|
Name |
Accession |
Description |
Interval |
E-value |
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-255 |
1.60e-131 |
|
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: 372.06 E-value: 1.60e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLG 80
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIRLFAGMSVLDNVRVPGQCRLRSGLWSQVVGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRR 160
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARLGRGLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 161 LEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
250
....*....|....*
gi 527030459 241 QDDEKVVQAYLGESA 255
Cdd:COG0411 241 RADPRVIEAYLGEEA 255
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-246 |
5.49e-111 |
|
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: 319.38 E-value: 5.49e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIGRT 84
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVRVPGQCRLRSGLWsqvvgLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLL-----LARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIREtFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQDDE 244
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
..
gi 527030459 245 KV 246
Cdd:cd03219 235 RV 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-254 |
1.66e-89 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 265.70 E-value: 1.66e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSA-ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARL 79
Cdd:PRK11300 1 MSQpLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 GIGRTFQNIRLFAGMSVLDNVRVPGQCRLRSGLWSQVVGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRR 159
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVAQHQQLKTGLFSGLLKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 160 RLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEE 239
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
250
....*....|....*
gi 527030459 240 VQDDEKVVQAYLGES 254
Cdd:PRK11300 241 IRNNPDVIKAYLGEA 255
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-253 |
8.44e-67 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 207.66 E-value: 8.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLG 80
Cdd:COG4674 7 HGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIRLFAGMSVLDNVRV--PGQCRLRSGLWSqvvGLSAARREEDEgrerawELLRLVGLESRAERAAGSLPYGDR 158
Cdd:COG4674 87 IGRKFQKPTVFEELTVFENLELalKGDRGVFASLFA---RLTAEERDRIE------EVLETIGLTDKADRLAGLLSHGQK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 159 RRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSltVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPE 238
Cdd:COG4674 158 QWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHS--VVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLD 235
|
250
....*....|....*
gi 527030459 239 EVQDDEKVVQAYLGE 253
Cdd:COG4674 236 EVQADPRVIEVYLGR 250
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-255 |
5.42e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 176.79 E-value: 5.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIgrT 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGY--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVRVpgQCRLRsglwsqvvGLSAArreedEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:COG1131 79 PQEPALYPDLTVRENLRF--FARLY--------GLPRK-----EARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQDD- 243
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARl 222
|
250
....*....|...
gi 527030459 244 -EKVVQAYLGESA 255
Cdd:COG1131 223 lEDVFLELTGEEA 235
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-254 |
7.40e-51 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 166.30 E-value: 7.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIGR 83
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 84 TFQNIRLFAGMSVLDNVRVPGQCRLRsglwsqvvgLSAARREEDEGrerawELLRLVGLESRAERAAGSLPYGDRRRLEI 163
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLEIRKD---------LDRAEREERLE-----ALLEEFQISHLRDNKAMSLSGGERRRVEI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 164 ARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIREtFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQDD 243
Cdd:TIGR04406 147 ARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKE-RGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVAN 225
|
250
....*....|.
gi 527030459 244 EKVVQAYLGES 254
Cdd:TIGR04406 226 EKVRRVYLGEQ 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-254 |
2.87e-50 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 164.82 E-value: 2.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 3 AILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIG 82
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RTFQNIRLFAGMSVLDNvrvpgqcrLRSGLwsQVVGLSAArreedEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLE 162
Cdd:COG1137 82 YLPQEASIFRKLTVEDN--------ILAVL--ELRKLSKK-----EREERLEELLEEFGITHLRKSKAYSLSGGERRRVE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 163 IARALALSPRLLLLDEPAAGMNP---SEKQALsgfIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEE 239
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVDPiavADIQKI---IRHLKER-GIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEE 222
|
250
....*....|....*
gi 527030459 240 VQDDEKVVQAYLGES 254
Cdd:COG1137 223 ILNNPLVRKVYLGED 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-252 |
4.14e-49 |
|
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: 161.56 E-value: 4.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIGRT 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVRVPgqcrlrsglwsqvvgLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:cd03218 81 PQEASIFRKLTVEENILAV---------------LEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIREtFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQDDE 244
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
....*...
gi 527030459 245 KVVQAYLG 252
Cdd:cd03218 225 LVRKVYLG 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-241 |
7.74e-49 |
|
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: 160.61 E-value: 7.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLiPEEIaRLGIGRT 84
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRE-PREV-RRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVRVPGQcrlrsglwsqVVGLSAARREEDEGrerawELLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHAR----------LYGVPGAERRERID-----ELLDFVGLLEAADRLVKTYSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQ 241
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-243 |
9.01e-49 |
|
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: 160.29 E-value: 9.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIGRT 84
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVRVPGQCRLRSGlwsqvvglsaarreedegreRAWELLRLVG----LESRAERAAGSLPYGDRRR 160
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAK--------------------RKARLERVYElfprLKERRKQLAGTLSGGEQQM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 161 LEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
...
gi 527030459 241 QDD 243
Cdd:cd03224 220 LAD 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-252 |
9.65e-48 |
|
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: 158.22 E-value: 9.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 2 SAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGI 81
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 82 GRTFQNIRLFAGMSVLDNVRVPGQCRlrsglwsqvvglsaarreeDEGRERAWELLRLVG----LESRAERAAGSLPYGD 157
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYAR-------------------RDRAEVRADLERVYElfprLKERRRQRAGTLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 158 RRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTP 237
Cdd:COG0410 142 QQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
250
....*....|....*
gi 527030459 238 EEVQDDEKVVQAYLG 252
Cdd:COG0410 221 AELLADPEVREAYLG 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-240 |
1.07e-44 |
|
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: 150.42 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGG----LTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEI--A 77
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 78 RLGIGRTFQNIRLFAGMSVLDNVRVPgqcrlrsglwsqvvgLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGD 157
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALP---------------LEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 158 RRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTP 237
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTV 225
|
...
gi 527030459 238 EEV 240
Cdd:cd03258 226 EEV 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-248 |
1.97e-44 |
|
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: 149.57 E-value: 1.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEE--IARLGIG 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RTFQNIRLFAGMSVLDNVRVPgqCRLRSGLWSQVVGLSAArreedegrerawELLRLVGLESRAERAAGSLPYGDRRRLE 162
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFP--LREHTRLSEEEIREIVL------------EKLEAVGLRGAEDLYPAELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 163 IARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQ- 241
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRa 226
|
....*...
gi 527030459 242 -DDEKVVQ 248
Cdd:cd03261 227 sDDPLVRQ 234
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-251 |
4.47e-44 |
|
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: 148.97 E-value: 4.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARL- 79
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 -GIGRTFQNIRLFAGMSVLDNVRVPgqcrLRsglwsQVVGLSAArreedEGRERAWELLRLVGLESRAERAAGSLPYGDR 158
Cdd:COG1127 82 rRIGMLFQGGALFDSLTVFENVAFP----LR-----EHTDLSEA-----EIRELVLEKLELVGLPGAADKMPSELSGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 159 RRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPE 238
Cdd:COG1127 148 KRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPE 227
|
250
....*....|....
gi 527030459 239 EVQD-DEKVVQAYL 251
Cdd:COG1127 228 ELLAsDDPWVRQFL 241
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-239 |
5.87e-44 |
|
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: 148.04 E-value: 5.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGL--TAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEeiARLGIG 82
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA--ARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RTFQNIRLFAGMSVLDNVRVpgQCRLRsglwsqvvGLSAARREEDEGrerawELLRLVGLESRAERAAGSLPYGDRRRLE 162
Cdd:cd03263 79 YCPQFDALFDELTVREHLRF--YARLK--------GLPKSEIKEEVE-----LLLRVLGLTDKANKRARTLSGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527030459 163 IARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIREtfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEE 239
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-242 |
1.57e-43 |
|
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: 147.70 E-value: 1.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEeiARLGIGRT 84
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE--ARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVRVpgQCRLRsGLWSQVVGLSAArreedegrerawELLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:COG4555 80 PDERGLYDRLTVRENIRY--FAELY-GLFDEELKKRIE------------ELIELLGLEEFLDRRVGELSTGMKKKVALA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQD 242
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-235 |
1.51e-41 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 141.50 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEeiaRLGIGRT 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE---RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVrvpgqcrlrsglwsqVVGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:cd03259 78 FQDYALFPHLTVAENI---------------AFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALG 235
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-240 |
2.89e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 144.86 E-value: 2.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEiaRlG 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--R-N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIRLFAGMSVLDNVRVPgqcrLRsglwsqVVGLSAARREEDegrerAWELLRLVGLESRAERAAGSLPYGDRRR 160
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFG----LR------MRGVPKAEIRAR-----VAELLELVGLEGLADRYPHQLSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 161 LEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-250 |
2.60e-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: 139.24 E-value: 2.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLT-AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEI--ARLGI 81
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 82 GRTFQNIRLFAGMSVLDNVRVPgqcRL--RSGLWSQVVGLSAARREEdegrerAWELLRLVGLESRAERAAGSLPYGDRR 159
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSG---RLgrRSTWRSLFGLFPKEEKQR------ALAALERVGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 160 RLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEE 239
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE 231
|
250
....*....|.
gi 527030459 240 VqDDEKVVQAY 250
Cdd:cd03256 232 L-TDEVLDEIY 241
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-242 |
5.05e-40 |
|
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: 138.63 E-value: 5.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEiarLGIGRT 84
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---RNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVRVPGQCRLRSGLWSQvvglsaarreeDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSERPPE-----------AEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQD 242
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-250 |
1.43e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.53 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLaGLIPEEIA--- 77
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-RRARRRIGyvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 78 -RLGIGRTFQnirlfagMSVLDNVrvpgqcrlRSGLWSQV---VGLSAArreedeGRERAWELLRLVGLESRAERAAGSL 153
Cdd:COG1121 82 qRAEVDWDFP-------ITVRDVV--------LMGRYGRRglfRRPSRA------DREAVDEALERVGLEDLADRPIGEL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 154 PYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNfGELIA 233
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLN-RGLVA 218
|
250
....*....|....*..
gi 527030459 234 LGTPEEVQDDEKVVQAY 250
Cdd:COG1121 219 HGPPEEVLTPENLSRAY 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-245 |
5.92e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 141.96 E-value: 5.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSF-----GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIAR 78
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 79 LG--IGRTFQNIR--LFAGMSVLDNVRVPgqCRLRSGLWSQVVGLSAArreedegrerawELLRLVGLESR-AERAAGSL 153
Cdd:COG1123 340 LRrrVQMVFQDPYssLNPRMTVGDIIAEP--LRLHGLLSRAERRERVA------------ELLERVGLPPDlADRYPHEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 154 PYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIA 233
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVE 485
|
250
....*....|..
gi 527030459 234 LGTPEEVQDDEK 245
Cdd:COG1123 486 DGPTEEVFANPQ 497
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3-253 |
2.76e-38 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 134.25 E-value: 2.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 3 AILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIG 82
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RTFQNIRLFAGMSVLDNVRvpGQCRLRSGLWSQvvglsaarreedEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLE 162
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLM--AVLQIRDDLSAE------------QREDRANELMEEFHIEHLRDSMGQSLSGGERRRVE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 163 IARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQD 242
Cdd:PRK10895 148 IARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
250
....*....|.
gi 527030459 243 DEKVVQAYLGE 253
Cdd:PRK10895 227 DEHVKRVYLGE 237
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-240 |
6.95e-38 |
|
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: 132.46 E-value: 6.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSF-GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgIGR 83
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 84 TFQNIR--LFAgMSVLDNVRVpGQCRLrsglwsqvvGLSAArreedEGRERAWELLRLVGLESRAERAAGSLPYGDRRRL 161
Cdd:COG1122 80 VFQNPDdqLFA-PTVEEDVAF-GPENL---------GLPRE-----EIRERVEEALELVGLEHLADRPPHELSGGQKQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 162 EIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-244 |
1.19e-37 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 132.49 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 3 AILEVSDLTKSF-GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARL-- 79
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 GIGRTFQNIRLFAGMSVLDNV------RVPGqcrLRS--GLWSQvvglsaarreedEGRERAWELLRLVGLESRAERAAG 151
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVlagrlgRTST---WRSllGLFPP------------EDRERALEALERVGLADKAYQRAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 152 SLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGEL 231
Cdd:COG3638 146 QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
250
....*....|...
gi 527030459 232 IALGTPEEVQDDE 244
Cdd:COG3638 226 VFDGPPAELTDAV 238
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-242 |
1.52e-37 |
|
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: 131.98 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPeeiARLGIGRT 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP---HKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVRVPgqCRLRsglwsqvvGLSAARREEDEGrerawELLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:cd03300 78 FQNYALFPHLTVFENIAFG--LRLK--------KLPKAEIKERVA-----EALDLVQLEGYANRKPSQLSGGQQQRVAIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQD 242
Cdd:cd03300 143 RALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-231 |
1.85e-37 |
|
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: 129.83 E-value: 1.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIgrT 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGY--L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVRvpgqcrlrsglwsqvvglsaarreedegrerawellrlvglesraeraagsLPYGDRRRLEIA 164
Cdd:cd03230 79 PEEPSLYENLTVRENLK---------------------------------------------------LSGGMKQRLALA 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGEL 231
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-250 |
2.52e-37 |
|
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: 131.70 E-value: 2.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgIGR 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 84 TFQNIRLFAGMSVLDNV---RVPGQcrlrsGLWSQvvgLSAArreedeGRERAWELLRLVGLESRAERAAGSLPYGDRRR 160
Cdd:COG1120 80 VPQEPPAPFGLTVRELValgRYPHL-----GLFGR---PSAE------DREAVEEALERTGLEHLADRPVDELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 161 LEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
250
....*....|
gi 527030459 241 QDDEKVVQAY 250
Cdd:COG1120 226 LTPELLEEVY 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-240 |
6.23e-36 |
|
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: 127.80 E-value: 6.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLT-AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARlGIGR 83
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR-KIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 84 TFQNIRLFAGMSVLDNVrvpgqcrlrsGLWSQVVGLSAARREEDegrerAWELLRLVGLESR--AERAAGSLPYGDRRRL 161
Cdd:cd03295 80 VIQQIGLFPHMTVEENI----------ALVPKLLKWPKEKIRER-----ADELLALVGLDPAefADRYPHELSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 162 EIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-254 |
1.48e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.45 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLG 80
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIRLFAGMSVLDNVRVpGQCRLRSGL--WSQVVGLSAarreedegrerawELLRLVGLESRAERAAGSLPYGDR 158
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFL-GREPRRGGLidWRAMRRRAR-------------ELLARLGLDIDPDTPVGDLSVAQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 159 RRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPE 238
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVA 225
|
250
....*....|....*.
gi 527030459 239 EVqDDEKVVQAYLGES 254
Cdd:COG1129 226 EL-TEDELVRLMVGRE 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-244 |
1.83e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 132.07 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLG 80
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIRLFAGMSVLDNVrVPGqcrlRSGLWSQVVGLSAARREEDegrerawELLRLVGLESRAERAAGSLPYGDRRR 160
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENI-VLG----LEPTKGGRLDRKAARARIR-------ELSERYGLDVDPDAKVEDLSVGEQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 161 LEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
....
gi 527030459 241 QDDE 244
Cdd:COG3845 229 SEEE 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-235 |
3.38e-35 |
|
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: 125.00 E-value: 3.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGsIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDlAGLIPEEIARLgIGRT 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD-VLKQPQKLRRR-IGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVRVpgQCRLRsglwsqvvGLSAARREEDEGrerawELLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:cd03264 78 PQEFGVYPNFTVREFLDY--IAWLK--------GIPSKEVKARVD-----EVLELVNLGDRAKKKIGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfsLTVLLIEHHVPMVMGLCDRIAVLNFGELIALG 235
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-249 |
5.07e-35 |
|
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: 131.18 E-value: 5.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSF--GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPT---SGRVAFAGRDLAGLIPEE 75
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 76 IARLgIGRTFQNirlfaGMSVLDNVRVPGQCRLrsglwsqvvGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPY 155
Cdd:COG1123 81 RGRR-IGMVFQD-----PMTQLNPVTVGDQIAE---------ALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 156 GDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALG 235
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
250
....*....|....
gi 527030459 236 TPEEVQDDEKVVQA 249
Cdd:COG1123 226 PPEEILAAPQALAA 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-240 |
6.83e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 127.50 E-value: 6.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSF----GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEI--A 77
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 78 RLGIGRTFQNIRLFAGMSVLDNVRVPgqcrLRsglwsqVVGLSAARREEDEGrerawELLRLVGLESRAERAAGSLPYGD 157
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALP----LE------IAGVPKAEIRKRVA-----ELLELVGLSDKADAYPSQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 158 RRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEH--HVpmVMGLCDRIAVLNFGELIALG 235
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHemDV--VRRICDRVAVLENGRIVEQG 223
|
....*
gi 527030459 236 TPEEV 240
Cdd:COG1135 224 PVLDV 228
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
5-251 |
1.89e-34 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 123.94 E-value: 1.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIgrT 84
Cdd:TIGR03864 2 LEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGV--V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVRvpgqcrlrsgLWSQVVGLSAARREEDEGrerawELLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:TIGR03864 80 FQQPTLDLDLSVRQNLR----------YHAALHGLSRAEARARIA-----ELLARLGLAERADDKVRELNGGHRRRVEIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVmGLCDRIAVLNFGELIALGTPEEV---Q 241
Cdd:TIGR03864 145 RALLHRPALLLLDEPTVGLDPASRAAITAHVRALARDQGLSVLWATHLVDEI-EASDRLVVLHRGRVLADGAAAELrgaT 223
|
250
....*....|
gi 527030459 242 DDEKVVQAYL 251
Cdd:TIGR03864 224 GGADLEAAFL 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-240 |
4.51e-34 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 125.68 E-value: 4.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 6 EVSDLTKSFGG----LTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEI--ARL 79
Cdd:PRK11153 3 ELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 GIGRTFQNIRLFAGMSVLDNVRVPgqcrlrsglwsqvvgLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRR 159
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALP---------------LELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 160 RLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEE 239
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
.
