---------DLHLVMAK 187
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-214 |
2.09e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.32 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSL---TGLRPHQRVRAGIAYVPQgreiFPRL-- 91
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpeTGNKNLKKLRKKVSLVFQ----FPEAql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 92 ---TVEENLLMGLSRFSARDARAVPDFIYELFPV-LRE-MKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQP 166
Cdd:PRK13641 99 fenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVgLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600055 167 SVIKEIGAVVRSLAARGDMAILLVEQFYDfAAELADQYLVMARGEIVQ 214
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGHTVILVTHNMDD-VAEYADDVLVLEHGKLIK 225
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-224 |
2.90e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 73.62 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTllrclmGLVPAR-----EGQVAWEGRSLTGLR------- 69
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAHv*gpdAGRRPWRF*TWCANRralrrti 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 70 -PHQRVRAGiayvpqGREIFprlTVEENLLMgLSR---FSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIG 145
Cdd:NF000106 88 g*HRPVR*G------RRESF---SGRENLYM-IGR*ldLSRKDARARADELLERFS-LTEAAGRAAAKYSGGMRRRLDLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600055 146 RALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLaARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDMESE 224
Cdd:NF000106 157 ASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-226 |
6.82e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.47 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMG-LVPAREGQVAwegrsltglrphqrVRAGIAYVPQGREIFpRLTVEE 95
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVV--------------IRGSVAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 96 NLLMGLSRFSARDARAVP----DFIYELFPV--LREMKQRrGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVI 169
Cdd:PLN03232 698 NILFGSDFESERYWRAIDvtalQHDLDLLPGrdLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVA 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 170 KEIGAVVRSLAARGDMAILLVEQFYDFAaeLADQYLVMARGEIVQQGRGRDMESEGV 226
Cdd:PLN03232 777 HQVFDSCMKDELKGKTRVLVTNQLHFLP--LMDRIILVSEGMIKEEGTFAELSKSGS 831
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-161 |
1.11e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.53 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 13 GSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAwegrsltglRPH--------QRV-------RAG 77
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA---------RPAgarvlflpQRPylplgtlREA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 78 IAYvPQGREIFPRLTVEENL-LMGLSRFSARdaravpdfiyelfpvLREmKQRRGGDLSGGQQQQLAIGRALASQPRLLI 156
Cdd:COG4178 446 LLY-PATAEAFSDAELREALeAVGLGHLAER---------------LDE-EADWDQVLSLGEQQRLAFARLLLHKPDWLF 508
|
....*
gi 15600055 157 LDEPT 161
Cdd:COG4178 509 LDEAT 513
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-221 |
1.99e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.93 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHI----LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLV--PAR--EGQVAWEGRSLTGLRPHQ 72
Cdd:PRK11022 3 LLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdyPGRvmAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 73 R---VRAGIAYVPQ------------GREIFPRLTVEEnllmGLSRfSARDARAV----------PDFIYELFPvlremk 127
Cdd:PRK11022 83 RrnlVGAEVAMIFQdpmtslnpcytvGFQIMEAIKVHQ----GGNK-KTRRQRAIdllnqvgipdPASRLDVYP------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 128 qrrgGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVM 207
Cdd:PRK11022 152 ----HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVM 227
|
250
....*....|....
gi 15600055 208 ARGEIVQQGRGRDM 221
Cdd:PRK11022 228 YAGQVVETGKAHDI 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-210 |
2.13e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.06 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVparEGQVAWEGRSLTGLRP----HQRVragIAYVPQGREIFPRL 91
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV---TTGVITGGDRLVNGRPldssFQRS---IGYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 92 TVEENLlmglsRFSA--RDARAVP-----DFIYELFPVLrEMKQRR-------GGDLSGGQQQQLAIGRALASQPRLLI- 156
Cdd:TIGR00956 852 TVRESL-----RFSAylRQPKSVSksekmEYVEEVIKLL-EMESYAdavvgvpGEGLNVEQRKRLTIGVELVAKPKLLLf 925
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 157 LDEPTEGIQPSVIKEIGAVVRSLAARGDmAIL---------LVEQFydfaaelaDQYLVMARG 210
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLADHGQ-AILctihqpsaiLFEEF--------DRLLLLQKG 979
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-216 |
2.27e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.68 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLM----GLVPAREGQVAWEGRSLTGLRPHQrvRAGIAYVPQGREIFPRL 91
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHY--RGDVVYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 92 TVEENL------------LMGLSRFSARDARAvpDFIYELFPvLREMKQRRGGD-----LSGGQQQQLAIGRALASQPRL 154
Cdd:TIGR00956 154 TVGETLdfaarcktpqnrPDGVSREEYAKHIA--DVYMATYG-LSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 155 LILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILL-VEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:TIGR00956 231 QCWDNATRGLDSATALEFIRALKTSANILDTTPLVaIYQCSQDAYELFDKVIVLYEGYQIYFG 293
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-207 |
2.91e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 15 HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLtglrPHQRVRAGIAYVPQGREIfprLTVE 94
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN----QFGREASLIDAIGRKGDF---KDAV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 95 ENL-LMGLSrfsarDAravpdfiyelfPVLRemkqRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIG 173
Cdd:COG2401 117 ELLnAVGLS-----DA-----------VLWL----RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170 180 190
....*....|....*....|....*....|....
gi 15600055 174 AVVRSLAARGDMAILLVEQFYDFAAELADQYLVM 207
Cdd:COG2401 177 RNLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
10-161 |
3.32e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.15 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 10 YYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEG---RSLTglrpHQRVRAGIAYVPQGRE 86
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVT----RASLRRNIAVVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 87 IFPRlTVEENLLMGlsRFSARDAR--------AVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILD 158
Cdd:PRK13657 420 LFNR-SIEDNIRVG--RPDATDEEmraaaeraQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILD 496
|
...
