|
Name |
Accession |
Description |
Interval |
E-value |
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-249 |
5.92e-158 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 438.35 E-value: 5.92e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEVTKGEVLFDGVNILELEVDERARMGLF 83
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGEDILELSPDERARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LAMQYPSEIPGITNAEFLRAAMNAGKEddEKISVREFITKLDEKMELLNMKEEMAERYLNEGFSGGEKKRNEILQLLMLE 163
Cdd:COG0396 81 LAFQYPVEIPGVSVSNFLRTALNARRG--EELSAREFLKLLKEKMKELGLDEDFLDRYVNEGFSGGEKKRNEILQMLLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 164 PTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITPDVVHVMMEGRVVLSGGPELAARLEREGYAK 243
Cdd:COG0396 159 PKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIKPDFVHVLVDGRIVKSGGKELALELEEEGYDW 238
|
....*.
gi 2038778719 244 LAEELG 249
Cdd:COG0396 239 LKEEAA 244
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
4-242 |
6.07e-140 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 392.78 E-value: 6.07e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEVTKGEVLFDGVNILELEVDERARMGLF 83
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVTSGTILFKGQDLLELEPDERARAGLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LAMQYPSEIPGITNAEFLRAAMNA--GKEDDEKISVREFITKLDEKMELLNMKEEMAERYLNEGFSGGEKKRNEILQLLM 161
Cdd:TIGR01978 81 LAFQYPEEIPGVSNLEFLRSALNArrSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEGFSGGEKKRNEILQMAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 162 LEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITPDVVHVMMEGRVVLSGGPELAARLEREGY 241
Cdd:TIGR01978 161 LEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKPDYVHVLLDGRIVKSGDVELAKELEAKGY 240
|
.
gi 2038778719 242 A 242
Cdd:TIGR01978 241 D 241
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-241 |
3.53e-117 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 335.46 E-value: 3.53e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 2 SVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEVTKGEVLFDGVNILELEVDERARMG 81
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGESILDLEPEERAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 82 LFLAMQYPSEIPGITNAEFLRAAMNA--GKEDDEKISVREFITKLDEKMELLNMKEEMAERYLNEGFSGGEKKRNEILQL 159
Cdd:CHL00131 86 IFLAFQYPIEIPGVSNADFLRLAYNSkrKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEGFSGGEKKRNEILQM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 160 LMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITPDVVHVMMEGRVVLSGGPELAARLERE 239
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHVMQNGKIIKTGDAELAKELEKK 245
|
..
gi 2038778719 240 GY 241
Cdd:CHL00131 246 GY 247
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-241 |
2.93e-115 |
|
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: 328.33 E-value: 2.93e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEVTKGEVLFDGVNILELEVDERARMGLF 83
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LAMQYPSEIPGITNAEFLraamnagkeddekisvrefitkldekmellnmkeemaeRYLNEGFSGGEKKRNEILQLLMLE 163
Cdd:cd03217 81 LAFQYPPEIPGVKNADFL--------------------------------------RYVNEGFSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038778719 164 PTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITPDVVHVMMEGRVVLSGGPELAARLEREGY 241
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYDGRIVKSGDKELALEIEKKGY 200
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-247 |
4.38e-98 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 286.69 E-value: 4.38e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEVTKGEVLFDGVNILELEVDERARMGL 82
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 FLAMQYPSEIPGITNAEFLRAAMNAGKE--DDEKISVREFITKLDEKMELLNMKEEMAERYLNEGFSGGEKKRNEILQLL 160
Cdd:PRK09580 81 FMAFQYPVEIPGVSNQFFLQTALNAVRSyrGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 161 MLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITPDVVHVMMEGRVVLSGGPELAARLEREG 240
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQG 240
|
....*..
gi 2038778719 241 YAKLAEE 247
Cdd:PRK09580 241 YGWLTEQ 247
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-203 |
3.70e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 111.83 E-value: 3.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNpnYEVTKGEVLFDGVNILELEVDE-RARMGL 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADL--DPPTSGEIYLDGKPLSAMPPPEwRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 FlaMQYPSEIPGITNAEFLRAAMNAGKEDDEKisvrefitKLDEKMELLNMKEEMAERYLNEgFSGGEKKRNEILQLLML 162
Cdd:COG4619 79 V--PQEPALWGGTVRDNLPFPFQLRERKFDRE--------RALELLERLGLPPDILDKPVER-LSGGERQRLALIRALLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2038778719 163 EPTFALLDEIDSGLDIDALKVVSKGVNA-MRGEGFGAMIITH 203
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSH 189
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-231 |
1.77e-29 |
|
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: 110.71 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERARMGL- 82
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVG--LVKPDSGKILLDGQDITKLPMHKRARLGIg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 FLAmQYPSEIPGITNAEFLRAAMNAGKEDDEkisvrEFITKLDEKMELLNMkEEMAERyLNEGFSGGEKKRNEILQLLML 162
Cdd:cd03218 79 YLP-QEASIFRKLTVEENILAVLEIRGLSKK-----EREEKLEELLEEFHI-THLRKS-KASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038778719 163 EPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITpDVVHVMMEGRVVLSGGPE 231
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSIT-DRAYIIYEGKVLAEGTPE 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-231 |
5.43e-29 |
|
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: 109.75 E-value: 5.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNILELEVDERARM 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGllKP----SSGEVLLDGRDLASLSRRELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 glfLAM--QYPSEIPGITNAE--------FLRAAMNAGKEDDEKIsvrefitklDEKMELLNMkEEMAERYLNEgFSGGE 150
Cdd:COG1120 77 ---IAYvpQEPPAPFGLTVRElvalgrypHLGLFGRPSAEDREAV---------EEALERTGL-EHLADRPVDE-LSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 151 KKRNEILQLLMLEPTFALLDEIDSGLDI----DALKVVSKGVnamRGEGFGAMIITHYqrlLN----YItpDVVHVMMEG 222
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLA---RERGRTVVMVLHD---LNlaarYA--DRLVLLKDG 214
|
....*....