gi 527030459 240 V 240
Cdd:PRK11153 228 V 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-230 |
7.46e-34 |
|
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: 120.75 E-value: 7.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPE-EIARLGIGR 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 84 TFQNIRLFAGMSVLDNVrvpgqcrlrsglwsqVVGLSAarreedegrerawellrlvglesraeraagslpyGDRRRLEI 163
Cdd:cd03229 81 VFQDFALFPHLTVLENI---------------ALGLSG----------------------------------GQQQRVAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527030459 164 ARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGE 230
Cdd:cd03229 112 ARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-227 |
1.64e-33 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 121.04 E-value: 1.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGG----LTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEeiarlg 80
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIRLFAGMSVLDNVRvpgqcrlrsglwsqvVGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRR 160
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVA---------------LGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527030459 161 LEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLN 227
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-233 |
1.79e-33 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 119.07 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIGRT 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQnirlfagmsvldnvrvpgqcrlrsglwsqvvglsaarreedegrerawellrlvglesraeraagsLPYGDRRRLEIA 164
Cdd:cd03216 81 YQ------------------------------------------------------------------LSVGERQMVEIA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIA 233
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-231 |
2.12e-33 |
|
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: 120.67 E-value: 2.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGG----LTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARL- 79
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 --GIGRTFQNIRLFAGMSVLDNVRVPgqcrlrsglwsqvvgLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGD 157
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELP---------------LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527030459 158 RRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVmGLCDRIAVLNFGEL 231
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-235 |
2.12e-33 |
|
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: 120.33 E-value: 2.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 6 EVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAgLIPEEIA----RLGI 81
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-KERKRIGyvpqRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 82 GRTFQnirlfagMSVLDNVrvpgqcrlRSGLWSQVVGLsaaRREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRL 161
Cdd:cd03235 80 DRDFP-------ISVRDVV--------LMGLYGHKGLF---RRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527030459 162 EIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNfGELIALG 235
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-251 |
2.50e-33 |
|
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: 120.71 E-value: 2.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIGRT 84
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVRVpgqcrlrsglwsqvvGLSAARREEDEGRERAWELLRLvgLESRAERAAGSLPYGDRRRLEIA 164
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLT---------------GLAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVqdDE 244
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL--DE 221
|
....*..
gi 527030459 245 KVVQAYL 251
Cdd:TIGR03410 222 DKVRRYL 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-235 |
3.25e-33 |
|
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: 120.30 E-value: 3.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSF----GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARL 79
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 G--IGRTFQNirlfaGMSVLDNVRVPGQCrLRSGLWSQVVGLSAARREEDEGrerawELLRLVGLesrAERAAGSLPY-- 155
Cdd:cd03257 81 RkeIQMVFQD-----PMSSLNPRMTIGEQ-IAEPLRIHGKLSKKEARKEAVL-----LLLVGVGL---PEEVLNRYPHel 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 156 --GDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIA 233
Cdd:cd03257 147 sgGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVE 226
|
..
gi 527030459 234 LG 235
Cdd:cd03257 227 EG 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-240 |
5.33e-33 |
|
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: 119.98 E-value: 5.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGM-----TRPTSGRVAFAGRDLAGLIPEEIA-R 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLElR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 79 LGIGRTFQNIRLFAgMSVLDNVRVpgqcrlrsGLWSQVVGLSAARREEDEgrerawELLRLVGLESRAER--AAGSLPYG 156
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAY--------GLRLHGIKLKEELDERVE------EALRKAALWDEVKDrlHALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 157 DRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfsLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGT 236
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
....
gi 527030459 237 PEEV 240
Cdd:cd03260 224 TEQI 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-233 |
1.54e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 118.61 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFG----GLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEI 76
Cdd:COG1136 1 MSPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 77 ARL---GIGRTFQNIRLFAGMSVLDNVRVPgqCRLRsglwsqvvGLSAARREEDegrerAWELLRLVGLESRAERAAGSL 153
Cdd:COG1136 81 ARLrrrHIGFVFQFFNLLPELTALENVALP--LLLA--------GVSRKERRER-----ARELLERVGLGDRLDHRPSQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 154 PYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHvPMVMGLCDRIAVLNFGELIA 233
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIVS 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-243 |
1.74e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 120.21 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLA-------GLIPEEi 76
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDpedrrriGYLPEE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 77 arlgigrtfqniR-LFAGMSVLDNVRVPGqcRLRsglwsqvvGLSAARREEDEGrerawELLRLVGLESRAERAAGSLPY 155
Cdd:COG4152 80 ------------RgLYPKMKVGEQLVYLA--RLK--------GLSKAEAKRRAD-----EWLERLGLGDRANKKVEELSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 156 GDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSlTVLLIEHHVPMVMGLCDRIAVLNFGELIALG 235
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGT-TVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
....*...
gi 527030459 236 TPEEVQDD 243
Cdd:COG4152 212 SVDEIRRQ 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-250 |
3.03e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 119.91 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLG 80
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNirLFAGMSVLDNVRVpgqcrlrsglWSQVVGLSAARREEDEGReraweLLRLVGLESRAERAAGSLPYGDRRR 160
Cdd:PRK13537 84 VVPQFDN--LDPDFTVRENLLV----------FGRYFGLSAAAARALVPP-----LLEFAKLENKADAKVGELSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 161 LEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
250
....*....|...
gi 527030459 241 QDDE---KVVQAY 250
Cdd:PRK13537 226 IESEigcDVIEIY 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-240 |
1.12e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 119.94 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPeeiARLG 80
Cdd:PRK11607 16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP---YQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIRLFAGMSVLDNVRVP-GQCRLRSGLWSQVVGlsaarreedegrerawELLRLVGLESRAERAAGSLPYGDRR 159
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGlKQDKLPKAEIASRVN----------------EMLGLVHMQEFAKRKPHQLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 160 RLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEE 239
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
|
.
gi 527030459 240 V 240
Cdd:PRK11607 237 I 237
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
12-240 |
1.36e-31 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 119.57 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 12 KSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEE---IARLGIGRTFQNI 88
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElreVRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 89 RLFAGMSVLDNVRVpgqcrlrsglwsqvvGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIARALA 168
Cdd:TIGR01186 81 ALFPHMTILQNTSL---------------GPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527030459 169 LSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:TIGR01186 146 AEPDILLMDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEI 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-166 |
3.02e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 115.15 E-value: 3.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSF-GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARL--G 80
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIRLFAGMSVLDNVRVPgqcrLRsglwsqVVGLSAARREEDEGrerawELLRLVGLESRAERAAGSLPYGDRRR 160
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALP----LR------VTGKSRKEIRRRVR-----EVLDLVGLSDKAKALPHELSGGEQQR 145
|
....*.
gi 527030459 161 LEIARA 166
Cdd:COG2884 146 VAIARA 151
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-240 |
1.17e-30 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 113.97 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTaVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEeiaRLGIGRT 84
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---KRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVrvpgqcrlrsglwsqVVGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:cd03299 77 PQNYALFPHMTVYKNI---------------AYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:cd03299 142 RALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-230 |
1.95e-30 |
|
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: 112.56 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 6 EVSDLTKSFGGLTAVA--GVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgIGR 83
Cdd:cd03225 1 ELKNLSFSYPDGARPAldDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 84 TFQNIRL-FAGMSVLDNVrvpgqcrlrsglwsqVVGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLE 162
Cdd:cd03225 80 VFQNPDDqFFGPTVEEEV---------------AFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 163 IARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGE 230
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-242 |
2.04e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 116.01 E-value: 2.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSaiLEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDL-AGLIPEEiaRl 79
Cdd:COG1118 1 MS--IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRE--R- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 GIGRTFQNIRLFAGMSVLDNVRVpgqcrlrsglwsqvvGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRR 159
Cdd:COG1118 76 RVGFVFQHYALFPHMTVAENIAF---------------GLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 160 RLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEE 239
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDE 220
|
...
gi 527030459 240 VQD 242
Cdd:COG1118 221 VYD 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-232 |
3.08e-30 |
|
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: 112.31 E-value: 3.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPeeiARLGIGRT 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE---ALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVRVpgQCRLRSGLWSQVVglsaarreedegrerawELLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:cd03268 78 IEAPGFYPNLTARENLRL--LARLLGIRKKRID-----------------EVLDVVGLKDSAKKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELI 232
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-235 |
3.91e-30 |
|
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: 111.99 E-value: 3.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRV-------AFAGRDLAGLIPEEia 77
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdgkplDIAARNRIGYLPEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 78 rlgigrtfqniR-LFAGMSVLDNVRVPGQCRlrsglwsqvvGLSAARREEDEGrerawELLRLVGLESRAERAAGSLPYG 156
Cdd:cd03269 79 -----------RgLYPKMKVIDQLVYLAQLK----------GLKKEEARRRID-----EWLERLELSEYANKRVEELSKG 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 157 DRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSlTVLLIEHHVPMVMGLCDRIAVLNFGELIALG 235
Cdd:cd03269 133 NQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-235 |
1.13e-29 |
|
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: 109.83 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 6 EVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgigrtf 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 86 qnirlfagMSVLdnvrvpgqcrlrsglwSQVvglsaarreedegrerawelLRLVGLESRAERAAGSLPYGDRRRLEIAR 165
Cdd:cd03214 75 --------IAYV----------------PQA--------------------LELLGLAHLADRPFNELSGGERQRVLLAR 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 166 ALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALG 235
Cdd:cd03214 111 ALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-243 |
2.71e-29 |
|
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: 110.66 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFG----GLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARlG 80
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR-R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIR--LFAGMSVLDNVRVPGQCRLRSGLWSQVvglsaarreedegreraWELLRLVGLESR-AERAAGSLPYGD 157
Cdd:COG1124 81 VQMVFQDPYasLHPRHTVDRILAEPLRIHGLPDREERI-----------------AELLEQVGLPPSfLDRYPHQLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 158 RRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTP 237
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTV 223
|
....*.
gi 527030459 238 EEVQDD 243
Cdd:COG1124 224 ADLLAG 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-240 |
2.95e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 112.86 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 3 AILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEiaRlGIG 82
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--R-NIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RTFQNIRLFAGMSVLDNVRVPgqCRLRsglwsqvvGLSAARREEDEGrerawELLRLVGLESRAERAAGSLPYGDRRRLE 162
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFP--LKLR--------KVPKAEIDRRVR-----EAAELLGLEDLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 163 IARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-226 |
3.59e-29 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 110.56 E-value: 3.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSF----GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEei 76
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 77 arlgIGRTFQNIRLFAGMSVLDNVRVPgqcrLRsglwsqVVGLSAARREEDegrerAWELLRLVGLESRAERaagsLPY- 155
Cdd:COG1116 82 ----RGVVFQEPALLPWLTVLDNVALG----LE------LRGVPKAERRER-----ARELLELVGLAGFEDA----YPHq 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527030459 156 ---GDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVL 226
Cdd:COG1116 139 lsgGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-235 |
1.42e-28 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 108.22 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSF----GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLiPEEiARL 79
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKE-PAE-ARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 GIGRTFQNIRLFAGMSVLDNVRVPGqcrlrsGLWsqvvGLSAARREEDEGrerawELLRLVGLESRAERAAGSLPYGDRR 159
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYFA------GLY----GLKGDELTARLE-----ELADRLGMEELLDRRVGGFSTGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527030459 160 RLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALG 235
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
8-240 |
1.64e-28 |
|
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: 109.27 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 8 SDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPE---EIARLGIGRT 84
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrELRRKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVrvpgqcrlrsglwsqVVGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:cd03294 108 FQSFALLPHRTVLENV---------------AFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:cd03294 173 RALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-181 |
1.65e-28 |
|
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: 105.81 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 22 GVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGlIPEEIARLGIGRTFQNIRLFAGMSVLDNVR 101
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD-DERKSLRKEIGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 102 VPGQCRLRSGLWSQVvglsaarreedegreRAWELLRLVGLESRAERAAG----SLPYGDRRRLEIARALALSPRLLLLD 177
Cdd:pfam00005 82 LGLLLKGLSKREKDA---------------RAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLD 146
|
....
gi 527030459 178 EPAA 181
Cdd:pfam00005 147 EPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-197 |
1.02e-27 |
|
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: 105.64 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 3 AILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIg 82
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 rTFQNIRLFAGMSVLDNVRvpgqcrlrsgLWSQVVGLSAArreedegRERAWELLRLVGLESRAERAAGSLPYGDRRRLE 162
Cdd:COG4133 80 -LGHADGLKPELTVRENLR----------FWAALYGLRAD-------REAIDEALEAVGLAGLADLPVRQLSAGQKRRVA 141
|
170 180 190
....*....|....*....|....*....|....*
gi 527030459 163 IARALALSPRLLLLDEPAAGMNPSEKQALSGFIRE 197
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-235 |
1.79e-27 |
|
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: 105.03 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEiaRlGIGRT 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--R-DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVRVPgqCRLRSGLWSQVVG--LSAArreedegrerawELLRLVGLESRAERAagsLPYGDRRRLE 162
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFG--LKLRKVPKDEIDErvREVA------------ELLQIEHLLDRKPKQ---LSGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527030459 163 IARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALG 235
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-253 |
1.86e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.25 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSaiLEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEiarLG 80
Cdd:PRK10851 1 MS--IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---RK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIRLFAGMSVLDNVR-----VPGQCRLRSGLWSQVVGlsaarreedegrerawELLRLVGLESRAERAAGSLPY 155
Cdd:PRK10851 76 VGFVFQHYALFRHMTVFDNIAfgltvLPRRERPNAAAIKAKVT----------------QLLEMVQLAHLADRYPAQLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 156 GDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALG 235
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG 219
|
250 260
....*....|....*....|
gi 527030459 236 TPEEVQDD--EKVVQAYLGE 253
Cdd:PRK10851 220 TPDQVWREpaTRFVLEFMGE 239
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-250 |
2.20e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.97 E-value: 2.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgigRT 84
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARR---RA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 F--QNIRLFAGMSVLDNVRvpgqcrlrsglwsqvVGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLE 162
Cdd:COG4559 79 VlpQHSSLAFPFTVEEVVA---------------LGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 163 IARALALSPRLLLL-------DEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALG 235
Cdd:COG4559 144 LARVLAQLWEPVDGgprwlflDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQG 222
|
250
....*....|....*
gi 527030459 236 TPEEVQDDEKVVQAY 250
Cdd:COG4559 223 TPEEVLTDELLERVY 237
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-250 |
2.73e-27 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 105.55 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 2 SAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSG-RVAFAGRDLAGLIPEEI-ARL 79
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELrKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 GIGRTFQNIRLFAGMSVLDNVRvpgqcrlrSGLWSqVVGLSAARREEDEGRerAWELLRLVGLESRAERAAGSLPYGDRR 159
Cdd:COG1119 81 GLVSPALQLRFPRDETVLDVVL--------SGFFD-SIGLYREPTDEQRER--ARELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 160 RLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEE 239
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEE 229
|
250
....*....|.
gi 527030459 240 VQDDEKVVQAY 250
Cdd:COG1119 230 VLTSENLSEAF 240
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-230 |
8.37e-27 |
|
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: 101.55 E-value: 8.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 6 EVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIaRLGIGRTF 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL-RRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 86 QnirlfagmsvldnvrvpgqcrlrsglwsqvvgLSAarreedegrerawellrlvglesraeraagslpyGDRRRLEIAR 165
Cdd:cd00267 80 Q--------------------------------LSG----------------------------------GQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527030459 166 ALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSlTVLLIEHHVPMVMGLCDRIAVLNFGE 230
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGR-TVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-253 |
1.01e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 103.68 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAgvSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEE--IARLgig 82
Cdd:COG3840 2 LRLDDLTYRYGDFPLRF--DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAErpVSML--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 rtFQNIRLFAGMSVLDNV---RVPGqCRLRSGLWSQVVglsaarreedegrerawELLRLVGLESRAERAAGSLPYGDRR 159
Cdd:COG3840 77 --FQENNLFPHLTVAQNIglgLRPG-LKLTAEQRAQVE-----------------QALERVGLAGLLDRLPGQLSGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 160 RLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEE 239
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
250
....*....|....*.
gi 527030459 240 VQDDE--KVVQAYLGE 253
Cdd:COG3840 217 LLDGEppPALAAYLGI 232
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-235 |
1.05e-26 |
|
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: 103.57 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSF------GGL---------------TAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAf 63
Cdd:cd03267 1 IEVSNLSKSYrvyskePGLigslkslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 64 agrdLAGLIPEEiarlgigrtfQNIRLFAGMSVldnvrVPGQcrlRSGLW------------SQVVGLSAARREEDEGre 131
Cdd:cd03267 80 ----VAGLVPWK----------RRKKFLRRIGV-----VFGQ---KTQLWwdlpvidsfyllAAIYDLPPARFKKRLD-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 132 rawELLRLVGLESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEH 211
Cdd:cd03267 136 ---ELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSH 212
|
250 260
....*....|....*....|....
gi 527030459 212 HVPMVMGLCDRIAVLNFGELIALG 235
Cdd:cd03267 213 YMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-253 |
1.32e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 105.68 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGliPEEIARLGIGRT 84
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA--RARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVRVPGQ-CRLRSGLWSQVVGlsaarreedegrerawELLRLVGLESRAERAAGSLPYGDRRRLEI 163
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRyFGMSTREIEAVIP----------------SLLEFARLESKADARVSDLSGGMKRRLTL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 164 ARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIReTFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQDD 243
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE 262
|
250
....*....|...
gi 527030459 244 E---KVVQAYLGE 253
Cdd:PRK13536 263 HigcQVIEIYGGD 275
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-240 |
6.04e-26 |
|
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: 106.46 E-value: 6.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLT--AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgIG 82
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ-IG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RTFQNIRLFAGmSVLDNVRvpgqcrlrsgLWSQVVGLSAarreedegrerAWELLRLVGLESRAER-----------AAG 151
Cdd:COG2274 553 VVLQDVFLFSG-TIRENIT----------LGDPDATDEE-----------IIEAARLAGLHDFIEAlpmgydtvvgeGGS 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 152 SLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIREtfSLTVLLIEHHVPMVMgLCDRIAVLNFGEL 231
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRI 687
|
....*....
gi 527030459 232 IALGTPEEV 240
Cdd:COG2274 688 VEDGTHEEL 696
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-258 |
2.03e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.38 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgIGRT 84
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRL---FAGMSVLDNVRVPGQCRLrsGLWSQvvglsaarreedEGRERAWELLRLVGLESRAERAAGSLPYGDRRRL 161
Cdd:PRK09536 83 PQDTSLsfeFDVRQVVEMGRTPHRSRF--DTWTE------------TDRAAVERAMERTGVAQFADRPVTSLSGGERQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 162 EIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIeHHVPMVMGLCDRIAVLNFGELIALGTPEEVQ 241
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
250
....*....|....*..