gi 15600055 159 EPT 161
Cdd:PRK13657 497 EAT 499
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-161 |
3.81e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.04 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYG-GSH---ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQR--V 74
Cdd:PRK10584 6 IVEVHHLKKSVGqGEHelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARakL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 75 RA-GIAYVPQGREIFPRLTVEEN-----LLMGLSRFSARDARAVPDFIYELFPVLREMKQRrggdLSGGQQQQLAIGRAL 148
Cdd:PRK10584 86 RAkHVGFVFQSFMLIPTLNALENvelpaLLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ----LSGGEQQRVALARAF 161
|
170
....*....|...
gi 15600055 149 ASQPRLLILDEPT 161
Cdd:PRK10584 162 NGRPDVLFADEPT 174
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-220 |
4.15e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.06 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVparegqvawEGRSLTGL------RPHQRVRAGIAYVPQGREIFP 89
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRI---------QGNNFTGTilannrKPTKQILKRTGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 90 RLTVEENL----LMGLSRFSARD--ARAVPDFIYELFpvLREMKQRRGGD-----LSGGQQQQLAIGRALASQPRLLILD 158
Cdd:PLN03211 154 HLTVRETLvfcsLLRLPKSLTKQekILVAESVISELG--LTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 159 EPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRD 220
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-216 |
4.25e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.45 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 21 SFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRP---HQRVRAGIAYVPQGREIFPRLTVEENL 97
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 98 LMGLSRFSARDARAVPDFIYELFPV-LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVV 176
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15600055 177 RSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-159 |
5.49e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.95 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 15 HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGR--SLTGLrphqrvraGIAYVPQgreifprLT 92
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsALLEL--------GAGFHPE-------LT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 93 VEEN-----LLMGLSRfsaRDARAVPDFIYElF---------PVlremkqrrgGDLSGGQQQQLAIGRALASQPRLLILD 158
Cdd:COG1134 105 GRENiylngRLLGLSR---KEIDEKFDEIVE-FaelgdfidqPV---------KTYSSGMRARLAFAVATAVDPDILLVD 171
|
.
gi 15600055 159 E 159
Cdd:COG1134 172 E 172
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-217 |
6.04e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 70.23 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIAYVPQGREIFPRlTVEE 95
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS-LRAAIGIVPQDTVLFND-TIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 96 NLLMGlsRFSARD------ARA--VPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPS 167
Cdd:COG5265 451 NIAYG--RPDASEeeveaaARAaqIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSR 528
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600055 168 VIKEIGAVVRSLAA-RGDMAIllveqfydfAAEL-----ADQYLVMARGEIVQQGR 217
Cdd:COG5265 529 TERAIQAALREVARgRTTLVI---------AHRLstivdADEILVLEAGRIVERGT 575
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
20-221 |
1.26e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.60 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 20 LSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAR---EGQVAWEGRSLTGLRPHQ--RVRA-GIAYVPQG--REIFPRL 91
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKElnKLRAeQISMIFQDpmTSLNPYM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 92 TVEENL---LM---GLSRfsardARAVPDFIYELFPV-LREMKQRRG---GDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:PRK09473 115 RVGEQLmevLMlhkGMSK-----AEAFEESVRMLDAVkMPEARKRMKmypHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 162 EGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDM 221
Cdd:PRK09473 190 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-168 |
1.31e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 66.41 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAwegrsltglRPhqrVRAGIAYVPQgREIFPRLTVEE 95
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG---------MP---EGEDLLFLPQ-RPYLPLGTLRE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 96 NLlmglsrfsardaravpdfIYelfPVLREmkqrrggdLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSV 168
Cdd:cd03223 83 QL------------------IY---PWDDV--------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-161 |
1.65e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.15 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAW-EGrsltglrphqrvrAGIAY 80
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWsEN-------------ANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREI-FPRltvEENLL--MGLSRFSARDARAVpdfiyelfpvlREMKQRR--GGD--------LSGGQQQQLAIGRA 147
Cdd:PRK15064 387 YAQDHAYdFEN---DLTLFdwMSQWRQEGDDEQAV-----------RGTLGRLlfSQDdikksvkvLSGGEKGRMLFGKL 452
|
170
....*....|....
gi 15600055 148 LASQPRLLILDEPT 161
Cdd:PRK15064 453 MMQKPNVLVMDEPT 466
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-216 |
2.10e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.73 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEG-------RSLTGLRPH-----QRVR-AGIAYVPQ 83
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVIELSEQsaaqmRHVRgADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 84 G--REIFPRLTVEEN------LLMGLSRFSA-RDARAVPDFIYelFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRL 154
Cdd:PRK10261 112 EpmTSLNPVFTVGEQiaesirLHQGASREEAmVEAKRMLDQVR--IPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 155 LILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-192 |
2.25e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.51 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSL-TGLRPHQRvraGIA 79
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQK---QLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 80 YVPQGREIFPRLTVEENLLMGLsRFSARDARAvpDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:PRK13540 78 FVGHRSGINPYLTLRENCLYDI-HFSPGAVGI--TELCRLFS-LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|...
