|
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 |
8.38e-141 |
|
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: 393.04 E-value: 8.38e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAYV 81
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLLMGLSRFPARDaRAVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPT 161
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRS-RKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995501 162 EGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDMEAEGVRGMVTI 232
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLAV 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-223 |
4.59e-120 |
|
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: 340.81 E-value: 4.59e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAY 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMGL-SRFPARDARAVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAyARRDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995501 160 PTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDMEA 223
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRLNREG-VTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-224 |
4.70e-115 |
|
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: 327.85 E-value: 4.70e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAYV 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLLMGLSRFPARDARAVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPT 161
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995501 162 EGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDMEAE 224
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEG-VTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-216 |
9.43e-61 |
|
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: 190.34 E-value: 9.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAYV 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLLMGLSR------FPARDARAVPEEIYQLFPVLKTMK-----QRRGGDLSGGQQQQLAIGRALAS 150
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQArtgsglLLARARREEREARERAEELLERVGladlaDRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503995501 151 RPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-216 |
1.41e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 189.89 E-value: 1.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIthRKPHQRVQSGIAYV 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV--ARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLLM--GLSRFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:COG1131 79 PQEPALYPDLTVRENLRFfaRLYGLPRKEARERIDELLELFG-LTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503995501 160 PTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEG-KTVLLSTHYLEEAERLCDRVAIIDKGRIVADG 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-216 |
1.11e-59 |
|
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: 188.32 E-value: 1.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAY 80
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMG------------LSRFP--ARDARAVPEEIYQL--FPVLKTMKQRRGGDLSGGQQQQLAI 144
Cdd:COG0411 84 TFQNPRLFPELTVLENVLVAaharlgrgllaaLLRLPraRREEREARERAEELleRVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995501 145 GRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-227 |
4.90e-56 |
|
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: 178.51 E-value: 4.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPhqRVQSGIAY 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR--EARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENL-----LMGLSRfpaRDARAVPEEIYQLFPVLKTMKqRRGGDLSGGQQQQLAIGRALASRPQLL 155
Cdd:COG4555 79 LPDERGLYDRLTVRENIryfaeLYGLFD---EELKKRIEELIELLGLEEFLD-RRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995501 156 ILDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDMEAEGVR 227
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEG-KTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-216 |
4.56e-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: 174.08 E-value: 4.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSgIAY 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMG-------LSRFPARDARAVPEeiyqlfpVLKTM-----KQRRGGDLSGGQQQQLAIGRAL 148
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGryphlglFGRPSAEDREAVEE-------ALERTglehlADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 149 ASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQG 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-227 |
8.68e-54 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 172.76 E-value: 8.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAY 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMGlSRFPARDA-RAVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMG-GFFAERDQfQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 160 PTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDMEA-EGVR 227
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREQG-MTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAnEAVR 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-210 |
2.25e-52 |
|
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: 166.80 E-value: 2.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIthRKPHQRVQSGIAYV 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI--KKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLlmglsrfpardaravpeeiyqlfpvlktmkqrrggDLSGGQQQQLAIGRALASRPQLLILDEPT 161
Cdd:cd03230 79 PEEPSLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503995501 162 EGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRG 210
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEG-KTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
2.53e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 169.11 E-value: 2.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHqrvqsgIAY 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR------IGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREI---FPrLTVEENLLMGL-------SRFPARDARAVPEeiyqlfpVLKTM-----KQRRGGDLSGGQQQQLAIG 145
Cdd:COG1121 80 VPQRAEVdwdFP-ITVRDVVLMGRygrrglfRRPSRADREAVDE-------ALERVgledlADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503995501 146 RALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAI 212
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREG-KTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-216 |
1.57e-49 |
|
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: 161.15 E-value: 1.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvqsGIAYV 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLLMGL--SRFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLklRGVPKAEIRARVRELLELVG-LEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503995501 160 PTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-217 |
6.21e-48 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 157.88 E-value: 6.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAY 80
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMGL--SRFPARDARAVPEEIYQLFPVLKtMKQRRGGDLSGGQQQQLAIGRALASRPQLLILD 158
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAVLelRKLSKKEREERLEELLEEFGITH-LRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995501 159 EPTEGIQPSVIKEIGEVIRQLANRGdMAILL----VEQfydfAAGLADRYLVMSRGAIIQQGN 217
Cdd:COG1137 162 EPFAGVDPIAVADIQKIIRHLKERG-IGVLItdhnVRE----TLGICDRAYIISEGKVLAEGT 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-216 |
1.86e-47 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 156.69 E-value: 1.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPH-QRVQSGIA 79
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDiNKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 80 YVPQGREIFPRLTVEENLLMGLSR---FPARDARAVPEEIyqlfpvLKT--MKQRRG---GDLSGGQQQQLAIGRALASR 151
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKvkkMSKAEAEERAMEL------LERvgLADKADaypAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995501 152 PQLLILDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKEG-MTMVVVTHEMGFAREVADRVVFMDGGRIVEEG 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-227 |
1.53e-46 |
|
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: 153.85 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAYV 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLLMGLSRFPARDARAVP--EEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEklEELLEEFH-ITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 160 PTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDM-EAEGVR 227
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRG-IGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIaANELVR 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-216 |
1.64e-46 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 157.57 E-value: 1.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvqsGIAY 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR---NVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMGLS--RFPARDARAVPEEIYQLfpV-LKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLIL 157
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRmrGVPKAEIRARVAELLEL--VgLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995501 158 DEPTEGIQPSVIKEIGEVIRQLANRGDMAILLV-----EqfydfAAGLADRYLVMSRGAIIQQG 216
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLQRELGITFIYVthdqeE-----ALALADRIAVMNDGRIEQVG 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-217 |
2.39e-46 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 153.26 E-value: 2.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQL-HQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSgIAY 80
Cdd:COG1122 1 IELENLsFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQgreiFPRL-----TVEENLLMGLSRF--PARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQ 153
Cdd:COG1122 80 VFQ----NPDDqlfapTVEEDVAFGPENLglPREEIRERVEEALELVG-LEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995501 154 LLILDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGN 217
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-212 |
4.30e-46 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 152.30 E-value: 4.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPH-QRVQSGIAY 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMGLSRFPARDARAVPEEIYQLFPV--LKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKvgLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503995501 159 EPTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAI 212
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-212 |
6.75e-46 |
|
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: 151.92 E-value: 6.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 3 QVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVlwqeknITHRKPHQRVQSGIAYVP 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI------RVFGKPLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 83 QGREI---FPrLTVEENLLMGL-------SRFPARDARAVPEeiyqlfpVLKT-----MKQRRGGDLSGGQQQQLAIGRA 147
Cdd:cd03235 75 QRRSIdrdFP-ISVRDVVLMGLyghkglfRRLSKADKAKVDE-------ALERvglseLADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995501 148 LASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAI 212
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREG-MTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-188 |
1.60e-45 |
|
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: 150.71 E-value: 1.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQsgIAY 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR--LAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMGLSRFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEP 160
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVG-LAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180
....*....|....*....|....*...
gi 503995501 161 TEGIQPSVIKEIGEVIRQLANRGDMAIL 188
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
2.56e-45 |
|
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: 157.76 E-value: 2.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGS-----HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQR-- 73
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 74 VQSGIAYVPQG--REIFPRLTVEENLLMGLSRFPARDARAVPEEIYQLfpvLK------TMKQRRGGDLSGGQQQQLAIG 145
Cdd:COG1123 340 LRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAEL---LErvglppDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995501 146 RALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-213 |
5.97e-45 |
|
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: 148.94 E-value: 5.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 8 HQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNItHRKPHQRVqsgIAYVPQ--GR 85
Cdd:cd03226 7 FSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-KAKERRKS---IGYVMQdvDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 86 EIFpRLTVEENLLMGLSRFPARDARAvpEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQ 165
Cdd:cd03226 83 QLF-TDSVREELLLGLKELDAGNEQA--ETVLKDLD-LYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503995501 166 PSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAII 213
Cdd:cd03226 159 YKNMERVGELIRELAAQG-KAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-230 |
2.19e-43 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 152.48 E-value: 2.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAY 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMG--LSRFPARDARAVPEEIYQLfpvLKTMK-----QRRGGDLSGGQQQQLAIGRALASRPQ 153
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGrePRRGGLIDWRAMRRRAREL---LARLGldidpDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 154 LLILDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLV----EQFYDfaagLADRYLVMSRGAIIQQGNGGDM-EAEGVRG 228
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQG-VAIIYIshrlDEVFE----IADRVTVLRDGRLVGTGPVAELtEDELVRL 235
|
..
gi 503995501 229 MV 230
Cdd:COG1129 236 MV 237
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-210 |
2.50e-43 |
|
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: 143.87 E-value: 2.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIT-HRKPHQRVQSGIAY 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMGlsrfpardaravpeeiyqlfpvlktmkqrrggdLSGGQQQQLAIGRALASRPQLLILDEP 160
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG---------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503995501 161 TEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRG 210
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-213 |
2.82e-43 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 145.97 E-value: 2.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQL-HQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPH--QRVQSG 77
Cdd:COG3638 2 MLELRNLsKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRalRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 78 IAYVPQGREIFPRLTVEENLLMG-----------LSRFPardaravPEEIYQLFPVLKTMK-----QRRGGDLSGGQQQQ 141
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGrlgrtstwrslLGLFP-------PEDRERALEALERVGladkaYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995501 142 LAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAII 213
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-210 |
1.09e-42 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 143.38 E-value: 1.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 8 HQYYGGSH-ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSgIAYVPQgre 86
Cdd:cd03225 7 FSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGLVFQ--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 87 iFPR-----LTVEENLLMGLSRF--PARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:cd03225 83 -NPDdqffgPTVEEEVAFGLENLglPEEEIEERVEEALELVG-LEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503995501 160 PTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRG 210
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-216 |
1.20e-42 |
|
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: 143.80 E-value: 1.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGS----HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQS 76
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 77 G--IAYVPQ--GREIFPRLTVEENLLMGL-SRFPARDARAVPEEIYQLFPVL---KTMKQRRGGDLSGGQQQQLAIGRAL 148
Cdd:cd03257 81 RkeIQMVFQdpMSSLNPRMTIGEQIAEPLrIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 149 ASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 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 |
1.86e-42 |
|
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: 141.80 E-value: 1.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 3 QVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSgIAYVP 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 83 QGREifprltveenlLMGLSRFpardaravpeeiyqlfpvlktmKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTE 162
Cdd:cd03214 80 QALE-----------LLGLAHL----------------------ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503995501 163 GIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-223 |
2.20e-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: 143.79 E-value: 2.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYG----GSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKP---HQR 73
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkafRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 74 VQsgiaYVPQ-GREIF-PRLTVEENLL--MGLSRFPARDARAvpEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALA 149
Cdd:COG1124 81 VQ----MVFQdPYASLhPRHTVDRILAepLRIHGLPDREERI--AELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995501 150 SRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDMEA 223
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-212 |
3.32e-42 |
|
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: 141.42 E-value: 3.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHqyygGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAY 80
Cdd:cd03215 4 VLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGRE---IFPRLTVEENLLMGLSrfpardaravpeeiyqlfpvlktmkqrrggdLSGGQQQQLAIGRALASRPQLLIL 157
Cdd:cd03215 80 VPEDRKregLVLDLSVAENIALSSL-------------------------------LSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503995501 158 DEPTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAI 212
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAG-KAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
2.09e-41 |
|
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: 147.36 E-value: 2.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYY--GGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPAR---SGEVLWQEKNITHRKPHQRVQ 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 76 SgIAYVPQGREI-FPRLTVEENLLMGL--SRFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRP 152
Cdd:COG1123 84 R-IGMVFQDPMTqLNPVTVGDQIAEALenLGLSRAEARARVLELLEAVG-LERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995501 153 QLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-216 |
8.17e-41 |
|
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: 139.56 E-value: 8.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQ----RVQSG 77
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 78 IAYvpQGREIFPRLTVEENLLMGL---SRFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQL 154
Cdd:cd03261 81 MLF--QSGALFDSLTVFENVAFPLrehTRLSEEEIREIVLEKLEAVG-LRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995501 155 LILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-216 |
1.54e-40 |
|
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: 138.02 E-value: 1.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGS--HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNI-THRKphqRVQSGI 78
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRK---AARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 79 AYVPQGREIFPRLTVEENL-----LMGLSRFPARDARAVPEEIYQLFPVLKtmkqRRGGDLSGGQQQQLAIGRALASRPQ 153
Cdd:cd03263 78 GYCPQFDALFDELTVREHLrfyarLKGLPKSEIKEEVELLLRVLGLTDKAN----KRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995501 154 LLILDEPTEGIQPSVIKEIGEVIRQLanRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-213 |
2.10e-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: 138.47 E-value: 2.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGS-HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPH--QRVQSGI 78
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 79 AYVPQGREIFPRLTVEENLLMG-----------LSRFPardaravPEEIYQLFPVLKT-----MKQRRGGDLSGGQQQQL 142
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrstwrslFGLFP-------KEEKQRALAALERvglldKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995501 143 AIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAII 213
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-216 |
3.92e-40 |
|
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: 136.96 E-value: 3.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITH-RKPHQRVQSGIAY 80
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKnIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 vPqgrEIFPRLTVEENLLMGlsrfpARDARAVPEEIYQLFPV--LKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILD 158
Cdd:cd03268 81 -P---GFYPNLTARENLRLL-----ARLLGIRKKRIDEVLDVvgLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995501 159 EPTEGIQPSVIKEIGEVIRQLANRGdMAILL-------VEQfydfaagLADRYLVMSRGAIIQQG 216
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQG-ITVLIsshllseIQK-------VADRIGIINKGKLIEEG 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-161 |
1.51e-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: 133.54 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIThRKPHQRVQSGIAYVPQGREIFPRLTVEEN 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-DDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995501 97 LLMGLsRFPARDARAVPEEIYQ------LFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPT 161
Cdd:pfam00005 80 LRLGL-LLKGLSKREKDARAEEaleklgLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-216 |
1.80e-39 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 138.74 E-value: 1.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNI-THRKPHQRvqsGIAY 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRER---RVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMGLS--RFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILD 158
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRvrPPSKAEIRARVEELLELVQ-LEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995501 159 EPTEGIQPSVIKEIGEVIRQLANRGDMAILLV-----EqfydfAAGLADRYLVMSRGAIIQQG 216
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVthdqeE-----ALELADRVVVMNQGRIEQVG 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-215 |
1.88e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 135.56 E-value: 1.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGS----HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQ- 75
Cdd:COG1136 4 LLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 76 --SGIAYVPQGREIFPRLTVEENLLMGL--SRFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASR 151
Cdd:COG1136 84 rrRHIGFVFQFFNLLPELTALENVALPLllAGVSRKERRERARELLERVG-LGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995501 152 PQLLILDEPT------EGiqpsviKEIGEVIRQLANRGDMAILLV--EQfydFAAGLADRYLVMSRGAIIQQ 215
Cdd:COG1136 163 PKLILADEPTgnldskTG------EEVLELLRELNRELGTTIVMVthDP---ELAARADRVIRLRDGRIVSD 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-212 |
2.29e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 134.94 E-value: 2.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQ-RVQsgIAY 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwRRQ--VAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQgrEifPRL---TVEENLLMGlsrFPARDARAVPEEIYQLFPVL---KTMKQRRGGDLSGGQQQQLAIGRALASRPQL 154
Cdd:COG4619 79 VPQ--E--PALwggTVRDNLPFP---FQLRERKFDRERALELLERLglpPDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995501 155 LILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLV----EQfydfAAGLADRYLVMSRGAI 212
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVshdpEQ----IERVADRVLTLEAGRL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-210 |
2.31e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 133.14 E-value: 2.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 3 QVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQrVQSGIAYVP 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE-LRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 83 QgreifprltveenllmglsrfpardaravpeeiyqlfpvlktmkqrrggdLSGGQQQQLAIGRALASRPQLLILDEPTE 162
Cdd:cd00267 80 Q--------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503995501 163 GIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRG 210
Cdd:cd00267 110 GLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
2.37e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 136.37 E-value: 2.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYY----GGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHqrvqs 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 77 gIAYVPQGREIFPRLTVEENLLMGL--SRFPARDARAVPEEIYQLfpV-LKTMKQRRGGDLSGGQQQQLAIGRALASRPQ 153
Cdd:COG1116 82 -RGVVFQEPALLPWLTVLDNVALGLelRGVPKAERRERARELLEL--VgLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 154 LLILDEP-------T-EGIQpsvikeigEVIRQLANRGDMAILLV-----EqfydfAAGLADRYLVMSRG 210
Cdd:COG1116 159 VLLMDEPfgaldalTrERLQ--------DELLRLWQETGKTVLFVthdvdE-----AVFLADRVVVLSAR 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-217 |
2.62e-39 |
|
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: 135.49 E-value: 2.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQR--VQSGI 78
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyeLRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 79 AYVPQGREIFPRLTVEENLLMGL---SRFPARDARAVPEE---------IYQLFPvlktmkqrrgGDLSGGQQQQLAIGR 146
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLrehTDLSEAEIRELVLEklelvglpgAADKMP----------SELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995501 147 ALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGN 217
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-226 |
4.02e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 140.92 E-value: 4.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLhqyyGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAY 80
Cdd:COG1129 256 VLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VP-----QGreIFPRLTVEENLLMG----LSRF----PARDARAVPEEIYQL--------FPVlktmkqrrgGDLSGGQQ 139
Cdd:COG1129 332 VPedrkgEG--LVLDLSIRENITLAsldrLSRGglldRRRERALAEEYIKRLriktpspeQPV---------GNLSGGNQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 140 QQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLV-----EqfydfAAGLADRYLVMSRGAIIQ 214
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEG-KAVIVIsselpE-----LLGLSDRILVMREGRIVG 474
|
250
....*....|..