gi 527030459 242 DDEKVVQAYLGESALGE 258
Cdd:PRK09536 228 TADTLRAAFDARTAVGT 244
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-243 |
2.06e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.03 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSF-GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgIG 82
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF-VG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RTFQNI--RLFAgMSVLDNVRVpGQCRLrsGLWSQVVGLSAArreedegrerawELLRLVGLESRAERAAGSLPYGDRRR 160
Cdd:PRK13652 82 LVFQNPddQIFS-PTVEQDIAF-GPINL--GLDEETVAHRVS------------SALHMLGLEELRDRVPHHLSGGEKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 161 LEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
....*
gi 527030459 241 --QDD 243
Cdd:PRK13652 226 flQPD 230
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-252 |
3.10e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 99.95 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLG 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIRLFAGMSVLDNVRVPgqcrlrsglwsqvvGLSAARREEDEGRERAWELL-RLvgLESRAERaAGSLPYGDRR 159
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMG--------------GFFAERDQFQERIKWVYELFpRL--HERRIQR-AGTMSGGEQQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 160 RLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEE 239
Cdd:PRK11614 145 MLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDA 223
|
250
....*....|...
gi 527030459 240 VQDDEKVVQAYLG 252
Cdd:PRK11614 224 LLANEAVRSAYLG 236
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-231 |
4.53e-25 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 98.63 E-value: 4.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSF-GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIA--RLGI 81
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 82 GRTFQNIRLFAGMSVLDNVRVPGQCRLRSG-LWSQVVGlsaarreedegrerawELLRLVGLESRAERAAGSLPYGDRRR 160
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPrEIRKRVP----------------AALELVGLSHKHRALPAELSGGEQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527030459 161 LEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGEL 231
Cdd:cd03292 145 VAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-254 |
5.00e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.95 E-value: 5.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 2 SAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEeiaRLGI 81
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE---NRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 82 GRTFQNIRLFAGMSVLDNVrvpgqcrlrsglwsqVVGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRL 161
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENV---------------AFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 162 EIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQ 241
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIY 233
|
250
....*....|....*
gi 527030459 242 DDEK--VVQAYLGES 254
Cdd:PRK09452 234 EEPKnlFVARFIGEI 248
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-240 |
5.89e-25 |
|
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: 102.96 E-value: 5.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSF-----GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAF-AGR---DLAGLIPE 74
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDewvDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 75 EIARLG--IGRTFQNIRLFAGMSVLDNVrvpgqcrlrsglwSQVVGLSaarREEDEGRERAWELLRLVGL-ESRAERAAG 151
Cdd:TIGR03269 359 GRGRAKryIGILHQEYDLYPHRTVLDNL-------------TEAIGLE---LPDELARMKAVITLKMVGFdEEKAEEILD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 152 SLPY----GDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLN 227
Cdd:TIGR03269 423 KYPDelseGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMR 502
|
250
....*....|...
gi 527030459 228 FGELIALGTPEEV 240
Cdd:TIGR03269 503 DGKIVKIGDPEEI 515
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-251 |
6.07e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.81 E-value: 6.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSF-GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIaRL 79
Cdd:PRK13647 1 MDNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV-RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 GIGRTFQNI--RLFAgMSVLDNVrvpgqcrlrsGLWSQVVGLSAARREEDEGrerawELLRLVGLESRAERAAGSLPYGD 157
Cdd:PRK13647 80 KVGLVFQDPddQVFS-STVWDDV----------AFGPVNMGLDKDEVERRVE-----EALKAVRMWDFRDKPPYHLSYGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 158 RRRLEIARALALSPRLLLLDEPAAGMNPSEKQALsgfiREIRETFS---LTVLLIEHHVPMVMGLCDRIAVLNFGELIAL 234
Cdd:PRK13647 144 KKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL----MEILDRLHnqgKTVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
250
....*....|....*..
gi 527030459 235 GTPEEVQDDEKVVQAYL 251
Cdd:PRK13647 220 GDKSLLTDEDIVEQAGL 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-246 |
6.42e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 102.94 E-value: 6.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLG 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIRLFAGMSVLDNVRVpGQCRLRSGLWSQVVGLSaarreedEGRERAWELLRLVGLESRAERAAGSLPYGDRRR 160
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYI-GRHLTKKVCGVNIIDWR-------EMRVRAAMMLLRVGLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 161 LEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
....*.
gi 527030459 241 QDDEKV 246
Cdd:PRK09700 233 SNDDIV 238
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-185 |
1.42e-24 |
|
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: 97.22 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLaGLIPEEIARL--GIG 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELrqKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RTFQNIRLFAGMSVLDNVRVPGQcrlrsglwsQVVGLSAArreedEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLE 162
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPI---------KVKGMSKA-----EAEERALELLEKVGLADKADAYPAQLSGGQQQRVA 145
|
170 180
....*....|....*....|...
gi 527030459 163 IARALALSPRLLLLDEPAAGMNP 185
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDP 168
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-249 |
2.24e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 101.28 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLG 80
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIRLFAGMSVLDNVrvpgqcrlrsglwsqVVGLSAARREEDEGRerawELLRLVGLESRAERAAGSLPYGDRRR 160
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENI---------------LFGLPKRQASMQKMK----QLLAALGCQLDLDSSAGSLEVADRQI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 161 LEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGElIALGTPEEV 240
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGT-IALSGKTAD 226
|
....*....
gi 527030459 241 QDDEKVVQA 249
Cdd:PRK15439 227 LSTDDIIQA 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-233 |
6.23e-24 |
|
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: 95.96 E-value: 6.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 2 SAILEVSDLTKSFGG----LTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIA 77
Cdd:COG4181 6 APIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 78 RL---GIGRTFQNIRLFAGMSVLDNVRVPgqcrlrsglwSQVVGLSAARREedegrerAWELLRLVGLESRAERAAGSLP 154
Cdd:COG4181 86 RLrarHVGFVFQSFQLLPTLTALENVMLP----------LELAGRRDARAR-------ARALLERVGLGHRLDHYPAQLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 155 YGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVmGLCDRIAVLNFGELIA 233
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-240 |
6.78e-24 |
|
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: 97.82 E-value: 6.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSF----GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRP---TSGRVAFAGRDLAGLIPEEI 76
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 77 ARL---GIGRTFQNirlfaGMSVLDnvrvPgqcRLRSGlwSQVV-------GLSAARREEDEGrerawELLRLVGLeSRA 146
Cdd:COG0444 81 RKIrgrEIQMIFQD-----PMTSLN----P---VMTVG--DQIAeplrihgGLSKAEARERAI-----ELLERVGL-PDP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 147 ERAAGSLPY----GDRRRLEIARALALSPRLLLLDEPAAGMNPS-EKQALSgFIREIRETFSLTVLLIEHHVPMVMGLCD 221
Cdd:COG0444 141 ERRLDRYPHelsgGMRQRVMIARALALEPKLLIADEPTTALDVTiQAQILN-LLKDLQRELGLAILFITHDLGVVAEIAD 219
|
250
....*....|....*....
gi 527030459 222 RIAVLNFGELIALGTPEEV 240
Cdd:COG0444 220 RVAVMYAGRIVEEGPVEEL 238
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-250 |
1.92e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 95.61 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 3 AILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIA-RLGI 81
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELArRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 82 GRtfQNIRLFAGMSVLDNVRVpgqcrlrsglwsqvvGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRL 161
Cdd:PRK13548 81 LP--QHSSLSFPFTVEEVVAM---------------GRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 162 EIARALALSPRLLLL------DEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALG 235
Cdd:PRK13548 144 QLARVLAQLWEPDGPprwlllDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
250
....*....|....*
gi 527030459 236 TPEEVQDDEKVVQAY 250
Cdd:PRK13548 224 TPAEVLTPETLRRVY 238
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-248 |
2.60e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 95.53 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSF-GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGR----DLAGLIPeeiAR 78
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikyDKKSLLE---VR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 79 LGIGRTFQNI--RLFAGmSVLDNVRVpGQCRLrsglwsqvvGLSAARREEDEGrerawELLRLVGLESRAERAAGSLPYG 156
Cdd:PRK13639 78 KTVGIVFQNPddQLFAP-TVEEDVAF-GPLNL---------GLSKEEVEKRVK-----EALKAVGMEGFENKPPHHLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 157 DRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGT 236
Cdd:PRK13639 142 QKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
250
....*....|..
gi 527030459 237 PEEVQDDEKVVQ 248
Cdd:PRK13639 221 PKEVFSDIETIR 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-243 |
2.95e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.41 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 19 AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIP---EEIARLGIGRTFQNIRLFAGMS 95
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 96 VLDNVrvpgqcrlrsglwsqVVGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIARALALSPRLLL 175
Cdd:PRK10070 123 VLDNT---------------AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 176 LDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQDD 243
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-256 |
4.28e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 96.33 E-value: 4.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAgliPEEIARLGIGRT 84
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT---HRSIQQRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVrvpgqcrlrsGLWSQVVGLSAARREEDEGrerawELLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:PRK11432 84 FQSYALFPHMSLGENV----------GYGLKMLGVPKEERKQRVK-----EALELVDLAGFEDRYVDQISGGQQQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV--QD 242
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELyrQP 228
|
250
....*....|....
gi 527030459 243 DEKVVQAYLGESAL 256
Cdd:PRK11432 229 ASRFMASFMGDANI 242
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-243 |
8.00e-23 |
|
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: 95.56 E-value: 8.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 23 VSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDL----AGLI-PEEIARLGIgrTFQNIRLFAGMSVL 97
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFlPPEKRRIGY--VFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 98 DNvrvpgqcrLRSGLWSQVVGLSAARREedegrerawELLRLVGLESRAERAAGSLPYGDRRRLEIARALALSPRLLLLD 177
Cdd:TIGR02142 94 GN--------LRYGMKRARPSERRISFE---------RVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527030459 178 EPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQDD 243
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-243 |
9.14e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 93.92 E-value: 9.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMT---RPTSGRVAFAGRDL--AGLIPEE 75
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVqrEGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 76 I--ARLGIGRTFQNIRLFAGMSVLDNVrvpgqcrLRSGLWSQVVGLSAARREEDEGRERAWELLRLVGLESRAERAAGSL 153
Cdd:PRK09984 81 IrkSRANTGYIFQQFNLVNRLSVLENV-------LIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 154 PYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIA 233
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFY 233
|
250
....*....|
gi 527030459 234 LGTPEEVQDD 243
Cdd:PRK09984 234 DGSSQQFDNE 243
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-168 |
3.50e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 91.59 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLaGLIPEEIARL--GI 81
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLrrKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 82 GRTFQNIRLFAGMSVLDNVRVpGQCRLRsglwsqvvGLSAARREEDegrerAWELLRLVGLESRAERAAGSLPYGDRRRL 161
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTL-APIKVK--------KMSKAEAEER-----AMELLERVGLADKADAYPAQLSGGQQQRV 145
|
....*..
gi 527030459 162 EIARALA 168
Cdd:COG1126 146 AIARALA 152
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-239 |
5.53e-22 |
|
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: 94.45 E-value: 5.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 2 SAILEVSDLTKSF--GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARL 79
Cdd:COG4987 331 GPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 gIGRTFQNIRLFAGmSVLDNVRVpgqcrlrsglwsqvvGLSAARREEdegrerAWELLRLVGLESRAERAAGSLPY---- 155
Cdd:COG4987 411 -IAVVPQRPHLFDT-TLRENLRL---------------ARPDATDEE------LWAALERVGLGDWLAALPDGLDTwlge 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 156 -------GDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALsgfIREIRETF-SLTVLLIEHHvPMVMGLCDRIAVLN 227
Cdd:COG4987 468 ggrrlsgGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL---LADLLEALaGRTVLLITHR-LAGLERMDRILVLE 543
|
250
....*....|..
gi 527030459 228 FGELIALGTPEE 239
Cdd:COG4987 544 DGRIVEQGTHEE 555
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-241 |
7.75e-22 |
|
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: 94.70 E-value: 7.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGLT--AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGI 81
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 82 GRTFQNI-RLFAGmsvldnvrvpgqcRLRSGLWSQVVGLSAARREEDEGreraWELLRLvGLESRAERAAGSLPYGDRRR 160
Cdd:TIGR01257 2017 CPQFDAIdDLLTG-------------REHLYLYARLRGVPAEEIEKVAN----WSIQSL-GLSLYADRLAGTYSGGNKRK 2078
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 161 LEIARALALSPRLLLLDEPAAGMNPSEKQAL----SGFIREIRetfslTVLLIEHHVPMVMGLCDRIAVLNFGELIALGT 236
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLwntiVSIIREGR-----AVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
....*
gi 527030459 237 PEEVQ 241
Cdd:TIGR01257 2154 IQHLK 2158
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-243 |
1.99e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 92.76 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLG 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIRLFAGMSVLDNVRVPGQCRLRSG--LWSQVvglsaarreedegRERAWELLRLVGLESRAERAAGSLPYGDR 158
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGREFVNRFGriDWKKM-------------YAEADKLLARLNLRFSSDKLVGELSIGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 159 RRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPE 238
Cdd:PRK10762 148 QMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVA 226
|
....*
gi 527030459 239 EVQDD 243
Cdd:PRK10762 227 DLTED 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-239 |
2.44e-21 |
|
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: 92.90 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSF-GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgIGR 83
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ-IAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 84 TFQNIRLFAGmSVLDNVRVPGQCRLRSGLWS--QVVGLsaarreedegreraWELLRLV--GLESR-AERAAGsLPYGDR 158
Cdd:COG4988 416 VPQNPYLFAG-TIRENLRLGRPDASDEELEAalEAAGL--------------DEFVAALpdGLDTPlGEGGRG-LSGGQA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 159 RRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfsLTVLLIEHHvPMVMGLCDRIAVLNFGELIALGTPE 238
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHR-LALLAQADRILVLDDGRIVEQGTHE 556
|
.
gi 527030459 239 E 239
Cdd:COG4988 557 E 557
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-255 |
2.82e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.92 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSF----------GGL-----------TAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVA 62
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkGALkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 63 FAGRDlagliP----EEIARlgigrtfqNIRLfagmsvldnvrVPGQcrlRSGLW------------SQVVGLSAARREE 126
Cdd:COG4586 81 VLGYV-----PfkrrKEFAR--------RIGV-----------VFGQ---RSQLWwdlpaidsfrllKAIYRIPDAEYKK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 127 DEGrerawELLRLVGLESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTV 206
Cdd:COG4586 134 RLD-----ELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTI 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 527030459 207 LLIEHHvpmvMG----LCDRIAVLNFGELIALGTPEEVQD---DEKVVQAYLGESA 255
Cdd:COG4586 209 LLTSHD----MDdieaLCDRVIVIDHGRIIYDGSLEELKErfgPYKTIVLELAEPV 260
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-240 |
3.83e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 90.56 E-value: 3.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSF---GGL--------TAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLI 72
Cdd:COG4608 7 LLEVRDLKKHFpvrGGLfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 73 PEEIARL--GIGRTFQ------NIRlfagMSVLDNVRVPgqcrLR-SGLWSQvvglsaarreeDEGRERAWELLRLVGLe 143
Cdd:COG4608 87 GRELRPLrrRMQMVFQdpyaslNPR----MTVGDIIAEP----LRiHGLASK-----------AERRERVAELLELVGL- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 144 sRAErAAGSLPY----GDRRRLEIARALALSPRLLLLDEPAAGMNPS-EKQALSgFIREIRETFSLTVLLIEHHVPMVMG 218
Cdd:COG4608 147 -RPE-HADRYPHefsgGQRQRIGIARALALNPKLIVCDEPVSALDVSiQAQVLN-LLEDLQDELGLTYLFISHDLSVVRH 223
|
250 260
....*....|....*....|..
gi 527030459 219 LCDRIAVLNFGELIALGTPEEV 240
Cdd:COG4608 224 ISDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-235 |
3.98e-21 |
|
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: 88.12 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 29 EGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDL------AGLIPEeiaRLGIGRTFQNIRLFAGMSVLDNVrV 102
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkINLPPQ---QRKIGLVFQQYALFPHLNVRENL-A 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 103 PGQCRLRSGLWSQVVGlsaarreedegrerawELLRLVGLESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAG 182
Cdd:cd03297 98 FGLKRKRNREDRISVD----------------ELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 527030459 183 MNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALG 235
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-240 |
4.01e-21 |
|
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: 92.17 E-value: 4.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMT--RPTSGRV----------------AFAGR 66
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 67 DL----AGLIPEEI--------------ARLGI--GRTFQnirLFAGMSVLDNVrvpgqcrLRSglwsqvvgLSAARREE 126
Cdd:TIGR03269 81 PCpvcgGTLEPEEVdfwnlsdklrrrirKRIAImlQRTFA---LYGDDTVLDNV-------LEA--------LEEIGYEG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 127 DEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTV 206
Cdd:TIGR03269 143 KEAVGRAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISM 222
|
250 260 270
....*....|....*....|....*....|....
gi 527030459 207 LLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:TIGR03269 223 VLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
5-243 |
6.89e-21 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 90.16 E-value: 6.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVsDLTKSFGGLTAVagVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDL----AGL-IPEEiaRL 79
Cdd:COG4148 3 LEV-DFRLRRGGFTLD--VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsaRGIfLPPH--RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 GIGRTFQNIRLFAGMSVLDNvrvpgqcrLRSGLWSQVVGLSAARREedegrerawELLRLVGLESRAERAAGSLPYGDRR 159
Cdd:COG4148 78 RIGYVFQEARLFPHLSVRGN--------LLYGRKRAPRAERRISFD---------EVVELLGIGHLLDRRPATLSGGERQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 160 RLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEE 239
Cdd:COG4148 141 RVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAE 220
|
....
gi 527030459 240 VQDD 243
Cdd:COG4148 221 VLSR 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-235 |
7.32e-21 |
|
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: 87.55 E-value: 7.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGglTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPeeiARLGIGRT 84
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP---ADRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVrvpgqcrlrsGLwsqvvGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:cd03298 76 FQENNLFAHLTVEQNV----------GL-----GLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALG 235
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-248 |
7.68e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.89 E-value: 7.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 2 SAILEVSDLTKSFGGLT--AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIaRL 79
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI-RK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 GIGRTFQNI-RLFAGMSV-------LDNVRVPgqcrlRSGLWSQVVGLSAArreedegrerawellrlVGLESRAERAAG 151
Cdd:PRK13632 84 KIGIIFQNPdNQFIGATVeddiafgLENKKVP-----PKKMKDIIDDLAKK-----------------VGMEDYLDKEPQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 152 SLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMgLCDRIAVLNFGEL 231
Cdd:PRK13632 142 NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKL 220
|
250
....*....|....*..