gi 15600055 160 PTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQ 192
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-216 |
2.42e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.80 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAW----------------EGRSLTGLRPHQR------- 73
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkekekVLEKLVIQKTRFKkikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 74 VRAGIAYVPQGRE--IFPRlTVEENLL-----MGLSRFSARDaRAVpDFIyELFPVLREMKQRRGGDLSGGQQQQLAIGR 146
Cdd:PRK13651 103 IRRRVGVVFQFAEyqLFEQ-TIEKDIIfgpvsMGVSKEEAKK-RAA-KYI-ELVGLDESYLQRSPFELSGGQKRRVALAG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 147 ALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDmAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-219 |
2.94e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 15 HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPH--QRVRAGIAYVPQG--REIFPR 90
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQALRRDIQFIFQDpyASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 91 LTVEENLLMGL---SRFSARDARAVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPS 167
Cdd:PRK10261 418 QTVGDSIMEPLrvhGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600055 168 VIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGR 219
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRR 549
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-216 |
3.29e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.59 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLvPAR---EGQVAWEGRSLTGLRPHQRVRAG 77
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PAYkilEGDILFKGESILDLEPEERAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 78 IAYVPQgreiFPrltVE------ENLLMgLSRFSARDARAVPDF-IYELFPVLRE------MKQR-------RGgdLSGG 137
Cdd:CHL00131 86 IFLAFQ----YP---IEipgvsnADFLR-LAYNSKRKFQGLPELdPLEFLEIINEklklvgMDPSflsrnvnEG--FSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 138 QQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLaARGDMAILLVEQFYDFAAELADQYL-VMARGEIVQQG 216
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYQRLLDYIKPDYVhVMQNGKIIKTG 234
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-160 |
3.89e-13 |
|
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: 66.20 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGR---SLTGLRPHQRVRAGIAYVPQgREIFPRLTV 93
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnesEPSFEATRSRNRYSVAYAAQ-KPWLLNATV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 94 EENLLMGlSRFSARDARAV-------PDFiyELFPVLREMK-QRRGGDLSGGQQQQLAIGRALASQPRLLILDEP 160
Cdd:cd03290 96 EENITFG-SPFNKQRYKAVtdacslqPDI--DLLPFGDQTEiGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-225 |
6.24e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.46 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 15 HILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQvawegrsltglrpHQRVRAGIAYVPQGREIFpRLTVE 94
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA-------------SVVIRGTVAYVPQVSWIF-NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 95 ENLLMGLSRFSARDARAVP----DFIYELFPV--LREMKQRrGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSV 168
Cdd:PLN03130 697 DNILFGSPFDPERYERAIDvtalQHDLDLLPGgdLTEIGER-GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 169 IKEIGAVVRSLAARGDMAILLVEQFYdFAAELaDQYLVMARGEIVQQGRGRDMESEG 225
Cdd:PLN03130 776 GRQVFDKCIKDELRGKTRVLVTNQLH-FLSQV-DRIILVHEGMIKEEGTYEELSNNG 830
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-210 |
8.17e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 67.35 E-value: 8.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGG--SHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLtgLRPHQRVRAGI 78
Cdd:TIGR01257 1937 ILRLNELTKVYSGtsSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 79 AYVPQGREIFPRLTVEENLLM--GLSRFSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLI 156
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHLYLyaRLRGVPAEEIEKVANWSIQSLG-LSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600055 157 LDEPTEGIQPSVIKEIGAVVRSLaARGDMAILLVEQFYDFAAELADQYLVMARG 210
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-161 |
1.63e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.51 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 10 YYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQR--VRAGIAYVPQGREI 87
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLRRQIGMIFQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 88 FPRLTVEENLLMGL--SRFSARDAR----AVPDFIYEL-----FPVlremkqrrggDLSGGQQQQLAIGRALASQPRLLI 156
Cdd:PRK10908 91 LMDRTVYDNVAIPLiiAGASGDDIRrrvsAALDKVGLLdkaknFPI----------QLSGGEQQRVGIARAVVNKPAVLL 160
|
....*
gi 15600055 157 LDEPT 161
Cdd:PRK10908 161 ADEPT 165
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
27-217 |
4.77e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 64.16 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 27 GEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVA----WEGRSLTGLRPHQRvRAGIayvpqGRE---IF--------PRL 91
Cdd:COG4170 33 GEIRGLVGESGSGKSLIAKAICGITKDNWHVTAdrfrWNGIDLLKLSPRER-RKII-----GREiamIFqepsscldPSA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 92 TVEENLLMGL----------SRFSARDARAV----------PDFIYELFPVlremkqrrggDLSGGQQQQLAIGRALASQ 151
Cdd:COG4170 107 KIGDQLIEAIpswtfkgkwwQRFKWRKKRAIellhrvgikdHKDIMNSYPH----------ELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600055 152 PRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGR 217
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGP 242
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-188 |
4.98e-12 |
|
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: 64.81 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSfEAKVGEVTCLLGRNGVGKTTLLRCLMG-LVP---AREGQVAWE-------GrslTGLRP 70
Cdd:COG1245 75 LEEDPVHRYGENGFRLYGLP-VPKKGKVTGILGPNGIGKSTALKILSGeLKPnlgDYDEEPSWDevlkrfrG---TELQD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 71 H-QRVRAG---IAYVPQGREIFPRL---TVEEnLLMGLsrfsarDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLA 143
Cdd:COG1245 151 YfKKLANGeikVAHKPQYVDLIPKVfkgTVRE-LLEKV------DERGKLDELAEKLG-LENILDRDISELSGGELQRVA 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 144 IGRALASQPRLLILDEPTegiqpSV--IKE---IGAVVRSLAARG--------DMAIL 188
Cdd:COG1245 223 IAAALLRDADFYFFDEPS-----SYldIYQrlnVARLIRELAEEGkyvlvvehDLAIL 275
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-226 |
5.03e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 64.65 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGR-----SLTGLRPH-----QRVRA-------GIA 79
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdyTLASLRNQvalvsQNVHLfndtianNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 80 YVPQGReiFPRLTVEEnllmglsrfSARDARAVpDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:PRK11176 439 YARTEQ--YSREQIEE---------AARMAYAM-DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDE 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 160 PTEGIQPSVIKEIGAVVRSLaaRGDMAILLVEQFYDfAAELADQYLVMARGEIVQQGRGRD-MESEGV 226
Cdd:PRK11176 507 ATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAElLAQNGV 571
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-161 |
9.89e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 9.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 27 GEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEgRSLTGLRPHQR------------VRAGIAYVPQGREIFPRLT-- 92
Cdd:PRK11147 29 NERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVARLQQDpprnvegtvydfVAEGIEEQAEYLKRYHDIShl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 93 VE----ENLLMGLSRFSAR---------DARavpdfIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:PRK11147 108 VEtdpsEKNLNELAKLQEQldhhnlwqlENR-----INEVLAQLGLDPDAALSSLSGGWLRKAALGRALVSNPDVLLLDE 182
|
..