gi 2038778719 223 RVVLSGGPE 231
Cdd:COG1120 215 RIVAQGPPE 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-239 |
6.13e-29 |
|
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: 109.56 E-value: 6.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERARMGL 82
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAG--LLKPDSGSILIDGEDVRKEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 FlamqyPSEI---PGIT---NAEFLRAAMnagkeddeKISVREFITKLDEKMELLNMKEEMAERYlnEGFSGGEKKRNEI 156
Cdd:COG4555 79 L-----PDERglyDRLTvreNIRYFAELY--------GLFDEELKKRIEELIELLGLEEFLDRRV--GELSTGMKKKVAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 157 LQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITpDVVHVMMEGRVVLSGGP-ELAAR 235
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALC-DRVVILHKGKVVAQGSLdELREE 222
|
....
gi 2038778719 236 LERE 239
Cdd:COG4555 223 IGEE 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-223 |
9.35e-29 |
|
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: 106.56 E-value: 9.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 5 EIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVdERARMGLFL 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAG--LLKPTSGEILIDGKDIAKLPL-EELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 85 AMQypseipgitnaeflraamnagkeddekisvrefitkldekmellnmkeemaerylnegFSGGEKKRNEILQLLMLEP 164
Cdd:cd00267 78 VPQ----------------------------------------------------------LSGGQRQRVALARALLLNP 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2038778719 165 TFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYItPDVVHVMMEGR 223
Cdd:cd00267 100 DLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELA-ADRVIVLKDGK 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-171 |
2.16e-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: 105.42 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEV-DERARMGLFlaMQYPSEIPGITN 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAG--LLSPTEGTILLDGQDLTDDERkSLRKEIGYV--FQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038778719 98 AEFLRAAMNAGKEDDEKISVRefitkLDEKMELLNMKEEMAER--YLNEGFSGGEKKRNEILQLLMLEPTFALLDE 171
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDAR-----AEEALEKLGLGDLADRPvgERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-231 |
2.21e-27 |
|
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: 105.21 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERARMGLF 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISG--FLRPTSGSVLFDGEDITGLPPHEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LAMQYPSEIPGITNAEFLRAAMNAGKED--------DEKISVREFITKLDEKMELLNMKEEMAerylnEGFSGGEKKRNE 155
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMVAAQARTGSglllararREEREARERAEELLERVGLADLADRPA-----GELSYGQQRRLE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038778719 156 ILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITpDVVHVMMEGRVVLSGGPE 231
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLA-DRVTVLDQGRVIAEGTPD 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-231 |
3.38e-27 |
|
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: 109.22 E-value: 3.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MS-VLEIKDLHVEIEG--KEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG-NPNYEVTKGEVLFDGVNILELEVDE 76
Cdd:COG1123 1 MTpLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGlLPHGGRISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 77 RARMGLFLAMQYPSEIPGITNAEFLRAAMNAGKEDDEKIsvREFITKLDEKMELlnmkEEMAERYLNEgFSGGEKKRNEI 156
Cdd:COG1123 81 RGRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEA--RARVLELLEAVGL----ERRLDRYPHQ-LSGGQRQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038778719 157 LQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGE-GFGAMIITHYQRLLNYItPDVVHVMMEGRVVLSGGPE 231
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEI-ADRVVVMDDGRIVEDGPPE 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-234 |
5.23e-27 |
|
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: 104.05 E-value: 5.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERARMGLF 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMG--LLPPRSGSIRFDGRDITGLPPHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LAMQYPSEIPGITNAEFLRAAMNAGKEDDEKisvrefiTKLDEKMELLNMKEEMAERyLNEGFSGGEKKRNEILQLLMLE 163
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARRRAKRK-------ARLERVYELFPRLKERRKQ-LAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038778719 164 PTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITpDVVHVMMEGRVVLSGGP-ELAA 234
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIA-DRAYVLERGRVVLEGTAaELLA 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-225 |
5.37e-27 |
|
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: 104.12 E-value: 5.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGK----EILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERA 78
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILG--LLKPTSGSIIFDGKDLLKLSRRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 79 RMGLFLAM--QYPSEI--PGITNAEFLRAAM-NAGKEDDEKisvrEFITKLDEKMELLNMKEEMAERYLNEgFSGGEKKR 153
Cdd:cd03257 79 IRRKEIQMvfQDPMSSlnPRMTIGEQIAEPLrIHGKLSKKE----ARKEAVLLLLVGVGLPEEVLNRYPHE-LSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038778719 154 NEILQLLMLEPTFALLDEIDSGLD-------IDALKvvskgvNAMRGEGFGAMIITHYQRLLNYITpDVVHVMMEGRVV 225
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDvsvqaqiLDLLK------KLQEELGLTLLFITHDLGVVAKIA-DRVAVMYAGKIV 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-223 |
4.81e-26 |
|
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: 101.00 E-value: 4.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 5 EIKDLHVEIEGKE--ILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERARMgL 82
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNG--LLGPTSGEVLVDGKDLTKLSLKELRRK-V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 FLAMQYP-SEIPGITNAE---FlrAAMNAGKEDDEkisVREfitKLDEKMELLNMkEEMAERYLNEgFSGGEKKRNEILQ 158
Cdd:cd03225 78 GLVFQNPdDQFFGPTVEEevaF--GLENLGLPEEE---IEE---RVEEALELVGL-EGLRDRSPFT-LSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038778719 159 LLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITpDVVHVMMEGR 223
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELA-DRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-231 |
5.35e-26 |
|
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: 101.26 E-value: 5.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEI-EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNILELEVDE-RAR 79
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGllKP----TSGEVLVDGKDITKKNLRElRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 80 MGL-FlamQYPS----------EIpgitnaEFlrAAMNAGKEDDEkisVREfitKLDEKMELLNMkEEMAERYLNEgFSG 148
Cdd:COG1122 77 VGLvF---QNPDdqlfaptveeDV------AF--GPENLGLPREE---IRE---RVEEALELVGL-EHLADRPPHE-LSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 149 GEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITPDVVhVMMEGRVVLSG 228
Cdd:COG1122 138 GQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVI-VLDDGRIVADG 216
|
...