gi 527030459 232 IALGTPEEVQDDEKVVQ 248
Cdd:PRK13632 221 IAQGKPKEILNNKEILE 237
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-248 |
8.42e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 88.67 E-value: 8.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEI--ARLGI 81
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 82 GRTFQNIRLFAGMSVLDNVRVP--GQCRLRSGLWSQVVGLSaarreedegrerawelLRLVGLESRAERAAGSLPYGDRR 159
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPlrEHTQLPAPLLHSTVMMK----------------LEAVGLRGAAKLMPSELSGGMAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 160 RLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEE 239
Cdd:PRK11831 151 RAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA 230
|
250
....*....|.
gi 527030459 240 VQ--DDEKVVQ 248
Cdd:PRK11831 231 LQanPDPRVRQ 241
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-243 |
1.41e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.46 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRD-LAGLIPEEIARLGIG 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RTFQNIRLFAGMSVLDNVRVpGQCRLRsglwsqvvGLSAARREEDegrerAWELLRLVGLESRAERAAGSLPYGDRRRLE 162
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMF-GPLRVR--------GASKEEAEKQ-----ARELLAKVGLAERAHHYPSELSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 163 IARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQD 242
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
.
gi 527030459 243 D 243
Cdd:PRK09493 226 N 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-240 |
2.06e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 87.76 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLT--AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIaR 78
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV-R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 79 LGIGRTFQNI-RLFAGMSVLDNVrvpgqcrlrsglwsqVVGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGD 157
Cdd:PRK13635 81 RQVGMVFQNPdNQFVGATVQDDV---------------AFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 158 RRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGlCDRIAVLNFGELIALGTP 237
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTP 224
|
...
gi 527030459 238 EEV 240
Cdd:PRK13635 225 EEI 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-252 |
2.07e-20 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 89.88 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMtRPT---SGRVAFAGRDLAGLIPEEIARLG 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIRLFAGMSVLDNVRVPGQCRLRSGLwsqvvglsaarREEDEGRERAWELLRLVGLE-SRAERAAGSLPYGDRR 159
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEITLPGGR-----------MAYNAMYLRAKNLLRELQLDaDNVTRPVGDYGGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 160 RLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALgTPEE 239
Cdd:TIGR02633 149 LVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVAT-KDMS 226
|
250
....*....|...
gi 527030459 240 VQDDEKVVQAYLG 252
Cdd:TIGR02633 227 TMSEDDIITMMVG 239
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-245 |
3.13e-20 |
|
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: 85.66 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGM--TRPTSGRVAFAGRDLAGLIPEEIARLGIG 82
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RTFQNIRLFAGMSVLDNVRvpgqcrlrsglwSQVVGLSAarreedegrerawellrlvglesraeraagslpyGDRRRLE 162
Cdd:cd03217 81 LAFQYPPEIPGVKNADFLR------------YVNEGFSG----------------------------------GEKKRNE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 163 IARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHH-------VPmvmglcDRIAVLNFGELIALG 235
Cdd:cd03217 115 ILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYqrlldyiKP------DRVHVLYDGRIVKSG 187
|
250
....*....|
gi 527030459 236 TPEEVQDDEK 245
Cdd:cd03217 188 DKELALEIEK 197
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-240 |
4.91e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.03 E-value: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 19 AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLA--GLIPEEIaRLGIGRTFQ--NIRLFAGM 94
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDI-RKKVGLVFQypEYQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 95 SVLDNVRVPgqcrlrsglwsQVVGLSaarreEDEGRERAWELLRLVGL--ESRAERAAGSLPYGDRRRLEIARALALSPR 172
Cdd:PRK13637 101 IEKDIAFGP-----------INLGLS-----EEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 173 LLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-232 |
1.02e-19 |
|
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: 84.23 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 6 EVSDLTKSFGGLT-AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDlaglIPEEIARLGIGRT 84
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP----IKAKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIR--LFaGMSVLDNVRvpgqcrlrsglwsqvVGLSAArreeDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLE 162
Cdd:cd03226 77 MQDVDyqLF-TDSVREELL---------------LGLKEL----DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLA 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 163 IARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSlTVLLIEHHVPMVMGLCDRIAVLNFGELI 232
Cdd:cd03226 137 IAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-233 |
1.55e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.29 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTrPT---SGRVAFAGRDLAGLIPEEIA 77
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 78 RLGIGRTFQNIRLFAGMSVLDNVRVpGQCRLRSGL--WSQVVglsaarreedegrERAWELLRLVGLESRAERAAGSLPY 155
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFL-GNEITPGGImdYDAMY-------------LRAQKLLAQLKLDINPATPVGNLGL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 156 GDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIA 233
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHIG 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-248 |
1.67e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.28 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 2 SAILEVSDLTKSFG-GLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRdlagliPEEIARLG 80
Cdd:PRK13636 3 DYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK------PIDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIrlfaGMSVLDnvrvPGQCRLRSGLWSQV-VGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRR 159
Cdd:PRK13636 77 LMKLRESV----GMVFQD----PDNQLFSASVYQDVsFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 160 RLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEE 239
Cdd:PRK13636 149 RVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKE 228
|
....*....
gi 527030459 240 VQDDEKVVQ 248
Cdd:PRK13636 229 VFAEKEMLR 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-230 |
1.72e-19 |
|
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: 82.82 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGG--LTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgIG 82
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RTFQNIRLFAGmSVLDNVrvpgqcrlrsglwsqvvgLSAarreedegrerawellrlvglesraeraagslpyGDRRRLE 162
Cdd:cd03228 80 YVPQDPFLFSG-TIRENI------------------LSG----------------------------------GQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 163 IARALALSPRLLLLDEPAAGMNP-SEKQALSGfIREIRETfsLTVLLIEHHVPMVMgLCDRIAVLNFGE 230
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPeTEALILEA-LRALAKG--KTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-235 |
1.78e-19 |
|
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: 83.79 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 19 AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIaRLGIGRTFQNIRLFAGmSVLD 98
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL-RRNIGYVPQDVTLFYG-TLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 99 NVrvpgqcRLRSGLWSQVVGLSAARREEDEgrerawELLRL--VGLESR-AERAAGsLPYGDRRRLEIARALALSPRLLL 175
Cdd:cd03245 97 NI------TLGAPLADDERILRAAELAGVT------DFVNKhpNGLDLQiGERGRG-LSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527030459 176 LDEPAAGM-NPSE---KQALSGFIREIretfslTVLLIEHHVPMvMGLCDRIAVLNFGELIALG 235
Cdd:cd03245 164 LDEPTSAMdMNSEerlKERLRQLLGDK------TLIIITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-242 |
1.87e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.47 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSF----GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEI 76
Cdd:PRK10535 1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 77 ARL---GIGRTFQNIRLFAGMSVLDNVRVPGqcrlrsglwsqvvglSAARREEDEGRERAWELLRLVGLESRAERAAGSL 153
Cdd:PRK10535 81 AQLrreHFGFIFQRYHLLSHLTAAQNVEVPA---------------VYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 154 PYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHvPMVMGLCDRIAVLNFGELIA 233
Cdd:PRK10535 146 SGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHD-PQVAAQAERVIEIRDGEIVR 223
|
....*....
gi 527030459 234 LGTPEEVQD 242
Cdd:PRK10535 224 NPPAQEKVN 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-229 |
2.12e-19 |
|
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: 84.05 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 22 GVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRdlaglipeEIARLGIGR--TFQNIRLFAGMSVLDN 99
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK--------QITEPGPDRmvVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 100 VRVPGQC---RLRSGLWSQVVGlsaarreedegrerawELLRLVGLESRAERAAGSLPYGDRRRLEIARALALSPRLLLL 176
Cdd:TIGR01184 75 IALAVDRvlpDLSKSERRAIVE----------------EHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 527030459 177 DEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFG 229
Cdd:TIGR01184 139 DEPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-237 |
2.73e-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: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 7 VSDLTKSF--GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIpeEIARLGIGRT 84
Cdd:TIGR01257 931 VKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNL--DAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVRVPGQCRLRSglWSQVVGLSAArreedegreraweLLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRS--WEEAQLEMEA-------------MLEDTGLHHKRNEEAQDLSGGMQRKLSVA 1073
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIREtfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTP 237
Cdd:TIGR01257 1074 IAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-226 |
2.85e-19 |
|
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: 86.57 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLT-AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGlIPEEIARLGIGR 83
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD-ADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 84 TFQNIRLFAGmSVLDNVRV--PGQcrlrsglwsqvvglSAARREEDEGRERAWELLRLV--GLESRAERAAGSLPYGDRR 159
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLarPDA--------------SDAEIREALERAGLDEFVAALpqGLDTPIGEGGAGLSGGQAQ 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527030459 160 RLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfsLTVLLIEHHvPMVMGLCDRIAVL 226
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHR-LALAALADRIVVL 529
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-213 |
5.46e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 83.37 E-value: 5.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAiLEVSDLTKSFGG----LTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEi 76
Cdd:COG4525 1 MSM-LTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 77 arlgiGRTFQNIRLFAGMSVLDNVRVPgqCRLRsglwsqvvGLSAARREEDegrerAWELLRLVGLESRAERAAGSLPYG 156
Cdd:COG4525 79 -----GVVFQKDALLPWLNVLDNVAFG--LRLR--------GVPKAERRAR-----AEELLALVGLADFARRRIWQLSGG 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527030459 157 DRRRLEIARALALSPRLLLLDEPAAgmnpsekqALSGFIREIRETFSLT--------VLLIEHHV 213
Cdd:COG4525 139 MRQRVGIARALAADPRFLLMDEPFG--------ALDALTREQMQELLLDvwqrtgkgVFLITHSV 195
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-211 |
1.37e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.44 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEiarlgiGR 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER------GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 84 TFQNIRLFAGMSVLDNVrvpgqcrlrsglwsqVVGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEI 163
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNV---------------AFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGI 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 527030459 164 ARALALSPRLLLLDEPAAgmnpsekqALSGFIREIRETFSLT--------VLLIEH 211
Cdd:PRK11248 140 ARALAANPQLLLLDEPFG--------ALDAFTREQMQTLLLKlwqetgkqVLLITH 187
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-240 |
2.14e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 81.72 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAIlEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAF------AGRDLA---GL 71
Cdd:PRK11264 1 MSAI-EVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSqqkGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 72 IPEeiARLGIGRTFQNIRLFAGMSVLDNVrVPGQCRLRSGLWSQVVGLsaarreedegrerAWELLRLVGLESRAERAAG 151
Cdd:PRK11264 80 IRQ--LRQHVGFVFQNFNLFPHRTVLENI-IEGPVIVKGEPKEEATAR-------------ARELLAKVGLAGKETSYPR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 152 SLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGEL 231
Cdd:PRK11264 144 RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
....*....
gi 527030459 232 IALGTPEEV 240
Cdd:PRK11264 223 VEQGPAKAL 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-240 |
4.09e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 81.11 E-value: 4.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 3 AILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTR-----PTSGRVAFAGRDLAGL------ 71
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMdvielr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 72 --------IPEEIARLGIgrtFQNIRLFAGMSVLDNVRVPGQCRLRSGLwsqvvglsaarreedeGRERAWELLRlvgle 143
Cdd:PRK14247 82 rrvqmvfqIPNPIPNLSI---FENVALGLKLNRLVKSKKELQERVRWAL----------------EKAQLWDEVK----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 144 SRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIREtfSLTVLLIEHHVPMVMGLCDRI 223
Cdd:PRK14247 138 DRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYV 215
|
250
....*....|....*..
gi 527030459 224 AVLNFGELIALGTPEEV 240
Cdd:PRK14247 216 AFLYKGQIVEWGPTREV 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-166 |
6.98e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 6.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 7 VSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRdlaglipEEIARLGigrtfQ 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-------LRIGYLP-----Q 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 87 NIRLFAGMSVLDNVrVPGQCRLRSgLWSQVVGLSAARREEDEGRERAWEL---LRLVG---LESRAERAA---------- 150
Cdd:COG0488 69 EPPLDDDLTVLDTV-LDGDAELRA-LEAELEELEAKLAEPDEDLERLAELqeeFEALGgweAEARAEEILsglgfpeedl 146
|
170 180
....*....|....*....|
gi 527030459 151 ----GSLPYGDRRRLEIARA 166
Cdd:COG0488 147 drpvSELSGGWRRRVALARA 166
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-250 |
8.24e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.22 E-value: 8.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 2 SAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARlGI 81
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR-KV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 82 GRTFQNIRLFAGMSVLDNV---RVPgqcrlrsglWSQVVGLSAARREEDEGrerawELLRLVGLESRAERAAGSLPYGDR 158
Cdd:PRK10575 88 AYLPQQLPAAEGMTVRELVaigRYP---------WHGALGRFGAADREKVE-----EAISLVGLKPLAHRLVDSLSGGER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 159 RRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPE 238
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPA 233
|
250
....*....|..
gi 527030459 239 EVQDDEKVVQAY 250
Cdd:PRK10575 234 ELMRGETLEQIY 245
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-78 |
1.34e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 79.36 E-value: 1.34e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527030459 6 EVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIAR 78
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK 75
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-240 |
3.10e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.55 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 23 VSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTR------PTSGRVAFAGRDLAGLIPEEIaRLGIGRTFQNIRLFAGMSV 96
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKL-RKEVGMVFQQPNPFPHLSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 97 LDNVRVPGQcrlrsglwsqvvglSAARREEDEGRERAWELLRLVGL----ESRAERAAGSLPYGDRRRLEIARALALSPR 172
Cdd:PRK14246 108 YDNIAYPLK--------------SHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 173 LLLLDEPAAGMNPSEKQALSGFIREIREtfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
22-240 |
3.14e-17 |
|
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: 78.04 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 22 GVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGlIPEEIARLGIGRTFQNIRLFAGmSVLDNVR 101
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRD-ISRKSLRSMIGVVLQDTFLFSG-TIMENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 102 vpgqcrlrsglwsqvVGLSAARREEDEGRERAWELLRLV-----GLESRAERAAGSLPYGDRRRLEIARALALSPRLLLL 176
Cdd:cd03254 99 ---------------LGRPNATDEEVIEAAKEAGAHDFImklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527030459 177 DEPAAGMNPSEKQALSGFIREIREtfSLTVLLIEHHVPMVMGlCDRIAVLNFGELIALGTPEEV 240
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-252 |
3.76e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLG 80
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIRLFAGMSVLDNVRVpGQCRLRSGlwsqVVGLSAArreedegRERAWELLRLVGLESRAERAAGSLPYGDRRR 160
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYL-GQLPHKGG----IVNRRLL-------NYEAREQLEHLGVDIDPDTPLKYLSIGQRQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 161 LEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIAlgTPEEV 240
Cdd:PRK11288 149 VEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA--TFDDM 225
|
250
....*....|....
gi 527030459 241 Q--DDEKVVQAYLG 252
Cdd:PRK11288 226 AqvDRDQLVQAMVG 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-61 |
4.45e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 4.45e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRV 61
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV 372
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-95 |
5.43e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.81 E-value: 5.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSF----------------------GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTS 58
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 527030459 59 GRVAFAGR-----DL-AGLIPEEIARlgigrtfQNIRLFA---GMS 95
Cdd:COG1134 81 GRVEVNGRvsallELgAGFHPELTGR-------ENIYLNGrllGLS 119
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-240 |
5.50e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 5.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARlGIGR 83
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR-RLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 84 TFQNIRLFAGMSVLDNV---RVPgqcrlRSGLWSQvvgLSAArreEDEGRERAWELLRLVGLesrAERAAGSLPYGDRRR 160
Cdd:PRK11231 81 LPQHHLTPEGITVRELVaygRSP-----WLSLWGR---LSAE---DNARVNQAMEQTRINHL---ADRRLTDLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 161 LEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-236 |
8.96e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.98 E-value: 8.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSaiLEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGR--DLAGLI-PEEIA 77
Cdd:PRK11124 1 MS--IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPsDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 78 RL--GIGRTFQNIRLFAGMSVLDNVrVPGQCRlrsglwsqVVGLSAARREEDegrerAWELLRLVGLESRAERAAGSLPY 155
Cdd:PRK11124 79 ELrrNVGMVFQQYNLWPHLTVQQNL-IEAPCR--------VLGLSKDQALAR-----AEKLLERLRLKPYADRFPLHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 156 GDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALG 235
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
.
gi 527030459 236 T 236
Cdd:PRK11124 224 D 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-231 |
9.35e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 76.74 E-value: 9.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGG----LTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARL 79
Cdd:PRK10584 6 IVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 ---GIGRTFQNIRLFAGMSVLDNVRVPGQCRLRSGLWSQvvglsaarreedegrERAWELLRLVGLESRAERAAGSLPYG 156
Cdd:PRK10584 86 rakHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSR---------------NGAKALLEQLGLGKRLDHLPAQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527030459 157 DRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHvPMVMGLCDRIAVLNFGEL 231
Cdd:PRK10584 151 EQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-240 |
1.04e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.46 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLT---AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIA 77
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 78 RLgIGRTFQNI-RLFAGMSVLDNVRVpgqcrlrsGLWSQVVGLSAARREEDegrerawELLRLVGLESRAERAAGSLPYG 156
Cdd:PRK13650 81 HK-IGMVFQNPdNQFVGATVEDDVAF--------GLENKGIPHEEMKERVN-------EALELVGMQDFKEREPARLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 157 DRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVmGLCDRIAVLNFGELIALGT 236
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTST 223
|
....
gi 527030459 237 PEEV 240
Cdd:PRK13650 224 PREL 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-236 |
1.63e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 76.20 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSaiLEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGR--DLAGLIPEEIAR 78
Cdd:COG4161 1 MS--IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 79 L---GIGRTFQNIRLFAGMSVLDNVrVPGQCRlrsglwsqVVGLSAARREEDegrerAWELLRLVGLESRAERAAGSLPY 155
Cdd:COG4161 79 LlrqKVGMVFQQYNLWPHLTVMENL-IEAPCK--------VLGLSKEQAREK-----AMKLLARLRLTDKADRFPLHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 156 GDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALG 235
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
.
gi 527030459 236 T 236
Cdd:COG4161 224 D 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-231 |
1.64e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.07 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 14 FGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIA--RLGIGRTFQNIRLF 91
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 92 AGMSVLDNVRVPgqcrlrsglwsqvvgLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIARALALSP 171
Cdd:PRK10908 92 MDRTVYDNVAIP---------------LIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527030459 172 RLLLLDEPAAGMNpsekQALSGFIREIRETFS---LTVLLIEHHVPMVMGLCDRIAVLNFGEL 231
Cdd:PRK10908 157 AVLLADEPTGNLD----DALSEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-261 |
1.87e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.58 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDL----AGLIPeeiARL 79
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskRGLLA---LRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 GIGRTFQNirlfagmsvldnvrvPGQCRLRSGLWSQVV-GLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDR 158
Cdd:PRK13638 78 QVATVFQD---------------PEQQIFYTDIDSDIAfSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 159 RRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSlTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPE 238
Cdd:PRK13638 143 KRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPG 221
|
250 260
....*....|....*....|....