gi 15600055 160 PT 161
Cdd:PRK11147 183 PT 184
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
12-214 |
1.21e-11 |
|
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: 62.56 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 12 GGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPArEGQVAWEGRSLTGLrPHQRVRAGIAYVPQGREIFPRl 91
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSV-PLQKWRKAFGVIPQKVFIFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 92 TVEENlLMGLSRFSARDARAVPD-----FIYELFPVLREMKQRRGG-DLSGGQQQQLAIGRALASQPRLLILDEPTEGIQ 165
Cdd:cd03289 92 TFRKN-LDPYGKWSDEEIWKVAEevglkSVIEQFPGQLDFVLVDGGcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600055 166 PSVIKEIGAVVRSlaARGDMAILLVEQFYDFAAElADQYLVMARGEIVQ 214
Cdd:cd03289 171 PITYQVIRKTLKQ--AFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQ 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-166 |
1.40e-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: 63.78 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 12 GGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVpAREGQVAWEGRSLTGLrPHQRVRAGIAYVPQGREIFPRl 91
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSV-TLQTWRKAFGVIPQKVFIFSG- 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 92 TVEENlLMGLSRFSARDARAVPD-----FIYELFPVLREMKQRRGG-DLSGGQQQQLAIGRALASQPRLLILDEPTEGIQ 165
Cdd:TIGR01271 1307 TFRKN-LDPYEQWSDEEIWKVAEevglkSVIEQFPDKLDFVLVDGGyVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
.
gi 15600055 166 P 166
Cdd:TIGR01271 1386 P 1386
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-216 |
1.46e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.43 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGrsltglrphqrvraGIAYVPQGREIfPRLTVEEN 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------------SVAYVPQQAWI-QNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 97 LLMGLS------RFSARDARAVPDFiyELFPV-LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVI 169
Cdd:TIGR00957 719 ILFGKAlnekyyQQVLEACALLPDL--EILPSgDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600055 170 KEI-GAVVRSLAARGDMAILLVEQFYDFAAELaDQYLVMARGEIVQQG 216
Cdd:TIGR00957 797 KHIfEHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-161 |
1.47e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 23 EAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRsltglrphqrvragIAYVPQGREIFPRLTVEENLLMGLS 102
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK--------------ISYKPQYIKPDYDGTVEDLLRSITD 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 103 RFSArdaravpDFIYE--LFPV-LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:PRK13409 427 DLGS-------SYYKSeiIKPLqLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-206 |
1.53e-11 |
|
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: 62.04 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 27 GEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSltglrphqrvragIAYVPQGREIFPRLTVEEnLLMGLSrfsa 106
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-------------VSYKPQYIKADYEGTVRD-LLSSIT---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 107 RDARAVPDFIYELF-PV-LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGD 184
Cdd:cd03237 87 KDFYTHPYFKTEIAkPLqIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
170 180
....*....|....*....|..
gi 15600055 185 MAILLVEQFYDFAAELADQYLV 206
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-216 |
2.14e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.73 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 20 LSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLT----GLRPhQRVRagIAYVPQGREIFPRLTVEE 95
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySYRS-QRIR--MIFQDPSTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 96 NLLMGLSRFSARDARAVPDFIYElfpVLREMKQRRGGD------LSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVI 169
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIE---TLRQVGLLPDHAsyyphmLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15600055 170 KEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERG 232
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-216 |
2.77e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 61.35 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGL--VPAREGQVAWEGRSLTGLRPHQRVRAGI 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 79 AYVPQGREIFPrlTVEENLLMGLSRFSARDARAVP--------DFIYELFPVLR---EMKQRR-GGDLSGGQQQQLAIGR 146
Cdd:PRK09580 81 FMAFQYPVEIP--GVSNQFFLQTALNAVRSYRGQEpldrfdfqDLMEEKIALLKmpeDLLTRSvNVGFSGGEKKRNDILQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600055 147 ALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLaARGDMAILLVEQFYDFAAELADQYL-VMARGEIVQQG 216
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIKPDYVhVLYQGRIVKSG 228
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-213 |
3.34e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.11 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 8 HQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAR--EGQVAWEGRSLTGLRPHQRVRAGIAYVPQGR 85
Cdd:NF040905 267 HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRniSGTVFKDGKEVDVSTVSDAIDAGLAYVTEDR 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 86 EifpRL------TVEENL-LMGLSRFSARdarAVPDFIYElFPVLREMKQR----------RGGDLSGGQQQQLAIGRAL 148
Cdd:NF040905 347 K---GYglnlidDIKRNItLANLGKVSRR---GVIDENEE-IKVAEEYRKKmniktpsvfqKVGNLSGGNQQKVVLSKWL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600055 149 ASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLVeqfydfAAEL------ADQYLVMARGEIV 213
Cdd:NF040905 420 FTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEG-KGVIVI------SSELpellgmCDRIYVMNEGRIT 483
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-219 |
3.92e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.03 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 19 GLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAR-----EGQVAWEGRS--------LTGLRPHQrvragIAYVPQGR 85
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESllhaseqtLRGVRGNK-----IAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 86 EIF--PRLTVEENL--LMGLSRFSARDArAVPDFIYELFPV-LREMKQRRGG---DLSGGQQQQLAIGRALASQPRLLIL 157
Cdd:PRK15134 102 MVSlnPLHTLEKQLyeVLSLHRGMRREA-ARGEILNCLDRVgIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600055 158 DEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGR 219