gi 2038778719 229 GPE 231
Cdd:COG1122 217 TPR 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-247 |
2.47e-25 |
|
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: 104.53 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 14 EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNpnYEVTKGEVLFDGVNILELEVDE-RARMG-------LF-- 83
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL--YEPTSGRILIDGIDLRQIDPASlRRQIGvvlqdvfLFsg 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 -----LAMQYPSeipgITNAEFLRAAMNAGkeddekisVREFITKLDEKMELLnmkeeMAERylNEGFSGGEKKRNEILQ 158
Cdd:COG2274 564 tirenITLGDPD----ATDEEIIEAARLAG--------LHDFIEALPMGYDTV-----VGEG--GSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 159 LLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGeGFGAMIITHYQRLLNYItpDVVHVMMEGRVVLSGGP-ELAARLE 237
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRLA--DRIIVLDKGRIVEDGTHeELLARKG 701
|
250
....*....|
gi 2038778719 238 RegYAKLAEE 247
Cdd:COG2274 702 L--YAELVQQ 709
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-237 |
1.17e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 97.83 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERARMGLF 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLG--LLRPTSGEVRVLGEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LamQYPSEIPGITNAEFLR--AAMNagkeddeKISVREFITKLDEKMELLNMKEEMAERYlnEGFSGGEKKRNEILQLLM 161
Cdd:COG1131 79 P--QEPALYPDLTVRENLRffARLY-------GLPRKEARERIDELLELFGLTDAADRKV--GTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 162 LEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHY----QRLLnyitpDVVHVMMEGRVVLSGGPE--LAAR 235
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYleeaERLC-----DRVAIIDKGRIVADGTPDelKARL 222
|
..
gi 2038778719 236 LE 237
Cdd:COG1131 223 LE 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-231 |
4.64e-24 |
|
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: 96.59 E-value: 4.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNILELEVDE---- 76
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGllRP----DSGEILVDGQDITGLSEKElyel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 77 RARMG-------LFLAMqypseipgiT---NAEF-LRaaMNAGKEDDEkisvrefITKL-DEKMELLNMkEEMAERYLNE 144
Cdd:COG1127 81 RRRIGmlfqggaLFDSL---------TvfeNVAFpLR--EHTDLSEAE-------IRELvLEKLELVGL-PGAADKMPSE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 145 gFSGGEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGE-GFGAMIITHYQRLLNYITPDVVhVMMEGR 223
Cdd:COG1127 142 -LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVA-VLADGK 219
|
....*...
gi 2038778719 224 VVLSGGPE 231
Cdd:COG1127 220 IIAEGTPE 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-228 |
4.79e-24 |
|
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: 95.68 E-value: 4.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 5 EIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG-NPNyevTKGEVLFDGVNIleleVDERARMGlF 83
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGlLKP---TSGSIRVFGKPL----EKERKRIG-Y 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LAmQYPS---EIPgITNAEF--------LRAAMNAGKEDDEKIsvrefitklDEKMELLNMkEEMAERYLNEgFSGGEKK 152
Cdd:cd03235 73 VP-QRRSidrDFP-ISVRDVvlmglyghKGLFRRLSKADKAKV---------DEALERVGL-SELADRQIGE-LSGGQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038778719 153 RNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITPDVvhVMMEGRVVLSG 228
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRV--LLLNRTVVASG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-231 |
5.63e-24 |
|
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: 99.98 E-value: 5.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVE-----IEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDER 77
Cdd:COG1123 260 LLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG--LLRPTSGSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 78 ARMGLFLAM--QYPS-----------EIpgitnAEFLRAAMNAGKEDDEKisvrefitKLDEKMELLNMKEEMAERYLNE 144
Cdd:COG1123 338 RELRRRVQMvfQDPYsslnprmtvgdII-----AEPLRLHGLLSRAERRE--------RVAELLERVGLPPDLADRYPHE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 145 gFSGGEKKRNEILQLLMLEPTFALLDEIDSGLD----------IDALKvvskgvnamRGEGFGAMIITHYQRLLNYITPD 214
Cdd:COG1123 405 -LSGGQRQRVAIARALALEPKLLILDEPTSALDvsvqaqilnlLRDLQ---------RELGLTYLFISHDLAVVRYIADR 474
|
250
....*....|....*..