gi 503995501 215 QGNGGDMEAEGV 226
Cdd:COG1129 475 ELDREEATEEAI 486
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-216 |
5.62e-39 |
|
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: 137.92 E-value: 5.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYygGSHILRgVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSG------EVLWQEKNITHRKPHQRv 74
Cdd:COG4148 2 MLEVDFRLRR--GGFTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGrirlggEVLQDSARGIFLPPHRR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 75 qsGIAYVPQGREIFPRLTVEENLLMGLSRFPARDARAVPEEIYQLF---PVLKtmkqRRGGDLSGGQQQQLAIGRALASR 151
Cdd:COG4148 78 --RIGYVFQEARLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLgigHLLD----RRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995501 152 PQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASG 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-216 |
8.24e-39 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 137.13 E-value: 8.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvqsGIAY 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR---NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMGL--SRFPARD-ARAVPE--EIYQLFPVLKtmkqRRGGDLSGGQQQQLAIGRALASRPQLL 155
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLklRKVPKAEiDRRVREaaELLGLEDLLD----RKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 156 ILDEP-------------TEgiqpsvikeigevIRQLANRGDMAILLV-----EqfydfAAGLADRYLVMSRGAIIQQG 216
Cdd:COG3839 156 LLDEPlsnldaklrvemrAE-------------IKRLHRRLGTTTIYVthdqvE-----AMTLADRIAVMNDGRIQQVG 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
17-217 |
1.06e-38 |
|
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: 134.00 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvqsGIAYVPQGREIFPRLTVEEN 96
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---DISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 97 LLMGLsRFPARDARAVPEEIYQLFPVLKT--MKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEG----IQPSVIK 170
Cdd:cd03299 92 IAYGL-KKRKVDKKEIERKVLEIAEMLGIdhLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAldvrTKEKLRE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503995501 171 EIGEVIRQLanrgDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGN 217
Cdd:cd03299 171 ELKKIRKEF----GVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGK 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-213 |
1.33e-38 |
|
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: 131.40 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAYV 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQgreifprltveenllmglsrfpardaravpeeiyqlfpvlktmkqrrggdLSGGQQQQLAIGRALASRPQLLILDEPT 161
Cdd:cd03216 81 YQ--------------------------------------------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503995501 162 EGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAII 213
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-221 |
2.84e-38 |
|
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: 132.49 E-value: 2.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIThRKPhQRVQSGIAYV 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV-REP-REVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLLM--GLSRFPARDARAVPEEIYQLFPVLKtMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:cd03265 79 FQDLSVDDELTGWENLYIhaRLYGVPGAERRERIDELLDFVGLLE-AADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995501 160 PTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDM 221
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
6.34e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 133.70 E-value: 6.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQrvqsgIAY 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR-----IGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENL-----LMGLSRfpaRDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLL 155
Cdd:COG4152 76 LPEERGLYPKMKVGEQLvylarLKGLSK---AEAKRRADEWLERLG-LGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995501 156 ILDEPTEGIQP---SVIKeigEVIRQLANRGdMAIL-------LVEQfydfaagLADRYLVMSRGAIIQQGN 217
Cdd:COG4152 152 ILDEPFSGLDPvnvELLK---DVIRELAAKG-TTVIfsshqmeLVEE-------LCDRIVIINKGRKVLSGS 212
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-216 |
7.03e-38 |
|
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: 134.78 E-value: 7.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvQSGIayV 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKR-DYGI--V 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLLMGLS--RFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKnrGMGRAEVAERVAELLDLVG-LPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503995501 160 PTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVG 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-216 |
9.57e-38 |
|
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: 130.95 E-value: 9.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYY----GGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNiTHRKPhQRVQS 76
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD-VVKEP-AEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 77 GIAYVPQGREIFPRLTVEENL-----LMGLSRfpaRDARAVPEEIYQLFPVLKTMkQRRGGDLSGGQQQQLAIGRALASR 151
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLeyfagLYGLKG---DELTARLEELADRLGMEELL-DRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995501 152 PQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDmAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-220 |
1.17e-36 |
|
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: 129.00 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvqsGIAYV 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLLMGL------SRFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLL 155
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLrvkprsERPPEAEIRAKVHELLKLVQ-LDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995501 156 ILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGD 220
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-212 |
1.42e-36 |
|
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: 127.99 E-value: 1.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGG----SHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQ-- 75
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 76 -SGIAYVPQGREIFPRLTVEENLLMGL--SRFPARDARAVPEEIYQLFPVLKTMKqRRGGDLSGGQQQQLAIGRALASRP 152
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLllAGVPKKERRERAEELLERVGLGDRLN-HYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995501 153 QLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLV---EQFydfaAGLADRYLVMSRGAI 212
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVthdPEL----AEYADRIIELRDGKI 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
11-220 |
1.79e-35 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 125.43 E-value: 1.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 11 YGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvqsGIAYVPQGREIFPR 90
Cdd:cd03300 10 YGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---PVNTVFQNYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 91 LTVEENLLMGLS--RFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSV 168
Cdd:cd03300 87 LTVFENIAFGLRlkKLPKAEIKERVAEALDLVQ-LEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503995501 169 IKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGD 220
Cdd:cd03300 166 RKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-216 |
3.04e-35 |
|
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: 124.60 E-value: 3.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLI----PAR-SGEVLWQEKNITHRKPH-QRVQ 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipGAPdEGEVLLDGKDIYDLDVDvLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 76 SGIAYVPQGREIFPrLTVEENLLMGLSRFPARDARAVPEEIYQlfpVLKTM------KQR-RGGDLSGGQQQQLAIGRAL 148
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEE---ALRKAalwdevKDRlHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995501 149 ASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANrgDMAILLV----EQfydfAAGLADRYLVMSRGAIIQQG 216
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVthnmQQ----AARVADRTAFLLNGRLVEFG 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-213 |
4.31e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 130.15 E-value: 4.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAY 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMGL--SRFPARDARAVPEEIYQLfpvlktMKQ--------RRGGDLSGGQQQQLAIGRALAS 150
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGLepTKGGRLDRKAARARIREL------SERygldvdpdAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 151 RPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLV-----EqfydfAAGLADRYLVMSRGAII 213
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEG-KSIIFIthklrE-----VMAIADRVTVLRRGKVV 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-215 |
5.61e-35 |
|
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: 123.74 E-value: 5.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGS----HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHqrvqsg 77
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 78 IAYVPQGREIFPRLTVEENLLMGLS--RFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLL 155
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLElqGVPKAEARERAEELLELVG-LSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 156 ILDEP-------TEGiqpsvikEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSR--GAIIQQ 215
Cdd:cd03293 154 LLDEPfsaldalTRE-------QLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-216 |
1.02e-34 |
|
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: 123.95 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYG-GSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPH--QRVQSG 77
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 78 IAYVPQGREIFPRLTVEENLLMG-----------LSRFPARDARavpEEIYQLFPV-LKTMKQRRGGDLSGGQQQQLAIG 145
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGrlgykptwrslLGRFSEEDKE---RALSALERVgLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995501 146 RALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDG 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-217 |
1.79e-34 |
|
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: 129.11 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLH-QYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvQSGIAY 80
Cdd:COG4988 337 IELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW-RRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPrLTVEENLLMGLSRFP-------ARDARAvPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQ 153
Cdd:COG4988 416 VPQNPYLFA-GTIRENLRLGRPDASdeeleaaLEAAGL-DEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 154 LLILDEPTEGIQPSVIKEIGEVIRQLAnRGDMAIL------LVEQfydfaaglADRYLVMSRGAIIQQGN 217
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILithrlaLLAQ--------ADRILVLDDGRIVEQGT 554
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-216 |
2.03e-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: 122.40 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 27 GEITCLLGRNGVGKTTLLKCLMGLIPARSGEV-----LWQ--EKNItHRKPHQRvqsGIAYVPQGREIFPRLTVEENLLM 99
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtVLFdsRKKI-NLPPQQR---KIGLVFQQYALFPHLNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 100 GLSRFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQL 179
Cdd:cd03297 99 GLKRKRNREDRISVDELLDLLG-LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 503995501 180 ANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:cd03297 178 KKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-216 |
2.48e-34 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 123.18 E-value: 2.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAY 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLM------------GLSRFPA---RDARAVPEEIYQLFPV-LKTMKQRRGGDLSGGQQQQLAI 144
Cdd:PRK11300 85 TFQHVRLFREMTVIENLLVaqhqqlktglfsGLLKTPAfrrAESEALDRAATWLERVgLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995501 145 GRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-216 |
4.94e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 121.79 E-value: 4.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGsHILRgVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvqsGIAY 80
Cdd:COG3840 1 MLRLDDLTYRYGD-FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER---PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMGLS---RFPARDARAVPEEIYQLfpVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLIL 157
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLGLRpglKLTAEQRAQVEQALERV--GLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 158 DEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADG 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-216 |
1.09e-33 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 120.08 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQrvqsgIAYV 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR-----IGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENL-----LMGLSRfpaRDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLI 156
Cdd:cd03269 76 PEERGLYPKMKVIDQLvylaqLKGLKK---EEARRRIDEWLERLE-LSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 157 LDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAG-KTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-226 |
1.60e-33 |
|
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: 123.30 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 20 VDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGE-----VLWQEKnithRK-----PHQRvqsGIAYVPQGREIFP 89
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEivlngRTLFDS----RKgiflpPEKR---RIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 90 RLTVEENLLMGLSRFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVI 169
Cdd:TIGR02142 89 HLSVRGNLRYGMKRARPSERRISFERVIELLG-IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503995501 170 KEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDMEAEGV 226
Cdd:TIGR02142 168 YEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-217 |
2.67e-32 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 123.79 E-value: 2.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 11 YGGSH--ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSgIAYVPQGREIF 88
Cdd:COG2274 483 YPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ-IGVVLQDVFLF 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 89 PRlTVEENLLMGLSRFP-------ARDArAVPEEIYQLfPV-LKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEP 160
Cdd:COG2274 562 SG-TIRENITLGDPDATdeeiieaARLA-GLHDFIEAL-PMgYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEA 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995501 161 TEGIQPSVIKEIGEVIRQLAnrGDMAILLVeqfydfA-----AGLADRYLVMSRGAIIQQGN 217
Cdd:COG2274 639 TSALDAETEAIILENLRRLL--KGRTVIII------AhrlstIRLADRIIVLDKGRIVEDGT 692
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-216 |
4.41e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.57 E-value: 4.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSgIAY 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR-RAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREI-FPrLTVEENLLMGLS--RFPARDARAVPEEIYQLFPVLKtMKQRRGGDLSGGQQQQLAIGRALA------SR 151
Cdd:PRK13548 81 LPQHSSLsFP-FTVEEVVAMGRAphGLSRAEDDALVAAALAQVDLAH-LAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995501 152 PQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-221 |
9.31e-32 |
|
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: 116.25 E-value: 9.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 9 QYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPhQRVQSGIAYVPQGREIF 88
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP-VELRRKIGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 89 PRLTVEENL-----LMGLSRfPARDARAvpeeiYQLFPVL----KTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:cd03295 88 PHMTVEENIalvpkLLKWPK-EKIRERA-----DELLALVgldpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995501 160 PTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDM 221
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-216 |
1.06e-31 |
|
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: 117.85 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYY----GGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPAR---SGEVLWQEKNITHRKPHQR 73
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 74 VQ---SGIAYVPQgrEIF----PRLTVEENLLMGLSRF-----PARDARAV----------PEEIYQLFPvlktmkqrrg 131
Cdd:COG0444 81 RKirgREIQMIFQ--DPMtslnPVMTVGDQIAEPLRIHgglskAEARERAIellervglpdPERRLDRYP---------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 132 GDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQfyDFA--AGLADRYLVMSR 209
Cdd:COG0444 149 HELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITH--DLGvvAEIADRVAVMYA 226
|
....*..
gi 503995501 210 GAIIQQG 216
Cdd:COG0444 227 GRIVEEG 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-213 |
1.36e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 120.52 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 12 GGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAYVP---QGREIF 88
Cdd:COG3845 269 RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAYIPedrLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 89 PRLTVEENLLMGLSRFPA---------RDARAVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:COG3845 349 PDMSVAENLILGRYRRPPfsrggfldrKAIRAFAEELIEEFDVRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503995501 160 PTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAII 213
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLELRDAG-AAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-216 |
1.45e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 117.21 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIayV 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV--V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLLMgLSRFPARDARAVPEEIYQL--FPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLV-FGRYFGLSAAAARALVPPLleFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503995501 160 PTEGIQPSVIKEIGEVIRQLANRGDmAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-217 |
5.46e-31 |
|
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: 114.31 E-value: 5.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCL--MG-LIPAR--SGEVLWQEKNITHRK---PHQR 73
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrMNdLVPGVriEGKVLFDGQDIYDKKidvVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 74 VQSGIayVPQGREIFPrLTVEENLLMGLSRFPARDaRAVPEEIYQ-------LFPVLKTMKQRRGGDLSGGQQQQLAIGR 146
Cdd:TIGR00972 82 RRVGM--VFQKPNPFP-MSIYDNIAYGPRLHGIKD-KKELDEIVEeslkkaaLWDEVKDRLHDSALGLSGGQQQRLCIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995501 147 ALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLanRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGN 217
Cdd:TIGR00972 158 ALAVEPEVLLLDEPTSALDPIATGKIEELIQEL--KKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGP 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-212 |
6.04e-31 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 118.57 E-value: 6.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLhqyyGGSHIlRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAYV 81
Cdd:PRK10762 258 LKVDNL----SGPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGRE---IFPRLTVEENL----LMGLSRFPAR----DARAVPEEIYQLFPVlKT--MKQRRGgDLSGGQQQQLAIGRAL 148
Cdd:PRK10762 333 SEDRKrdgLVLGMSVKENMsltaLRYFSRAGGSlkhaDEQQAVSDFIRLFNI-KTpsMEQAIG-LLSGGNQQKVAIARGL 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995501 149 ASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAI 212
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEG-LSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-216 |
6.23e-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: 113.12 E-value: 6.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvqsGIAYV 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLlmglsRFPARDARAVPEEIYQ-LFPVLKTMK-----QRRGGDLSGGQQQQLAIGRALASRPQLL 155
Cdd:cd03301 78 FQNYALYPHMTVYDNI-----AFGLKLRKVPKDEIDErVREVAELLQiehllDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995501 156 ILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-217 |
7.86e-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: 7.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGE--VLWQEKNITHRKPHQRVQS--- 76
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQlnIAGHQFDFSQKPSEKAIRLlrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 77 GIAYVPQGREIFPRLTVEENLL------MGLSRFPARD------ARAVPEEIYQLFPVLktmkqrrggdLSGGQQQQLAI 144
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIeapckvLGLSKEQAREkamkllARLRLTDKADRFPLH----------LSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995501 145 GRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAIlLVEQFYDFAAGLADRYLVMSRGAIIQQGN 217
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQV-IVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-221 |
9.06e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 113.65 E-value: 9.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVL--WQEKNITHRKPHQ-RVQSG 77
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdGLKVNDPKVDERLiRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 78 IayVPQGREIFPRLTVEENLLMGlsrfPARDARAVPEEIYQLFPVLKT---MKQRRG---GDLSGGQQQQLAIGRALASR 151
Cdd:PRK09493 81 M--VFQQFYLFPHLTALENVMFG----PLRVRGASKEEAEKQARELLAkvgLAERAHhypSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 152 PQLLILDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDM 221
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-216 |
2.53e-30 |
|
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: 111.52 E-value: 2.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGeITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKphQRVQSGIAYV 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP--QKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENL--LMGLSRFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:cd03264 78 PQEFGVYPNFTVREFLdyIAWLKGIPSKEVKARVDEVLELVN-LGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995501 160 PTEGIQP-------SVIKEIGEvirqlanrgDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:cd03264 157 PTAGLDPeerirfrNLLSELGE---------DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-224 |
2.88e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 112.29 E-value: 2.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAYV 81
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLLMGLS-----RFPARDARAvpEEIYQLFPVlKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLI 156
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQirddlSAEQREDRA--NELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 157 LDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDMEAE 224
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSG-LGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-216 |
3.48e-30 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 112.15 E-value: 3.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGI-- 78
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 79 -----AYVPQGREIFPRLTVEENLLMG---LSRFPARDARAVPEEIyqLFPVLKTMKQ----RRggdLSGGQQQQLAIGR 146
Cdd:PRK11264 83 lrqhvGFVFQNFNLFPHRTVLENIIEGpviVKGEPKEEATARAREL--LAKVGLAGKEtsypRR---LSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995501 147 ALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLAN-RGDMAILLVEQfyDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEM--SFARDVADRAIFMDQGRIVEQG 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-216 |
6.05e-30 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 111.13 E-value: 6.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGS----HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRV-- 74
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 75 QSGIAYVPQGREIFPRLTVEENL-----LMGLSRfpardaRAVPEEIYQLFPV--LKTMKQRRGGDLSGGQQQQLAIGRA 147
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENValpleIAGVPK------AEIEERVLELLELvgLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 148 LASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEG 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-212 |
8.51e-30 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 115.41 E-value: 8.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 20 VDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARS-GEVLWQEKNITHRKPHQRVQSGIAYVPQGRE---IFPRLTVEE 95
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKrdgIVPVMGVGK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 96 NL-LMGLSRFP-------ARDARAVPEEIYQLfpVLKTMKQR-RGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQP 166
Cdd:PRK13549 361 NItLAALDRFTggsriddAAELKTILESIQRL--KVKTASPElAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503995501 167 SVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAI 212
Cdd:PRK13549 439 GAKYEIYKLINQLVQQG-VAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-219 |
8.78e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 110.53 E-value: 8.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSH-ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQ----RVQ 75
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 76 SGIayVPQGREIFPRLTVEENLLMGL--SRFPARDARAVPEEIYQLfpV-LKTMKQRRGGDLSGGQQQQLAIGRALASRP 152
Cdd:COG2884 81 IGV--VFQDFRLLPDRTVYENVALPLrvTGKSRKEIRRRVREVLDL--VgLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995501 153 QLLILDEPTEGIQPSVIKEIGEVIRQLANRGdMAIL-------LVEQFydfaaglADRYLVMSRGAIIQQGNGG 219
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRG-TTVLiathdleLVDRM-------PKRVLELEDGRLVRDEARG 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-216 |
1.52e-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: 115.25 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLH-QYYGGSH-ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRkPHQRVQSGIA 79
Cdd:COG4987 334 LELEDVSfRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDL-DEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 80 YVPQGREIFpRLTVEENLLMGlsrfparDARAVPEEIYQ------LFPVLKTMKQR-------RGGDLSGGQQQQLAIGR 146
Cdd:COG4987 413 VVPQRPHLF-DTTLRENLRLA-------RPDATDEELWAalervgLGDWLAALPDGldtwlgeGGRRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995501 147 ALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLAnrGDMAILLV---EQfydfAAGLADRYLVMSRGAIIQQG 216
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEAL--AGRTVLLIthrLA----GLERMDRILVLEDGRIVEQG 551
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-216 |
1.97e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 114.76 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAY 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMGLSRfPARDARAVPEEIYQLFPVLKTMKQrrGGDLSGGQQQQLAIGRALASRPQLLILDEP 160
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPK-RQASMQKMKQLLAALGCQLDLDSS--AGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503995501 161 TEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQG-VGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-216 |
1.99e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 112.23 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 11 YGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIayVPQGREIFPR 90
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGV--VPQFDNLDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 91 LTVEENLLMgLSRFPARDARAVPEEIYQL--FPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSV 168
Cdd:PRK13536 129 FTVRENLLV-FGRYFGMSTREIEAVIPSLleFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503995501 169 IKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK13536 208 RHLIWERLRSLLARG-KTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-210 |
3.23e-29 |
|
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: 107.47 E-value: 3.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 11 YGGSH--ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSgIAYVPQGREIF 88
Cdd:cd03228 10 YPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IAYVPQDPFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 89 PRlTVEENLLmglsrfpardaravpeeiyqlfpvlktmkqrrggdlSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSV 168
Cdd:cd03228 89 SG-TIRENIL------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503995501 169 IKEIGEVIRQLanRGDMAILLVeqfydfA-----AGLADRYLVMSRG 210
Cdd:cd03228 132 EALILEALRAL--AKGKTVIVI------AhrlstIRDADRIIVLDDG 170
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-183 |
7.82e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 106.93 E-value: 7.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 11 YGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVlwqeknitHRKPHQRVqsgiAYVPQGREI--- 87
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV--------RRAGGARV----AYVPQRSEVpds 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 88 FPrLTVEENLLMG------LSRFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPT 161
Cdd:NF040873 70 LP-LTVRDLVAMGrwarrgLWRRLTRDDRAAVDDALERVG-LADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180
....*....|....*....|..