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-166 |
3.99e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.06 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 21 SFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQvAWegrsLTGlrphQRVRAG-------IAYVPQGREIFPRLTV 93
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE-AW----LFG----QPVDAGdiatrrrVGYMSQAFSLYGELTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 94 EENLL-------MGLSRFSARDARAVPDFiyELFPVLREmkqrRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQP 166
Cdd:NF033858 357 RQNLElharlfhLPAAEIAARVAEMLERF--DLADVADA----LPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP 430
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-217 |
6.38e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 6.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 20 LSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPArEGQVAWEGRSLTGLRPHQ--RVRagiAYVPQGREIFPRLTVEENL 97
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAElaRHR---AYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 98 lmGLSRFSARDARAVPDFIYELFPVLREMKQ--RRGGDLSGGQQQQ-------LAIGRALASQPRLLILDEPTEGIQPSV 168
Cdd:PRK03695 91 --TLHQPDKTRTEAVASALNEVAEALGLDDKlgRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600055 169 IKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIVQQGR 217
Cdd:PRK03695 169 QAALDRLLSELCQQG-IAVVMSSHDLNHTLRHADRVWLLKQGKLLASGR 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-161 |
6.50e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 6.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 3 QVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGqvawegrsltglrphqRVRAG----I 78
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSG----------------RIHCGtkleV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 79 AYVPQGREIF-PRLTVEENLLMGLSR--FSARDaRAV----PDFiyeLFPVLREMKQRRGgdLSGGQQQQLAIGRALASQ 151
Cdd:PRK11147 385 AYFDQHRAELdPEKTVMDNLAEGKQEvmVNGRP-RHVlgylQDF---LFHPKRAMTPVKA--LSGGERNRLLLARLFLKP 458
|
170
....*....|
gi 15600055 152 PRLLILDEPT 161
Cdd:PRK11147 459 SNLLILDEPT 468
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-161 |
7.61e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.96 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPA--REGQVAWEG--RSLTGLRPHQRVraGIAYVPQGREIFPRLT 92
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGevCRFKDIRDSEAL--GIVIIHQELALIPYLS 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 93 VEENLLMG--LSRFSARDARAVPDFIYELFP-V-LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:NF040905 95 IAENIFLGneRAKRGVIDWNETNRRARELLAkVgLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-172 |
7.72e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.46 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 13 GSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRsltglrphqrvragIAYVPQGREIFPRlT 92
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMPG-T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 93 VEENLLMGLSRFSARDARAVPDFIYE----LFPVLREMKQRRGG-DLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPS 167
Cdd:TIGR01271 503 IKDNIIFGLSYDEYRYTSVIKACQLEediaLFPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
....*
gi 15600055 168 VIKEI 172
Cdd:TIGR01271 583 TEKEI 587
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-178 |
8.77e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.11 E-value: 8.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIAYVPQGREIFprltvEE 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD-LRFKITIIPQDPVLF-----SG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 96 NLLMGLSRFS---------ARDARAVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQP 166
Cdd:TIGR00957 1375 SLRMNLDPFSqysdeevwwALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170
....*....|..
gi 15600055 167 SVIKEIGAVVRS 178
Cdd:TIGR00957 1455 ETDNLIQSTIRT 1466
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
12-166 |
9.69e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 60.16 E-value: 9.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 12 GGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQ--RVRAGIAYVPQGREIFP 89
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlyTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 90 RLTVEENLlmglsRFSARDARAVPDFI------YELFPV-LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTE 162
Cdd:PRK11831 98 DMNVFDNV-----AYPLREHTQLPAPLlhstvmMKLEAVgLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
....
gi 15600055 163 GIQP 166
Cdd:PRK11831 173 GQDP 176
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-161 |
1.47e-10 |
|
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: 60.18 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 23 EAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRsltglrphqrvragIAYVPQGREIFPRLTVEENLlmgls 102
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--------------ISYKPQYISPDYDGTVEEFL----- 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 103 rfSARDARAVPDFIYE---LFPV-LREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:COG1245 423 --RSANTDDFGSSYYKteiIKPLgLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-221 |
1.93e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.23 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAgIAYV 81
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 82 PQGREIFPRLTVEENLLMG-------LSRFSARDARAVPDFIYElfPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRL 154
Cdd:PRK10253 87 AQNATTPGDITVQELVARGryphqplFTRWRKEDEEAVTKAMQA--TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600055 155 LILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGRGRDM 221
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-161 |
4.13e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFeAKVGEVTCLLGRNGVGKTTLLRCLMG-LVP---AREGQVAWE-------GrslTGLRP 70
Cdd:PRK13409 75 LEEEPVHRYGVNGFKLYGLPI-PKEGKVTGILGPNGIGKTTAVKILSGeLIPnlgDYEEEPSWDevlkrfrG---TELQN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 71 H-QRVRAG---IAYVPQGREIFPRL---TVEEnLLMGLsrfsarDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLA 143
Cdd:PRK13409 151 YfKKLYNGeikVVHKPQYVDLIPKVfkgKVRE-LLKKV------DERGKLDEVVERLG-LENILDRDISELSGGELQRVA 222
|
170
....*....|....*...