gi 527030459 239 EV-QDDEKVVQAYLGESALGESHA 261
Cdd:PRK13638 222 EVfACTEAMEQAGLTQPWLVKLHT 245
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-240 |
2.09e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 77.54 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSF----GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMT----RPTSGRVAFAGRDLAGLIPEE 75
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 76 IARLgIGRT----FQNIRlfagmSVLDNVRVPGQCRLRS-------GLWSQVVGLSaarreedegRERAWELLRLVGLES 144
Cdd:PRK15093 83 RRKL-VGHNvsmiFQEPQ-----SCLDPSERVGRQLMQNipgwtykGRWWQRFGWR---------KRRAIELLHRVGIKD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 145 RAErAAGSLPY----GDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLC 220
Cdd:PRK15093 148 HKD-AMRSFPYelteGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWA 226
|
250 260
....*....|....*....|
gi 527030459 221 DRIAVLNFGELIALGTPEEV 240
Cdd:PRK15093 227 DKINVLYCGQTVETAPSKEL 246
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-241 |
3.12e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.86 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 3 AIlEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAgliPEEIA-RLGI 81
Cdd:NF033858 266 AI-EARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDIAtRRRV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 82 GRTFQNIRLFAGMSVLDNVRvpgqcrlrsgLWSQVVGLSAARREEDEGrerawELLRLVGLESRAERAAGSLPYGDRRRL 161
Cdd:NF033858 342 GYMSQAFSLYGELTVRQNLE----------LHARLFHLPAAEIAARVA-----EMLERFDLADVADALPDSLPLGIRQRL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 162 EIARALALSPRLLLLDEPAAGMNPsekQALSGFIReiretfsltvLLIE-------------HhvpmVMG---LCDRIAV 225
Cdd:NF033858 407 SLAVAVIHKPELLILDEPTSGVDP---VARDMFWR----------LLIElsredgvtifistH----FMNeaeRCDRISL 469
|
250
....*....|....*.
gi 527030459 226 LNFGELIALGTPEEVQ 241
Cdd:NF033858 470 MHAGRVLASDTPAALV 485
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-231 |
7.32e-16 |
|
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: 73.24 E-value: 7.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 3 AILEVSDLTksfgGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIG 82
Cdd:cd03215 3 PVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 -----RtfQNIRLFAGMSVLDNVRVPgqcRLRSGlwsqvvglsaarreedegrerawellrlvglesraeraagslpyGD 157
Cdd:cd03215 79 yvpedR--KREGLVLDLSVAENIALS---SLLSG--------------------------------------------GN 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527030459 158 RRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGEL 231
Cdd:cd03215 110 QQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-216 |
7.43e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.55 E-value: 7.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIP---EEIARLGi 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDephENILYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 82 grtfQNIRLFAGMSVLDNVRvpgqcrlrsgLWSQVVGlsaarreedEGRERAWELLRLVGLESRAERAAGSLPYGDRRRL 161
Cdd:TIGR01189 80 ----HLPGLKPELSALENLH----------FWAAIHG---------GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 527030459 162 EIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMV 216
Cdd:TIGR01189 137 ALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-231 |
8.71e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 74.71 E-value: 8.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVafagrdLAGLIPEEIARLGIGRT 84
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAGMSVLDNVrvpgqcrlrsGLwsqvvGLSAARREEdegrerAWELLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:PRK11247 87 FQDARLLPWKKVIDNV----------GL-----GLKGQWRDA------ALQALAAVGLADRANEWPAALSGGQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGEL 231
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-85 |
9.78e-16 |
|
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: 72.10 E-value: 9.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPE----EIARLG 80
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQlsggEKMRLA 80
|
....*
gi 527030459 81 IGRTF 85
Cdd:cd03221 81 LAKLL 85
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-231 |
1.23e-15 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 72.63 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTA--VAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgIG 82
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH-VG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RTFQNIRLFAGmSVLDNVrvpgqcrlrsglwsqvvgLSAarreedegrerawellrlvglesraeraagslpyGDRRRLE 162
Cdd:cd03246 80 YLPQDDELFSG-SIAENI------------------LSG----------------------------------GQRQRLG 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 163 IARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSlTVLLIEHHvPMVMGLCDRIAVLNFGEL 231
Cdd:cd03246 107 LARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGA-TRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-240 |
1.27e-15 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 75.94 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 20 VAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgIGRTFQNIRLFAGmSVLDN 99
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH-IGYLPQDVELFDG-TIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 100 VrvpgqCRLRSGLWSQVVglSAArreedeGRERAWEL-LRL-VGLESRAERAAGSLPYGDRRRLEIARALALSPRLLLLD 177
Cdd:COG4618 426 I-----ARFGDADPEKVV--AAA------KLAGVHEMiLRLpDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLD 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527030459 178 EPAAGMNPSEKQALSGFIREIRETFSlTVLLIEHHvPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:COG4618 493 EPNSNLDDEGEAALAAAIRALKARGA-TVVVITHR-PSLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-223 |
3.60e-15 |
|
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: 72.47 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSF-----GG--LTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRV----AFAGRDLA 69
Cdd:COG4778 1 MTTLLEVENLSKTFtlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhDGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 70 GLIPEEIARL---GIGRTFQNIRLFAGMSVLDNVRVPgqcrlrsgLWSQVVGLSAARREedegrerAWELLRLVGLESRA 146
Cdd:COG4778 81 QASPREILALrrrTIGYVSQFLRVIPRVSALDVVAEP--------LLERGVDREEARAR-------ARELLARLNLPERL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 147 ERAA-----GslpyGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCD 221
Cdd:COG4778 146 WDLPpatfsG----GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVAD 220
|
..
gi 527030459 222 RI 223
Cdd:COG4778 221 RV 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-240 |
4.30e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.24 E-value: 4.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 19 AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDL-AGLIPEEI--ARLGIGRTFQ--NIRLFAg 93
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIkqIRKKVGLVFQfpESQLFE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 94 MSVLDNVrvpgqcrlrsGLWSQVVGLSaarreEDEGRERAWELLRLVGL-ESRAERAAGSLPYGDRRRLEIARALALSPR 172
Cdd:PRK13649 101 ETVLKDV----------AFGPQNFGVS-----QEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 173 LLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-63 |
5.48e-15 |
|
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: 74.20 E-value: 5.48e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAF 63
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-240 |
6.20e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.38 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTS-----GRVAFAGRDlaglIPEEiaRL 79
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQN----IYER--RV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 GIGR-------TFQNIRLFAgMSVLDNV----RVPGqcrlrsglWSQVVGLSAARREEDEGRERaWELLRlvgleSRAER 148
Cdd:PRK14258 82 NLNRlrrqvsmVHPKPNLFP-MSVYDNVaygvKIVG--------WRPKLEIDDIVESALKDADL-WDEIK-----HKIHK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 149 AAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLN- 227
Cdd:PRK14258 147 SALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKg 226
|
250
....*....|....*..
gi 527030459 228 ----FGELIALGTPEEV 240
Cdd:PRK14258 227 nenrIGQLVEFGLTKKI 243
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-232 |
6.31e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.67 E-value: 6.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMtRPT---SGRVAFAG-----RDLAglipeE 75
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGevcrfKDIR-----D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 76 IARLGIGRTFQNIRLFAGMSVLDNVRVpGQCRLRSGL--WSQVvglsaarreedegRERAWELLRLVGLESRAERAAGSL 153
Cdd:NF040905 75 SEALGIVIIHQELALIPYLSIAENIFL-GNERAKRGVidWNET-------------NRRARELLAKVGLDESPDTLVTDI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 154 PYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELI 232
Cdd:NF040905 141 GVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-232 |
6.99e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.41 E-value: 6.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGG---------LTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPE 74
Cdd:PRK10419 3 LLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 75 EIA--RLGIGRTFQ------NIRlfagMSVLDNVRVPgqcrLRsglwsQVVGLSAARREEDEGrerawELLRLVGL-ESR 145
Cdd:PRK10419 83 QRKafRRDIQMVFQdsisavNPR----KTVREIIREP----LR-----HLLSLDKAERLARAS-----EMLRAVDLdDSV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 146 AERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAV 225
Cdd:PRK10419 145 LDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMV 224
|
....*..
gi 527030459 226 LNFGELI 232
Cdd:PRK10419 225 MDNGQIV 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
32-240 |
7.69e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.98 E-value: 7.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 32 IFGLigpNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAG------LIPEeiaRLGIGRTFQNIRLFAGMSVLDNVRVpGQ 105
Cdd:PRK11144 29 IFGR---SGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPE---KRRIGYVFQDARLFPHYKVRGNLRY-GM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 106 CRLRSGLWSQVVglsaarreedegrerawellRLVGLESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNP 185
Cdd:PRK11144 102 AKSMVAQFDKIV--------------------ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 527030459 186 SEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:PRK11144 162 PRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-243 |
8.77e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.88 E-value: 8.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGR-----DLAGLIPEE 75
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 76 IARLgiGRT-----FQNIR--LFAGMSVLDNV---------RVPGQCRLRSGLWSQVVGLSAarreedegrerawellrl 139
Cdd:PRK11701 83 RRRL--LRTewgfvHQHPRdgLRMQVSAGGNIgerlmavgaRHYGDIRATAGDWLERVEIDA------------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 140 vgleSRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGL 219
Cdd:PRK11701 143 ----ARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLL 218
|
250 260
....*....|....*....|....
gi 527030459 220 CDRIAVLNFGELIALGTPEEVQDD 243
Cdd:PRK11701 219 AHRLLVMKQGRVVESGLTDQVLDD 242
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-240 |
1.55e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.15 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAG------RDLAG-LIPEEIA 77
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvRDKDGqLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 78 RLGIGRT-----FQNIRLFAGMSVLDNV-RVPgqcrlrsglwSQVVGLSAArreedEGRERAWELLRLVGLESRAE-RAA 150
Cdd:PRK10619 86 QLRLLRTrltmvFQHFNLWSHMTVLENVmEAP----------IQVLGLSKQ-----EARERAVKYLAKVGIDERAQgKYP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 151 GSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSekqaLSGFIREIRETFS---LTVLLIEHHVPMVMGLCDRIAVLN 227
Cdd:PRK10619 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE----LVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLH 226
|
250
....*....|...
gi 527030459 228 FGELIALGTPEEV 240
Cdd:PRK10619 227 QGKIEEEGAPEQL 239
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-240 |
1.74e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.91 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVafagrdlaglipEEIARLG 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 81 IGRTFQNIRLFAGMSVldnvRVPGQCRLRSGLWSQVVgLSAarreedegrerawelLRLVGLESRAERAAGSLPYGDRRR 160
Cdd:PRK09544 69 IGYVPQKLYLDTTLPL----TVNRFLRLRPGTKKEDI-LPA---------------LKRVQAGHLIDAPMQKLSGGETQR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 161 LEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNfGELIALGTPEEV 240
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVV 207
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-61 |
1.81e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.46 E-value: 1.81e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRV 61
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-184 |
2.80e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.23 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 23 VSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARL---GIGRTFQNIRLFAGMSVLDN 99
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqKLGFIYQFHHLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 100 VRVPgqcrlrsglwsqvvgLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEP 179
Cdd:PRK11629 108 VAMP---------------LLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
....*
gi 527030459 180 AAGMN 184
Cdd:PRK11629 173 TGNLD 177
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-252 |
3.36e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.26 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTF---FNMLTGMTRPT--SGRVAFAGRDLAG--LIP 73
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLlrtFNRLLELNEEArvEGEVRLFGRNIYSpdVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 74 EEIaRLGIGRTFQNIRLFAGMSVLDNVR--------VPGQCRL---------RSGLWSQVvglsaarreedegrerawel 136
Cdd:PRK14267 81 IEV-RREVGMVFQYPNPFPHLTIYDNVAigvklnglVKSKKELdervewalkKAALWDEV-------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 137 lrlvglESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFslTVLLIEHHVPMV 216
Cdd:PRK14267 140 ------KDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQA 211
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 527030459 217 MGLCDRIAVLNFGELIALGTPEEVQDD------EKVVQAYLG 252
Cdd:PRK14267 212 ARVSDYVAFLYLGKLIEVGPTRKVFENpeheltEKYVTGALG 253
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-184 |
4.13e-14 |
|
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: 69.06 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLA---GLIPEEIARLGi 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDfqrDSIARGLLYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 82 grtfQNIRLFAGMSVLDNVRvpgqcrlrsgLWSQVVGLSAarreedegrerAWELLRLVGLESRAERAAGSLPYGDRRRL 161
Cdd:cd03231 80 ----HAPGIKTTLSVLENLR----------FWHADHSDEQ-----------VEEALARVGLNGFEDRPVAQLSAGQQRRV 134
|
170 180
....*....|....*....|...
gi 527030459 162 EIARALALSPRLLLLDEPAAGMN 184
Cdd:cd03231 135 ALARLLLSGRPLWILDEPTTALD 157
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-245 |
4.18e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.89 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFG-------------GLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAG 70
Cdd:PRK15079 8 LLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 71 LIPEEI--ARLGIGRTFQ------NIRlfagMSVLDNVRVPgqcrLRS---GLWSQVVglsaarreedegRERAWELLRL 139
Cdd:PRK15079 88 MKDDEWraVRSDIQMIFQdplaslNPR----MTIGEIIAEP----LRTyhpKLSRQEV------------KDRVKAMMLK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 140 VGL-ESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMG 218
Cdd:PRK15079 148 VGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKH 227
|
250 260
....*....|....*....|....*..
gi 527030459 219 LCDRIAVLNFGELIALGTPEEVQDDEK 245
Cdd:PRK15079 228 ISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-255 |
4.38e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.24 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 23 VSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAG---------RDLAGLipeeiaRLGIGRTFQ--NIRLF 91
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnKNLKKL------RKKVSLVFQfpEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 92 AGmSVLDNVRVpgqcrlrsglwsqvvGLSAARREEDEGRERAWELLRLVGL-ESRAERAAGSLPYGDRRRLEIARALALS 170
Cdd:PRK13641 100 EN-TVLKDVEF---------------GPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 171 PRLLLLDEPAAGMNP-SEKQALSGFIREIRETFslTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQDDEKVVQA 249
Cdd:PRK13641 164 PEILCLDEPAAGLDPeGRKEMMQLFKDYQKAGH--TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLKK 241
|
....*..
gi 527030459 250 -YLGESA 255
Cdd:PRK13641 242 hYLDEPA 248
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-252 |
4.73e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.05 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 23 VSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDL-AGLIPEEIARL----GIGRTFQNIRLFAGMSVL 97
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLrkkvGIVFQFPEHQLFEETVEK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 98 DNVRVPgqcrlrsglwsQVVGLSAARREEDegrerAWELLRLVGL-ESRAERAAGSLPYGDRRRLEIARALALSPRLLLL 176
Cdd:PRK13634 106 DICFGP-----------MNFGVSEEDAKQK-----AREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527030459 177 DEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV-QDDEKVVQAYLG 252
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIfADPDELEAIGLD 246
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-248 |
5.64e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 69.78 E-value: 5.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 23 VSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIaRLGIGRTFQNI-RLFAGMSVLDNVr 101
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL-RKHIGIVFQNPdNQFVGSIVKYDV- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 102 vpgqcrlrsglwsqVVGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAA 181
Cdd:PRK13648 106 --------------AFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527030459 182 GMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGlCDRIAVLNFGELIALGTPEEVQDDEKVVQ 248
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELT 237
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-101 |
6.25e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.29 E-value: 6.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGmtRP----TSGRVAFAGRDLAGLIPEEIARL 79
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDLEPEERAHL 84
|
90 100
....*....|....*....|..
gi 527030459 80 GIGRTFQNIRLFAGMSVLDNVR 101
Cdd:CHL00131 85 GIFLAFQYPIEIPGVSNADFLR 106
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-240 |
6.29e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.74 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 9 DLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSG-----RVAFAGRDLAGLIPEEIARLGIGR 83
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 84 TFQNIRLFAgMSVLDNV---------------RVPGQCRLRS-GLWSQVvglsaarreedegrerawellrlvglESRAE 147
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVlagvrahklvprkefRGVAQARLTEvGLWDAV--------------------------KDRLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 148 RAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIREtfSLTVLLIEHHVPMVMGLCDRIAVLN 227
Cdd:PRK14271 159 DSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFF 236
|
250
....*....|...
gi 527030459 228 FGELIALGTPEEV 240
Cdd:PRK14271 237 DGRLVEEGPTEQL 249
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-240 |
1.06e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 68.91 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTF---FN-M--LTGMTRpTSGRVAFAGRDL--AGLI 72
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLlrcLNrMndLIPGAR-VEGEILLDGEDIydPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 73 PEEIaRLGIGRTFQNIRLFAgMSVLDNV----RVPG------------QCRLRSGLWSQVvglsaarreedegrerawel 136
Cdd:COG1117 87 VVEL-RRRVGMVFQKPNPFP-KSIYDNVayglRLHGikskseldeiveESLRKAALWDEV-------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 137 lrlvglESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFslTVLLIEHHVPMV 216
Cdd:COG1117 145 ------KDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQA 216
|
250 260
....*....|....*....|....
gi 527030459 217 MGLCDRIAVLNFGELIALGTPEEV 240
Cdd:COG1117 217 ARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-250 |
1.14e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.99 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 19 AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPE-EIA----RLGIGRTFQNIRLFAg 93
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkEIKpvrkKVGVVFQFPESQLFE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 94 MSVLDNVrvpgqcrlrsGLWSQVVGLSAARREEDegrerAWELLRLVGLESRA-ERAAGSLPYGDRRRLEIARALALSPR 172
Cdd:PRK13643 100 ETVLKDV----------AFGPQNFGIPKEKAEKI-----AAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 173 LLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQDDEKVVQAY 250
Cdd:PRK13643 165 VLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAH 241
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-240 |
2.57e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.20 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSF---GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGlipEEI- 76
Cdd:PRK13642 1 MNKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 77 -ARLGIGRTFQNI-RLFAGMSVLDNVrvpgqcrlrsglwsqVVGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLP 154
Cdd:PRK13642 78 nLRRKIGMVFQNPdNQFVGATVEDDV---------------AFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 155 YGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGlCDRIAVLNFGELIAL 234
Cdd:PRK13642 143 GGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKE 221
|
....*.