gi 503995501 162 EGIQPSVIKEIGEVIRQLANRG 183
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARG 169
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-216 |
8.13e-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: 107.25 E-value: 8.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLI--PARSGEVLWQEKNITHRKPHQRvqsgIAYVPQGREIFPRLTV 93
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGRPLDKRSFRKI----IGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 94 EENLlmglsRFPArdaravpeeiyqlfpvlktmkQRRGgdLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIG 173
Cdd:cd03213 100 RETL-----MFAA---------------------KLRG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503995501 174 EVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:cd03213 152 SLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-216 |
8.34e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 108.56 E-value: 8.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLW-----------QEKNIthRKP 70
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsktpSDKAI--REL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 71 HQRVqsgiAYVPQGREIFPRLTVEENLL------MGLSRFPARdARAvpEEIyqlfpvLKTMKQRRGGD-----LSGGQQ 139
Cdd:PRK11124 81 RRNV----GMVFQQYNLWPHLTVQQNLIeapcrvLGLSKDQAL-ARA--EKL------LERLRLKPYADrfplhLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503995501 140 QQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETG-ITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
10-217 |
1.09e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 112.95 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 10 YYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQrVQSGIAYVPQGREIFP 89
Cdd:COG1132 349 YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES-LRRQIGVVPQDTFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 90 RlTVEENLLMGlsrfparDARAVPEEIY------QLFPVLKTMKQ-------RRGGDLSGGQQQQLAIGRALASRPQLLI 156
Cdd:COG1132 428 G-TIRENIRYG-------RPDATDEEVEeaakaaQAHEFIEALPDgydtvvgERGVNLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 157 LDEPTEGIQPSVIKEIGEVIRQLanRGDMAILL-------VEQfydfaaglADRYLVMSRGAIIQQGN 217
Cdd:COG1132 500 LDEATSALDTETEALIQEALERL--MKGRTTIViahrlstIRN--------ADRILVLDDGRIVEQGT 557
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-216 |
1.46e-28 |
|
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: 107.36 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIP---ARSGEVLWQEKnitHRKPHQrVQSGIAYVPQGREIFPRLT 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQ---PRKPDQ-FQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 93 VEENLL-MGLSRFPARDARAVPEEIYQLFPVLKTMKQRRGGD----LSGGQQQQLAIGRALASRPQLLILDEPTEGIQPS 167
Cdd:cd03234 98 VRETLTyTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503995501 168 VIKEIGEVIRQLANRGDMAILLVEQ-----FYDFaaglaDRYLVMSRGAIIQQG 216
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILTIHQprsdlFRLF-----DRILLLSSGEIVYSG 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-216 |
2.22e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.79 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvqsGIAYV 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR---KVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLLMGLSRFPAR---DARAVPEEIYQLFPV--LKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLI 156
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGLTVLPRRerpNAAAIKAKVTQLLEMvqLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 157 LDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-216 |
3.15e-28 |
|
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: 108.74 E-value: 3.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 32 LLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvqsGIAYVPQGREIFPRLTVEENLLMGLS--RFPARDA 109
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLR---HINMVFQSYALFPHMTVEENVAFGLKmrKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 110 RAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILL 189
Cdd:TIGR01187 78 KPRVLEALRLVQ-LEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180
....*....|....*....|....*..
gi 503995501 190 VEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIG 183
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-212 |
3.26e-28 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 111.30 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 18 RGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAYVPQGRE---IFPRLTVE 94
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQssgLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 95 ENL------LMGLSRFPARDaRAVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSV 168
Cdd:PRK15439 360 WNVcalthnRRGFWIKPARE-NAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503995501 169 IKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAI 212
Cdd:PRK15439 439 RNDIYQLIRSIAAQN-VAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-216 |
4.34e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 109.54 E-value: 4.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvqsGIAY 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQR---PINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMGLS--RFPARDARAVPEEIYQLFPVLKTMKqRRGGDLSGGQQQQLAIGRALASRPQLLILD 158
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGLKqdKLPKAEIASRVNEMLGLVHMQEFAK-RKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 159 EPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-221 |
5.08e-28 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 106.81 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIT-------HRKPH-- 71
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgELVPAdr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 72 ---QRVQSGIAYVPQGREIFPRLTVEENLL------MGLSRFPARD-ARAVPEEIyqlfpvlkTMKQRRG---GDLSGGQ 138
Cdd:COG4598 88 rqlQRIRTRLGMVFQSFNLWSHMTVLENVIeapvhvLGRPKAEAIErAEALLAKV--------GLADKRDaypAHLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 139 QQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNG 218
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEG-RTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPP 238
|
...
gi 503995501 219 GDM 221
Cdd:COG4598 239 AEV 241
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-188 |
7.79e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 104.96 E-value: 7.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvqsgIAY 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA----CHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMgLSRFPARDARAVPE--EIYQLFPVLktmkQRRGGDLSGGQQQQLAIGRALASRPQLLILD 158
Cdd:PRK13539 78 LGHRNAMKPALTVAENLEF-WAAFLGGEELDIAAalEAVGLAPLA----HLPFGYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|
gi 503995501 159 EPTEGIQPSVIKEIGEVIRQLANRGDMAIL 188
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLAQGGIVIA 182
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-216 |
1.23e-27 |
|
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: 106.00 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHR--KPHQRVQSGIAYVPQgreiFPR---- 90
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKkkKKLKDLRKKVGLVFQ----FPEhqlf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 91 -LTVEENLLMGLSRFPARDARA------------VPEEIYQLFPVlktmkqrrggDLSGGQQQQLAIGRALASRPQLLIL 157
Cdd:TIGR04521 97 eETVYKDIAFGPKNLGLSEEEAeervkealelvgLDEEYLERSPF----------ELSGGQMRRVAIAGVLAMEPEVLIL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 158 DEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:TIGR04521 167 DEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDG 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-217 |
2.65e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 104.73 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCL--MG-LIP-AR-SGEVLWQEKNITHRK--PHQrV 74
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNdLIPgARvEGEILLDGEDIYDPDvdVVE-L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 75 QSGIAYVPQGREIFPrLTVEENLLMGLSRFPARDaRAVPEEIyqlfpVLKTMKQ------------RRGGDLSGGQQQQL 142
Cdd:COG1117 91 RRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKS-KSELDEI-----VEESLRKaalwdevkdrlkKSALGLSGGQQQRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 143 AIGRALASRPQLLILDEPTEGIQP-SVIKeIGEVIRQLanRGDMAILLV----EQfydfAAGLADRYLVMSRGAIIQQGN 217
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPiSTAK-IEELILEL--KKDYTIVIVthnmQQ----AARVSDYTAFFYLGELVEFGP 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-214 |
2.73e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 108.72 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 18 RGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAYVPQGRE---IFPRLTVE 94
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 95 ENL-------------LMGLsrFPARDARAVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPT 161
Cdd:PRK09700 360 QNMaisrslkdggykgAMGL--FHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503995501 162 EGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQ 214
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDG-KVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-216 |
3.27e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.96 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvqsGIAYV 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR---HVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLLMGL--SRFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLrmQKTPAAEITPRVMEALRMVQ-LEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503995501 160 PTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-210 |
4.78e-27 |
|
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: 103.70 E-value: 4.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVqsgiayVPQGREIFPRLTVEEN 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV------VFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 97 LLMGLSR----FPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEI 172
Cdd:TIGR01184 75 IALAVDRvlpdLSKSERRAIVEEHIALVG-LTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 503995501 173 GEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRG 210
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-161 |
5.23e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.84 E-value: 5.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVlwqeknithrKPHQRVQsgIAY 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----------KLGETVK--IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIF-PRLTVEENLLMGLSRFPARDARAV-------PEEIYQlfPVlktmkqrrgGDLSGGQQQQLAIGRALASRP 152
Cdd:COG0488 383 FDQHQEELdPDKTVLDELRDGAPGGTEQEVRGYlgrflfsGDDAFK--PV---------GVLSGGEKARLALAKLLLSPP 451
|
....*....
gi 503995501 153 QLLILDEPT 161
Cdd:COG0488 452 NVLLLDEPT 460
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-216 |
6.26e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 103.90 E-value: 6.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIT------------HRK 69
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvaDKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 70 PHQRVQSGIAYVPQGREIFPRLTVEENLL------MGLSRFPARDaRAV--------PEEIYQLFPVlktmkqrrggDLS 135
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMeapiqvLGLSKQEARE-RAVkylakvgiDERAQGKYPV----------HLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 136 GGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFyDFAAGLADRYLVMSRGAIIQQ 215
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM-GFARHVSSHVIFLHQGKIEEE 233
|
.
gi 503995501 216 G 216
Cdd:PRK10619 234 G 234
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
10-217 |
6.34e-27 |
|
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: 103.07 E-value: 6.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 10 YYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNItHRKPHQRVQSGIAYVPQGREIFP 89
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI-RDISRKSLRSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 90 RlTVEENLLMGLSRFPARDARAVPEE------IYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEG 163
Cdd:cd03254 91 G-TIMENIRLGRPNATDEEVIEAAKEagahdfIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 164 IQPSVIKEIGEVIRQLaNRGDMAILLveqfydfAAGL-----ADRYLVMSRGAIIQQGN 217
Cdd:cd03254 170 IDTETEKLIQEALEKL-MKGRTSIII-------AHRLstiknADKILVLDDGKIIEEGT 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-188 |
1.05e-26 |
|
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: 101.67 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 12 GGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQrvQSGIAYVPQGREIFPRL 91
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP--HENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 92 TVEENLlmglsRFPARDARAVPEEIYQLFPV--LKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVI 169
Cdd:TIGR01189 89 SALENL-----HFWAAIHGGAQRTIEDALAAvgLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170
....*....|....*....
gi 503995501 170 KEIGEVIRQLANRGDMAIL 188
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLL 182
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-210 |
2.16e-26 |
|
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: 106.06 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 20 VDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPAR-SGEVLWQEKNITHRKPHQRVQSGIAYVPQGRE---IFPRLTVEE 95
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 96 NL-LMGLSRF-------PARDARAVPEEIYQLfpVLKTMKQRRG-GDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQP 166
Cdd:TIGR02633 359 NItLSVLKSFcfkmridAAAELQIIGSAIQRL--KVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503995501 167 SVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRG 210
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEG-VAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-216 |
3.01e-26 |
|
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: 106.36 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYG-GSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSgIAY 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF-INY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRlTVEENLLMGLSR-------FPARDARAVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQ 153
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLLGAKEnvsqdeiWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995501 154 LLILDEPTEGIqpSVIKEiGEVIRQLANRGDMAILLVEQFYDFAAgLADRYLVMSRGAIIQQG 216
Cdd:TIGR01193 632 VLILDESTSNL--DTITE-KKIVNNLLNLQDKTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQG 690
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
3.26e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.62 E-value: 3.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYG-GSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITH-RKPHQRVQSGI 78
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 79 AYVPQG--REIFPRlTVEENLLMGLS--RFPARDARAVPEEIYQLFPVlKTMKQRRGGDLSGGQQQQLAIGRALASRPQL 154
Cdd:PRK13636 85 GMVFQDpdNQLFSA-SVYQDVSFGAVnlKLPEDEVRKRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 155 LILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDMEAE 224
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-207 |
3.29e-26 |
|
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: 105.83 E-value: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQL-HQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvQSGIAY 80
Cdd:TIGR02857 322 LEFSGVsVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRlTVEENLLMGLsrfPARDARAVPEEIYQ--LFPVLKTMKQ-------RRGGDLSGGQQQQLAIGRALASR 151
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLAR---PDASDAEIREALERagLDEFVAALPQgldtpigEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503995501 152 PQLLILDEPTEGIQPSVIKEIGEVIRQLANRgdmAILLVEQFYDFAAGLADRYLVM 207
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQG---RTVLLVTHRLALAALADRIVVL 529
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-212 |
6.56e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 104.61 E-value: 6.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 20 VDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAYVPQGRE---IFPRLTVEEN 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 97 LLMGLSRF---------PARDARAVPEEIYQLfpVLKTMKQRRG-GDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQP 166
Cdd:PRK11288 352 INISARRHhlragclinNRWEAENADRFIRSL--NIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503995501 167 SVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAI 212
Cdd:PRK11288 430 GAKHEIYNVIYELAAQG-VAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-217 |
7.16e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 101.66 E-value: 7.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRK---PHQRVQSGIAYVPQGREIFPRlTV 93
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklSDIRKKVGLVFQYPEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 94 EENLLMGLSRFPARDaravpEEIYQlfPVLKTM----------KQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEG 163
Cdd:PRK13637 102 EKDIAFGPINLGLSE-----EEIEN--RVKRAMnivgldyedyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503995501 164 IQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGN 217
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-160 |
8.91e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 101.09 E-value: 8.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGS----HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVqs 76
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 77 giayVPQGREIFPRLTVEENLLMGLsRF---PARDARAVPEEIYQLfpV-LKTMKQRRGGDLSGGQQQQLAIGRALASRP 152
Cdd:COG4525 81 ----VFQKDALLPWLNVLDNVAFGL-RLrgvPKAERRARAEELLAL--VgLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
....*...
gi 503995501 153 QLLILDEP 160
Cdd:COG4525 154 RFLLMDEP 161
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-216 |
2.03e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.70 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSgIAY 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMGLS-------RFPARDARAVPEEIYQLFpvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQ 153
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSpwlslwgRLSAEDNARVNQAMEQTR--INHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995501 154 LLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVeqfYDF--AAGLADRYLVMSRGAIIQQG 216
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVL---HDLnqASRYCDHLVVLANGHVMAQG 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-216 |
2.42e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 100.48 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIT-HRKPHQ----RVQSGIAYVPQGREIFPRl 91
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKlkplRKKVGIVFQFPEHQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 92 TVEENLLMGLSRF--PARDARAVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVI 169
Cdd:PRK13634 102 TVEKDICFGPMNFgvSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503995501 170 KEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK13634 182 KEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-160 |
2.61e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 98.32 E-value: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPAR---SGEVLWQEKNITHRKPHQRvqsG 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQR---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 78 IAYVPQGREIFPRLTVEENLLMGLSRFPARDAR-----AVPEEIYqlfpvLKTMKQRRGGDLSGGQQQQLAIGRALASRP 152
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFALPPTIGRAQRrarveQALEEAG-----LAGFADRDPATLSGGQRARVALLRALLAEP 152
|
....*...
gi 503995501 153 QLLILDEP 160
Cdd:COG4136 153 RALLLDEP 160
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-230 |
3.23e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 102.94 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAY 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMGlsRFPARDARAVP----------EEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALAS 150
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIG--RHLTKKVCGVNiidwremrvrAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 151 RPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAgLADRYLVMSRGAIIQQGNGGDMEAEG-VRGM 229
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRR-ICDRYTVMKDGSSVCSGMVSDVSNDDiVRLM 241
|
.
gi 503995501 230 V 230
Cdd:PRK09700 242 V 242
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-218 |
3.33e-25 |
|
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: 98.39 E-value: 3.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 21 DFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAyvpQGREIFPRLTVEENLLMG 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLF---QENNLFAHLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 101 LSrfPARDARAVPEEiyQLFPVLKTMK-----QRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEV 175
Cdd:TIGR01277 95 LH--PGLKLNAEQQE--KVVDAAQQVGiadylDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503995501 176 IRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNG 218
Cdd:TIGR01277 171 VKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-216 |
3.62e-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: 98.43 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPhQRVQSGIAYVPQGREIFPRlTVEEN 96
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP-ADLRRNIGYVPQDVTLFYG-TLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 97 LLMGLSrfPARDAR-------AVPEEIYQLFPV-LKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSV 168
Cdd:cd03245 98 ITLGAP--LADDERilraaelAGVTDFVNKHPNgLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503995501 169 IKEIGEVIRQLAnrGDMAILLVEQFYDFAAgLADRYLVMSRGAIIQQG 216
Cdd:cd03245 176 EERLKERLRQLL--GDKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-216 |
3.75e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 99.22 E-value: 3.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLI-----PARSGEVLWQEKNItHRKPHQRVQS 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDI-FKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 77 GIAYVPQGREIFPRLTVEENLLMG--LSRFpARDARAVPE------EIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRAL 148
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGlkLNRL-VKSKKELQErvrwalEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 149 ASRPQLLILDEPTEGIQPSVIKEIGEVIRQLanRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-161 |
4.50e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.45 E-value: 4.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 4 VNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVlWQEKNIThrkphqrvqsgIAYVPQ 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-SIPKGLR-----------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 84 GREIFPRLTVEENLLMGLSrfPARDARAVPEEIYQLFP------------------------------VLKTMK------ 127
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDA--ELRALEAELEELEAKLAepdedlerlaelqeefealggweaearaeeILSGLGfpeedl 146
|
170 180 190
....*....|....*....|....*....|....
gi 503995501 128 QRRGGDLSGGQQQQLAIGRALASRPQLLILDEPT 161
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-213 |
4.72e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.00 E-value: 4.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYG-GS----HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQ 75
Cdd:COG1101 1 MLELKNLSKTFNpGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 76 SgIAYVPQ----GreIFPRLTVEENLLMGLSRFPARD-ARAVPEEIYQLF-PVLKT--------MKQRRgGDLSGGQQQQ 141
Cdd:COG1101 81 Y-IGRVFQdpmmG--TAPSMTIEENLALAYRRGKRRGlRRGLTKKRRELFrELLATlglglenrLDTKV-GLLSGGQRQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503995501 142 LAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLV----EQfydfAAGLADRYLVMSRGAII 213
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVthnmEQ----ALDYGNRLIMMHEGRII 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-221 |
7.48e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 98.31 E-value: 7.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCL--MG-LIP--ARSGEVLWQEKNI-THRKPHQRV 74
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNdLNPevTITGSIVYNGHNIySPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 75 QSGIAYVPQGREIFPrLTVEENLLMGLsRFPARDARAVPEEIyqlfpVLKTMKQRRGGD------------LSGGQQQQL 142
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGL-RLKGIKDKQVLDEA-----VEKSLKGASIWDevkdrlhdsalgLSGGQQQRV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 143 AIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLanRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDM 221
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-217 |
1.43e-24 |
|
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: 97.71 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIT--HRKPHQRVQSG-IAYVPQGREIFPRLTV 93
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamSRKELRELRRKkISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 94 EENLLMGLS--RFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKE 171
Cdd:cd03294 120 LENVAFGLEvqGVPRAEREERAAEALELVG-LEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503995501 172 IGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGN 217
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGT 244
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-216 |
2.00e-24 |
|
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: 96.02 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 21 DFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAyvpQGREIFPRLTVEENLLMG 100
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLF---QENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 101 LS---RFPARDARAVPEEIYQLFpvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIR 177
Cdd:cd03298 95 LSpglKLTAEDRQAIEVALARVG--LAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 503995501 178 QLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
9-216 |
2.20e-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: 98.24 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 9 QYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQ--RvqsGIAYVPQGRE 86
Cdd:COG1125 10 RYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrR---RIGYVIQQIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 87 IFPRLTVEEN-----LLMGLSRfPARDARAvpEEIYQLF---PvlKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILD 158
Cdd:COG1125 87 LFPHMTVAENiatvpRLLGWDK-ERIRARV--DELLELVgldP--EEYRDRYPHELSGGQQQRVGVARALAADPPILLMD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 159 EPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:COG1125 162 EPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYD 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-216 |
2.23e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.57 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 8 HQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQ-RVQSGIAYVPQGRE 86
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvRKFVGLVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 87 IFPRlTVEENLLMGLSRFpARDARAVPEEIYQLFPVL--KTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGI 164
Cdd:PRK13652 91 IFSP-TVEQDIAFGPINL-GLDEETVAHRVSSALHMLglEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503995501 165 QPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK13652 169 DPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYG 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-190 |
2.26e-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: 97.08 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 10 YYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSG---EVLWQEK---NITHRKPHqrvqsgIAYV-P 82
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFGERRggeDVWELRKR------IGLVsP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 83 Q-GREIFPRLTVEENLL------MGLSRFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLL 155
Cdd:COG1119 86 AlQLRFPRDETVLDVVLsgffdsIGLYREPTDEQRERARELLELLG-LAHLADRPFGTLSQGEQRRVLIARALVKDPELL 164
|
170 180 190
....*....|....*....|....*....|....*
gi 503995501 156 ILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLV 190
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLV 199
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-192 |
2.45e-24 |
|
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: 95.64 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPhqRVQSGIAYV 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD--SIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLlmglsRFPARD-ARAvpeeiyQLFPVLKTMKQRRGGD-----LSGGQQQQLAIGRALASRPQLL 155
Cdd:cd03231 79 GHAPGIKTTLSVLENL-----RFWHADhSDE------QVEEALARVGLNGFEDrpvaqLSAGQQRRVALARLLLSGRPLW 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 503995501 156 ILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQ 192
Cdd:cd03231 148 ILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
2.46e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 97.37 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSH--ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIT-HRKPHQRVQSG 77
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 78 IAYV-PQGReiFPRLTVEENLLMGLS--RFPARDARAVPEEIYQLFPVLKTMKqRRGGDLSGGQQQQLAIGRALASRPQL 154
Cdd:PRK13632 87 IIFQnPDNQ--FIGATVEDDIAFGLEnkKVPPKKMKDIIDDLAKKVGMEDYLD-KEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995501 155 LILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDfAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMD-EAILADKVIVFSEGKLIAQG 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-217 |
2.82e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 98.23 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGS----HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQ--RV 74
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 75 QSGIAYVPQGREIFPRLTVEENL-----LMGLSRfPARDARAvpEEIYQLfpV-LKTMKQRRGGDLSGGQQQQLAIGRAL 148
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENValpleIAGVPK-AEIRKRV--AELLEL--VgLSDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503995501 149 ASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILL-------VEQfydfaagLADRYLVMSRGAIIQQGN 217
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLithemdvVRR-------ICDRVAVLENGRIVEQGP 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
11-216 |
3.47e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 98.25 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 11 YGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvqsGIAYVPQGREIFPR 90
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR---DICMVFQSYALFPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 91 LTVEENLLMGLS--RFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSV 168
Cdd:PRK11432 93 MSLGENVGYGLKmlGVPKEERKQRVKEALELVD-LAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503995501 169 IKEIGEVIRQLANRGDMAILLV--EQFYDFAagLADRYLVMSRGAIIQQG 216
Cdd:PRK11432 172 RRSMREKIRELQQQFNITSLYVthDQSEAFA--VSDTVIVMNKGKIMQIG 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-183 |
6.31e-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: 99.13 E-value: 6.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIP--ARSGEVLWQEKNITHRKPHQRVQSGI 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 79 AYVPQGREIFPRLTVEENLLMG--------LSRFPARDARAvpEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALAS 150
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGneitlpggRMAYNAMYLRA--KNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNK 158
|
170 180 190
....*....|....*....|....*....|...