gi 15600055 144 IGRALASQPRLLILDEPT 161
Cdd:PRK13409 223 IAAALLRDADFYFFDEPT 240
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
13-160 |
4.17e-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: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 13 GSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRsltglrphqrvragIAYVPQGREIFPRlT 92
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600055 93 VEENLLMGLSRFSARDARAVPDFIYE----LFPVLREMKQRRGG-DLSGGQQQQLAIGRALASQPRLLILDEP 160
Cdd:cd03291 114 IKENIIFGVSYDEYRYKSVVKACQLEeditKFPEKDNTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSP 186
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-161 |
5.13e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.79 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQyyGGSHILRG--LSF--EAKVGevtcLLGRNGVGKTTLLRCLMGLVPAREGQvAWEGRSLTglrphqrvra 76
Cdd:TIGR03719 7 MNRVSKVVP--PKKEILKDisLSFfpGAKIG----VLGLNGAGKSTLLRIMAGVDKDFNGE-ARPQPGIK---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 77 gIAYVPQGREIFPRLTVEENLLMGLSrfSARDARAVPDFIYELF--------PVLREMK------QRRGG---------- 132
Cdd:TIGR03719 70 -VGYLPQEPQLDPTKTVRENVEEGVA--EIKDALDRFNEISAKYaepdadfdKLAAEQAelqeiiDAADAwdldsqleia 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600055 133 --------------DLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:TIGR03719 147 mdalrcppwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-216 |
7.08e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.40 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPA----REGQVAWEGRSLTGLRPHQRVRAGIAYVPqgREIF-PR 90
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIATIMQNP--RSAFnPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 91 LT-----VEENLLMGLSRFSARDARAV-------PDFIYELFPVlrEMkqrrggdlSGGQQQQLAIGRALASQPRLLILD 158
Cdd:PRK10418 96 HTmhthaRETCLALGKPADDATLTAALeavglenAARVLKLYPF--EM--------SGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 159 EPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQG 216
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQG 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-222 |
9.66e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.82 E-value: 9.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 25 KVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRVRAGIAYVPQGREIFPRLTVEENLLMGlsRF 104
Cdd:PRK10982 22 RPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSVMDNMWLG--RY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 105 SA-----------RDARAVPDFI-YELFPvlremkQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEI 172
Cdd:PRK10982 100 PTkgmfvdqdkmyRDTKAIFDELdIDIDP------RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600055 173 GAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMARGEIV--QQGRGRDME 222
Cdd:PRK10982 174 FTIIRKLKERG-CGIVYISHKMEEIFQLCDEITILRDGQWIatQPLAGLTMD 224
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-217 |
1.14e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 57.80 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSH--ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQrVRAGIA 79
Cdd:PRK10789 314 LDVNIRQFTYPQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS-WRSRLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 80 YVPQGREIFPRlTVEENLLMGLSRFSARD----AR--AVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPR 153
Cdd:PRK10789 393 VVSQTPFLFSD-TVANNIALGRPDATQQEiehvARlaSVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600055 154 LLILDEPTEGIQPSVIKEIgavVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEIVQQGR 217
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQI---LHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-169 |
1.91e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.63 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGlrpHQRVRAgIAYVPQGREIFPRLTVEE 95
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRF-MAYLGHLPGLKADLSTLE 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600055 96 NLLMgLSRFSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVI 169
Cdd:PRK13543 102 NLHF-LCGLHGRRAKQMPGSALAIVG-LAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGI 173
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-220 |
1.98e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVaWEGRSltglrphqrvragIAYVPQGREIFpRLTVEE 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERS-------------IAYVPQQAWIM-NATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 96 NLLMGLSRFSARDARAVPdfIYELFPVLREMKQ-------RRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSV 168
Cdd:PTZ00243 740 NILFFDEEDAARLADAVR--VSQLEADLAQLGGgleteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600055 169 IKEIGAVVRSLAARGDMAILLVEQFYDFAaeLADQYLVMARGEIVQQGRGRD 220
Cdd:PTZ00243 818 GERVVEECFLGALAGKTRVLATHQVHVVP--RADYVVALGDGRVEFSGSSAD 867
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-213 |
2.56e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.66 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPHQRV---RAGIAYVPQGREIFPRLT 92
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqlrREHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 93 VEEN-----LLMGLSRfSARDARAVpDFIYELFpvLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPS 167
Cdd:PRK10535 103 AAQNvevpaVYAGLER-KQRLLRAQ-ELLQRLG--LEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600055 168 VIKEIGAVVRSLAARGDMAIlLVEQFYDFAAElADQYLVMARGEIV 213
Cdd:PRK10535 179 SGEEVMAILHQLRDRGHTVI-IVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-216 |
3.53e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 55.74 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYY----------GGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLRPH 71
Cdd:PRK11308 6 LQAIDLKKHYpvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 72 QR--VRAGIAYV---PQGrEIFPRLTV----EENLLM--GLSRfSARDARAvpdfiyelfpvlREMKQRRGgdL------ 134
Cdd:PRK11308 86 AQklLRQKIQIVfqnPYG-SLNPRKKVgqilEEPLLIntSLSA-AERREKA------------LAMMAKVG--Lrpehyd 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 135 ------SGGQQQQLAIGRALASQPRLLILDEPTEGIQPSvikeIGAVVRSLAARgdmailLVEQF---YDFAAE------ 199
Cdd:PRK11308 150 ryphmfSGGQRQRIAIARALMLDPDVVVADEPVSALDVS----VQAQVLNLMMD------LQQELglsYVFISHdlsvve 219
|
250
....*....|....*...