gi 2038778719 215 VVhVMMEGRVVLSGGPE 231
Cdd:COG1123 475 VA-VMYDGRIVEDGPTE 490
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-228 |
6.68e-24 |
|
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: 94.42 E-value: 6.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 5 EIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERARmglfl 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAG--LLKPSSGEILLDGKDLASLSPKELAR----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 85 amqypseipgitnaeflraamnagkeddeKISVrefitkLDEKMELLNMkEEMAERYLNEgFSGGEKKRNEILQLLMLEP 164
Cdd:cd03214 74 -----------------------------KIAY------VPQALELLGL-AHLADRPFNE-LSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038778719 165 TFALLDEIDSGLDID-ALKVVSKGVNAMRGEGFGAMIITHYqrlLN--YITPDVVHVMMEGRVVLSG 228
Cdd:cd03214 117 PILLLDEPTSHLDIAhQIELLELLRRLARERGKTVVMVLHD---LNlaARYADRVILLKDGRIVAQG 180
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-243 |
1.84e-23 |
|
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: 95.26 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHV----EIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG-NPNYEvtkGEVLFDGVnilelEVDERA 78
Cdd:COG1124 2 LEVRNLSVsygqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGlERPWS---GEVTFDGR-----PVTRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 79 RMGLFLAMQ------YPSEIPGITNAEFLRAAMNAGKEDDEKisvrefiTKLDEKMELLNMKEEMAERYLNEgFSGGEKK 152
Cdd:COG1124 74 RKAFRRRVQmvfqdpYASLHPRHTVDRILAEPLRIHGLPDRE-------ERIAELLEQVGLPPSFLDRYPHQ-LSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 153 RNEILQLLMLEPTFALLDEIDSGLDIdalkVVSKGV----NAMRGE-GFGAMIITHYQRLLNYITpDVVHVMMEGRVVLS 227
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDV----SVQAEIlnllKDLREErGLTYLFVSHDLAVVAHLC-DRVAVMQNGRIVEE 220
|
250
....*....|....*.
gi 2038778719 228 GGPELAARLEREGYAK 243
Cdd:COG1124 221 LTVADLLAGPKHPYTR 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-231 |
4.25e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 93.94 E-value: 4.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPNyevtKGEVLFDGVNILELEVDERA 78
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGlvKPD----SGRIFLDGEDITHLPMHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 79 RMGL-FLAmQYPSEIPGITNAEFLRAamnagkeddekisVREFiTKLDEKmellnMKEEMAERYLNEgF----------- 146
Cdd:COG1137 77 RLGIgYLP-QEASIFRKLTVEDNILA-------------VLEL-RKLSKK-----EREERLEELLEE-Fgithlrkskay 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 147 --SGGEKKRNEILQLLMLEPTFALLDEIDSGLD----IDALKVVSKgvnaMRGEGFGAMIITHyqrllNY-----ITpDV 215
Cdd:COG1137 136 slSGGERRRVEIARALATNPKFILLDEPFAGVDpiavADIQKIIRH----LKERGIGVLITDH-----NVretlgIC-DR 205
|
250
....*....|....*.
gi 2038778719 216 VHVMMEGRVVLSGGPE 231
Cdd:COG1137 206 AYIISEGKVLAEGTPE 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-234 |
1.10e-22 |
|
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: 92.74 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNyeVTKGEVLFDGVNILELEVDERARM 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP--PRSGSIRFDGEDITGLPPHRIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 GLFLAMQYPSEIPGITNAEFLRAAMNAGKEDDEKISVREFItkldekmelLNMKEEMAERYLNEG--FSGGEKKrneilQ 158
Cdd:COG0410 79 GIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERV---------YELFPRLKERRRQRAgtLSGGEQQ-----M 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 159 L-----LMLEPTFALLDEIDSGL------DI-DALK-VVSKGV-------NAMRgegfgAMIITHYqrllnyitpdvVHV 218
Cdd:COG0410 145 LaigraLMSRPKLLLLDEPSLGLapliveEIfEIIRrLNREGVtillveqNARF-----ALEIADR-----------AYV 208
|
250
....*....|....*..
gi 2038778719 219 MMEGRVVLSGGP-ELAA 234
Cdd:COG0410 209 LERGRIVLEGTAaELLA 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-231 |
1.13e-22 |
|
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: 92.56 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNpnYEVTKGEVLFDGVNILELEVDE----RAR 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGL--LRPDSGEVLIDGEDISGLSEAElyrlRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 80 MGlflaMQYPSeipgitNAEFlraamnagkeDDekISVREFI-------TKLDEKM--ELLNMKEEM-----AERYLNEG 145
Cdd:cd03261 79 MG----MLFQS------GALF----------DS--LTVFENVafplrehTRLSEEEirEIVLEKLEAvglrgAEDLYPAE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 146 FSGGEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGE-GFGAMIITHYqrlLN--YITPDVVHVMMEG 222
Cdd:cd03261 137 LSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHD---LDtaFAIADRIAVLYDG 213
|
....*....