gi 503995501 151 RPQLLILDEPTEGIQPSVIKEIGEVIRQLANRG 183
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAHG 191
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-216 |
8.59e-24 |
|
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: 94.13 E-value: 8.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPAR--SGEVLWQEKNITHRKPHQRVQSGIA 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 80 YVPQGREIFPRLTVEENLlmglsrfpardaRAVPEeiyqlfpvlktmkqrrggDLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:cd03217 81 LAFQYPPEIPGVKNADFL------------RYVNE------------------GFSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 160 PTEGIQPSVIKEIGEVIRQLANRGdMAILLV---EQFYDFAAglADRYLVMSRGAIIQQG 216
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREEG-KSVLIIthyQRLLDYIK--PDRVHVLYDGRIVKSG 187
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-216 |
1.46e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.91 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIP----AR-SGEVLWQEKNITHRKPHQ-RVQ 75
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeARvEGEVRLFGRNIYSPDVDPiEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 76 SGIAYVPQGREIFPRLTVEENLLMGLSRFPARDARAVPEEIYQ-------LFPVLKTMKQRRGGDLSGGQQQQLAIGRAL 148
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEwalkkaaLWDEVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 149 ASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANrgDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-190 |
1.66e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.10 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARS-----GEVLWQEKNITHRKPH-QRVQ 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 76 SGIAYVPQGREIFPrLTVEENLLMGLSRF---PARDARAVPEEIYQ---LFPVLKTMKQRRGGDLSGGQQQQLAIGRALA 149
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVgwrPKLEIDDIVESALKdadLWDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 503995501 150 SRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLV 190
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIV 207
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1-183 |
1.76e-23 |
|
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: 93.63 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQlhQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRK----PHQRVQS 76
Cdd:cd03292 3 FINVTK--TYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraiPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 77 GIAYvpQGREIFPRLTVEENLLMGL--SRFPARDARA-VPEEIYQLfpVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQ 153
Cdd:cd03292 81 GVVF--QDFRLLPDRNVYENVAFALevTGVPPREIRKrVPAALELV--GLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190
....*....|....*....|....*....|
gi 503995501 154 LLILDEPTEGIQPSVIKEIGEVIRQLANRG 183
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAG 186
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-161 |
1.81e-23 |
|
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: 94.04 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGS----HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQ- 75
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 76 --SGIAYVPQGREIFPRLTVEENLLMGLSRFPARDARAVPEEIyqlfpvLKTM--KQRRG---GDLSGGQQQQLAIGRAL 148
Cdd:COG4181 88 raRHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARAL------LERVglGHRLDhypAQLSGGEQQRVALARAF 161
|
170
....*....|...
gi 503995501 149 ASRPQLLILDEPT 161
Cdd:COG4181 162 ATEPAILFADEPT 174
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
2.55e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 94.76 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLH-QYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKP---HQRVQS 76
Cdd:PRK13639 1 ILETRDLKySYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 77 GIAYVPQGREIFPRlTVEEN-----LLMGLSRFP----ARDA-RAVPEEIYQLFPvlktmkqrrGGDLSGGQQQQLAIGR 146
Cdd:PRK13639 81 GIVFQNPDDQLFAP-TVEEDvafgpLNLGLSKEEvekrVKEAlKAVGMEGFENKP---------PHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 147 ALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLaNRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEG 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-216 |
2.60e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.83 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNItHRKPHQRVQSGIAY 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV-EALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMG----LSRFPAR---DARAVPEEIYQLfpVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQ 153
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGrtphRSRFDTWtetDRAAVERAMERT--GVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995501 154 LLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFyDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDL-DLAARYCDELVLLADGRVRAAG 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-215 |
3.22e-23 |
|
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: 94.10 E-value: 3.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQR--VQSGIAYVPQG--REIFPRL 91
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRraFRRDVQLVFQDspSAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 92 TVEENL---LMGLSRFPARDARAVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSV 168
Cdd:TIGR02769 106 TVRQIIgepLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503995501 169 IKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQ 215
Cdd:TIGR02769 186 QAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-211 |
3.57e-23 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 93.27 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYY-----GGSHI--LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEK----NITHRK 69
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 70 PHQRV---QSGIAYVPQGREIFPRLT----VEENLL-MGLSRFPARD-ARA------VPEEIYQLFPVlkTmkqrrggdL 134
Cdd:COG4778 84 PREILalrRRTIGYVSQFLRVIPRVSaldvVAEPLLeRGVDREEARArAREllarlnLPERLWDLPPA--T--------F 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 135 SGGQQQQLAIGRALASRPQLLILDEPTEGIQPS----VIkeigEVIRQLANRGdMAILLVeqFYD--FAAGLADRYLVMS 208
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAAnravVV----ELIEEAKARG-TAIIGI--FHDeeVREAVADRVVDVT 226
|
...
gi 503995501 209 RGA 211
Cdd:COG4778 227 PFS 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-216 |
3.99e-23 |
|
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: 97.06 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPArSGEVLWQEKNITHRKPHQ------RVQSgiayvpqgreIF-- 88
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRAlrplrrRMQV----------VFqd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 89 ------PRLTVE----ENLL---MGLSRfPARDARAV--------PEEIYQLFPvlktmkqrrgGDLSGGQQQQLAIGRA 147
Cdd:COG4172 371 pfgslsPRMTVGqiiaEGLRvhgPGLSA-AERRARVAealeevglDPAARHRYP----------HEFSGGQRQRIAIARA 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995501 148 LASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEqfYDFA--AGLADRYLVMSRGAIIQQG 216
Cdd:COG4172 440 LILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFIS--HDLAvvRALAHRVMVMKDGKVVEQG 508
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
10-172 |
2.06e-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: 94.73 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 10 YYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNItHRKPHQRVQSGIAYVPQGREIFP 89
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV-SSLDQDEVRRRVSVCAQDAHLFD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 90 RlTVEENLLMGLSRFPARDARAVPEE------IYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEG 163
Cdd:TIGR02868 423 T-TVRENLRLARPDATDEELWAALERvgladwLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
....*....
gi 503995501 164 IQPSVIKEI 172
Cdd:TIGR02868 502 LDAETADEL 510
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-216 |
2.14e-22 |
|
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: 94.81 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSgIAYVPQGREIFPRlTVEE 95
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH-IGYLPQDVELFDG-TIAE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 96 NLlmglSRFPARDARAVPE--------EIYQLFPV-LKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEP-----T 161
Cdd:COG4618 425 NI----ARFGDADPEKVVAaaklagvhEMILRLPDgYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPnsnldD 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995501 162 EGIQpsvikEIGEVIRQLANRG--------DMAILlveqfydfaaGLADRYLVMSRGAIIQQG 216
Cdd:COG4618 501 EGEA-----ALAAAIRALKARGatvvvithRPSLL----------AAVDKLLVLRDGRVQAFG 548
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-160 |
2.55e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.56 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 11 YGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvqsGIAYVPQGREIFPR 90
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER---GVGMVFQSYALYPH 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995501 91 LTVEENLLMGLSRFPARDA---RAVPE--EIYQLFPVLktmkQRRGGDLSGGQQQQLAIGRALASRPQLLILDEP 160
Cdd:PRK11000 90 LSVAENMSFGLKLAGAKKEeinQRVNQvaEVLQLAHLL----DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-183 |
2.71e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 94.61 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIP--ARSGEVLWQEKNITHRKPHQRVQSGI 78
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 79 AYVPQGREIFPRLTVEENLLMG--LSRFPARDARAVPEEIYQLFPVLK--TMKQRRGGDLSGGQQQQLAIGRALASRPQL 154
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGneITPGGIMDYDAMYLRAQKLLAQLKldINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180
....*....|....*....|....*....
gi 503995501 155 LILDEPTEGIQPSVIKEIGEVIRQLANRG 183
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLKAHG 193
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-216 |
2.81e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 91.28 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGlIPA---RSGEVLWQEKNITHRKPHQRVQSGI 78
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HPKyevTSGSILLDGEDILELSPDERARAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 79 AYVPQGREIFPRLTVEeNLL---MGLSRFPARDARAVPEEIYQLFPVLKtMKQ---RRG--GDLSGGQQQQLAIGRALAS 150
Cdd:COG0396 80 FLAFQYPVEIPGVSVS-NFLrtaLNARRGEELSAREFLKLLKEKMKELG-LDEdflDRYvnEGFSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 151 RPQLLILDEPTEGIQPSVIKEIGEVIRQLANRgDMAILLV---EQFYDFAAglADRYLVMSRGAIIQQG 216
Cdd:COG0396 158 EPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIIthyQRILDYIK--PDFVHVLVDGRIVKSG 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-216 |
5.60e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 88.91 E-value: 5.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGS--HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIThrKPHQRVQSGIA 79
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS--DLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 80 YVPQGREIFPRlTVEENLlmglsrfpardaravpeeiyqlfpvlktmkqrrGGDLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:cd03247 79 VLNQRPYLFDT-TLRNNL---------------------------------GRRFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 160 PTEGIQPSVIKEIGEVIRQLANrgDMAILLVEQFYdfaAGL--ADRYLVMSRGAIIQQG 216
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLK--DKTLIWITHHL---TGIehMDKILFLENGKIIMQG 178
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
9-216 |
5.78e-22 |
|
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: 93.78 E-value: 5.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 9 QYYG-GSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQrVQSGIAYVPQGrei 87
Cdd:TIGR03375 472 AYPGqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAD-LRRNIGYVPQD--- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 88 fPRL---TVEENLLMGlsRFPARDARAVpeEIYQLFPVLKTMKQ----------RRGGDLSGGQQQQLAIGRALASRPQL 154
Cdd:TIGR03375 548 -PRLfygTLRDNIALG--APYADDEEIL--RAAELAGVTEFVRRhpdgldmqigERGRSLSGGQRQAVALARALLRDPPI 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995501 155 LILDEPTEGIQPSVIKEIGEVIRQLAnrGDMAILLVE---QFYDfaagLADRYLVMSRGAIIQQG 216
Cdd:TIGR03375 623 LLLDEPTSAMDNRSEERFKDRLKRWL--AGKTLVLVThrtSLLD----LVDRIIVMDNGRIVADG 681
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-216 |
9.02e-22 |
|
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: 88.86 E-value: 9.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPAR---SGEVLWqeKNITHRKPHQRVQSGIAYVPQGREIFPRLT 92
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHY--NGIPYKEFAEKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 93 VEENLlmglsRFPARdaravpeeiyqlfpvLKTMKQRRGgdLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEI 172
Cdd:cd03233 100 VRETL-----DFALR---------------CKGNEFVRG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503995501 173 GEVIRQLANRGDMAILL-VEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:cd03233 158 LKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-188 |
9.32e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.09 E-value: 9.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKP--HQRV---- 74
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeyHQDLlylg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 75 -QSGIAyvpqgreifPRLTVEENLlmglsRFPARDARAVPEEiyQLFPVLKTMKQRRGGD-----LSGGQQQQLAIGRAL 148
Cdd:PRK13538 81 hQPGIK---------TELTALENL-----RFYQRLHGPGDDE--ALWEALAQVGLAGFEDvpvrqLSAGQQRRVALARLW 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503995501 149 ASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAIL 188
Cdd:PRK13538 145 LTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVIL 184
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-216 |
1.03e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 90.33 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHI-LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGE--VLWQEKNITHRkphqrvQSGI 78
Cdd:PRK15056 7 IVVNDVTVTWRNGHTaLRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKisILGQPTRQALQ------KNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 79 AYVPQGREI---FPRLtVEENLLMG-------LSRFPARDARAVPEEIYQLfpVLKTMKQRRGGDLSGGQQQQLAIGRAL 148
Cdd:PRK15056 81 AYVPQSEEVdwsFPVL-VEDVVMMGryghmgwLRRAKKRDRQIVTAALARV--DMVEFRHRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995501 149 ASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAIL------LVEQFYDfaagladrYLVMSRGAIIQQG 216
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVsthnlgSVTEFCD--------YTVMVKGTVLASG 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-216 |
1.18e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.80 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 14 SHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPA---RSGEVLWQEKNITHRKPHQRVqsgiAYVPQGREIFPR 90
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIS----AYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 91 LTVEENLL-MGLSRFPARDA----RAVPEEIYQLFPVLKTMKQRRG--GD---LSGGQQQQLAIGRALASRPQLLILDEP 160
Cdd:TIGR00955 114 LTVREHLMfQAHLRMPRRVTkkekRERVDEVLQALGLRKCANTRIGvpGRvkgLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 161 TEGIQP----SVIKeigeVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:TIGR00955 194 TSGLDSfmaySVVQ----VLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG 249
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-210 |
1.20e-21 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 92.48 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAYVPQGRE---IFPRLTV 93
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEERRstgIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 94 EENLL----------MGL--SRFPARDARAVPEEIYQLFPVLKTMKqrrgGDLSGGQQQQLAIGRALASRPQLLILDEPT 161
Cdd:PRK10982 344 GFNSLisnirnyknkVGLldNSRMKSDTQWVIDSMRVKTPGHRTQI----GSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503995501 162 EGIQPSVIKEIGEVIRQLANRgDMAILLVEQFYDFAAGLADRYLVMSRG 210
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-217 |
3.75e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.10 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYggSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAy 80
Cdd:PRK10771 1 MLKLTDITWLY--HHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLF- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 vpQGREIFPRLTVEENLLMGLSrfPA----RDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLI 156
Cdd:PRK10771 78 --QENNLFSHLTVAQNIGLGLN--PGlklnAAQREKLHAIARQMG-IEDLLARLPGQLSGGQRQRVALARCLVREQPILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995501 157 LDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGN 217
Cdd:PRK10771 153 LDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-217 |
6.79e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 90.55 E-value: 6.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIT---HRKPHQRVqsgiAYVPQGREIFPRlT 92
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqydHHYLHRQV----ALVGQEPVLFSG-S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 93 VEENLLMGLSRFPARDARAVPEE------IYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQp 166
Cdd:TIGR00958 571 VRENIAYGLTDTPDEEIMAAAKAanahdfIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD- 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503995501 167 sviKEIGEVIRQLANRGDMAILLVEQFYDFAAGlADRYLVMSRGAIIQQGN 217
Cdd:TIGR00958 650 ---AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGT 696
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-216 |
1.01e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 87.29 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHR------KPHQR- 73
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRdlyalsEAERRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 74 -VQSGIAYVPQGREIFPRLTVEE--NL---LMGLSRFPARDARAVPE------EIyqlfpvlktmKQRRGGDL----SGG 137
Cdd:PRK11701 86 lLRTEWGFVHQHPRDGLRMQVSAggNIgerLMAVGARHYGDIRATAGdwlervEI----------DAARIDDLpttfSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 138 QQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-214 |
1.51e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.05 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQL-HQYYGGS--------HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIT--HRK 69
Cdd:PRK10419 3 LLNVSGLsHHYAHGGlsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 70 PHQRVQSGIAYVPQGR--EIFPRLTVEENL------LMGLSRfPARDARAvpEEIYQLFPVLKTMKQRRGGDLSGGQQQQ 141
Cdd:PRK10419 83 QRKAFRRDIQMVFQDSisAVNPRKTVREIIreplrhLLSLDK-AERLARA--SEMLRAVDLDDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 142 LAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAIL-------LVEQFydfaaglADRYLVMSRGAIIQ 214
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLfithdlrLVERF-------CQRVMVMDNGQIVE 232
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-225 |
2.12e-20 |
|
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: 86.00 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 13 GSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNI-THRKPHQRVQSGiaYVPQGREIFPRl 91
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVG--VVLQENVLFNR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 92 TVEENLLMGLSRFPARDARAVP------EEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQ 165
Cdd:cd03252 91 SIRDNIALADPGMSMERVIEAAklagahDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 166 PSVIKEIGEVIRQLAnRGDMAILLVEQFYdfAAGLADRYLVMSRGAIIQQGNGGDMEAEG 225
Cdd:cd03252 171 YESEHAIMRNMHDIC-AGRTVIIIAHRLS--TVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
13-226 |
2.35e-20 |
|
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: 85.75 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 13 GSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQrVQSGIAYVPQGREIFPRlT 92
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS-LRRQIGLVSQDVFLFND-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 93 VEENLLMGLS-------RFPARDARAVpEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQ 165
Cdd:cd03251 92 VAENIAYGRPgatreevEEAARAANAH-EFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 166 PSVIKEIGEVIRQL-ANRGDMAIllveqfydfAAGL-----ADRYLVMSRGAIIQQGNGGD-MEAEGV 226
Cdd:cd03251 171 TESERLVQAALERLmKNRTTFVI---------AHRLstienADRIVVLEDGKIVERGTHEElLAQGGV 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-190 |
2.94e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 85.54 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSgIAY 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ-VSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRlTVEENLLmglsrFPARDARAVPEEIYQL-----FPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLL 155
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLI-----FPWQIRNQQPDPAIFLddlerFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190
....*....|....*....|....*....|....*
gi 503995501 156 ILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLV 190
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREQNIAVLWV 194
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-216 |
6.15e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.57 E-value: 6.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQ-----RVQSGIAYVPQGREIFPRl 91
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqiRKKVGLVFQFPESQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 92 TVEENLLMGLSRF--PARDARAVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVI 169
Cdd:PRK13649 102 TVLKDVAFGPQNFgvSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503995501 170 KEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK13649 182 KELMTLFKKLHQSG-MTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-224 |
7.23e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.56 E-value: 7.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 13 GSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQS-----GIAYVPQGREI 87
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPvrkkvGVVFQFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 88 FPRlTVEENLLMGLSRF--PARDARAVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQ 165
Cdd:PRK13643 98 FEE-TVLKDVAFGPQNFgiPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 166 PSVIKEIGEVIRQLANRGDmAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDMEAE 224
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-161 |
7.69e-20 |
|
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: 82.11 E-value: 7.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNithrkphqrvqsGIAYV 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV------------KIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQgreifprltveenllmglsrfpardaravpeeiyqlfpvlktmkqrrggdLSGGQQQQLAIGRALASRPQLLILDEPT 161
Cdd:cd03221 69 EQ--------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-160 |
9.76e-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: 83.67 E-value: 9.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVlwqeknithrkphqRVQSGIAYVPQGREIFPRlTVEE 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV--------------SVPGSIAYVSQEPWIQNG-TIRE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995501 96 NLLMGLSRFPARDARAVpeEIYQLFPVLKTMKqrrGGD----------LSGGQQQQLAIGRALASRPQLLILDEP 160
Cdd:cd03250 85 NILFGKPFDEERYEKVI--KACALEPDLEILP---DGDlteigekginLSGGQKQRISLARAVYSDADIYLLDDP 154
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-216 |
1.13e-19 |
|
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: 87.38 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 26 QGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIthRKPHQRVQSGIAYVPQGREIFPRLTVEENLLMglsrFP 105
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQSLGMCPQHNILFHHLTVAEHILF----YA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 106 ARDARAVPEEIYQLFPVLKTM-----KQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIrqLA 180
Cdd:TIGR01257 1029 QLKGRSWEEAQLEMEAMLEDTglhhkRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LK 1106
|
170 180 190
....*....|....*....|....*....|....*.