gi 15600055 200 -LADQYLVMARGEIVQQG 216
Cdd:PRK11308 220 hIADEVMVMYLGRCVEKG 237
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
133-221 |
4.70e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.58 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 133 DLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLVMARGEI 212
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
....*....
gi 15600055 213 VQQGRGRDM 221
Cdd:PRK15093 238 VETAPSKEL 246
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-221 |
1.61e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLT--GLRphqRVRAGIAYVPQGREIFPRlTV 93
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGayGLR---ELRRQFSMIPQDPVLFDG-TV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 94 EENLLMGLSRFSARDARAVpdfiyELFPvLRE-----------MKQRRGGDLSGGQQQQLAIGRALASQPRLLIL-DEPT 161
Cdd:PTZ00243 1401 RQNVDPFLEASSAEVWAAL-----ELVG-LRErvasesegidsRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEAT 1474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 162 EGIQPSVIKEIGAVVRSlAARGDMAILLVEQFYDFAAelADQYLVMARGEIVQQGRGRDM 221
Cdd:PTZ00243 1475 ANIDPALDRQIQATVMS-AFSAYTVITIAHRLHTVAQ--YDKIIVMDHGAVAEMGSPREL 1531
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-161 |
1.72e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQyyGGSHILRG--LSF--EAKVGevtcLLGRNGVGKTTLLRCLMGLVPAREGqvawEGRSLTGLRphqrvra 76
Cdd:PRK11819 9 MNRVSKVVP--PKKQILKDisLSFfpGAKIG----VLGLNGAGKSTLLRIMAGVDKEFEG----EARPAPGIK------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 77 gIAYVPQGREIFPRLTVEENLLMGLSrfSARDARAVPDFIYELFP--------------VLREMKQRRGG---------- 132
Cdd:PRK11819 72 -VGYLPQEPQLDPEKTVRENVEEGVA--EVKAALDRFNEIYAAYAepdadfdalaaeqgELQEIIDAADAwdldsqleia 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600055 133 --------------DLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:PRK11819 149 mdalrcppwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-168 |
3.76e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.21 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 20 LSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQvawegrsLTGLRPHQrvragIAYVPQgREIFPRLTVEENLLM 99
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGR-------LTKPAKGK-----LFYVPQ-RPYMTLGTLRDQIIY 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 100 GLSRFSARDaRAVPDfiYELFPVLREMK-----QRRGG---------DLSGGQQQQLAIGRALASQPRLLILDEPTEGIQ 165
Cdd:TIGR00954 538 PDSSEDMKR-RGLSD--KDLEQILDNVQlthilEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
...
gi 15600055 166 PSV 168
Cdd:TIGR00954 615 VDV 617
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-161 |
4.33e-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: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGqvawegrsltglrphqRVRAG---- 77
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSG----------------TIEIGetvk 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 78 IAYVPQGRE-IFPRLTVEENLLMGLSRFSARDaRAVPDFIY-ELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLL 155
Cdd:TIGR03719 387 LAYVDQSRDaLDPNKTVWEEISGGLDIIKLGK-REIPSRAYvGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
....*.
gi 15600055 156 ILDEPT 161
Cdd:TIGR03719 466 LLDEPT 471
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-164 |
1.45e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLT--GLRPHQRVragIAYVPQGREIFP---R 90
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfGLTDLRRV---LSIIPQSPVLFSgtvR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 91 LTV----EEN---LLMGLSRFSARDARAVPDFiyelfpVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEG 163
Cdd:PLN03232 1328 FNIdpfsEHNdadLWEALERAHIKDVIDRNPF------GLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
.
gi 15600055 164 I 164
Cdd:PLN03232 1402 V 1402
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
129-226 |
1.96e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 129 RRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGdMAILLVEQFYDFAAELADQYLVMA 208
Cdd:PRK10938 131 RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSG-ITLVLVLNRFDEIPDFVQFAGVLA 209
|
90
....*....|....*...
gi 15600055 209 RGEIVQQGRGRDMESEGV 226
Cdd:PRK10938 210 DCTLAETGEREEILQQAL 227
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
2-191 |
6.81e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 48.90 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFeAKVGEVTCLLGRNGVGKTTLLRCLMG-LVP---AREGQVAWEG--RSLTGLRPH---Q 72
Cdd:cd03236 2 LEDEPVHRYGPNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKILAGkLKPnlgKFDDPPDWDEilDEFRGSELQnyfT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 73 RVRAG---IAYVPQGREIFPRL---TVEENLlmglsrfSARDARAVPDFIYELFPvLREMKQRRGGDLSGGQQQQLAIGR 146
Cdd:cd03236 81 KLLEGdvkVIVKPQYVDLIPKAvkgKVGELL-------KKKDERGKLDELVDQLE-LRHVLDRNIDQLSGGELQRVAIAA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600055 147 ALASQPRLLILDEPTEGIQpsvIKE---IGAVVRSLaARGDMAILLVE 191
Cdd:cd03236 153 ALARDADFYFFDEPSSYLD---IKQrlnAARLIREL-AEDDNYVLVVE 196
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
131-190 |
1.04e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 1.04e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 131 GGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILLV 190
Cdd:PTZ00265 1356 GKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1415
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-161 |
7.51e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 2 LQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGqvawegrsltglrphqRVRAG---- 77
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSG----------------TIKIGetvk 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 78 IAYVPQGRE-IFPRLTVEEN-------LLMG---------LSRFSARDaravPDfiyelfpvlremKQRRGGDLSGGQQQ 140
Cdd:PRK11819 389 LAYVDQSRDaLDPNKTVWEEisggldiIKVGnreipsrayVGRFNFKG----GD------------QQKKVGVLSGGERN 452
|
170 180
....*....|....*....|.