gi 527030459 235 GTPEEV 240
Cdd:PRK13642 222 AAPSEL 227
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-101 |
4.82e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 68.27 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 19 AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgIGRTFQNIRLFAGmSVLD 98
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ-IGVVPQDTFLFSG-TIRE 432
|
...
gi 527030459 99 NVR 101
Cdd:COG1132 433 NIR 435
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-245 |
5.89e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.42 E-value: 5.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGG-----LTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDL-----AGLIPE 74
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEknkkkTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 75 EIARLGIGRT-FQNIRlfagmsvldNVRvpgQCRLRSG---------LWSQVV------GLSAARREEDEGRERAWELLR 138
Cdd:PRK13651 83 VLEKLVIQKTrFKKIK---------KIK---EIRRRVGvvfqfaeyqLFEQTIekdiifGPVSMGVSKEEAKKRAAKYIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 139 LVGL-ESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVM 217
Cdd:PRK13651 151 LVGLdESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVL 229
|
250 260
....*....|....*....|....*...
gi 527030459 218 GLCDRIAVLNFGELIALGTPEEVQDDEK 245
Cdd:PRK13651 230 EWTKRTIFFKDGKIIKDGDTYDILSDNK 257
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-240 |
1.06e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.97 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLT---------AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAgl 71
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 72 ipeeiarLG-IGRTFQNIRL-FAGMSVLDNVRVP-GQC-----RLRSGLWSQvvglsaarreedEGRERAWELLRLVGL- 142
Cdd:PRK15112 79 -------FGdYSYRSQRIRMiFQDPSTSLNPRQRiSQIldfplRLNTDLEPE------------QREKQIIETLRQVGLl 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 143 ESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDR 222
Cdd:PRK15112 140 PDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQ 219
|
250
....*....|....*...
gi 527030459 223 IAVLNFGELIALGTPEEV 240
Cdd:PRK15112 220 VLVMHQGEVVERGSTADV 237
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
19-248 |
1.21e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.98 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 19 AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTS---GRVAFAGRDLAGLIPEEIaRLGIGRTFQNI-RLFAGM 94
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDI-REKVGIVFQNPdNQFVGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 95 SVLDNVrvpgqcrlrsglwsqVVGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIARALALSPRLL 174
Cdd:PRK13640 101 TVGDDV---------------AFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527030459 175 LLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGlCDRIAVLNFGELIALGTPEEVQDDEKVVQ 248
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-101 |
1.22e-12 |
|
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: 65.25 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 18 TAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRdLAGLIpeeiaRLGIGrtFQNirlfaGMSVL 97
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSLL-----GLGGG--FNP-----ELTGR 102
|
....
gi 527030459 98 DNVR 101
Cdd:cd03220 103 ENIY 106
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
10-250 |
1.44e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.78 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 10 LTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgIGRTFQNIR 89
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 90 LFAGMSVLDNV---RVPGQ---CRLRSGLWSQVVGlsaarreedegreraweLLRLVGLESRAERAAGSLPYGDRRRLEI 163
Cdd:PRK10253 92 TPGDITVQELVargRYPHQplfTRWRKEDEEAVTK-----------------AMQATGITHLADQSVDTLSGGQRQRAWI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 164 ARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQDD 243
Cdd:PRK10253 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
....*..
gi 527030459 244 EKVVQAY 250
Cdd:PRK10253 235 ELIERIY 241
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-250 |
1.48e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.34 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 23 VSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTrPTSGRVAFAGRDLAGLIPEEIARLgigRTF--QNIRLFAGMSVLdnv 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARH---RAYlsQQQTPPFAMPVF--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 101 rvpgqcrlrsglwsQVVGLS-AARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRR-------LEIARALALSPR 172
Cdd:PRK03695 88 --------------QYLTLHqPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 173 LLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQDDEKVVQAY 250
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-239 |
1.62e-12 |
|
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: 66.66 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGG--LTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIaRLGIG 82
Cdd:TIGR02203 331 VEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASL-RRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RTFQNIRLFAGmSVLDNVRvpgqcrlrsglWSQVVGLSAARREEDEGRERAWELLRLV--GLESRAERAAGSLPYGDRRR 160
Cdd:TIGR02203 410 LVSQDVVLFND-TIANNIA-----------YGRTEQADRAEIERALAAAYAQDFVDKLplGLDTPIGENGVLLSGGQRQR 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 161 LEIARALALSPRLLLLDEPAAGM-NPSEKQALSGFIREIRETfslTVLLIEHHVPMVMGlCDRIAVLNFGELIALGTPEE 239
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALdNESERLVQAALERLMQGR---TTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNE 553
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-244 |
1.85e-12 |
|
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: 65.20 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 23 VSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAgLIPEEIARLGIGRTFQNIRLFAGmSVLDNVRV 102
Cdd:cd03252 21 ISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA-LADPAWLRRQVGVVLQENVLFNR-SIRDNIAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 103 --PGQCRLRSGLWSQVVGlsaarreedegrerAWELLR--------LVGlesraERAAGsLPYGDRRRLEIARALALSPR 172
Cdd:cd03252 99 adPGMSMERVIEAAKLAG--------------AHDFISelpegydtIVG-----EQGAG-LSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527030459 173 LLLLDEPAAGMNPSEKQALSGFIREIREtfSLTVLLIEHHVPMVMGlCDRIAVLNFGELIALGTPEEVQDDE 244
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-212 |
2.47e-12 |
|
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: 66.23 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVA-GVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgIGR 83
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLdGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-VSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 84 TFQNIRLFAgMSVLDNVRVpgqcrlrsglwsqvvglsaarREEDEGRERAWELLRLVGLESRAER-----------AAGS 152
Cdd:TIGR02868 414 CAQDAHLFD-TTVRENLRL---------------------ARPDATDEELWAALERVGLADWLRAlpdgldtvlgeGGAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527030459 153 LPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALsgfIREIRETFS-LTVLLIEHH 212
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL---LEDLLAALSgRTVVLITHH 529
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-197 |
3.50e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.74 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDL-AGLIPEEIARLGigr 83
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIdDPDVAEACHYLG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 84 tFQNIrLFAGMSVLDNVRvpgqcrlrsgLWSQVVGlsaarreedEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEI 163
Cdd:PRK13539 80 -HRNA-MKPALTVAENLE----------FWAAFLG---------GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVAL 138
|
170 180 190
....*....|....*....|....*....|....
gi 527030459 164 ARALALSPRLLLLDEPAAGMNPSEKQALSGFIRE 197
Cdd:PRK13539 139 ARLLVSNRPIWILDEPTAALDAAAVALFAELIRA 172
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-255 |
3.60e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSfgglTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLA------------GL 71
Cdd:COG1129 256 VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdairagiAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 72 IPEEiaRLGIGrtfqnirLFAGMSVLDNVRVPGQCRLRSGLWsqvvgLSAArreedEGRERAWELLRLVGLE-SRAERAA 150
Cdd:COG1129 332 VPED--RKGEG-------LVLDLSIRENITLASLDRLSRGGL-----LDRR-----RERALAEEYIKRLRIKtPSPEQPV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 151 GSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGE 230
Cdd:COG1129 393 GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGR 471
|
250 260
....*....|....*....|....*
gi 527030459 231 LIALGTPEEVqDDEKVVQAYLGESA 255
Cdd:COG1129 472 IVGELDREEA-TEEAIMAAATGGAA 495
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-235 |
6.50e-12 |
|
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: 63.44 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 22 GVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRP---TSGRVAFAGRDL-AGLIPEEIARLGigrtfQNIRLFAGMSVL 97
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRkPDQFQKCVAYVR-----QDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 98 DNVRVPGQCRLRSGLWSQVVGLSAARreedegrerawELLRLVGLESRAERAAGSLPYGDRRRLEIARALALSPRLLLLD 177
Cdd:cd03234 100 ETLTYTAILRLPRKSSDAIRKKRVED-----------VLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 178 EPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALG 235
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-251 |
6.62e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 6.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGltAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIGR 83
Cdd:PRK09700 265 VFEVRNVTSRDRK--KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 84 TFQNIR---LFAGMSVLDNVRVPGQcrLRSGLWSQVVGLsaarREEDEGRERAWELLRLVGLE-SRAERAAGSLPYGDRR 159
Cdd:PRK09700 343 ITESRRdngFFPNFSIAQNMAISRS--LKDGGYKGAMGL----FHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 160 RLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEE 239
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
250
....*....|..
gi 527030459 240 VQDDEKVVQAYL 251
Cdd:PRK09700 496 DMSEEEIMAWAL 507
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-240 |
8.16e-12 |
|
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: 64.71 E-value: 8.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGG----LTAVAGVSLSIEEGSIFGLIGPNGAGKTtffnmLTGMT---------RPTSGRVAFAGRD 67
Cdd:COG4172 3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKS-----VTALSilrllpdpaAHPSGSILFDGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 68 LAGLIPEEIARL---GIGRTFQNirlfaGMSVLDNVRVPGQcrlrsglwsQVV-------GLSAARREEDegrerAWELL 137
Cdd:COG4172 78 LLGLSERELRRIrgnRIAMIFQE-----PMTSLNPLHTIGK---------QIAevlrlhrGLSGAAARAR-----ALELL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 138 RLVGLEsRAERAAGSLPY----GDRRRLEIARALALSPRLLLLDEPAAGMNPS-EKQALSgFIREIRETFSLTVLLIEHH 212
Cdd:COG4172 139 ERVGIP-DPERRLDAYPHqlsgGQRQRVMIAMALANEPDLLIADEPTTALDVTvQAQILD-LLKDLQRELGMALLLITHD 216
|
250 260
....*....|....*....|....*...
gi 527030459 213 VPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:COG4172 217 LGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-240 |
8.55e-12 |
|
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: 64.71 E-value: 8.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSF-----------GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTrPTSGRVAFAGRDLAGLI 72
Cdd:COG4172 275 LLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 73 PEEIARLgigRT-----FQ------NIRlfagMSVLDNVRvpgqcrlrSGLWSQVVGLSAARREEDegrerAWELLRLVG 141
Cdd:COG4172 354 RRALRPL---RRrmqvvFQdpfgslSPR----MTVGQIIA--------EGLRVHGPGLSAAERRAR-----VAEALEEVG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 142 L-ESRAERaagslpY------GDRRRLEIARALALSPRLLLLDEPAAGMNPS-EKQALSgFIREIRETFSLTVLLIEHHV 213
Cdd:COG4172 414 LdPAARHR------YphefsgGQRQRIAIARALILEPKLLVLDEPTSALDVSvQAQILD-LLRDLQREHGLAYLFISHDL 486
|
250 260
....*....|....*....|....*..
gi 527030459 214 PMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:COG4172 487 AVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-240 |
1.01e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 63.26 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGM-----TRPTSGRVAFAGRDLAGLIPEE 75
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 76 IA-RLGIGRTFQNIRLFAgMSVLDNV----RVPG---QCRLRSGLWSQVVGLSaarreedegrerAWELLRlvgleSRAE 147
Cdd:PRK14239 82 VDlRKEIGMVFQQPNPFP-MSIYENVvyglRLKGikdKQVLDEAVEKSLKGAS------------IWDEVK-----DRLH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 148 RAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFslTVLLIEHHVPMVMGLCDRIAVLN 227
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFL 221
|
250
....*....|...
gi 527030459 228 FGELIALGTPEEV 240
Cdd:PRK14239 222 DGDLIEYNDTKQM 234
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-235 |
1.07e-11 |
|
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: 61.95 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGG--LTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLipEEIARLGIG 82
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL--EKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RTFQNIRLFAGmSVLDNVrvpgqcrlrsglwsqvvglsaarreedegrerawellrlvglesrAERAAGslpyGDRRRLE 162
Cdd:cd03247 79 VLNQRPYLFDT-TLRNNL---------------------------------------------GRRFSG----GERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527030459 163 IARALALSPRLLLLDEPAAGMNP-SEKQALSGFIREIRETfslTVLLIEHHVPMVMGLcDRIAVLNFGELIALG 235
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPiTERQLLSLIFEVLKDK---TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-240 |
1.20e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 63.18 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 18 TAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIGRTFQNI--RLFAGMS 95
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPdnQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 96 VLD------NVRV-PGQCRLRSGlwsqvvglsaarreedegrerawELLRLVGLESRAERAAGSLPYGDRRRLEIARALA 168
Cdd:PRK13633 104 EEDvafgpeNLGIpPEEIRERVD-----------------------ESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527030459 169 LSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGlCDRIAVLNFGELIALGTPEEV 240
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-250 |
1.51e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.92 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 23 VSLSIEEGSIFGLIGPNGAGKTTFFNMLTG-MTRP-------TSGRVAFAGRDLAGLIPEEIARLGIGRTFQNIRLFAgM 94
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAFA-F 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 95 SVLDNV---RVPGQCRlrsglwsqvvglsaARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIARA----- 166
Cdd:PRK13547 99 SAREIVllgRYPHARR--------------AGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVlaqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 167 ----LALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQD 242
Cdd:PRK13547 165 pphdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
....*...
gi 527030459 243 DEKVVQAY 250
Cdd:PRK13547 245 PAHIARCY 252
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-227 |
1.79e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 62.49 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 2 SAILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTF---FNMLTGM--TRPTSGRVAFAGRDL--AGLIPE 74
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTIlrcFNRLNDLipGFRVEGKVTFHGKNLyaPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 75 EIARLgIGRTFQNIRLFAgMSVLDNV----RVPG---------QCRLR-SGLWSQVVglsaarreedegrerawELLRLV 140
Cdd:PRK14243 88 EVRRR-IGMVFQKPNPFP-KSIYDNIaygaRINGykgdmdelvERSLRqAALWDEVK-----------------DKLKQS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 141 GLesraeraagSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFslTVLLIEHHVPMVMGLC 220
Cdd:PRK14243 149 GL---------SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVS 217
|
....*..
gi 527030459 221 DRIAVLN 227
Cdd:PRK14243 218 DMTAFFN 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-107 |
2.75e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.65 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 2 SAILEVSDLTKSFGGLTAVAGVSLSIEEGSiFGLI-GPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIaRLG 80
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY-RQQ 82
|
90 100
....*....|....*....|....*..
gi 527030459 81 IGRTFQNIRLFaGMSVLDNVRVPGQCR 107
Cdd:PRK10247 83 VSYCAQTPTLF-GDTVYDNLIFPWQIR 108
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-239 |
4.12e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 62.35 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 9 DLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPeeiARLGIGRTFQNI 88
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP---AERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 89 RLFAGMSVLDNVRvpgqcrlrsglwsqvVGL---SAARREEDEGRERAWELLRLVGLESRAERAagsLPYGDRRRLEIAR 165
Cdd:PRK11000 85 ALYPHLSVAENMS---------------FGLklaGAKKEEINQRVNQVAEVLQLAHLLDRKPKA---LSGGQRQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527030459 166 ALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEE 239
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-252 |
4.48e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.14 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 24 SLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPeeiARLGIGRTFQNIRLFAGMSVLDNVrvp 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP---SRRPVSMLFQENNLFSHLTVAQNI--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 104 gqcrlrsGLwsqvvGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGM 183
Cdd:PRK10771 93 -------GL-----GLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 184 NPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQDDEKVVQAYLG 252
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLG 229
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4-225 |
4.77e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.49 E-value: 4.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGG--LTAVAGvslSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAgrdlaglipeeiarLGI 81
Cdd:COG1245 341 LVEYPDLTKSYGGfsLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED--------------LKI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 82 GRTFQNIRLFAGMSVLDNVRVPGQCRLRSGLWSQvvglsaarreedegrerawELLRLVGLESRAERAAGSLPYGDRRRL 161
Cdd:COG1245 404 SYKPQYISPDYDGTVEEFLRSANTDDFGSSYYKT-------------------EIIKPLGLEKLLDKNVKDLSGGELQRV 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527030459 162 EIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAV 225
Cdd:COG1245 465 AIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-248 |
4.79e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.79 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLT-----KSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRV----------AFAGRDL 68
Cdd:PRK13631 21 ILRVKNLYcvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 69 AGLIPEEIA-----RLGIGRTFQ--NIRLFAGMSVLDNVRVP---GQCRLRSglwsqvvglsaarreedegRERAWELLR 138
Cdd:PRK13631 101 TNPYSKKIKnfkelRRRVSMVFQfpEYQLFKDTIEKDIMFGPvalGVKKSEA-------------------KKLAKFYLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 139 LVGL-ESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVM 217
Cdd:PRK13631 162 KMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVL 240
|
250 260 270
....*....|....*....|....*....|.
gi 527030459 218 GLCDRIAVLNFGELIALGTPEEVQDDEKVVQ 248
Cdd:PRK13631 241 EVADEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-240 |
5.85e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.97 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLT-KSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIG 82
Cdd:COG3845 257 VLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RtfqnI---R----LFAGMSVLDNV--RVPGQCRLRSGLWsqvvglsaarreedegrerawelLRLVGLESRAER----- 148
Cdd:COG3845 337 Y----IpedRlgrgLVPDMSVAENLilGRYRRPPFSRGGF-----------------------LDRKAIRAFAEElieef 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 149 ---------AAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLI-----Ehhvp 214
Cdd:COG3845 390 dvrtpgpdtPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLIsedldE---- 464
|
250 260
....*....|....*....|....*.
gi 527030459 215 mVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:COG3845 465 -ILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
8-225 |
6.06e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.88 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 8 SDLTKSFGG--LTAVAGvslSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAgLIPEEIARLGIGRtf 85
Cdd:cd03237 4 PTMKKTLGEftLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKADYEGT-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 86 qnIRLFAgMSVLDNVRVPGQCRLrsglwsqvvglsaarreedegrerawELLRLVGLESRAERAAGSLPYGDRRRLEIAR 165
Cdd:cd03237 78 --VRDLL-SSITKDFYTHPYFKT--------------------------EIAKPLQIEQILDREVPELSGGELQRVAIAA 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 166 ALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAV 225
Cdd:cd03237 129 CLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-254 |
1.04e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 8 SDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIGRTFQN 87
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 88 IRLFAGMSVLDNvrvpgqcrlrsgLWSQVVGLSAARREEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIARAL 167
Cdd:PRK10982 82 LNLVLQRSVMDN------------MWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 168 ALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALgTPEEVQDDEKVV 247
Cdd:PRK10982 150 SYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIAT-QPLAGLTMDKII 227
|
....*..