gi 503995501 181 NRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:TIGR01257 1107 YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-221 |
1.18e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 84.71 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARS------GEVLWQEKNItHRKPHQRV 74
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDI-FQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 75 QSGIAYVPQGREIFPRLTVEENLLMGLSRFPARDARAVP---EEIYQLFPVLKTMKQR---RGGDLSGGQQQQLAIGRAL 148
Cdd:PRK14246 89 RKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKkivEECLRKVGLWKEVYDRlnsPASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995501 149 ASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANrgDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDM 221
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-212 |
1.25e-19 |
|
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: 83.67 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 14 SHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKpHQRVQSGIAYVPQGREIFPRlTV 93
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE-HKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 94 EENLLMGLSRFP------ARDARAVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPS 167
Cdd:cd03248 105 QDNIAYGLQSCSfecvkeAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503995501 168 VIKEIGEVIRQLANRGDMAIL-----LVEQfydfaaglADRYLVMSRGAI 212
Cdd:cd03248 185 SEQQVQQALYDWPERRTVLVIahrlsTVER--------ADQILVLDGGRI 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-217 |
1.28e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.70 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYygGSHILRgVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGE------VLWQEKNITHRKPHQRv 74
Cdd:PRK11144 1 MLELNFKQQL--GDLCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRivlngrVLFDAEKGICLPPEKR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 75 qsGIAYVPQGREIFPRLTVEENLLMGLSRFpardARAVPEEIYQLF---PVLKtmkqRRGGDLSGGQQQQLAIGRALASR 151
Cdd:PRK11144 77 --RIGYVFQDARLFPHYKVRGNLRYGMAKS----MVAQFDKIVALLgiePLLD----RYPGSLSGGEKQRVAIGRALLTA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503995501 152 PQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGN 217
Cdd:PRK11144 147 PELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-216 |
2.31e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.99 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 11 YGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPA-----RSGEVLWQEKNITHRKPHQRVQSGIAYVPQGR 85
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 86 EIFPrLTVEENLLMGLSR---FPARDARAVPEEIYQLFPVLKTMKQRRGGD---LSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRAhklVPRKEFRGVAQARLTEVGLWDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503995501 160 PTEGIQPSVIKEIGEVIRQLANRgdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEG 244
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-216 |
3.42e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 84.47 E-value: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGS----HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITH--RKPHQRV 74
Cdd:PRK11153 1 MIELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlsEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 75 QSGIAYVPQGREIFPRLTVEEN--LLMGLSRFPARDARAVPEEIYQLfpV-LKTMKQRRGGDLSGGQQQQLAIGRALASR 151
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNvaLPLELAGTPKAEIKARVTELLEL--VgLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995501 152 PQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQG 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-217 |
4.14e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.60 E-value: 4.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEV------------LWQEKN---ITHRKPHQR-----VQS 76
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtsdeenLWDIRNkagMVFQNPDNQivatiVEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 77 GIAYVPQGREIFP---RLTVEENLlmglsrfpardaRAVPEEIYQLF-PVLktmkqrrggdLSGGQQQQLAIGRALASRP 152
Cdd:PRK13633 106 DVAFGPENLGIPPeeiRERVDESL------------KKVGMYEYRRHaPHL----------LSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995501 153 QLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGlADRYLVMSRGAIIQQGN 217
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGT 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-212 |
4.18e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.19 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLwqekniTHRKPHQRVQSGIAYV 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL------AGTAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLLMGLS---RFPARDA-RAVPEEiyqlfpvlktmkqRRGGD----LSGGQQQQLAIGRALASRPQ 153
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGLKgqwRDAALQAlAAVGLA-------------DRANEwpaaLSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 154 LLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAI 212
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-216 |
4.24e-19 |
|
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: 85.12 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLH----QYYGGSHILRGVDFAARQGEITCLLGRNGVGKT-TLLkCLMGLIPAR----SGEVLWQEKNITHRKPH 71
Cdd:COG4172 6 LLSVEDLSvafgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTAL-SILRLLPDPaahpSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 72 Q--RVQsgiayvpqGREI---F--------PRLTVE----ENLL--MGLSRFPARdARAV----------PEEIYQLFPv 122
Cdd:COG4172 85 ElrRIR--------GNRIamiFqepmtslnPLHTIGkqiaEVLRlhRGLSGAAAR-ARALellervgipdPERRLDAYP- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 123 lktmKQrrggdLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILL-------VEQFyd 195
Cdd:COG4172 155 ----HQ-----LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLithdlgvVRRF-- 223
|
250 260
....*....|....*....|.
gi 503995501 196 faaglADRYLVMSRGAIIQQG 216
Cdd:COG4172 224 -----ADRVAVMRQGEIVEQG 239
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-216 |
4.52e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 83.14 E-value: 4.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQ-RVQSGIAYV-PQGReiFPRLTVE 94
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvRRQVGMVFQnPDNQ--FVGATVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 95 ENLLMGLsrfparDARAVPEE--IYQLFPVLKTMK-----QRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPS 167
Cdd:PRK13635 101 DDVAFGL------ENIGVPREemVERVDQALRQVGmedflNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503995501 168 VIKEIGEVIRQLANRGDMAILLVEQFYDFAAGlADRYLVMSRGAIIQQG 216
Cdd:PRK13635 175 GRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-216 |
7.42e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.73 E-value: 7.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 8 HQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAYVPQGREI 87
Cdd:PRK13644 9 YSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPET 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 88 -FPRLTVEENLLMG---LSRFPARDARAVPEEIYQLfpVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEG 163
Cdd:PRK13644 89 qFVGRTVEEDLAFGpenLCLPPIEIRKRVDRALAEI--GLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503995501 164 IQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAglADRYLVMSRGAIIQQG 216
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD--ADRIIVMDRGKIVLEG 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-216 |
8.04e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.37 E-value: 8.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARS---------GEVLWQEKNITHRKPH 71
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 72 QRVQSGiaYVPQGREIFPRLTVEENLLMG-----------LSRFpardARAVPEEIYQLFPV--LKTMKQRRGGDLSGGQ 138
Cdd:PRK09984 84 SRANTG--YIFQQFNLVNRLSVLENVLIGalgstpfwrtcFSWF----TREQKQRALQALTRvgMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 139 QQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-183 |
9.52e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.28 E-value: 9.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAY 80
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMG---LSRFPARDARAVPEEIYQLFPVL--KTMKQRRGGDLSGGQQQQLAIGRALASRPQLL 155
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLGrefVNRFGRIDWKKMYAEADKLLARLnlRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180
....*....|....*....|....*...
gi 503995501 156 ILDEPTEGIQPSVIKEIGEVIRQLANRG 183
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIRELKSQG 191
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-217 |
9.90e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.52 E-value: 9.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHR---KPHQRVQSGIAYVPQgreiFPRL-- 91
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdKYIRPVRKRIGMVFQ----FPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 92 ---TVEENLLMGLSRFpARDARAVPEEIYQL-----FPvlKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEG 163
Cdd:PRK13646 99 fedTVEREIIFGPKNF-KMNLDEVKNYAHRLlmdlgFS--RDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503995501 164 IQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGN 217
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTS 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-212 |
1.24e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 82.09 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 14 SHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEV-----LWQEKNITHRKPHqrvqsgIAYVPQGRE-I 87
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdLLTEENVWDIRHK------IGMVFQNPDnQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 88 FPRLTVEENLLMGLSR--FPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQ 165
Cdd:PRK13650 94 FVGATVEDDVAFGLENkgIPHEEMKERVNEALELVG-MQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503995501 166 PSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAgLADRYLVMSRGAI 212
Cdd:PRK13650 173 PEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-215 |
1.25e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.40 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYG----GSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQ- 75
Cdd:PRK11629 5 LLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 76 --SGIAYVPQGREIFPRLTVEENLLMGLSRFPARDARAVPEEIYQLFPV-LKTMKQRRGGDLSGGQQQQLAIGRALASRP 152
Cdd:PRK11629 85 rnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVgLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995501 153 QLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLaDRYLVMSRGAIIQQ 215
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-160 |
1.76e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 81.28 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVqsgiay 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMGL--SRFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILD 158
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLqlAGVEKMQRLEIAHQMLKKVG-LEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
..
gi 503995501 159 EP 160
Cdd:PRK11248 154 EP 155
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-217 |
2.03e-18 |
|
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: 80.23 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHrKPHQRVQSGIAYVPQGREIFPRlTVEE 95
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISK-IGLHDLRSRISIIPQDPVLFSG-TIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 96 NLlmglsrfparDA--RAVPEEIYQ-------------LFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEP 160
Cdd:cd03244 97 NL----------DPfgEYSDEELWQalervglkefvesLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995501 161 TEGIQPSVIKEIGEVIRQlaNRGDMAILLVeqfydfAAGL-----ADRYLVMSRGAIIQQGN 217
Cdd:cd03244 167 TASVDPETDALIQKTIRE--AFKDCTVLTI------AHRLdtiidSDRILVLDKGRVVEFDS 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-216 |
2.25e-18 |
|
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: 80.15 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHrKPHQRVQSGIAYVPQGREIFPRlTVEE 95
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIST-IPLEDLRSSLTIIPQDPTLFSG-TIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 96 NLlmglsrfparDaravPEEIY---QLFPVLKTmkqRRGGD-LSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKE 171
Cdd:cd03369 101 NL----------D----PFDEYsdeEIYGALRV---SEGGLnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503995501 172 IGEVIRQLANRGDMAILL--VEQFYDFaaglaDRYLVMSRGAIIQQG 216
Cdd:cd03369 164 IQKTIREEFTNSTILTIAhrLRTIIDY-----DKILVMDAGEVKEYD 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-225 |
2.31e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.21 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKP---HQRVQSG 77
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 78 IAYVPQGREIFpRLTVEENLLMGLSRF---PARDARAVPEEIYQLFPvlKTMKQRRGGDLSGGQQQQLAIGRALASRPQL 154
Cdd:PRK13638 81 TVFQDPEQQIF-YTDIDSDIAFSLRNLgvpEAEITRRVDEALTLVDA--QHFRHQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995501 155 LILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFyDFAAGLADRYLVMSRGAIIQQGNGGDMEAEG 225
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDI-DLIYEISDAVYVLRQGQILTHGAPGEVFACT 227
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-224 |
2.51e-18 |
|
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: 83.17 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSgIAYVPQGREIFPRlTVEE 95
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH-IGYLPQDVELFPG-TVAE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 96 NLlmglSRFPAR-DARAVPE--------EIYQLFPV-LKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTegiq 165
Cdd:TIGR01842 411 NI----ARFGENaDPEKIIEaaklagvhELILRLPDgYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPN---- 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995501 166 pSVIKEIGEV-----IRQLANRGDMAILLVEQFYdfAAGLADRYLVMSRGAIIQQGNGGDMEAE 224
Cdd:TIGR01842 483 -SNLDEEGEQalanaIKALKARGITVVVITHRPS--LLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-216 |
2.70e-18 |
|
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: 80.45 E-value: 2.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAYvPQGREIFPRLTVEE- 95
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVF-GQKTQLWWDLPVIDs 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 96 -NLLMGLSRFPARDARAVPEEIYQLFPVLKTMKQ--RRggdLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEI 172
Cdd:cd03267 116 fYLLAAIYDLPPARFKKRLDELSELLDLEELLDTpvRQ---LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503995501 173 GEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:cd03267 193 RNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-209 |
2.79e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.54 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 11 YGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLwqeknithRKPHQRvqsgIAYVPQgreifpR 90
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKLR----IGYVPQ------K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 91 LTVEENLLMGLSRFPARDARAVPEEIyqlFPVLKTMK-----QRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQ 165
Cdd:PRK09544 76 LYLDTTLPLTVNRFLRLRPGTKKEDI---LPALKRVQaghliDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503995501 166 PSVIKEIGEVIRQLANRGDMAILLVEQfydfaaglaDRYLVMSR 209
Cdd:PRK09544 153 VNGQVALYDLIDQLRRELDCAVLMVSH---------DLHLVMAK 187
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
9-217 |
2.84e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 80.95 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 9 QYYG-GSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKpHQRVQSGIAYVPQGRE- 86
Cdd:PRK13648 16 QYQSdASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN-FEKLRKHIGIVFQNPDn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 87 IFPRLTVEENLLMGLSRFpardarAVP-EEIYQLFP-VLK--TMKQRRGGD---LSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:PRK13648 95 QFVGSIVKYDVAFGLENH------AVPyDEMHRRVSeALKqvDMLERADYEpnaLSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 160 PTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGlADRYLVMSRGAIIQQGN 217
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGT 225
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
9-160 |
3.03e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 82.20 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 9 QYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRvqsGIAYVPQGREIF 88
Cdd:PRK11650 12 SYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR---DIAMVFQNYALY 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 89 PRLTVEENLLMGLS--RFP-----ARDARAVpeEIYQLFPVLktmkQRRGGDLSGGQQQQLAIGRALASRPQLLILDEP 160
Cdd:PRK11650 89 PHMSVRENMAYGLKirGMPkaeieERVAEAA--RILELEPLL----DRKPRELSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-166 |
4.27e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.48 E-value: 4.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 3 QVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLkclmGLIP-AR---SGEVLWQEKNITHRKPHQRVQSGI 78
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL----SLIAgARkiqQGRVEVLGGDMADARHRRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 79 AYVPQG--REIFPRLTVEENL-----LMGLSRfPARDARAvpEEIYQ---LFPVLKtmkqRRGGDLSGGQQQQLAIGRAL 148
Cdd:NF033858 79 AYMPQGlgKNLYPTLSVFENLdffgrLFGQDA-AERRRRI--DELLRatgLAPFAD----RPAGKLSGGMKQKLGLCCAL 151
|
170
....*....|....*...
gi 503995501 149 ASRPQLLILDEPTEGIQP 166
Cdd:NF033858 152 IHDPDLLILDEPTTGVDP 169
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-216 |
4.48e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 79.50 E-value: 4.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 15 HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVlwqeknITHRKPHQRVQSGIAYVPQgreifprLTVE 94
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV------TVRGRVSSLLGLGGGFNPE-------LTGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 95 EN-----LLMGLSRfpaRDARAVPEEIYQlFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVI 169
Cdd:cd03220 103 ENiylngRLLGLSR---KEIDEKIDEIIE-FSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503995501 170 KEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:cd03220 179 EKCQRRLRELLKQG-KTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-161 |
6.15e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 80.93 E-value: 6.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGS-----------HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKP 70
Cdd:COG4608 8 LEVRDLKKHFPVRgglfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 71 HQ------RVQSgiayvpqgreIF--------PRLTVEENL-----LMGLSRFPARDARAV--------PEEIYQLFPvl 123
Cdd:COG4608 88 RElrplrrRMQM----------VFqdpyaslnPRMTVGDIIaeplrIHGLASKAERRERVAellelvglRPEHADRYP-- 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 503995501 124 ktmkqrrgGDLSGGQQQQLAIGRALASRPQLLILDEPT 161
Cdd:COG4608 156 --------HEFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-216 |
7.46e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.78 E-value: 7.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYY-GGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQ-RVQSGIA 79
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 80 YVPQGREIFPrLTVEENLLMGlsrfpARDARAVPEEIYQ-----LFPV-LKTMKQRRGGDLSGGQQQQLAIGRALASRPQ 153
Cdd:PRK13647 85 FQDPDDQVFS-STVWDDVAFG-----PVNMGLDKDEVERrveeaLKAVrMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995501 154 LLILDEPTEGIQPSVIKEIGEVIRQLANRGDmAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-216 |
8.27e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 80.52 E-value: 8.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 19 GVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQR--VQSGIAYVPQG--REIFPRLTVE 94
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWraVRSDIQMIFQDplASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 95 ENLLMGLSRF-PARDARAVPEEIYQLFP---VLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIK 170
Cdd:PRK15079 119 EIIAEPLRTYhPKLSRQEVKDRVKAMMLkvgLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503995501 171 EIGEVIRQLanRGDMAILLVEQFYDFAA--GLADRYLVMSRGAIIQQG 216
Cdd:PRK15079 199 QVVNLLQQL--QREMGLSLIFIAHDLAVvkHISDRVLVMYLGHAVELG 244
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-223 |
8.38e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 79.75 E-value: 8.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKP-HQRVQSGIAYVPQGREiFPRLTVEE 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVFQNPDNQ-FVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 96 NLLMGLSR--FPARDARAVPEEIYQLFPVLKtMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIG 173
Cdd:PRK13642 102 DVAFGMENqgIPREEMIKRVDEALLAVNMLD-FKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503995501 174 EVIRQLANRGDMAILLVEQFYDFAAGlADRYLVMSRGAIIQQGNGGDMEA 223
Cdd:PRK13642 181 RVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-221 |
9.62e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 79.49 E-value: 9.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPAR--------SGEVLWQEKNItHRKPHQ 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPL-AAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 73 RVQSGIAYVPQ-GREIFPrLTVEENLLMGlsRFParDARAVPEEIYQLFPVLKTMKQRRGGD---------LSGGQQQQL 142
Cdd:PRK13547 80 RLARLRAVLPQaAQPAFA-FSAREIVLLG--RYP--HARRAGALTHRDGEIAWQALALAGATalvgrdvttLSGGELARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 143 AIGRALA---------SRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAII 213
Cdd:PRK13547 155 QFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
....*...
gi 503995501 214 QQGNGGDM 221
Cdd:PRK13547 235 AHGAPADV 242
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-225 |
1.07e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 79.30 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLiPAR---SGEVLWQEKNITHRKPHQRVQSG 77
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PAYkilEGDILFKGESILDLEPEERAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 78 IAYVPQgreiFPrltVE------ENLLMgLSRFPARDARAVPE----EIYQLF-PVLK--TMKQR-------RGgdLSGG 137
Cdd:CHL00131 86 IFLAFQ----YP---IEipgvsnADFLR-LAYNSKRKFQGLPEldplEFLEIInEKLKlvGMDPSflsrnvnEG--FSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 138 QQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRgDMAILLVEQFYDFAAGLADRYL-VMSRGAIIQQG 216
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRLLDYIKPDYVhVMQNGKIIKTG 234
|
250
....*....|..