gi 15600055 141 QLAIGRALASQPRLLILDEPT 161
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPT 473
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
133-166 |
1.26e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.39 E-value: 1.26e-05
10 20 30
....*....|....*....|....*....|....
gi 15600055 133 DLSGGQQQQLAIGRALASQPRLLILDEPTEGIQP 166
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-161 |
2.18e-05 |
|
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: 43.13 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 27 GEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAwegrsltglrphqrvragiayvpqgreifprltveenllmglsRFSA 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI-------------------------------------------YIDG 38
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15600055 107 RDARAVPDFIYELFPVLremkqRRGGDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:smart00382 39 EDILEEVLDQLLLIIVG-----GKKASGSGELRLRLALALARKLKPDVLILDEIT 88
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
11-206 |
6.66e-05 |
|
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: 42.17 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 11 YGGSHILRGLSfEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSltglrphqrvragIAYVPQgreifpr 90
Cdd:cd03222 10 YGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT-------------PVYKPQ------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 91 ltveenllmglsrfsardaravpdFIyelfpvlremkqrrggDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIK 170
Cdd:cd03222 69 ------------------------YI----------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRL 108
|
170 180 190
....*....|....*....|....*....|....*.
gi 15600055 171 EIGAVVRSLAARGDMAILLVEQFYDFAAELADQYLV 206
Cdd:cd03222 109 NAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-213 |
1.22e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 42.38 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 17 LRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMG-LVPArEGQVawegrSLTGLRPHQRvRagIAYVpqgREI-------- 87
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVPT-SGEV-----RVLGYVPFKR-R--KEFA---RRIgvvfgqrs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 88 --FPRLTVEE--NLLMGLSRFSARDARAVPDFIYELFPVLREMKQ--RRggdLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:COG4586 106 qlWWDLPAIDsfRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTpvRQ---LSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600055 162 EGIQPSVIKEIGAVVRSLAARGDMAILL-------VEQfydfaaeLADQYLVMARGEIV 213
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYNRERGTTILLtshdmddIEA-------LCDRVIVIDHGRII 234
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
29-159 |
1.24e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.78 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 29 VTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGL-RPHqrvragIAYVPQGREIFPRLTVEENLLMGLSRFSAr 107
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIaKPY------CTYIGHNLGLKLEMTVFENLKFWSEIYNS- 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15600055 108 dARAVPDFIYelFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDE 159
Cdd:PRK13541 101 -AETLYAAIH--YFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-161 |
1.31e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 1 MLQVDKLHQYYGGSHILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEgrslTGLRphqrvragIAY 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA----KGIK--------LGY 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 81 VPQGREIFprLTVEENLLMGLSRFSARdaravpdfiyELFPVLREMKQRRG--GD--------LSGGQQQQLAIGRALAS 150
Cdd:PRK10636 380 FAQHQLEF--LRADESPLQHLARLAPQ----------ELEQKLRDYLGGFGfqGDkvteetrrFSGGEKARLVLALIVWQ 447
|
170
....*....|.
gi 15600055 151 QPRLLILDEPT 161
Cdd:PRK10636 448 RPNLLLLDEPT 458
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-164 |
1.68e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 1.68e-04
10 20 30
....*....|....*....|....*....|.
gi 15600055 134 LSGGQQQQLAIGRALASQPRLLILDEPTEGI 164
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
125-161 |
2.75e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 2.75e-04
10 20 30
....*....|....*....|....*....|....*..
gi 15600055 125 EMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPT 161
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPT 372
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
16-214 |
3.76e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 40.66 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 16 ILRGLSFEAKVGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLTGLrPHQRVRAGIAYVPQGREIFP---RLT 92
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL-PLHTLRSRLSIILQDPILFSgsiRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600055 93 VEENLLMGLSR-FSARDARAVPDFIYELFPVLREMKQRRGGDLSGGQQQQLAIGRALASQPRLLILDEPTEGIQPSVIKE 171
Cdd:cd03288 115 LDPECKCTDDRlWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600055 172 IGAVVrsLAARGDMAILLVEQFYDFAAElADQYLVMARGEIVQ 214
Cdd:cd03288 195 LQKVV--MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVE 234
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-66 |
5.01e-04 |
|
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: 40.55 E-value: 5.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 15600055 20 LSFEAkvGEVTCLLGRNGVGKTTLLRCLMGLVPAREGQVAWEGRSLT 66
Cdd:COG4615 353 LTIRR--GELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT 397
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-202 |
1.42e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 1.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600055 134 LSGGQQQQLAIGRALASQPR--LLILDEPTEGIQPSVIKEIGAVVRSLAARGDmAILLVE---QFYDFAAELAD 202
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEhdeQMISLADRIID 549
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-189 |
2.00e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 2.00e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600055 134 LSGGQQQQLAIGRALAS---QPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILL 189
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVII 868
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
134-189 |
2.34e-03 |
|
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: 37.69 E-value: 2.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 134 LSGGQQQQLAIGRALASQPR--LLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILL 189
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILI 145
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
134-188 |
2.67e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 37.98 E-value: 2.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600055 134 LSGGQQQQLAIGRAL---ASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAIL 188
Cdd:cd03271 170 LSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVV 227
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-189 |
6.16e-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: 37.30 E-value: 6.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600055 134 LSGGQQQQLAIGRAL---ASQPRLLILDEPTEGIQPSVIKEIGAVVRSLAARGDMAILL 189
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVI 888
|
|
| |