gi 527030459 248 QAYLGES 254
Cdd:PRK10982 228 AMMVGRS 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
22-237 |
1.41e-10 |
|
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: 59.43 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 22 GVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGlIPEEIARLGIGRTFQNIRLFAGmSVLDNVR 101
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISK-IGLHDLRSRISIIPQDPVLFSG-TIRSNLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 102 VPGQC---RL-----RSGLWSQVVGLSAarreedegrerawellrlvGLESRAERAAGSLPYGDRRRLEIARALALSPRL 173
Cdd:cd03244 100 PFGEYsdeELwqaleRVGLKEFVESLPG-------------------GLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527030459 174 LLLDEPAAGMNP-SEKQalsgfIRE-IRETFS-LTVLLIEHHVPMVMGlCDRIAVLNFGELIALGTP 237
Cdd:cd03244 161 LVLDEATASVDPeTDAL-----IQKtIREAFKdCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-243 |
1.51e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.00 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 16 GLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIGRTFQNIRL-FAGM 94
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETqFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 95 SVLDNVRV-PGQCRLRSGLWSQVVGLSAARreedegrerawellrlVGLESRAERAAGSLPYGDRRRLEIARALALSPRL 173
Cdd:PRK13644 94 TVEEDLAFgPENLCLPPIEIRKRVDRALAE----------------IGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 174 LLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMvMGLCDRIAVLNFGELIALGTPEEVQDD 243
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-240 |
1.85e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 59.98 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKS-------FGG---LTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAG 70
Cdd:PRK11308 2 QQPLLQAIDLKKHypvkrglFKPerlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 71 LIPEEIARL--GIGRTFQNIrlFAGMsvldNVRvpgqcrlrsglwsQVVG------------LSAARREEDegrerAWEL 136
Cdd:PRK11308 82 ADPEAQKLLrqKIQIVFQNP--YGSL----NPR-------------KKVGqileepllintsLSAAERREK-----ALAM 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 137 LRLVGLesRAERAaGSLPY----GDRRRLEIARALALSPRLLLLDEPAAGMNPS-EKQALSGFIrEIRETFSLTVLLIEH 211
Cdd:PRK11308 138 MAKVGL--RPEHY-DRYPHmfsgGQRQRIAIARALMLDPDVVVADEPVSALDVSvQAQVLNLMM-DLQQELGLSYVFISH 213
|
250 260
....*....|....*....|....*....
gi 527030459 212 HVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:PRK11308 214 DLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-225 |
1.91e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGG--LTAVAGvslSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAgrdlaglipeeiarLGI 81
Cdd:PRK13409 340 LVEYPDLTKKLGDfsLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--------------LKI 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 82 GRTFQNIRLFAGMSVLDNVRVPGQcRLRSGLWSQvvglsaarreedegrerawELLRLVGLESRAERAAGSLPYGDRRRL 161
Cdd:PRK13409 403 SYKPQYIKPDYDGTVEDLLRSITD-DLGSSYYKS-------------------EIIKPLQLERLLDKNVKDLSGGELQRV 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527030459 162 EIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAV 225
Cdd:PRK13409 463 AIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-250 |
2.27e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 59.08 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 20 VAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTrPTSGRVAFAGRDLAGLIPEEIARLgigRTF--QNIRLFAGMSVL 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARH---RAYlsQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 98 dnvrvpgqcrlrsglwsQVVGLSAARREEDEGRERAW-ELLRLVGLESRAERAAGSLPYGDRRRLEIARA-------LAL 169
Cdd:COG4138 88 -----------------QYLALHQPAGASSEAVEQLLaQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVllqvwptINP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 170 SPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQDDEKVVQA 249
Cdd:COG4138 151 EGQLLLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEV 229
|
.
gi 527030459 250 Y 250
Cdd:COG4138 230 F 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
23-244 |
2.71e-10 |
|
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: 58.78 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 23 VSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgIGRTFQNIRLFAGmSVLDNVR- 101
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-IGLVSQDVFLFND-TVAENIAy 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 102 -VPGQCRlrsglwSQVVglSAArreedeGRERAWELLRLV--GLESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDE 178
Cdd:cd03251 99 gRPGATR------EEVE--EAA------RAANAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527030459 179 PAAGM-NPSEKqALSGFIREIREtfSLTVLLIEHHVPMVMGlCDRIAVLNFGELIALGTPEEVQDDE 244
Cdd:cd03251 165 ATSALdTESER-LVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-99 |
3.65e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 59.47 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 3 AILEVSDLTKSF-GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEiaRlGI 81
Cdd:PRK11650 2 AGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--R-DI 78
|
90
....*....|....*...
gi 527030459 82 GRTFQNIRLFAGMSVLDN 99
Cdd:PRK11650 79 AMVFQNYALYPHMSVREN 96
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
3-240 |
3.88e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 59.15 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 3 AILEVSDLTKSF----GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRP----TSGRVAFAGRDLAGLIPE 74
Cdd:COG4170 2 PLLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 75 EIARLgIGR----TFQNirlfaGMSVLD-NVRVPGQ------CRLRSGLWSQVVGLSAARreedegrerAWELLRLVGLE 143
Cdd:COG4170 82 ERRKI-IGReiamIFQE-----PSSCLDpSAKIGDQlieaipSWTFKGKWWQRFKWRKKR---------AIELLHRVGIK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 144 SRaERAAGSLPY----GDRRRLEIARALALSPRLLLLDEPAAGMNPSEK-QALSGFIReIRETFSLTVLLIEHHVPMVMG 218
Cdd:COG4170 147 DH-KDIMNSYPHelteGECQKVMIAMAIANQPRLLIADEPTNAMESTTQaQIFRLLAR-LNQLQGTSILLISHDLESISQ 224
|
250 260
....*....|....*....|..
gi 527030459 219 LCDRIAVLNFGELIALGTPEEV 240
Cdd:COG4170 225 WADTITVLYCGQTVESGPTEQI 246
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-240 |
5.27e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.48 E-value: 5.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 19 AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPE--EIARL--GIGRTFQ--NIRLFA 92
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVKRLrkEIGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 93 GMSVLDNVRVPgqcrlrsglwsqvVGLSAARREEDEGRErawELLRLVGL-ESRAERAAGSLPYGDRRRLEIARALALSP 171
Cdd:PRK13645 106 ETIEKDIAFGP-------------VNLGENKQEAYKKVP---ELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 172 RLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-241 |
6.10e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.59 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFfNMLTGMTRPTSGRVAFAGRDLAGlipeeiARLGIGRT 84
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCA------NRRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRlfagmSVLDNVRVPGQCRLRSGLWSQVVGLSaarreEDEGRERAWELLRLVGLESRAERAAGSLPYGDRRRLEIA 164
Cdd:NF000106 87 IG*HR-----PVR*GRRESFSGRENLYMIGR*LDLS-----RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 165 RALALSPRLLLLDEPAAGMNPSEKQALSGFIRE-IREtfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEVQ 241
Cdd:NF000106 157 ASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSmVRD--GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-239 |
8.32e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.82 E-value: 8.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 6 EVSDLTKSFGGLT-AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIaRLGIGRT 84
Cdd:PRK13657 336 EFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL-RRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAgMSVLDNVRVpGQcrlrsglwsqvVGLSAARREEDEGRERAWELL--RLVGLESRAERAAGSLPYGDRRRLE 162
Cdd:PRK13657 415 FQDAGLFN-RSIEDNIRV-GR-----------PDATDEEMRAAAERAQAHDFIerKPDGYDTVVGERGRQLSGGERQRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527030459 163 IARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIREtfSLTVLLIEHHVPMVMGlCDRIAVLNFGELIALGTPEE 239
Cdd:PRK13657 482 IARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDE 555
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-64 |
9.43e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.36 E-value: 9.43e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFA 64
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS 379
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-252 |
1.29e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.48 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 19 AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEI---ARLGIGRTFQ--NIRLFAg 93
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYirpVRKRIGMVFQfpESQLFE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 94 msvlDNVRvpgqcrlRSGLWsqvvGLSAARREEDEGRERAWELLRLVGLESRA-ERAAGSLPYGDRRRLEIARALALSPR 172
Cdd:PRK13646 101 ----DTVE-------REIIF----GPKNFKMNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 173 LLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV-QDDEKVVQAYL 251
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELfKDKKKLADWHI 245
|
.
gi 527030459 252 G 252
Cdd:PRK13646 246 G 246
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-86 |
1.39e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMT--RPTSGRVAFAGRDLAGLIPEEIARLGI 81
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
....*
gi 527030459 82 GRTFQ 86
Cdd:PRK09580 81 FMAFQ 85
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
5-165 |
1.47e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEeiarlgigrt 84
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIRLFAG--------MSVLDNVRVpgQCRLrsglwSQVVGLSAarreedegrerAWELLRLVGLESRAERAAGSLPYG 156
Cdd:PRK13538 72 YHQDLLYLGhqpgikteLTALENLRF--YQRL-----HGPGDDEA-----------LWEALAQVGLAGFEDVPVRQLSAG 133
|
....*....
gi 527030459 157 DRRRLEIAR 165
Cdd:PRK13538 134 QQRRVALAR 142
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-246 |
2.20e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 57.42 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 22 GVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGL----IPEEIARLGigrtfQNIRLFAGmSVL 97
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYdhhyLHRQVALVG-----QEPVLFSG-SVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 98 DNVRVPgqcrLRSGLWSQVvgLSAARREEDEGRERAWEllrlVGLESRAERAAGSLPYGDRRRLEIARALALSPRLLLLD 177
Cdd:TIGR00958 573 ENIAYG----LTDTPDEEI--MAAAKAANAHDFIMEFP----NGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 178 EPAAGMNPSEKQALsgfiREIRETFSLTVLLIEHHVPMVMGlCDRIAVLNFGELIALGTPEEVQDDEKV 246
Cdd:TIGR00958 643 EATSALDAECEQLL----QESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-261 |
2.20e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLT-KSFggltavAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGI- 81
Cdd:PRK15439 268 VLTVEDLTgEGF------RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLv 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 82 ----GRtfQNIRLFAGMSVLDNVrvpgqCRL---RSGLWSQVVGLSAARREEDegrerawellRLVGLE-SRAERAAGSL 153
Cdd:PRK15439 342 ylpeDR--QSSGLYLDAPLAWNV-----CALthnRRGFWIKPARENAVLERYR----------RALNIKfNHAEQAARTL 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 154 PYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIA 233
Cdd:PRK15439 405 SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISG 483
|
250 260
....*....|....*....|....*...
gi 527030459 234 LGTPEEVQDDEkVVQAYLGESALGESHA 261
Cdd:PRK15439 484 ALTGAAINVDT-IMRLAFGEHQAQEASC 510
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-244 |
2.60e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.16 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLT-KSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTrPTSGRVAFAGRDLAGLIPEE----IARL 79
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESwrkhLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 GigrtfQNIRLFAGmSVLDNVRvPGQcrlrsglwsqvVGLSAARREEDEGRERAWELLRLV--GLESR-AERAAGsLPYG 156
Cdd:PRK11174 429 G-----QNPQLPHG-TLRDNVL-LGN-----------PDASDEQLQQALENAWVSEFLPLLpqGLDTPiGDQAAG-LSVG 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 157 DRRRLEIARALALSPRLLLLDEPAAGMNP-SEKQALSGFIREIRetfSLTVLLIEHHVPMVMGlCDRIAVLNFGELIALG 235
Cdd:PRK11174 490 QAQRLALARALLQPCQLLLLDEPTASLDAhSEQLVMQALNAASR---RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
|
....*....
gi 527030459 236 TPEEVQDDE 244
Cdd:PRK11174 566 DYAELSQAG 574
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-237 |
3.64e-09 |
|
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: 55.11 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGG--LTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGlIPEEIARLGIG 82
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIST-IPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RTFQNIRLFAGM--SVLD------NVRVPGQCRLRSGlwsqvvglsaarreedegrerawellrlvGLesraeraagSLP 154
Cdd:cd03369 86 IIPQDPTLFSGTirSNLDpfdeysDEEIYGALRVSEG-----------------------------GL---------NLS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 155 YGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREirETFSLTVLLIEHHVPMVMGlCDRIAVLNFGELIAL 234
Cdd:cd03369 128 QGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIID-YDKILVMDAGEVKEY 204
|
...
gi 527030459 235 GTP 237
Cdd:cd03369 205 DHP 207
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-244 |
9.56e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.75 E-value: 9.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 22 GVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgIGRTFQNIRLFAGmSVLDNVR 101
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV-LSIIPQSPVLFSG-TVRFNID 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 102 vPGQCRLRSGLWSqvvGLSAARREEDEGRERawellrlVGLESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAA 181
Cdd:PLN03232 1332 -PFSEHNDADLWE---ALERAHIKDVIDRNP-------FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527030459 182 GMNPSEKQALSgfiREIRETF-SLTVLLIEHHVPMVMGlCDRIAVLNFGELIALGTPEEVQDDE 244
Cdd:PLN03232 1401 SVDVRTDSLIQ---RTIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-240 |
1.05e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.12 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSF----GGLTAVAGVSLSIEEGSIFGLIGPNGAGK--TTFFNM-LTGMTRPTSGRVAFAGRDLAGLIP 73
Cdd:PRK09473 9 ADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKsqTAFALMgLLAANGRIGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 74 EEIARL---GIGRTFQNirlfaGMSVLDN-VRVPGQCrlrsglwSQVV----GLSAARreedegrerAWE----LLRLVG 141
Cdd:PRK09473 89 KELNKLraeQISMIFQD-----PMTSLNPyMRVGEQL-------MEVLmlhkGMSKAE---------AFEesvrMLDAVK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 142 L-ESRaeRAAGSLPY----GDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMV 216
Cdd:PRK09473 148 MpEAR--KRMKMYPHefsgGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVV 225
|
250 260
....*....|....*....|....
gi 527030459 217 MGLCDRIAVLNFGELIALGTPEEV 240
Cdd:PRK09473 226 AGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-240 |
1.51e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.71 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 2 SAILEVSDLTKSF---GGL--------TAVAGVSLSIEEGSIFGLIGPNGAGKTTffnmlTGMTR----PTSGRVAFAGR 66
Cdd:PRK15134 273 SPLLDVEQLQVAFpirKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKST-----TGLALlrliNSQGEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 67 DLAGLIPEEI--ARLGIGRTFQNIRlfagmSVLdNVRVPGQCRLRSGLWSQVVGLSAARREEDEGrerawELLRLVGL-- 142
Cdd:PRK15134 348 PLHNLNRRQLlpVRHRIQVVFQDPN-----SSL-NPRLNVLQIIEEGLRVHQPTLSAAQREQQVI-----AVMEEVGLdp 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 143 ESRaERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPS-EKQALSgFIREIRETFSLTVLLIEHHVPMVMGLCD 221
Cdd:PRK15134 417 ETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTvQAQILA-LLKSLQQKHQLAYLFISHDLHVVRALCH 494
|
250
....*....|....*....
gi 527030459 222 RIAVLNFGELIALGTPEEV 240
Cdd:PRK15134 495 QVIVLRQGEVVEQGDCERV 513
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-252 |
1.56e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.12 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSF-GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIarl 79
Cdd:PRK15056 3 QQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 gIGRTFQNIRLFAGMSVL-DNVRVPGQcrlrsglWSQVVGLSAARREEDEGRERAweLLRLVGLESRaERAAGSLPYGDR 158
Cdd:PRK15056 80 -VAYVPQSEEVDWSFPVLvEDVVMMGR-------YGHMGWLRRAKKRDRQIVTAA--LARVDMVEFR-HRQIGELSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 159 RRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDrIAVLNFGELIALGTPE 238
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTE 226
|
250
....*....|....
gi 527030459 239 EVQDDEKVVQAYLG 252
Cdd:PRK15056 227 TTFTAENLELAFSG 240
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-235 |
3.08e-08 |
|
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: 52.17 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTK------SFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRP--TSGRVAFAGRDLaglIPEEI 76
Cdd:cd03213 4 LSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL---DKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 77 ARLgIGRTFQNIRLFAGMSVLDNVRVPGQCRlrsglwsqvvGLSAarreedegrerawellrlvglesraeraagslpyG 156
Cdd:cd03213 81 RKI-IGYVPQDDILHPTLTVRETLMFAAKLR----------GLSG----------------------------------G 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 157 DRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVM-GLCDRIAVLNFGELIALG 235
Cdd:cd03213 116 ERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSSEIfELFDKLLLLSQGRVIYFG 194
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-235 |
4.39e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.71 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSF---GGLT--------AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLI 72
Cdd:PRK10261 313 ILQVRNLVTRFplrSGLLnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 73 PEEIA--RLGIGRTFQNI------RLFAGMSVLDNVRVPGQCRlrsglwsqvvGLSAARREedegrerAWeLLRLVGLE- 143
Cdd:PRK10261 393 PGKLQalRRDIQFIFQDPyasldpRQTVGDSIMEPLRVHGLLP----------GKAAAARV-------AW-LLERVGLLp 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 144 SRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRI 223
Cdd:PRK10261 455 EHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRV 534
|
250
....*....|..
gi 527030459 224 AVLNFGELIALG 235
Cdd:PRK10261 535 AVMYLGQIVEIG 546
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-252 |
4.76e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.47 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSfggltAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGIGRT 84
Cdd:PRK10762 258 LKVDNLSGP-----GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 85 FQNIR---LFAGMSVLDNVRVpgqCRLRSgLWSQVVGLSAARREEDEGrerawELLRLVGLE--SRaERAAGSLPYGDRR 159
Cdd:PRK10762 333 SEDRKrdgLVLGMSVKENMSL---TALRY-FSRAGGSLKHADEQQAVS-----DFIRLFNIKtpSM-EQAIGLLSGGNQQ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 160 RLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEE 239
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQ 481
|
250
....*....|...
gi 527030459 240 VqDDEKVVQAYLG 252
Cdd:PRK10762 482 A-TQEKLMAAAVG 493
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-231 |
4.78e-08 |
|
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: 52.09 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 22 GVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAgLIPEEIARLGIGRTFQNIRLFAGmSVLDNVR 101
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHKYLHSKVSLVGQEPVLFAR-SLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 102 VpgqcrlrsGLWSQVVGLSAARREEDEGRERAWELLRlvGLESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAA 181
Cdd:cd03248 110 Y--------GLQSCSFECVKEAAQKAHAHSFISELAS--GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 527030459 182 GMNPSEKQALSGFIREIREtfSLTVLLIEHHVPMVMGlCDRIAVLNFGEL 231
Cdd:cd03248 180 ALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-69 |
1.53e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 1.53e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLA 69
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA 66
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-61 |
2.08e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 2.08e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRV 61
Cdd:PRK11147 319 VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
34-89 |
3.94e-07 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 47.61 E-value: 3.94e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527030459 34 GLIG-PNgAGKTTFFNMLTGM----------TR-PTSGRVAFAGR-----DLAGLIPEEIARLGIGRTFQNIR 89
Cdd:pfam01926 3 ALVGrPN-VGKSTLINALTGAkaivsdypgtTRdPNEGRLELKGKqiilvDTPGLIEGASEGEGLGRAFLAII 74
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
230-253 |
4.13e-07 |
|
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00005. There is a conserved AYLG sequence motif. This family is the C terminal of an ATP dependent branched-chain amino acid transporter. This domain is essential for LPS transport, through critical interactions with Walker A and switch helix domains.