gi 503995501 217 N---GGDMEAEG 225
Cdd:CHL00131 235 DaelAKELEKKG 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-216 |
1.26e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.00 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 19 GVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVL------WQEknITHRKPHQ--RVQSGIAYVPQGREIFPR 90
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdeWVD--MTKPGPDGrgRAKRYIGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 91 LTVEENLLMGLS-RFParDARAVPEEIYQLFPV------LKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEG 163
Cdd:TIGR03269 380 RTVLDNLTEAIGlELP--DELARMKAVITLKMVgfdeekAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503995501 164 IQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-216 |
1.30e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.46 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMG-LIPARSGEVLWQEKNIT-HRKPHQRVQSGIAYVPQGRE-IFPRLT 92
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDNPNSKITVDGITlTAKTVWDIREKVGIVFQNPDnQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 93 VEENLLMGLsrfparDARAVPEEiyQLFPVLKTMKQRRG---------GDLSGGQQQQLAIGRALASRPQLLILDEPTEG 163
Cdd:PRK13640 102 VGDDVAFGL------ENRAVPRP--EMIKIVRDVLADVGmldyidsepANLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503995501 164 IQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGlADRYLVMSRGAIIQQG 216
Cdd:PRK13640 174 LDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQG 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-217 |
1.31e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 79.74 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAYVPQGREIFPRL----- 91
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKTRFKKIkkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 92 -------------------TVEENLLMGLSRF--PARDARAVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALAS 150
Cdd:PRK13651 103 irrrvgvvfqfaeyqlfeqTIEKDIIFGPVSMgvSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503995501 151 RPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDmAILLVEQFYDFAAGLADRYLVMSRGAIIQQGN 217
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKIIKDGD 248
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
9-212 |
2.60e-17 |
|
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: 76.49 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 9 QYYGGSH-ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSgIAYVPQGREI 87
Cdd:cd03246 9 RYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH-VGYLPQDDEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 88 FPRlTVEENLlmglsrfpardaravpeeiyqlfpvlktmkqrrggdLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPS 167
Cdd:cd03246 88 FSG-SIAENI------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503995501 168 VIKEIGEVIRQLANRGDMAILLVEQFYDFAAglADRYLVMSRGAI 212
Cdd:cd03246 131 GERALNQAIAALKAAGATRIVIAHRPETLAS--ADRILVLEDGRV 173
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-220 |
3.48e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.92 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARS--GEVLwqeknITHRKPHQRVQSGIAYVPQGREIFPRLTV 93
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTIL-----ANNRKPTKQILKRTGFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 94 EENLLM-GLSRFP----ARDARAVPEEIYQLFPVLKTMKQRRGGD----LSGGQQQQLAIGRALASRPQLLILDEPTEGI 164
Cdd:PLN03211 158 RETLVFcSLLRLPksltKQEKILVAESVISELGLTKCENTIIGNSfirgISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503995501 165 QPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGD 220
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-190 |
3.51e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.57 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAYVPQGREIFPRLTVEEN 96
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 97 LLMGlsRFPAR----DARAVpeeIYQLFPVLKTM-----KQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPS 167
Cdd:PRK11288 100 LYLG--QLPHKggivNRRLL---NYEAREQLEHLgvdidPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR 174
|
170 180
....*....|....*....|...
gi 503995501 168 VIKEIGEVIRQLANRGdMAILLV 190
Cdd:PRK11288 175 EIEQLFRVIRELRAEG-RVILYV 196
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-217 |
4.35e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.50 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 20 VDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARsGEVLWQ-----EKNITHRKPHqrvqsgIAYVPQGreifPRL--- 91
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINgielrELDPESWRKH------LSWVGQN----PQLphg 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 92 TVEENLLMGlsRFPARDARA--------VPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEG 163
Cdd:PRK11174 438 TLRDNVLLG--NPDASDEQLqqalenawVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503995501 164 IQPSVIKEIGEVIRQlANRGDMAILLVEQFYDFAAglADRYLVMSRGAIIQQGN 217
Cdd:PRK11174 516 LDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQ--WDQIWVMQDGQIVQQGD 566
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-216 |
4.78e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 79.36 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 15 HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARsGEVLWQEKNITHRKPHQR--VQSGIAYVPQ--GREIFPR 90
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLlpVRHRIQVVFQdpNSSLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 91 LTVEENLLMGLS-RFPARDARAVPEEiyqlfpVLKTM---------KQRRGGDLSGGQQQQLAIGRALASRPQLLILDEP 160
Cdd:PRK15134 379 LNVLQIIEEGLRvHQPTLSAAQREQQ------VIAVMeevgldpetRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503995501 161 TEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-210 |
7.66e-17 |
|
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: 75.74 E-value: 7.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCL-----MGLIparSGEVLwqeknITHRKPHQRVQSGIAYVPQGREIFPR 90
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVI---TGEIL-----INGRPLDKNFQRSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 91 LTVEENLlmglsRFPArdaravpeeiyqlfpVLktmkqrRGgdLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIK 170
Cdd:cd03232 94 LTVREAL-----RFSA---------------LL------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503995501 171 EIGEVIRQLANRGdMAIL---------LVEQFydfaaglaDRYLVMSRG 210
Cdd:cd03232 146 NIVRFLKKLADSG-QAILctihqpsasIFEKF--------DRLLLLKRG 185
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-200 |
8.96e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 76.36 E-value: 8.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYG-GSH---ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQ- 75
Cdd:PRK10584 6 IVEVHHLKKSVGqGEHelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 76 --SGIAYVPQGREIFPRLTVEEN-----LLMGLSRFPARDARAVPEEIYQLFPVLKTMKQRrggdLSGGQQQQLAIGRAL 148
Cdd:PRK10584 86 raKHVGFVFQSFMLIPTLNALENvelpaLLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ----LSGGEQQRVALARAF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503995501 149 ASRPQLLILDEPTegiqpsvikeiGEVIRQLANRgdMAILLVEQFYDFAAGL 200
Cdd:PRK10584 162 NGRPDVLFADEPT-----------GNLDRQTGDK--IADLLFSLNREHGTTL 200
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-217 |
1.00e-16 |
|
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: 76.11 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 9 QYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQrVQSGIAYVPQGREIF 88
Cdd:cd03253 9 AYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS-LRRAIGVVPQDTVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 89 PRlTVEENLLMGlsrfparDARAVPEEIY------QLFPVLKTMKQ-------RRGGDLSGGQQQQLAIGRALASRPQLL 155
Cdd:cd03253 88 ND-TIGYNIRYG-------RPDATDEEVIeaakaaQIHDKIMRFPDgydtivgERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995501 156 ILDEPTEGIQPSVIKEIGEVIRQLAnRGDMAILLVEQFYDFAAglADRYLVMSRGAIIQQGN 217
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN--ADKIIVLKDGRIVERGT 218
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-217 |
1.19e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 78.33 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYY--GGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRkPHQRVQSGIA 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY-SEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 80 YVPQGREIFPRlTVEENLLMGLSRfpARDAravpeeiyQLFPVL------KTMKQRRG-----GD----LSGGQQQQLAI 144
Cdd:PRK11160 418 VVSQRVHLFSA-TLRDNLLLAAPN--ASDE--------ALIEVLqqvgleKLLEDDKGlnawlGEggrqLSGGEQRRLGI 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 145 GRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLAnrGDMAILLV-------EQFydfaaglaDRYLVMSRGAIIQQGN 217
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA--QNKTVLMIthrltglEQF--------DRICVMDNGQIIEQGT 556
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-216 |
1.29e-16 |
|
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: 76.04 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQrVQSGIAYVPQGREIFPRlTVEE 95
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRW-LRSQIGLVSQEPVLFDG-TIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 96 NLLMGlsRFPARDA---RAVPE-EIYQL---FP-VLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPS 167
Cdd:cd03249 96 NIRYG--KPDATDEeveEAAKKaNIHDFimsLPdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503995501 168 VIKEIGEVIRQLAnRGDMAILLveqfydfAAGL-----ADRYLVMSRGAIIQQG 216
Cdd:cd03249 174 SEKLVQEALDRAM-KGRTTIVI-------AHRLstirnADLIAVLQNGQVVEQG 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-202 |
2.34e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.59 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKC---LMGLIP-AR-SGEVLWQEKNI--THRKPHQrV 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPgFRvEGKVTFHGKNLyaPDVDPVE-V 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 75 QSGIAYVPQGREIFPRlTVEENLLMG--LSRFPARDARAVPEEIYQ--LFPVLKTMKQRRGGDLSGGQQQQLAIGRALAS 150
Cdd:PRK14243 90 RRRIGMVFQKPNPFPK-SIYDNIAYGarINGYKGDMDELVERSLRQaaLWDEVKDKLKQSGLSLSGGQQQRLCIARAIAV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503995501 151 RPQLLILDEPTEGIQPSVIKEIGEVIRQLANRgdMAILLVEQFYDFAAGLAD 202
Cdd:PRK14243 169 QPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-217 |
2.68e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.81 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQE----KNITHRKPHQRVQSGIAYVPQgreiFPRL- 91
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEVKRLRKEIGLVFQ----FPEYq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 92 ----TVEENLLMGLSRFPARDaravpEEIYQLFPVLKTMKQ-------RRGGDLSGGQQQQLAIGRALASRPQLLILDEP 160
Cdd:PRK13645 103 lfqeTIEKDIAFGPVNLGENK-----QEAYKKVPELLKLVQlpedyvkRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503995501 161 TEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGN 217
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
16-210 |
3.90e-16 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 74.37 E-value: 3.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRV---QSGIAYVPQGREIFPRLT 92
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIilrRELIGYIFQSFNLIPHLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 93 VEENLLMGLSRfpardaRAVP--EEIYQLFPVLKTM-----KQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQ 165
Cdd:NF038007 100 IFDNVALPLKY------RGVAkkERIERVNQVLNLFgidnrRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503995501 166 PSVIKEIGEVIRQLANRGDMAILLVEQfyDFAAGLADRYLVMSRG 210
Cdd:NF038007 174 SKNARAVLQQLKYINQKGTTIIMVTHS--DEASTYGNRIINMKDG 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-211 |
4.41e-16 |
|
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: 76.98 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHIlRGVD---FAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKphQRVQSG 77
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSS-PAVDrlcVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNI--SDVHQN 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 78 IAYVPQGREIFPRLTVEENLLM--GLSRFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLL 155
Cdd:TIGR01257 2014 MGYCPQFDAIDDLLTGREHLYLyaRLRGVPAEEIEKVANWSIQSLG-LSLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503995501 156 ILDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGA 211
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSIIREG-RAVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
13-183 |
4.62e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 76.31 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 13 GSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQSGIAYVPQGREIFPRLT 92
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 93 VEENLLMGlsRFPA-----------RDARAVPEEIYqlfpvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPT 161
Cdd:PRK10982 90 VMDNMWLG--RYPTkgmfvdqdkmyRDTKAIFDELD-----IDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180
....*....|....*....|..
gi 503995501 162 EGIQPSVIKEIGEVIRQLANRG 183
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERG 184
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-224 |
4.69e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 75.93 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTllkclmGLIPAR-----SGEVLWQEKN-ITHRKPHQRVQ 75
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAHv*gpdAGRRPWRF*TwCANRRALRRTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 76 SGIAYVPQGREifPRLTVEENLLM-----GLSRfpaRDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALAS 150
Cdd:NF000106 88 G*HRPVR*GRR--ESFSGRENLYMigr*lDLSR---KDARARADELLERFS-LTEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995501 151 RPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDMEAE 224
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDG-ATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-166 |
6.82e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 76.32 E-value: 6.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 20 VDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGE--VLWQE---KNITHRKphqRVqsgiAYVPQGREIFPRLTVE 94
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawLFGQPvdaGDIATRR---RV----GYMSQAFSLYGELTVR 357
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995501 95 ENLLMG--LSRFPARDARAVPEEIYQLFPVLKTMKQrRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQP 166
Cdd:NF033858 358 QNLELHarLFHLPAAEIAARVAEMLERFDLADVADA-LPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP 430
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-210 |
1.42e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 75.53 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCL-----MGLIpaRSGEVLwqeknITHRKPHQRVQSGIAYVPQGREIFPR 90
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRL-----VNGRPLDSSFQRSIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 91 LTVEENLlmglsRFPA--RDARAVP--------EEIYQLFPvLKTMKQR----RGGDLSGGQQQQLAIGRALASRPQLLI 156
Cdd:TIGR00956 851 STVRESL-----RFSAylRQPKSVSksekmeyvEEVIKLLE-MESYADAvvgvPGEGLNVEQRKRLTIGVELVAKPKLLL 924
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995501 157 -LDEPTEGIQPSVIKEIGEVIRQLANRGDmAIL---------LVEQFydfaaglaDRYLVMSRG 210
Cdd:TIGR00956 925 fLDEPTSGLDSQTAWSICKLMRKLADHGQ-AILctihqpsaiLFEEF--------DRLLLLQKG 979
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
11-226 |
1.44e-15 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 75.14 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 11 YGGSHI--LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKpHQRVQSGIAYVPQGREIF 88
Cdd:TIGR02203 340 YPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT-LASLRRQVALVSQDVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 89 PRlTVEENLLMG-LSRFPARDARAVPEEIY------QLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPT 161
Cdd:TIGR02203 419 ND-TIANNIAYGrTEQADRAEIERALAAAYaqdfvdKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995501 162 EGIQPSVIKEIGEVIRQL-ANRGDMAIllveqfydfAAGL-----ADRYLVMSRGAIIQQGNGGD-MEAEGV 226
Cdd:TIGR02203 498 SALDNESERLVQAALERLmQGRTTLVI---------AHRLstiekADRIVVMDDGRIVERGTHNElLARNGL 560
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-216 |
1.60e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.28 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 26 QGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIT--HRKPHQRvqsGIAYVPQGREIFPRLTVEENLLMG--- 100
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFAR---KVAYLPQQLPAAEGMTVRELVAIGryp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 101 ----LSRFPARDARAVPEEIYQLFpvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVI 176
Cdd:PRK10575 113 whgaLGRFGAADREKVEEAISLVG--LKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALV 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503995501 177 RQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK10575 191 HRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
27-226 |
1.67e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.01 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 27 GEITCLLGRNGVGKTTLLKCLMG-LIPARSGEVLwqeknithrkphqrVQSGIAYVPQGREIFpRLTVEENLLMGLSRFP 105
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVV--------------IRGSVAYVPQVSWIF-NATVRENILFGSDFES 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 106 ARDARAVPEEIYQ----LFPVL-KTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLA 180
Cdd:PLN03232 708 ERYWRAIDVTALQhdldLLPGRdLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDE 787
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503995501 181 NRGDMAILLVEQFYDFAagLADRYLVMSRGAIIQQGNGGDMEAEGV 226
Cdd:PLN03232 788 LKGKTRVLVTNQLHFLP--LMDRIILVSEGMIKEEGTFAELSKSGS 831
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-213 |
2.59e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.06 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 8 HQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGlipaRS------GEVLWQEKNITHRKPHQRVQSGIAYV 81
Cdd:NF040905 267 HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG----RSygrnisGTVFKDGKEVDVSTVSDAIDAGLAYV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREifpRL------TVEENL----LMGLSRFPARDARA---VPEEiYQlfpvlKTMKQR------RGGDLSGGQQQQL 142
Cdd:NF040905 343 TEDRK---GYglnlidDIKRNItlanLGKVSRRGVIDENEeikVAEE-YR-----KKMNIKtpsvfqKVGNLSGGNQQKV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995501 143 AIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAII 213
Cdd:NF040905 414 VLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEG-KGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-217 |
3.25e-15 |
|
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: 74.07 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGL--IPARSGEVLW-------------QEKNIT 66
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 67 H-------------------RKPHQRVQSGIAYVPQGR-EIFPRLTVEENLLMGLSR--FPARDA--RAVpEEIYQLFPV 122
Cdd:TIGR03269 81 PcpvcggtlepeevdfwnlsDKLRRRIRKRIAIMLQRTfALYGDDTVLDNVLEALEEigYEGKEAvgRAV-DLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 123 LKTMKQRRggDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLAD 202
Cdd:TIGR03269 160 HRITHIAR--DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250
....*....|....*
gi 503995501 203 RYLVMSRGAIIQQGN 217
Cdd:TIGR03269 238 KAIWLENGEIKEEGT 252
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-192 |
3.50e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 71.52 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIthRKPHQRVQSGIAY 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--KKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQGREIFPRLTVEENLLMGLsRFPARDARAvpEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEP 160
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDI-HFSPGAVGI--TELCRLFS-LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 503995501 161 TEGIQPSVIKEIGEVIRQLANRGDMAILLVEQ 192
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-214 |
3.62e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.55 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNI---THRKPHQRVQSGIAYVPQgreiFPRL-- 91
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpeTGNKNLKKLRKKVSLVFQ----FPEAql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 92 ---TVEENLLMGLSRFPARDARAVPEEIYQLFPV-LKT-MKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQP 166
Cdd:PRK13641 99 fenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVgLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503995501 167 SVIKEIGEVIRQLANRGDMAILLVEQFYDFAAgLADRYLVMSRGAIIQ 214
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGHTVILVTHNMDDVAE-YADDVLVLEHGKLIK 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-216 |
3.74e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.96 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHR---------------KPHQRVQSGIAY 80
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKknnhelitnpyskkiKNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 81 VPQgreiFP-----RLTVEENLLMGLSRFPARDARAVPEEIYQLFPV-LK-TMKQRRGGDLSGGQQQQLAIGRALASRPQ 153
Cdd:PRK13631 121 VFQ----FPeyqlfKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMgLDdSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995501 154 LLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFyDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTM-EHVLEVADEVIVMDKGKILKTG 258
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-210 |
5.28e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 71.44 E-value: 5.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 10 YYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRK----PHQRVQSGIAYvpQGR 85
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnrevPFLRRQIGMIF--QDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 86 EIFPRLTVEENLLMGLSRFPA------RDARAVPEEIYQL-----FPVlktmkqrrggDLSGGQQQQLAIGRALASRPQL 154
Cdd:PRK10908 89 HLLMDRTVYDNVAIPLIIAGAsgddirRRVSAALDKVGLLdkaknFPI----------QLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503995501 155 LILDEPTEGIQPSVIKEIGEVIRQLaNRGDMAILLVEQFYDFAAGLADRYLVMSRG 210
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-214 |
7.27e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 7.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 15 HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIthrkPHQRVQSGIAYVPQGREIfprLTVE 94
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN----QFGREASLIDAIGRKGDF---KDAV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 95 ENL-LMGLSrfparDAravpeeiyQLFpvlktmkQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIG 173
Cdd:COG2401 117 ELLnAVGLS-----DA--------VLW-------LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503995501 174 EVIRQLANRGDMAILLVEQFYDFAAGLA-DRYLVMSRGAIIQ 214
Cdd:COG2401 177 RNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-161 |
1.13e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 72.23 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKnithrkphqrvqSGIAYV 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN------------ANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREI-FPRltvEENLL--MGLSRFPARDARAVPEEIYQ-LFP---VLKTMKQrrggdLSGGQQQQLAIGRALASRPQL 154
Cdd:PRK15064 388 AQDHAYdFEN---DLTLFdwMSQWRQEGDDEQAVRGTLGRlLFSqddIKKSVKV-----LSGGEKGRMLFGKLMMQKPNV 459
|
....*..