gi 2038778719 223 RVVLSGGPE 231
Cdd:cd03261 214 KIVAEGTPE 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-231 |
2.68e-22 |
|
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: 91.47 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG-NPNYEVTK--GEVLFDGVNILELEVDE---R 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlNDLIPGAPdeGEVLLDGKDIYDLDVDVlelR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 78 ARMGlfLAMQYPSEIPGiTNAEFLRAAMNAGKEDDEKIsVREFITKLDEKMELlnmKEEMAERYLNEGFSGGEKKRNEIL 157
Cdd:cd03260 81 RRVG--MVFQKPNPFPG-SIYDNVAYGLRLHGIKLKEE-LDERVEEALRKAAL---WDEVKDRLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038778719 158 QLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEgFGAMIITH----YQRLlnyitPDVVHVMMEGRVVLSGGPE 231
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHnmqqAARV-----ADRTAFLLNGRLVEFGPTE 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-224 |
3.31e-22 |
|
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: 89.76 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERARMGlf 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILG--LLKPDSGEIKVLGKDIKKEPEEVKRRIG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LAMQYPSEIPGITNAEFLRaamnagkeddekisvrefitkldekmellnmkeemaerylnegFSGGEKKRNEILQLLMLE 163
Cdd:cd03230 77 YLPEEPSLYENLTVRENLK-------------------------------------------LSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038778719 164 PTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITpDVVHVMMEGRV 224
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLC-DRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-231 |
5.88e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 90.92 E-value: 5.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILElevdERARM 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILG--LLPPTSGTVRLFGKPPRR----ARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 GlflamqY-P--SEIPG---ITNAEFLraAMN----------AGKEDDEKIsvrefitklDEKMELLNMkEEMAERYLNE 144
Cdd:COG1121 78 G------YvPqrAEVDWdfpITVRDVV--LMGrygrrglfrrPSRADREAV---------DEALERVGL-EDLADRPIGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 145 gFSGGEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITH-YQRLLNYItPDVVHvmMEGR 223
Cdd:COG1121 140 -LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHdLGAVREYF-DRVLL--LNRG 215
|
....*...
gi 2038778719 224 VVLSGGPE 231
Cdd:COG1121 216 LVAHGPPE 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-231 |
6.69e-22 |
|
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: 90.91 E-value: 6.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNpNYEVTKGEV-LFD----GVNILELevd 75
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGD-LPPTYGNDVrLFGerrgGEDVWEL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 76 eRARMGLF---LAMQYPSEIPG-----------------ITNAEFLRAamnagkeddekisvrefitklDEKMELLNMkE 135
Cdd:COG1119 77 -RKRIGLVspaLQLRFPRDETVldvvlsgffdsiglyrePTDEQRERA---------------------RELLELLGL-A 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 136 EMAERYLNEgFSGGEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMI-ITHYqrlLNYITPD 214
Cdd:COG1119 134 HLADRPFGT-LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlVTHH---VEEIPPG 209
|
250
....*....|....*....
gi 2038778719 215 VVHVMM--EGRVVLSGGPE 231
Cdd:COG1119 210 ITHVLLlkDGRVVAAGPKE 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-208 |
7.53e-22 |
|
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: 90.01 E-value: 7.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 5 EIKDLHVEI-EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILElevDERARMGlF 83
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG--LIKESSGSILLNGKPIKA---KERRKSI-G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LAMQYP-SEIPGITNAEFLRAAMNAGKEDDEKISvrefitKLDEKMELLNMKEEmaeryLNEGFSGGEKKRNEILQLLML 162
Cdd:cd03226 75 YVMQDVdYQLFTDSVREELLLGLKELDAGNEQAE------TVLKDLDLYALKER-----HPLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2038778719 163 EPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLL 208
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFL 189
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-231 |
1.75e-21 |
|
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: 90.10 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERARM 80
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITG--FYRPTSGRILFDGRDITGLPPHRIARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 GLFLAMQYPSEIPGIT-------------NAEFLRAAMNAGKEDDEKISVREFITKLDEKMELLNMKEEMAerylnEGFS 147
Cdd:COG0411 80 GIARTFQNPRLFPELTvlenvlvaaharlGRGLLAALLRLPRARREEREARERAEELLERVGLADRADEPA-----GNLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 148 GGEKKRNEILQLLMLEPTFALLDEIDSGL---DIDALKVVSKGVNAMRGEGFgaMIITHYQRLLNYITpDVVHVMMEGRV 224
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLnpeETEELAELIRRLRDERGITI--LLIEHDMDLVMGLA-DRIVVLDFGRV 231
|
....*..