Pssm-ID: 463560 Cd Length: 25 Bit Score: 45.32 E-value: 4.13e-07
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-239 |
4.73e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.49 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 1 MSAILEVSDLTKSFGGLTAV-AGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLiPEEIARL 79
Cdd:PRK10790 337 QSGRIDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL-SHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 80 GIGRTFQNIRLFAGmSVLDNVRVPGQCRlRSGLWS--QVVGLSaarreedegrerawELLRLV--GLESRAERAAGSLPY 155
Cdd:PRK10790 416 GVAMVQQDPVVLAD-TFLANVTLGRDIS-EEQVWQalETVQLA--------------ELARSLpdGLYTPLGEQGNNLSV 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 156 GDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVllIEHHVPMVMGlCDRIAVLNFGELIALG 235
Cdd:PRK10790 480 GQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVV--IAHRLSTIVE-ADTILVLHRGQAVEQG 556
|
....
gi 527030459 236 TPEE 239
Cdd:PRK10790 557 THQQ 560
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-249 |
5.50e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 22 GVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGL-IPEEIARLGIgrTFQNIRLFAGmSVLDNV 100
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFgLMDLRKVLGI--IPQAPVLFSG-TVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 101 RvPGQCRLRSGLWSqvvGLSAARREedegrerawELLRL--VGLESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDE 178
Cdd:PLN03130 1334 D-PFNEHNDADLWE---SLERAHLK---------DVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527030459 179 PAAGMNPSEKQALSGFIREirETFSLTVLLIEHHVPMVMGlCDRIAVLNFGELIALGTPEEVQDDE-----KVVQA 249
Cdd:PLN03130 1401 ATAAVDVRTDALIQKTIRE--EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEgsafsKMVQS 1473
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
22-239 |
7.69e-07 |
|
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: 48.77 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 22 GVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIaRLGIGRTFQNIRLFAGmSVLDNVR 101
Cdd:cd03253 19 DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL-RRAIGVVPQDTVLFND-TIGYNIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 102 VpgqcrlrsGLWS----QVVglSAARREEDEGrerawELLRL-------VGleSRAERAAGslpyGDRRRLEIARALALS 170
Cdd:cd03253 97 Y--------GRPDatdeEVI--EAAKAAQIHD-----KIMRFpdgydtiVG--ERGLKLSG----GEKQRVAIARAILKN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 171 PRLLLLDEPAAGMNPSEKQALSGFIREIREtfSLTVLLIEHHVPMVMGlCDRIAVLNFGELIALGTPEE 239
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-226 |
9.46e-07 |
|
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: 48.70 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSF--GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRpTSGRVAFAGRDLAGlIPEEIARLGIG 82
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNS-VPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RTFQNIRLFAGmSVLDNVRVPGQcrlrsglWSQvvglsaarreedegrERAWELLRLVGLESRAERAAGSLPY------- 155
Cdd:cd03289 81 VIPQKVFIFSG-TFRKNLDPYGK-------WSD---------------EEIWKVAEEVGLKSVIEQFPGQLDFvlvdggc 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527030459 156 ----GDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSgfiREIRETFS-LTVLLIEHHVPMVMGlCDRIAVL 226
Cdd:cd03289 138 vlshGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIR---KTLKQAFAdCTVILSEHRIEAMLE-CQRFLVI 209
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-212 |
1.24e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 47.64 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDlaglIPEEIArlgigr 83
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS----IKKDLC------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 84 TFQNIRLFAG--MSVLDNVRVPGQCRLRSGLWSQVVGLSaarreedegrerawELLRLVGLESRAERAAGSLPYGDRRRL 161
Cdd:PRK13540 71 TYQKQLCFVGhrSGINPYLTLRENCLYDIHFSPGAVGIT--------------ELCRLFSLEHLIDYPCGLLSSGQKRQV 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 527030459 162 EIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSlTVLLIEHH 212
Cdd:PRK13540 137 ALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGG-AVLLTSHQ 186
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-239 |
1.26e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 49.05 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSF--GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLiPEEIARLGIG 82
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY-SEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 83 RTFQNIRLFAGmSVLDNVRvpgqcrlrsglwsqvvgLSAARREEDEGRerawELLRLVGLESRAERAAG----------S 152
Cdd:PRK11160 418 VVSQRVHLFSA-TLRDNLL-----------------LAAPNASDEALI----EVLQQVGLEKLLEDDKGlnawlgeggrQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 153 LPYGDRRRLEIARALALSPRLLLLDEPAAGMNP-SEKQALSGFIREIRETfslTVLLIEHHVpMVMGLCDRIAVLNFGEL 231
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAeTERQILELLAEHAQNK---TVLMITHRL-TGLEQFDRICVMDNGQI 551
|
....*...
gi 527030459 232 IALGTPEE 239
Cdd:PRK11160 552 IEQGTHQE 559
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-100 |
1.73e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAfagrdlagLIPEEiaRLGIGR 83
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVS--------LDPNE--RLGKLR 70
|
90
....*....|....*..
gi 527030459 84 tfQNIRLFAGMSVLDNV 100
Cdd:PRK15064 71 --QDQFAFEEFTVLDTV 85
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-72 |
2.04e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.35 E-value: 2.04e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 527030459 19 AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRdlAGLI 72
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS--AALI 90
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
147-239 |
3.18e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 147 ERAAGSLPYGDRRRLEIAR--ALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSlTVLLIEHHVPMVmGLCDRI- 223
Cdd:PRK00635 471 ERALATLSGGEQERTALAKhlGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMI-SLADRIi 548
|
90 100
....*....|....*....|.
gi 527030459 224 -----AVLNFGELIALGTPEE 239
Cdd:PRK00635 549 digpgAGIFGGEVLFNGSPRE 569
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-61 |
4.84e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.73 E-value: 4.84e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 527030459 19 AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRV 61
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
19-91 |
5.15e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.27 E-value: 5.15e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527030459 19 AVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgIGRTFQNIRLF 91
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-FSAVFTDFHLF 409
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
3-240 |
9.09e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.89 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 3 AILEVSDLTKSFGG----LTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMT----RPTSGRVAFAGRDLAGLIPE 74
Cdd:PRK11022 2 ALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 75 EIARL---GIGRTFQ------NIRLFAGMSVLDNVRV--PGQCRLRsglwsqvvglsaarreedegRERAWELLRLVGL- 142
Cdd:PRK11022 82 ERRNLvgaEVAMIFQdpmtslNPCYTVGFQIMEAIKVhqGGNKKTR--------------------RQRAIDLLNQVGIp 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 143 --ESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLC 220
Cdd:PRK11022 142 dpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAA 221
|
250 260
....*....|....*....|
gi 527030459 221 DRIAVLNFGELIALGTPEEV 240
Cdd:PRK11022 222 HKIIVMYAGQVVETGKAHDI 241
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-231 |
1.04e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.06 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 23 VSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLGI-----GRTFQNIrlFAGMSVL 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGImlcpeDRKAEGI--IPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 98 DNVRVpgQCR---LRSGLWsqvvglsaarreedegRERAWE------LLRLVGLESR-AERAAGSLPYGDRRRLEIARAL 167
Cdd:PRK11288 350 DNINI--SARrhhLRAGCL----------------INNRWEaenadrFIRSLNIKTPsREQLIMNLSGGNQQKAILGRWL 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527030459 168 ALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGEL 231
Cdd:PRK11288 412 SEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-61 |
1.14e-05 |
|
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: 45.94 E-value: 1.14e-05
10 20 30
....*....|....*....|....*....|....*....
gi 527030459 23 VSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRV 61
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-101 |
2.59e-05 |
|
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: 44.07 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 22 GVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDLAGLIPEEIARLgIGRTFQNIRLFAGmSVLDNVR 101
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-IGLVSQEPVLFDG-TIAENIR 98
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-66 |
4.62e-05 |
|
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: 43.23 E-value: 4.62e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 527030459 22 GVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGR 66
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS 67
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-213 |
5.63e-05 |
|
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: 44.13 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSF--GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRpTSGRVAFAG-----------RDLAGL 71
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGvswnsvtlqtwRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 72 IPeeiarlgigrtfQNIRLFAGMsvldnvrvpgqcrLRSGL-----WSQvvglsaarreedegrERAWELLRLVGLESRA 146
Cdd:TIGR01271 1297 IP------------QKVFIFSGT-------------FRKNLdpyeqWSD---------------EEIWKVAEEVGLKSVI 1336
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 147 ERAAGSLPY-----------GDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSgfiREIRETFS-LTVLLIEHHV 213
Cdd:TIGR01271 1337 EQFPDKLDFvlvdggyvlsnGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIR---KTLKQSFSnCTVILSEHRV 1412
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-240 |
7.13e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 43.15 E-value: 7.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 20 VAGVSLSIEEGSIFGLIGPNGAGKT----TFFNMLTGMTRPTSGRVAFAGRDLAgliPEEIARLGIGRTFQNIRlfagmS 95
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALRGRKIATIMQNPR-----S 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 96 VLDNVRVPGQCRLRSGLwsqVVGLSAARREEDegrerawELLRLVGLESrAERAAGSLPY----GDRRRLEIARALALSP 171
Cdd:PRK10418 91 AFNPLHTMHTHARETCL---ALGKPADDATLT-------AALEAVGLEN-AARVLKLYPFemsgGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 172 RLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-65 |
1.17e-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: 41.79 E-value: 1.17e-04
10 20 30
....*....|....*....|....*....|....*....
gi 527030459 27 IEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAG 65
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG 60
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-61 |
1.47e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.85 E-value: 1.47e-04
10 20 30
....*....|....*....|....*....|....
gi 527030459 28 EEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRV 61
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY 130
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-64 |
2.01e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 2.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527030459 4 ILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFA 64
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA 372
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-61 |
2.14e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.10 E-value: 2.14e-04
10 20 30
....*....|....*....|....*....|....*
gi 527030459 27 IEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRV 61
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY 130
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-212 |
4.63e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 40.33 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 6 EVSDLTKSFG------GLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTG--MTRPTSGRVAFA----GRDLAGLip 73
Cdd:COG2401 26 RVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPdnqfGREASLI-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 74 EEIARLGigrtfqnirlfagmSVLDNVRVPGQCrlrsglwsqvvGLSaarreedegreRAWELLRLVglesraeraaGSL 153
Cdd:COG2401 104 DAIGRKG--------------DFKDAVELLNAV-----------GLS-----------DAVLWLRRF----------KEL 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 154 PYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHH 212
Cdd:COG2401 138 STGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHH 196
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
35-212 |
5.04e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 35 LIGPNGAGKTTFFNMLTGmTRPT--SGRVAFAGRdlaglipeeiaRLGIGRTFQNIRLFAGM---SVLDNVRVpgQCRLR 109
Cdd:PRK10938 291 IVGPNGAGKSTLLSLITG-DHPQgySNDLTLFGR-----------RRGSGETIWDIKKHIGYvssSLHLDYRV--STSVR 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 110 ----SGLWSQVvGLSAARREEDEGRERAWelLRLVGLESR-AERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMN 184
Cdd:PRK10938 357 nvilSGFFDSI-GIYQAVSDRQQKLAQQW--LDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
170 180
....*....|....*....|....*....
gi 527030459 185 PSEKQALSGFIrEIRETFSLTVLL-IEHH 212
Cdd:PRK10938 434 PLNRQLVRRFV-DVLISEGETQLLfVSHH 461
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-185 |
6.19e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 39.83 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 3 AILEVSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAG---------RDLAGL-- 71
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktatrgdrsRFMAYLgh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 72 IPEEIARLGigrTFQNIRLFAGMSVLDNVRVPGQCrlrsglwsqvvglsaarreedegrerawelLRLVGLESRAERAAG 151
Cdd:PRK13543 90 LPGLKADLS---TLENLHFLCGLHGRRAKQMPGSA------------------------------LAIVGLAGYEDTLVR 136
|
170 180 190
....*....|....*....|....*....|....
gi 527030459 152 SLPYGDRRRLEIARALALSPRLLLLDEPAAGMNP 185
Cdd:PRK13543 137 QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
140-252 |
1.42e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 140 VGLESRA-ERAAGSLPYGDRRRLEIAR--ALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSlTVLLIEHHVPMv 216
Cdd:TIGR00630 475 VGLDYLSlSRAAGTLSGGEAQRIRLATqiGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGN-TLIVVEHDEDT- 552
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 527030459 217 MGLCDRI------AVLNFGELIALGTPEEV-QDDEKVVQAYLG 252
Cdd:TIGR00630 553 IRAADYVidigpgAGEHGGEVVASGTPEEIlANPDSLTGQYLS 595
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
32-60 |
2.51e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.86 E-value: 2.51e-03
10 20 30
....*....|....*....|....*....|...
gi 527030459 32 IFGLIGPNGAGKTTFFN----MLTGMTRPTSGR 60
Cdd:pfam13476 20 LTLITGPNGSGKTTILDaiklALYGKTSRLKRK 52
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
135-240 |
2.81e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 38.68 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 135 ELLRLVGLESRAERAAGSLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVP 214
Cdd:PRK10261 151 DQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMG 230
|
90 100
....*....|....*....|....*.
gi 527030459 215 MVMGLCDRIAVLNFGELIALGTPEEV 240
Cdd:PRK10261 231 VVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
7-52 |
3.29e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 38.71 E-value: 3.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 527030459 7 VSDLTKSFGGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTG 52
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG 116
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-66 |
3.33e-03 |
|
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: 38.30 E-value: 3.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 527030459 23 VSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGR 66
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR 99
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-66 |
3.55e-03 |
|
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: 38.74 E-value: 3.55e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 527030459 23 VSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGR 66
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR 488
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-229 |
4.16e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 38.15 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 2 SAILEVSDLTKSF--GGL--TAVAGVSLSIEEGSIFGLIGPNGAGKT-TFFNMLTGMTRP----TSGRVAFAG------- 65
Cdd:PRK15134 3 QPLLAIENLSVAFrqQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGesllhas 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 66 -RDLAGLIPEEIARLgigrtFQNirlfaGMSVLDNVRVpgqcrLRSGLwSQVVGLSAARREEDEGRERAWELLRlVGLES 144
Cdd:PRK15134 83 eQTLRGVRGNKIAMI-----FQE-----PMVSLNPLHT-----LEKQL-YEVLSLHRGMRREAARGEILNCLDR-VGIRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 145 RAERAAG---SLPYGDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETFSLTVLLIEHHVPMVMGLCD 221
Cdd:PRK15134 146 AAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLAD 225
|
....*...
gi 527030459 222 RIAVLNFG 229
Cdd:PRK15134 226 RVAVMQNG 233
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-60 |
4.27e-03 |
|
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: 37.73 E-value: 4.27e-03
10 20 30
....*....|....*....|....*....|...
gi 527030459 28 EEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGR 60
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK 56
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
35-102 |
6.00e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.60 E-value: 6.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527030459 35 LIGPNGAGKTTF---FNMLTGMTRptsGRVAFAGRDLAGLipEEIARLGIGRTFQNIRLFAGMSVLDNVRV 102
Cdd:COG4637 26 LIGANGSGKSNLldaLRFLSDAAR---GGLQDALARRGGL--EELLWRGPRTITEPIRLELEFAEEDERDL 91
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-240 |
6.40e-03 |
|
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: 38.00 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 23 VSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRDlaglipeeIARLGIgrtfQNIRLFAGMSVLDNVRV 102
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN--------IAKIGL----HDLRFKITIIPQDPVLF 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 103 PGQCRLRSGLWSQVvglsaarreedeGRERAWELLRLV-----------GLESRAERAAGSLPYGDRRRLEIARALALSP 171
Cdd:TIGR00957 1373 SGSLRMNLDPFSQY------------SDEEVWWALELAhlktfvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 172 RLLLLDEPAAGMNPSEKQALSGFIREIRETfsLTVLLIEHHVPMVMGLCdRIAVLNFGELIALGTPEEV 240
Cdd:TIGR00957 1441 KILVLDEATAAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-239 |
6.76e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 37.69 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 5 LEVSDLTKSFGG--LTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRVAFAGRD-----LAGLipeeia 77
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDlrdytLASL------ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 78 RLGIGRTFQNIRLFAGmSVLDNVRVPgqcrlRSGLWSQVVGLSAARREEdegrerAWELLRLV--GLESRAERAAGSLPY 155
Cdd:PRK11176 416 RNQVALVSQNVHLFND-TIANNIAYA-----RTEQYSREQIEEAARMAY------AMDFINKMdnGLDTVIGENGVLLSG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 156 GDRRRLEIARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIREtfSLTVLLIEHHVPMVMGlCDRIAVLNFGELIALG 235
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
....
gi 527030459 236 TPEE 239
Cdd:PRK11176 561 THAE 564
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
147-223 |
7.79e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 36.15 E-value: 7.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 147 ERAAGSLPYGDRRRLEIAR--ALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMvMGLCDRI 223
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHNLDV-LSSADWI 158
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-233 |
8.11e-03 |
|
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: 37.11 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 20 VAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPT-SGRVAFAGRDLA------------GLIPEEIARLGIGRTF- 85
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDirnpaqairagiAMVPEDRKRHGIVPILg 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 86 --QNIRLfagmSVLDnvRVPGQCRLRSGLWSQVVGLsaarreedegrerawELLRLVGLESRAERAAGSLPYGDRRRLEI 163
Cdd:TIGR02633 356 vgKNITL----SVLK--SFCFKMRIDAAAELQIIGS---------------AIQRLKVKTASPFLPIGRLSGGNQQKAVL 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527030459 164 ARALALSPRLLLLDEPAAGMNPSEKQALSGFIREIRETfSLTVLLIEHHVPMVMGLCDRIAVLNFGELIA 233
Cdd:TIGR02633 415 AKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-61 |
8.71e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.15 E-value: 8.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 527030459 4 ILEVSDLTKSF-GGLTAVAGVSLSIEEGSIFGLIGPNGAGKTTFFNMLTGMTRPTSGRV 61
Cdd:PLN03073 508 IISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
|
| |