gi 503995501 155 LILDEPT 161
Cdd:PRK15064 460 LVMDEPT 466
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
32-217 |
1.19e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.44 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 32 LLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIThRKPHQRVQSGIAYVPQ---------------GREIfprltVEEN 96
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-SLSHSVLRQGVAMVQQdpvvladtflanvtlGRDI-----SEEQ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 97 LLMGLSRFP-ARDARAVPEEIYqlfpvlkTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEV 175
Cdd:PRK10790 446 VWQALETVQlAELARSLPDGLY-------TPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQA 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503995501 176 IRQLANRGDMAIL------LVEqfydfaaglADRYLVMSRGAIIQQGN 217
Cdd:PRK10790 519 LAAVREHTTLVVIahrlstIVE---------ADTILVLHRGQAVEQGT 557
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-217 |
2.98e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.34 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 15 HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWqeknithrkpHQRVQS----GIAYVPQgreifpr 90
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV----------NGRVSAllelGAGFHPE------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 91 LTVEEN-----LLMGLSRfpaRDARAVPEEI----------YQlfPVlKTmkqrrggdLSGGQQQQLAIGRALASRPQLL 155
Cdd:COG1134 103 LTGRENiylngRLLGLSR---KEIDEKFDEIvefaelgdfiDQ--PV-KT--------YSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995501 156 ILDEPTegiqpSVikeiG---------EVIRQLANRGdMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGN 217
Cdd:COG1134 169 LVDEVL-----AV----GdaafqkkclARIRELRESG-RTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-161 |
4.67e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.61 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 13 GSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVlwqeknitHRKPHQRV----QSgiAYVPQG--RE 86
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGARVlflpQR--PYLPLGtlRE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 87 I---------FPRLTVEENL-LMGLSRFPAR-DARAVPEEIyqlfpvlktmkqrrggdLSGGQQQQLAIGRALASRPQLL 155
Cdd:COG4178 445 AllypataeaFSDAELREALeAVGLGHLAERlDEEADWDQV-----------------LSLGEQQRLAFARLLLHKPDWL 507
|
....*.
gi 503995501 156 ILDEPT 161
Cdd:COG4178 508 FLDEAT 513
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-216 |
6.28e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.06 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQE---KNITHRKPHQRVQSGI 78
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 79 AYVPQGREIFPRLTVEENLLMG--LSRFPARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLI 156
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGmeLAGINAEERREKALDALRQVG-LENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 157 LDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-217 |
8.49e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.88 E-value: 8.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLwQEKNITHRKPHQRVQSGIAYVPQGRE--------IF 88
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ-CDKMLLRRRSRQVIELSEQSAAQMRHvrgadmamIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 89 --------PRLTVEEN------LLMGLSRFPA-RDARAVPEEIYqlFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQ 153
Cdd:PRK10261 111 qepmtslnPVFTVGEQiaesirLHQGASREEAmVEAKRMLDQVR--IPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995501 154 LLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGN 217
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
26-166 |
1.02e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.25 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 26 QGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNI--THRKPHQRVQSGIAYVPQGREIFPRLTVEENLlmglsR 103
Cdd:PRK11831 32 RGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpaMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNV-----A 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503995501 104 FPARDARAVPEeiyqlfPVLKT---MKQR----RGG------DLSGGQQQQLAIGRALASRPQLLILDEPTEGIQP 166
Cdd:PRK11831 107 YPLREHTQLPA------PLLHStvmMKLEavglRGAaklmpsELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-221 |
1.21e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.98 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 21 DFAARQGEITCLLGRNGVGKTTLLKCLMGLIPAR---SGEVLWQEKNITHRKPHQ--RVQS-GIAYVPQG--REIFPRLT 92
Cdd:PRK09473 36 NFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKElnKLRAeQISMIFQDpmTSLNPYMR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 93 VEENL---LM---GLSRfpardARAVPEEIYQLFPVLKTMKQRRGG----DLSGGQQQQLAIGRALASRPQLLILDEPTE 162
Cdd:PRK09473 116 VGEQLmevLMlhkGMSK-----AEAFEESVRMLDAVKMPEARKRMKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 163 GIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDM 221
Cdd:PRK09473 191 ALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-206 |
1.38e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 24 ARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKnithrkphqrvqsgIAYVPQGREIFPRLTVEENLLMGLSR 103
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK--------------ISYKPQYIKPDYDGTVEDLLRSITDD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 104 FparDARAVPEEIyqLFPV-LKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPT------EGIQpsvikeIGEVI 176
Cdd:PRK13409 428 L---GSSYYKSEI--IKPLqLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSahldveQRLA------VAKAI 496
|
170 180 190
....*....|....*....|....*....|...
gi 503995501 177 RQLANRGDMAILLVE---QFYDFaagLADRYLV 206
Cdd:PRK13409 497 RRIAEEREATALVVDhdiYMIDY---ISDRLMV 526
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-216 |
1.54e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.37 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIP----ARSGEVLWQEKNITHRKPHQRVQSgiAYVPQGREIFPRL 91
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKKHYRGDV--VYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 92 TVEENL------------LMGLSRFP-ARDARAVPEEIYQLfpvLKTMKQRRGGDL----SGGQQQQLAIGRALASRPQL 154
Cdd:TIGR00956 154 TVGETLdfaarcktpqnrPDGVSREEyAKHIADVYMATYGL---SHTRNTKVGNDFvrgvSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503995501 155 LILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLV-----EQFYDfaagLADRYLVMSRGAIIQQG 216
Cdd:TIGR00956 231 QCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyqcsQDAYE----LFDKVIVLYEGYQIYFG 293
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-220 |
2.23e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.04 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVlWQEKNithrkphqrvqsgIAYVPQGREIFpRLTVEE 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERS-------------IAYVPQQAWIM-NATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 96 NLLMGLSRFPARDARAV-----PEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIK 170
Cdd:PTZ00243 740 NILFFDEEDAARLADAVrvsqlEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503995501 171 EIGEVIRQLANRGDMAILLVEQFYDFAagLADRYLVMSRGAIIQQGNGGD 220
Cdd:PTZ00243 820 RVVEECFLGALAGKTRVLATHQVHVVP--RADYVVALGDGRVEFSGSSAD 867
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-221 |
5.15e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 67.07 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHI-LRGVD---FAARQGEITCLLGRNGVGKTTLLKCLMGLI--PAR-SGEVL-WQEKNITHRKPHQ 72
Cdd:PRK11022 3 LLNVDKLSVHFGDESApFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdyPGRvMAEKLeFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 73 R---VQSGIAYVPQ------------GREIFPRLTVEEnllmGLSRfPARDARAV----------PEEIYQLFPvlktmk 127
Cdd:PRK11022 83 RrnlVGAEVAMIFQdpmtslnpcytvGFQIMEAIKVHQ----GGNK-KTRRQRAIdllnqvgipdPASRLDVYP------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 128 qrrgGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVM 207
Cdd:PRK11022 152 ----HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVM 227
|
250
....*....|....
gi 503995501 208 SRGAIIQQGNGGDM 221
Cdd:PRK11022 228 YAGQVVETGKAHDI 241
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-179 |
5.22e-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: 64.48 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVlwqeknithRKPhqrVQSGIAYVPQgREIFPRLTVEE 95
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------GMP---EGEDLLFLPQ-RPYLPLGTLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 96 NLLmglsrFPARDAravpeeiyqlfpvlktmkqrrggdLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEV 175
Cdd:cd03223 83 QLI-----YPWDDV------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
....
gi 503995501 176 IRQL 179
Cdd:cd03223 134 LKEL 137
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-161 |
5.33e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 11 YGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHR---KPHQRVQ--------SGIA 79
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARlqqDPPRNVEgtvydfvaEGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 80 YVPQGREIFPRLT--VE----ENLLMGLSRFPAR---------DARavpeeIYQLFPVLKTMKQRRGGDLSGGQQQQLAI 144
Cdd:PRK11147 93 EQAEYLKRYHDIShlVEtdpsEKNLNELAKLQEQldhhnlwqlENR-----INEVLAQLGLDPDAALSSLSGGWLRKAAL 167
|
170
....*....|....*..
gi 503995501 145 GRALASRPQLLILDEPT 161
Cdd:PRK11147 168 GRALVSNPDVLLLDEPT 184
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-161 |
6.70e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 67.12 E-value: 6.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARS--GEVLWQEKNITHRKPHQRVQSGIAYVPQGREIFPRLTVE 94
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEALGIVIIHQELALIPYLSIA 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995501 95 ENLLMG--LSRFPARDARAVPEEIYQLfpvLKTMK-----QRRGGDLSGGQQQQLAIGRALASRPQLLILDEPT 161
Cdd:NF040905 97 ENIFLGneRAKRGVIDWNETNRRAREL---LAKVGldespDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-206 |
8.75e-13 |
|
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: 66.73 E-value: 8.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 24 ARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKnithrkphqrvqsgIAYVPQGREIFPRLTVEENLlmglsr 103
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--------------ISYKPQYISPDYDGTVEEFL------ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 104 fpaRDA--RAVPEEIYQ---LFPV-LKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPT------EGIqpsvikE 171
Cdd:COG1245 423 ---RSAntDDFGSSYYKteiIKPLgLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSahldveQRL------A 493
|
170 180 190
....*....|....*....|....*....|....*...
gi 503995501 172 IGEVIRQLANRGDMAILLVE---QFYDFaagLADRYLV 206
Cdd:COG1245 494 VAKAIRRFAENRGKTAMVVDhdiYLIDY---ISDRLMV 528
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-225 |
1.25e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 15 HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGevlwqeKNITHRkphqrvqSGIAYVPQGREIFpRLTVE 94
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD------ASVVIR-------GTVAYVPQVSWIF-NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 95 ENLLMGLSRFPARDARAVPEEIYQ----LFPVLK-TMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVI 169
Cdd:PLN03130 697 DNILFGSPFDPERYERAIDVTALQhdldLLPGGDlTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVG 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503995501 170 KEIGEVIRQLANRGDMAILLVEQFYDFAAglADRYLVMSRGAIIQQGNGGDMEAEG 225
Cdd:PLN03130 777 RQVFDKCIKDELRGKTRVLVTNQLHFLSQ--VDRIILVHEGMIKEEGTYEELSNNG 830
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
10-227 |
1.46e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 66.14 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 10 YYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIT--HRKPHQRvqsGIAYVPQGREI 87
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRtvTRASLRR---NIAVVFQDAGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 88 FPRlTVEENLLMGlsrfparDARAVPEEIYQLFPV-------------LKTMKQRRGGDLSGGQQQQLAIGRALASRPQL 154
Cdd:PRK13657 421 FNR-SIEDNIRVG-------RPDATDEEMRAAAERaqahdfierkpdgYDTVVGERGRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 155 LILDEPTEGIQPSV---IKEIGEVIRQlaNRGDMAIllveqfydfAAGL-----ADRYLVMSRGAIIQQGNGGDMEAEGV 226
Cdd:PRK13657 493 LILDEATSALDVETeakVKAALDELMK--GRTTFII---------AHRLstvrnADRILVFDNGRVVESGSFDELVARGG 561
|
.
gi 503995501 227 R 227
Cdd:PRK13657 562 R 562
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-160 |
1.84e-12 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 64.27 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITH---RKPHQRVQSGIAYVPQgREIFPRLTV 93
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEpsfEATRSRNRYSVAYAAQ-KPWLLNATV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995501 94 EENLLMGlSRFPARDARAVPEEIyQLFPVL-------KTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEP 160
Cdd:cd03290 96 EENITFG-SPFNKQRYKAVTDAC-SLQPDIdllpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-223 |
5.91e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.27 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 20 VDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQRVQsgiayvpQGREIF--------PRL 91
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQ-------RIRMIFqdpstslnPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 92 TVEENLLMGLSRFPARDARAVPEEIYQLFPVLKTMKQRRG---GDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSV 168
Cdd:PRK15112 105 RISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASyypHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503995501 169 IKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGNGGDMEA 223
Cdd:PRK15112 185 RSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-206 |
7.15e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 62.81 E-value: 7.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 25 RQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNithrkphqrvqsgIAYVPQGREIFPRLTVEEnLLMGLSRF 104
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-------------VSYKPQYIKADYEGTVRD-LLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 105 PARDARAVPEEI--YQLFPVLktmkQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANR 182
Cdd:cd03237 89 FYTHPYFKTEIAkpLQIEQIL----DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAEN 164
|
170 180
....*....|....*....|....
gi 503995501 183 GDMAILLVEQFYDFAAGLADRYLV 206
Cdd:cd03237 165 NEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-188 |
8.27e-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: 64.04 E-value: 8.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 25 RQGEITCLLGRNGVGKTTLLKCLMG-LIP---ARSGEVLWQEknITHR------KPH-QRVQSG---IAYVPQGREIFPR 90
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGeLKPnlgDYDEEPSWDE--VLKRfrgtelQDYfKKLANGeikVAHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 91 L---TVEEnLLMGLsrfparDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTegiqpS 167
Cdd:COG1245 175 VfkgTVRE-LLEKV------DERGKLDELAEKLG-LENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS-----S 241
|
170 180 190
....*....|....*....|....*....|....
gi 503995501 168 V--IKE---IGEVIRQLANRG--------DMAIL 188
Cdd:COG1245 242 YldIYQrlnVARLIRELAEEGkyvlvvehDLAIL 275
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-216 |
1.43e-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: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVlwqeknithrkphqRVQSGIAYVPQGREIfPRLTVEEN 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV--------------HMKGSVAYVPQQAWI-QNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 97 LLMGLSRFPARdARAVPEEIyQLFPVL-------KTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVI 169
Cdd:TIGR00957 719 ILFGKALNEKY-YQQVLEAC-ALLPDLeilpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503995501 170 KEIGE-VIRQLANRGDMAILLVEQFYDFAAGLaDRYLVMSRGAIIQQG 216
Cdd:TIGR00957 797 KHIFEhVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-224 |
5.26e-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: 61.85 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 13 GSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMG-LIPArsgevlwqEKNITHrkphqrvqSG-IAYVPQGREIFPR 90
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPS--------EGKIKH--------SGrISFSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 91 lTVEENLLMGLSRFPARDARAVP----EEIYQLFPVL-KTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQ 165
Cdd:TIGR01271 502 -TIKDNIIFGLSYDEYRYTSVIKacqlEEDIALFPEKdKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995501 166 PSVIKEIGE--VIRQLANRgdMAILLVEQFYDFAAglADRYLVMSRGAIIQQGNGGDMEAE 224
Cdd:TIGR01271 581 VVTEKEIFEscLCKLMSNK--TRILVTSKLEHLKK--ADKILLLHEGVCYFYGTFSELQAK 637
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
13-182 |
8.88e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 60.26 E-value: 8.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 13 GSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEvlwqeknITHrkphqrvqSG-IAYVPQGREIFPRl 91
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK-------IKH--------SGrISFSSQFSWIMPG- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 92 TVEENLLMGLSRFPAR-----DARAVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQP 166
Cdd:cd03291 113 TIKENIIFGVSYDEYRyksvvKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170
....*....|....*...
gi 503995501 167 SVIKEIGE--VIRQLANR 182
Cdd:cd03291 193 FTEKEIFEscVCKLMANK 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-216 |
9.41e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.00 E-value: 9.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVlWQEKNITHRKPHQRVQSGIAYV 81
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHYASKEVARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGREIFPRLTVEENLLMG-------LSRFPARDARAVPEEIYQlfPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQL 154
Cdd:PRK10253 87 AQNATTPGDITVQELVARGryphqplFTRWRKEDEEAVTKAMQA--TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995501 155 LILDEPTEGIQPSVIKEIGEVIRQLaNRgdmaillvEQFYDFAAGLAD-----RY----LVMSRGAIIQQG 216
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSEL-NR--------EKGYTLAAVLHDlnqacRYashlIALREGKIVAQG 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-217 |
1.01e-10 |
|
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: 60.99 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQrVQSGIAYVPQGREIFPRlTVEE 95
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS-LRAAIGIVPQDTVLFND-TIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 96 NLLMGlsrfparDARAVPEEIYQ-------------LFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDE--- 159
Cdd:COG5265 451 NIAYG-------RPDASEEEVEAaaraaqihdfiesLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEats 523
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 160 ----PTEgiqpsviKEIGEVIRQLA-NRGDMAIllveqfydfAAGL-----ADRYLVMSRGAIIQQGN 217
Cdd:COG5265 524 aldsRTE-------RAIQAALREVArGRTTLVI---------AHRLstivdADEILVLEAGRIVERGT 575
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-213 |
1.29e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.10 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLwqeknITHRKPHQRvqsGIAYVpqgREI--------- 87
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR-----VLGYVPFKR---RKEFA---RRIgvvfgqrsq 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 88 -FPRLTVEE--NLLMGLSRFPARDARAVPEEIYQLFPVLKTMKQ--RRggdLSGGQQQQLAIGRALASRPQLLILDEPTE 162
Cdd:COG4586 107 lWWDLPAIDsfRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTpvRQ---LSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 163 GIQPSVIKEIGEVIRQLANRGDMAILL-------VEQfydfaagLADRYLVMSRGAII 213
Cdd:COG4586 184 GLDVVSKEAIREFLKEYNRERGTTILLtshdmddIEA-------LCDRVIVIDHGRII 234
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-216 |
1.39e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.33 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPA----RSGEVLWQEKNITHRKPHQRVQSGIAYVPqgREIF-PR 90
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIATIMQNP--RSAFnPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 91 LT-----VEENLLMGLsrfPARDARAV----------PEEIYQLFPVlktmkqrrggDLSGGQQQQLAIGRALASRPQLL 155
Cdd:PRK10418 96 HTmhthaRETCLALGK---PADDATLTaaleavglenAARVLKLYPF----------EMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995501 156 ILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQG 223
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-226 |
2.34e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 59.65 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 17 LRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIT-HRKPHQRVQsgIAYVPQGREIFPRlTVEE 95
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdYTLASLRNQ--VALVSQNVHLFND-TIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 96 NLLMGLSRF--------PARDARAVpEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPS 167
Cdd:PRK11176 436 NIAYARTEQysreqieeAARMAYAM-DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995501 168 VIKEIGEVIRQL-ANRGDMAIL----LVEQfydfaaglADRYLVMSRGAIIQQGNGGD-MEAEGV 226
Cdd:PRK11176 515 SERAIQAALDELqKNRTSLVIAhrlsTIEK--------ADEILVVEDGEIVERGTHAElLAQNGV 571
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-161 |
4.76e-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: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKnithrkphqrVQsgIAYV 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET----------VK--LAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGRE-IFPRLTVEENLLMGLSRFPARDaRAVPEEIY-QLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:TIGR03719 391 DQSRDaLDPNKTVWEEISGGLDIIKLGK-REIPSRAYvGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDE 469
|
..
gi 503995501 160 PT 161
Cdd:TIGR03719 470 PT 471
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-161 |
4.94e-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: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 10 YYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVlWQEKNIThrkphqrvqsgIAYVPQGREIFP 89
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA-RPQPGIK-----------VGYLPQEPQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 90 RLTVEENLLMGLSrfPARDARAVPEEIYQLFP--------------VLKTMKQRRGG----------------------- 132
Cdd:TIGR03719 82 TKTVRENVEEGVA--EIKDALDRFNEISAKYAepdadfdklaaeqaELQEIIDAADAwdldsqleiamdalrcppwdadv 159
|
170 180 190
....*....|....*....|....*....|
gi 503995501 133 -DLSGGQQQQLAIGRALASRPQLLILDEPT 161
Cdd:TIGR03719 160 tKLSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-217 |
7.39e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.19 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSH--ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQrVQSGIA 79
Cdd:PRK10789 314 LDVNIRQFTYPQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS-WRSRLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 80 YVPQGREIFPRlTVEENLLMGLSRFPARD----AR--AVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQ 153
Cdd:PRK10789 393 VVSQTPFLFSD-TVANNIALGRPDATQQEiehvARlaSVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995501 154 LLILDEPTEGIQPSVIKEIGEVIRQLanrGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGN 217
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQW---GEGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-161 |
8.01e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 3 QVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVlwqeknithrkpHQRVQSGIAYVP 82
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------------HCGTKLEVAYFD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 83 QGREIF-PRLTVEENLLMG----------------LSRFpardaravpeeiyqLFPVLKTMKQRRGgdLSGGQQQQLAIG 145
Cdd:PRK11147 389 QHRAELdPEKTVMDNLAEGkqevmvngrprhvlgyLQDF--------------LFHPKRAMTPVKA--LSGGERNRLLLA 452
|
170
....*....|....*.