gi 2038778719 225 VLSGGPE 231
Cdd:COG0411 232 IAEGTPA 238
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-223 |
2.08e-21 |
|
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: 87.82 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEG--KEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNpnYEVTKGEVLFDGVNILELEVDE-RARM 80
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRL--YDPTSGEILIDGVDLRDLDLESlRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 GLFLamQYPseipgitnaeFLRAAmnagkeddekiSVREFItkldekmellnmkeemaerylnegFSGGEKKRNEILQLL 160
Cdd:cd03228 79 AYVP--QDP----------FLFSG-----------TIRENI------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038778719 161 MLEPTFALLDEIDSGLDIDALKVVSKGVNAMRgEGFGAMIITHyqRLLNYITPDVVHVMMEGR 223
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALA-KGKTVIVIAH--RLSTIRDADRIIVLDDGR 171
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-228 |
2.59e-21 |
|
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: 88.40 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGeIAAIMGPNGTGKSTLSAAIMGNpnYEVTKGEVLFDGVNILELEVDERARMGlF 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATL--TPPSSGTIRIDGQDVLKQPQKLRRRIG-Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LAmQYPSEIPGITNAEFLR--AAMNagkeddeKISVREFITKLDEKMELLNMkEEMAERYLNeGFSGGEKKRNEILQLLM 161
Cdd:cd03264 77 LP-QEFGVYPNFTVREFLDyiAWLK-------GIPSKEVKARVDEVLELVNL-GDRAKKKIG-SLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038778719 162 LEPTFALLDEIDSGLDIdALKVVSKGVNAMRGEGFGAMIITHyqrllnyITPDV------VHVMMEGRVVLSG 228
Cdd:cd03264 147 GDPSILIVDEPTAGLDP-EERIRFRNLLSELGEDRIVILSTH-------IVEDVeslcnqVAVLNKGKLVFEG 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-228 |
3.58e-21 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 88.42 E-value: 3.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNpnYEVTKGEVLFDGVNILELEVDE-RARMG-------LF------- 83
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL--YKPTSGSVLLDGTDIRQLDPADlRRNIGyvpqdvtLFygtlrdn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LAMQYPSeipgITNAEFLRAAMNAGkeddekisVREFITKLDEKMELlnmkeEMAERylNEGFSGGEKKRNEILQLLMLE 163
Cdd:cd03245 98 ITLGAPL----ADDERILRAAELAG--------VTDFVNKHPNGLDL-----QIGER--GRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038778719 164 PTFALLDEIDSGLDIDALKVVSKGVNAMRGeGFGAMIITHYQRLLNYItpDVVHVMMEGRVVLSG 228
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLLDLV--DRIIVMDSGRIVADG 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-207 |
1.39e-20 |
|
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: 86.38 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNILELEVDERARM 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGllPP----SAGEVLWNGEPIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 gLFLAmQYPSEIPGITNAEFLRAAMNAGKEDDEKISVREFItkldEKMELLNMKEEMAeRYLnegfSGGEKKRNEILQLL 160
Cdd:COG4133 78 -AYLG-HADGLKPELTVRENLRFWAALYGLRADREAIDEAL----EAVGLAGLADLPV-RQL----SAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2038778719 161 MLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGfGAMIITHYQRL 207
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARG-GAVLLTTHQPL 192
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-228 |
3.79e-20 |
|
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: 85.79 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 16 KEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGN-PNYEVTKGEVLFDGVnilELEVDERARMGLFLAmQYPSEIPG 94
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvEGGGTTSGQILFNGQ---PRKPDQFQKCVAYVR-QDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 95 ITNAEFLR-AAMNAGKEddekISVREFITKLDEKMELLNMKEEMAERYLNEGFSGGEKKRNEILQLLMLEPTFALLDEID 173
Cdd:cd03234 96 LTVRETLTyTAILRLPR----KSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2038778719 174 SGLD-IDALKVVSKGVNAMRGeGFGAMIITHYQRLLNYITPDVVHVMMEGRVVLSG 228
Cdd:cd03234 172 SGLDsFTALNLVSTLSQLARR-NRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-238 |
5.96e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 85.94 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpnyEV--TKGEVLFDGVNILELEVDERARMg 81
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG----ELtpSSGEVRLNGRPLAAWSPWELARR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 82 lfLA-------MQYP---SEIpgitnAEFLRAAMNAGKEDDEKIsvrefitkLDEKMELLNMkEEMAERYLNEgFSGGEK 151
Cdd:COG4559 77 --RAvlpqhssLAFPftvEEV-----VALGRAPHGSSAAQDRQI--------VREALALVGL-AHLAGRSYQT-LSGGEQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 152 KR-------NEILQLLMLEPTFALLDEIDSGLDI----DALKVVSKgvnaMRGEGFGAMIITHYqrlLN----YitPDVV 216
Cdd:COG4559 140 QRvqlarvlAQLWEPVDGGPRWLFLDEPTSALDLahqhAVLRLARQ----LARRGGGVVAVLHD---LNlaaqY--ADRI 210
|
250 260
....*....|....*....|....*
gi 2038778719 217 HVMMEGRVVLSGGPE---LAARLER 238
Cdd:COG4559 211 LLLHQGRLVAQGTPEevlTDELLER 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-244 |
4.90e-19 |
|
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: 83.05 E-value: 4.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 15 GKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMgnPNYEVTKGEVLFDGVNILELEVDE-RARMG-------LFLA- 85
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF--RFYDVSSGSILIDGQDIREVTLDSlRRAIGvvpqdtvLFNDt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 86 ----MQYPSeiPGITNAEFLRAAMNAGkeddekisVREFITKLDEKMEllnmkEEMAERYLNegFSGGEKKRNEILQLLM 161
Cdd:cd03253 91 igynIRYGR--PDATDEEVIEAAKAAQ--------IHDKIMRFPDGYD-----TIVGERGLK--LSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 162 LEPTFALLDEIDSGLDIDALKVVSKGVNAMrGEGFGAMIITHyqRLLNYITPDVVHVMMEGRVVLSGGPElaARLEREG- 240
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAH--RLSTIVNADKIIVLKDGRIVERGTHE--ELLAKGGl 228
|
....