gi 503995501 146 RALASRPQLLILDEPT 161
Cdd:PRK11147 453 RLFLKPSNLLILDEPT 468
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-216 |
1.01e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.86 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 22 FAARQGEITCLLGRNGVGKTTLLKCLMGLIPArSGEVLWQEKNITHRKP----HQRvqsgiAYVPQGREIFPRLTVEENL 97
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAaelaRHR-----AYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 98 lmGLSRFPARDARAVPEEIYQLFPVLK-TMK-QRRGGDLSGGQQQQ-------LAIGRALASRPQLLILDEPTEGIQPSV 168
Cdd:PRK03695 91 --TLHQPDKTRTEAVASALNEVAEALGlDDKlGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503995501 169 IKEIGEVIRQLANRGdmaILLVEQFYDFAAGL--ADRYLVMSRGAIIQQG 216
Cdd:PRK03695 169 QAALDRLLSELCQQG---IAVVMSSHDLNHTLrhADRVWLLKQGKLLASG 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-216 |
1.07e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 15 HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPH--QRVQSGIAYVPQG--REIFPR 90
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQALRRDIQFIFQDpyASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 91 LTVEENLLMGL---SRFPARDARAVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPS 167
Cdd:PRK10261 418 QTVGDSIMEPLrvhGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503995501 168 VIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQG 216
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-191 |
1.42e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 25 RQGEITCLLGRNGVGKTTLLKCLMG-LIP---ARSGEVLWqEKNITHRKPH------QRVQSG---IAYVPQGREIFPRL 91
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILSGeLIPnlgDYEEEPSW-DEVLKRFRGTelqnyfKKLYNGeikVVHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 92 ---TVEEnLLMGLsrfparDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQpsv 168
Cdd:PRK13409 176 fkgKVRE-LLKKV------DERGKLDEVVERLG-LENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--- 244
|
170 180
....*....|....*....|....*.
gi 503995501 169 IKE---IGEVIRQLANrgDMAILLVE 191
Cdd:PRK13409 245 IRQrlnVARLIRELAE--GKYVLVVE 268
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
134-215 |
2.17e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.64 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 134 LSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAII 213
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
..
gi 503995501 214 QQ 215
Cdd:PRK15134 237 EQ 238
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-217 |
6.46e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.41 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGL--IPARSGEVLWQEKNITHRKPHQRVQSGI 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 79 AYVPQ--------GREIFPRLTV----EENLLMGLSRFPARDARAVPEEIYQLFPVLKTMKQRRGgdLSGGQQQQLAIGR 146
Cdd:PRK09580 81 FMAFQypveipgvSNQFFLQTALnavrSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVG--FSGGEKKRNDILQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995501 147 ALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANrGDMAILLVEQFYDFAAGLADRYL-VMSRGAIIQQGN 217
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSLRD-GKRSFIIVTHYQRILDYIKPDYVhVLYQGRIVKSGD 229
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-176 |
7.72e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVlwqEKNITHRKPHQRVQSgIAYVPQGREIFPRLTVEE 95
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI---QIDGKTATRGDRSRF-MAYLGHLPGLKADLSTLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 96 NL--LMGLSrfpARDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIG 173
Cdd:PRK13543 102 NLhfLCGLH---GRRAKQMPGSALAIVG-LAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVN 177
|
...
gi 503995501 174 EVI 176
Cdd:PRK13543 178 RMI 180
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-178 |
1.37e-08 |
|
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: 54.92 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYY--GGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIpARSGE-----VLWQEKNIthrkphQRV 74
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEiqidgVSWNSVTL------QTW 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 75 QSGIAYVPQGREIFPRlTVEENlLMGLSRFPARDARAVPEEI-----YQLFPVLKTMKQRRGG-DLSGGQQQQLAIGRAL 148
Cdd:TIGR01271 1291 RKAFGVIPQKVFIFSG-TFRKN-LDPYEQWSDEEIWKVAEEVglksvIEQFPDKLDFVLVDGGyVLSNGHKQLMCLARSI 1368
|
170 180 190
....*....|....*....|....*....|
gi 503995501 149 ASRPQLLILDEPTEGIQPSVIKEIGEVIRQ 178
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-188 |
1.49e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 54.34 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITH---------RKPHqrvqsgIAYVPQGRE 86
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadalaqlRREH------FGFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 87 IFPRLTVEEN-----LLMGLSRfPARDARAVpeeiyqlfpvlkTMKQRRG---------GDLSGGQQQQLAIGRALASRP 152
Cdd:PRK10535 97 LLSHLTAAQNvevpaVYAGLER-KQRLLRAQ------------ELLQRLGledrveyqpSQLSGGQQQRVSIARALMNGG 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 503995501 153 QLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAIL 188
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII 199
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-214 |
4.09e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIThrkphqrvQSGIAYVPQGREIFPRLTVee 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA--------KFGLTDLRRVLSIIPQSPV-- 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 96 nLLMGLSRF------PARDA-------RAVPEEIYQLFPVLKTMKQRRGGD-LSGGQQQQLAIGRALASRPQLLILDEPT 161
Cdd:PLN03232 1321 -LFSGTVRFnidpfsEHNDAdlwealeRAHIKDVIDRNPFGLDAEVSEGGEnFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503995501 162 EGIQPSVIKEIGEVIRQLANRGDMAILL--VEQFYDfaaglADRYLVMSRGAIIQ 214
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIREEFKSCTMLVIAhrLNTIID-----CDKILVLSSGQVLE 1449
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-168 |
7.39e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.89 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYY----------GGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPH 71
Cdd:PRK11308 6 LQAIDLKKHYpvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 72 ------QRVQsgIAYV-PQGrEIFPRLTV----EENLLM--GLSRfPARDARAV---------PEEiYQLFPVLktmkqr 129
Cdd:PRK11308 86 aqkllrQKIQ--IVFQnPYG-SLNPRKKVgqilEEPLLIntSLSA-AERREKALammakvglrPEH-YDRYPHM------ 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 503995501 130 rggdLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSV 168
Cdd:PRK11308 155 ----FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
12-214 |
7.40e-08 |
|
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: 51.78 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 12 GGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARsGE-----VLWQeknithRKPHQRVQSGIAYVPQGRE 86
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDiqidgVSWN------SVPLQKWRKAFGVIPQKVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 87 IFPRlTVEENlLMGLSRFPARDARAVPEE-----IYQLFPVLKTMKQRRGG-DLSGGQQQQLAIGRALASRPQLLILDEP 160
Cdd:cd03289 88 IFSG-TFRKN-LDPYGKWSDEEIWKVAEEvglksVIEQFPGQLDFVLVDGGcVLSHGHKQLMCLARSVLSKAKILLLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503995501 161 TEGIQPSVIKEIGEVIRQlaNRGDMAILLVEQFYDfAAGLADRYLVMSRGAIIQ 214
Cdd:cd03289 166 SAHLDPITYQVIRKTLKQ--AFADCTVILSEHRIE-AMLECQRFLVIEENKVRQ 216
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-210 |
8.68e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGlipARSGEVLWQEKNITHRKPHQRVQSGIA-YVPQGREIFPRLTVE 94
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRISGFPKKQETFARISgYCEQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 95 ENLLM-GLSRFPA----RDARAVPEEIYQLFPvLKTMKQRRGG-----DLSGGQQQQLAIGRALASRPQLLILDEPTEGI 164
Cdd:PLN03140 972 ESLIYsAFLRLPKevskEEKMMFVDEVMELVE-LDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503995501 165 QPSVIKEIGEVIRQLANRGDMAILLVEQ-----FYDFaaglaDRYLVMSRG 210
Cdd:PLN03140 1051 DARAAAIVMRTVRNTVDTGRTVVCTIHQpsidiFEAF-----DELLLMKRG 1096
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-215 |
1.08e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 1 MLQVNQ----LHQyyggSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITH---RKPHQR 73
Cdd:PRK10938 3 SLQISQgtfrLSD----TKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRlsfEQLQKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 74 VQ-----SGIAYVPQGREIFPRlTVEENLLMGLSRfPARdaravPEEIYQLFPVlKTMKQRRGGDLSGGQQQQLAIGRAL 148
Cdd:PRK10938 79 VSdewqrNNTDMLSPGEDDTGR-TTAEIIQDEVKD-PAR-----CEQLAQQFGI-TALLDRRFKYLSTGETRKTLLCQAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503995501 149 ASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGdMAILLV-------EQFYDFAAGLADRYLVMS--RGAIIQQ 215
Cdd:PRK10938 151 MSEPDLLILDEPFDGLDVASRQQLAELLASLHQSG-ITLVLVlnrfdeiPDFVQFAGVLADCTLAETgeREEILQQ 225
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-168 |
1.21e-07 |
|
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: 51.67 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 22 FAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNithrkphqrvqsGIAYVPQgREIFPRLTVEENLL--M 99
Cdd:TIGR00954 473 FEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKG------------KLFYVPQ-RPYMTLGTLRDQIIypD 539
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 100 GLSRFPARDAR-AVPEEIYQLFPvLKTMKQRRGG---------DLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSV 168
Cdd:TIGR00954 540 SSEDMKRRGLSdKDLEQILDNVQ-LTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-217 |
1.24e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 51.06 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 15 HILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPAR----SGEVLWQEKNITHRKPHQRVQSgiayvpQGRE---I 87
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRERRKI------IGREiamI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 88 F--------PRLTVEENLLMGL----------SRFPARDARAV----------PEEIYQLFPVlktmkqrrggDLSGGQQ 139
Cdd:COG4170 95 FqepsscldPSAKIGDQLIEAIpswtfkgkwwQRFKWRKKRAIellhrvgikdHKDIMNSYPH----------ELTEGEC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 140 QQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAIIQQGN 217
Cdd:COG4170 165 QKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGP 242
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-161 |
2.09e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 2 LQVNQLHQYYGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVlwqeknithrKPHQRVQsgIAYV 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI----------KIGETVK--LAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 82 PQGRE-IFPRLTVEEN-------LLMGLSRFPARD--ARavpeeiyqlFPVLKTMKQRRGGDLSGGQQQQLAIGRALASR 151
Cdd:PRK11819 393 DQSRDaLDPNKTVWEEisggldiIKVGNREIPSRAyvGR---------FNFKGGDQQKKVGVLSGGERNRLHLAKTLKQG 463
|
170
....*....|
gi 503995501 152 PQLLILDEPT 161
Cdd:PRK11819 464 GNVLLLDEPT 473
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-177 |
2.50e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.10 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 16 ILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPHQrVQSGIAYVPQGREIFprltvEE 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD-LRFKITIIPQDPVLF-----SG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 96 NLLMGLSRFpardARAVPEEIYQLFPV--LKTMKQRR-----------GGDLSGGQQQQLAIGRALASRPQLLILDEPTE 162
Cdd:TIGR00957 1375 SLRMNLDPF----SQYSDEEVWWALELahLKTFVSALpdkldhecaegGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170
....*....|....*
gi 503995501 163 GIQPSVIKEIGEVIR 177
Cdd:TIGR00957 1451 AVDLETDNLIQSTIR 1465
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
131-190 |
2.85e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 2.85e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 131 GGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLV 190
Cdd:PTZ00265 1356 GKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1415
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-161 |
3.74e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 32 LLGRNGVGKTTLLKCLMGLIPARSGEVLWQEkNIThrkphqrvqsgIAYVPQGREIFPRLTVEENLLMGLSrfPARDARA 111
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPAP-GIK-----------VGYLPQEPQLDPEKTVRENVEEGVA--EVKAALD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 112 VPEEIYQLF--PVL---KTMK---------QRRGG------------------------DLSGGQQQQLAIGRALASRPQ 153
Cdd:PRK11819 104 RFNEIYAAYaePDAdfdALAAeqgelqeiiDAADAwdldsqleiamdalrcppwdakvtKLSGGERRRVALCRLLLEKPD 183
|
....*...
gi 503995501 154 LLILDEPT 161
Cdd:PRK11819 184 MLLLDEPT 191
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
133-214 |
3.91e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.80 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 133 DLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLVMSRGAI 212
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
..
gi 503995501 213 IQ 214
Cdd:PRK15093 238 VE 239
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-159 |
3.94e-07 |
|
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: 50.18 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 20 VDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNIThrkPHQRVqsgiAYvpqgRE----------IFP 89
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNRE----AY----RQlfsavfsdfhLFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 90 RltveenlLMGLsrfparDARAVPEEIYQLfpvLKTMK-----QRRGG-----DLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:COG4615 420 R-------LLGL------DGEADPARAREL---LERLEldhkvSVEDGrfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
29-188 |
9.82e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 9.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 29 ITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITH-RKPHqrvqsgIAYVPQGREIFPRLTVEENLLMgLSRFpAR 107
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAKPY------CTYIGHNLGLKLEMTVFENLKF-WSEI-YN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 108 DARAVPEEIYqlFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAI 187
Cdd:PRK13541 100 SAETLYAAIH--YFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVL 177
|
.
gi 503995501 188 L 188
Cdd:PRK13541 178 L 178
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-191 |
1.57e-06 |
|
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: 47.75 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 25 RQGEITCLLGRNGVGKTTLLKCLMG-LIP---ARSGEVLWQEKnITH------RKPHQRVQSG---IAYVPQGREIFPRl 91
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGkLKPnlgKFDDPPDWDEI-LDEfrgselQNYFTKLLEGdvkVIVKPQYVDLIPK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 92 TVEENLLMGLSRfpaRDARAVPEEIYQLFPvLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQpsvIKE 171
Cdd:cd03236 102 AVKGKVGELLKK---KDERGKLDELVDQLE-LRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD---IKQ 174
|
170 180
....*....|....*....|...
gi 503995501 172 ---IGEVIRQLAnRGDMAILLVE 191
Cdd:cd03236 175 rlnAARLIRELA-EDDNYVLVVE 196
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
133-190 |
4.93e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 4.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 133 DLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILLV 190
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFV 458
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-208 |
1.48e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 11 YGGSHILRGVDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVlwqeknithrkphqRVQSGI--AYVPQGREIF 88
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI--------------GLAKGIklGYFAQHQLEF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 89 prLTVEENLLMGLSRFPARDARAVPEEIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPsv 168
Cdd:PRK10636 388 --LRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL-- 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503995501 169 ikeigevirqlanrgDMAILLVEQFYDFAAGLA----DRYLVMS 208
Cdd:PRK10636 464 ---------------DMRQALTEALIDFEGALVvvshDRHLLRS 492
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-161 |
1.50e-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: 43.52 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 26 QGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLwqeknithrkphqrvqsgiayvpqgreifpRLTVEENLlmglsrfp 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI------------------------------YIDGEDIL-------- 42
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 503995501 106 ardaravpeeIYQLFPVLKTMKQRRGGDLSGGQQQQLAIGRALASRPQLLILDEPT 161
Cdd:smart00382 43 ----------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEIT 88
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-213 |
1.82e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 134 LSGGQQQQLAIGRALASrpQLL----ILDEPTEGIQPSVIKEIGEVIRQLANRGDmAILLVEQfYDFAAGLADRYLVMSR 209
Cdd:PRK00635 477 LSGGEQERTALAKHLGA--ELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEH-DEQMISLADRIIDIGP 552
|
....
gi 503995501 210 GAII 213
Cdd:PRK00635 553 GAGI 556
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
134-189 |
2.64e-05 |
|
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: 43.47 E-value: 2.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 134 LSGGQQQQLAIGRALASRPQ--LLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILL 189
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILI 145
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
11-206 |
1.76e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.02 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 11 YGGSHIL-RGVDFaaRQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWqeknithrkphqrvqsgiayvpqgreifP 89
Cdd:cd03222 10 YGVFFLLvELGVV--KEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW----------------------------D 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 90 RLTVEENllmglsrfpardaravPEEIyqlfpvlktmkqrrggDLSGGQQQQLAIGRALASRPQLLILDEPTEGIQPSVI 169
Cdd:cd03222 60 GITPVYK----------------PQYI----------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQR 107
|
170 180 190
....*....|....*....|....*....|....*..
gi 503995501 170 KEIGEVIRQLANRGDMAILLVEQFYDFAAGLADRYLV 206
Cdd:cd03222 108 LNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-164 |
2.55e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 2.55e-04
10 20 30
....*....|....*....|....*....|.
gi 503995501 134 LSGGQQQQLAIGRALASRPQLLILDEPTEGI 164
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-159 |
3.41e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.11 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 20 VDFAARQGEITCLLGRNGVGKTTLLKCLMGLIPARSGEVLWQEKNITHRKPhQRVQSGIAYVPQGREIFPRltveenlLM 99
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP-EDYRKLFSAVFTDFHLFDQ-------LL 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 100 GLSRFPARDAravpeeiyQLFPVLKTMKQRR-----GG-----DLSGGQQQQLAIGRALASRPQLLILDE 159
Cdd:PRK10522 414 GPEGKPANPA--------LVEKWLERLKMAHkleleDGrisnlKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
134-188 |
4.89e-04 |
|
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: 40.29 E-value: 4.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 503995501 134 LSGGQQQQLAIGRALASR---PQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAIL 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 |
5.21e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 5.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 134 LSGGQQQQLAIGRALASR---PQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILL 189
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVI 888
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-161 |
5.52e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 32 LLGRNGVGKTTLLKcLMGL-----IPaRSGEVLWQEKNI-------------THRKPHQRVQSGIAYVPQGREifprltV 93
Cdd:PLN03073 208 LVGRNGTGKTTFLR-YMAMhaidgIP-KNCQILHVEQEVvgddttalqcvlnTDIERTQLLEEEAQLVAQQRE------L 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 94 EENLLMGLSRFPARDA------RAVPEEIYQLFPVLKT-------------------MKQRRGGDLSGGQQQQLAIGRAL 148
Cdd:PLN03073 280 EFETETGKGKGANKDGvdkdavSQRLEEIYKRLELIDAytaearaasilaglsftpeMQVKATKTFSGGWRMRIALARAL 359
|
170
....*....|...
gi 503995501 149 ASRPQLLILDEPT 161
Cdd:PLN03073 360 FIEPDLLLLDEPT 372
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-189 |
1.88e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 1.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 503995501 134 LSGGQQQQLAIGRALAS---RPQLLILDEPTEGIQPSVIKEIGEVIRQLANRGDMAILL 189
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVII 868
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
129-225 |
3.95e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 37.24 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995501 129 RRGGDLSGGQQQQLAIGRALASRPQ--LLILDEPTEGIQPSVIKEIGEVIRQLANRGDmAILLVEQFYDFAAgLADRYLV 206
Cdd:cd03270 133 RSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIR-AADHVID 210
|
90
....*....|....*....
gi 503995501 207 MSRGAIIqqgNGGDMEAEG 225
Cdd:cd03270 211 IGPGAGV---HGGEIVAQG 226
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
29-47 |
6.20e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 36.98 E-value: 6.20e-03
|
| |