gi 2038778719 241 YAKL 244
Cdd:cd03253 229 YAEM 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-246 |
6.57e-19 |
|
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: 82.59 E-value: 6.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 17 EILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMgnPNYEVTKGEVLFDGVNILELEVDE-RARMGlfLAMQYPSEIPGi 95
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLE--RFYDPTSGEILLDGVDIRDLNLRWlRSQIG--LVSQEPVLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 96 TNAEFLR-AAMNAGKEDDEKIS----VREFITKLDEKMEllnmkEEMAERYLNegFSGGEKKRNEILQLLMLEPTFALLD 170
Cdd:cd03249 92 TIAENIRyGKPDATDEEVEEAAkkanIHDFIMSLPDGYD-----TLVGERGSQ--LSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038778719 171 EIDSGLDIDALKVVSKGVNAMRgEGFGAMIITHyqRLLNYITPDVVHVMMEGRVVLSGGP-ELAARleREGYAKLAE 246
Cdd:cd03249 165 EATSALDAESEKLVQEALDRAM-KGRTTIVIAH--RLSTIRNADLIAVLQNGQVVEQGTHdELMAQ--KGVYAKLVK 236
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-228 |
6.92e-19 |
|
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: 82.18 E-value: 6.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNpnYEVTKGEVLFDGVNILELEVDERarmGLF 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL--ERPDSGEILIDGRDVTGVPPERR---NIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LAMQYPSEIPGITNAEFLRAAMNAGKEDDEKISVREfitklDEKMELLNMkEEMAERYLNEgFSGGEKKRNEILQLLMLE 163
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARV-----RELLELVGL-EGLLNRYPHE-LSGGQQQRVALARALARE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038778719 164 PTFALLDEIDSGLDIDaLKVvskgvnAMRGE--------GFGAMIITHYQRLLNYITpDVVHVMMEGRVVLSG 228
Cdd:cd03259 149 PSLLLLDEPLSALDAK-LRE------ELREElkelqrelGITTIYVTHDQEEALALA-DRIAVMNEGRIVQVG 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-231 |
8.91e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.90 E-value: 8.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpnyEVT--KGEVLFDGVNILELEVDERARM 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG----ELSpdSGEVRLNGRPLADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 glfLAM--QYPS--------EIPGITnaeflRAAMNAGKEDDEKIsvrefitkLDEKMELLNMkEEMAERYLNEgFSGGE 150
Cdd:PRK13548 78 ---RAVlpQHSSlsfpftveEVVAMG-----RAPHGLSRAEDDAL--------VAAALAQVDL-AHLAGRDYPQ-LSGGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 151 KKRneiLQLLML---------EPTFALLDEIDSGLDI----DALKVVSkgvNAMRGEGFGAMIITHYqrlLN----YitP 213
Cdd:PRK13548 140 QQR---VQLARVlaqlwepdgPPRWLLLDEPTSALDLahqhHVLRLAR---QLAHERGLAVIVVLHD---LNlaarY--A 208
|
250
....*....|....*...
gi 2038778719 214 DVVHVMMEGRVVLSGGPE 231
Cdd:PRK13548 209 DRIVLLHQGRLVADGTPA 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-228 |
1.11e-18 |
|
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: 81.49 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEvDERARMGLF 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILG--LIKPDSGEITFDGKSYQKNI-EALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LamQYPSEIPGITNAEFLRAAMNAGKEDDEKIsvrefitklDEKMELLNMKEEMAERYlnEGFSGGEKKRNEILQLLMLE 163
Cdd:cd03268 78 I--EAPGFYPNLTARENLRLLARLLGIRKKRI---------DEVLDVVGLKDSAKKKV--KGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038778719 164 PTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHyqrLLNYI--TPDVVHVMMEGRVVLSG 228
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSH---LLSEIqkVADRIGIINKGKLIEEG 208
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-225 |
1.15e-18 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 82.55 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 16 KEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNILELEVDERARMGLFLAMQYpSEIP 93
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGleKP----AQGTVSFRGQDLYQLDRKQRRAFRRDVQLVF-QDSP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 94 GITNAEF-LRAAMNAGKEDDEKISVREFITKLDEKMELLNMKEEMAERYLNEgFSGGEKKRNEILQLLMLEPTFALLDEI 172
Cdd:TIGR02769 99 SAVNPRMtVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ-LSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2038778719 173 DSGLDIDALKVVSKGVNAMRGE-GFGAMIITHYQRLLNYITPDVVhVMMEGRVV 225
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVA-VMDKGQIV 230
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-177 |
4.40e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 79.83 E-value: 4.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEVT-KGEVLFDGVNILELEVDERaRMGL 82
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSaSGEVLLNGRRLTALPAEQR-RIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 FlaMQYPSEIPGITNAEFLRAAMNAGkeddekISVREFITKLDEKMELLNMkEEMAERYLNEgFSGGEKKRNEILQLLML 162
Cdd:COG4136 81 L--FQDDLLFPHLSVGENLAFALPPT------IGRAQRRARVEQALEEAGL-AGFADRDPAT-LSGGQRARVALLRALLA 150
|
170
....*....|....*
gi 2038778719 163 EPTFALLDEIDSGLD 177
Cdd:COG4136 151 EPRALLLDEPFSKLD 165
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-231 |
5.58e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.32 E-value: 5.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEVtkGEVLFDGVNILELEVDERARM 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA--GNIIIDDEDISLLPLHARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 GLFLAMQYPSEIPGITNAEFLRAAMnagkEDDEKISVREFITKLDEKMELLNMkeEMAERYLNEGFSGGEKKRNEILQLL 160
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNLMAVL----QIRDDLSAEQREDRANELMEEFHI--EHLRDSMGQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038778719 161 MLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLlnyiTPDV---VHVMMEGRVVLSGGPE 231
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRE----TLAVcerAYIVSQGHLIAHGTPT 222
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-246 |
7.35e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 82.52 E-value: 7.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 14 EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDE-RARMG-------LF-- 83
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLR--FYDPTSGRILIDGVDIRDLTLESlRRQIGvvpqdtfLFsg 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 -------LAMqypseiPGITNAEFLRAAMNAGkeddekisVREFITKLDEKMEllnmkEEMAERYLNegFSGGEKKRNEI 156
Cdd:COG1132 429 tirenirYGR------PDATDEEVEEAAKAAQ--------AHEFIEALPDGYD-----TVVGERGVN--LSGGQRQRIAI 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 157 LQLLMLEPTFALLDEIDSGLD-------IDALKVVSKGVNamrgegfgAMIITHyqRL---LNYitpDVVHVMMEGRVVL 226
Cdd:COG1132 488 ARALLKDPPILILDEATSALDtetealiQEALERLMKGRT--------TIVIAH--RLstiRNA---DRILVLDDGRIVE 554
|
250 260
....*....|....*....|..
gi 2038778719 227 SGGP-ELaarLEREG-YAKLAE 246
Cdd:COG1132 555 QGTHeEL---LARGGlYARLYR 573
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-183 |
8.77e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 79.82 E-value: 8.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAI--MGNPNYEVT-KGEVLFDGVNILELEVDE--- 76
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTiTGSIVYNGHNIYSPRTDTvdl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 77 RARMGlfLAMQYPSEIPGITNAEFLRAAMNAGKEDDEkisvrefitKLDEKMEL----LNMKEEMAERYLNE--GFSGGE 150
Cdd:PRK14239 85 RKEIG--MVFQQPNPFPMSIYENVVYGLRLKGIKDKQ---------VLDEAVEKslkgASIWDEVKDRLHDSalGLSGGQ 153
|
170 180 190
....*....|....*....|....*....|....
gi 2038778719 151 KKRNEILQLLMLEPTFALLDEIDSGLD-IDALKV 183
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDpISAGKI 187
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-225 |
1.18e-17 |
|
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: 80.48 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKE----ILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG-NPNYEVTKGEVLFDGVNILELEVDER 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGlLPPPGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 78 ARM-GLFLAM--QYP--SEIPGITNAEFLRAAMNAGKeddeKISVREFITKLDEKMEL--LNMKEEMAERYLNEgFSGGE 150
Cdd:COG0444 81 RKIrGREIQMifQDPmtSLNPVMTVGDQIAEPLRIHG----GLSKAEARERAIELLERvgLPDPERRLDRYPHE-LSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 151 KKRNEILQLLMLEPTFALLDEIDSGLD-------IDALKvvskgvnAMRGE-GFGAMIITHYQRLLNYITpDVVHVMMEG 222
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDvtiqaqiLNLLK-------DLQRElGLAILFITHDLGVVAEIA-DRVAVMYAG 227
|
...
gi 2038778719 223 RVV 225
Cdd:COG0444 228 RIV 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-231 |
1.48e-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: 78.81 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 5 EIKDLHVE-IEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNpnYEVTKGEVLFDGVNILELEVDE-RARMGL 82
Cdd:cd03254 4 EFENVNFSyDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF--YDPQKGQILIDGIDIRDISRKSlRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 FLamQYPSEIPGiTNAEFLRAAMNAGKEDDEKISVRE-----FITKLDEKMEllnmkEEMAERylNEGFSGGEKKRNEIL 157
Cdd:cd03254 82 VL--QDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEagahdFIMKLPNGYD-----TVLGEN--GGNLSQGERQLLAIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038778719 158 QLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRgEGFGAMIITHyqRLLNYITPDVVHVMMEGRVVLSGGPE 231
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAH--RLSTIKNADKILVLDDGKIIEEGTHD 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-228 |
3.91e-17 |
|
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: 76.82 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEIEG------KEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEVTKGEVLFDGVNILELEV 74
Cdd:cd03213 1 GVTLSFRNLTVTVKSspsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 75 deRARMGlfLAMQYPSEIPGITNAEFLRaamnagkeddekisvreFITKLdekmellnmkeemaerylnEGFSGGEKKRN 154
Cdd:cd03213 81 --RKIIG--YVPQDDILHPTLTVRETLM-----------------FAAKL-------------------RGLSGGERKRV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038778719 155 EI-LQLLMlEPTFALLDEIDSGLD-IDALKVVSKgVNAMRGEGFGAMIITHYQRLLNYITPDVVHVMMEGRVVLSG 228
Cdd:cd03213 121 SIaLELVS-NPSLLFLDEPTSGLDsSSALQVMSL-LRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-224 |
5.19e-17 |
|
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: 77.14 E-value: 5.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVE----IEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNILELEVDER 77
Cdd:cd03255 1 IELKNLSKTygggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGldRP----TSGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 78 AR-----MG-LFlamQYPSEIPGIT---NAEFlrAAMNAGKEDDEKisvREFITKLDEKMELlnmkEEMAERYLNEgFSG 148
Cdd:cd03255 77 AAfrrrhIGfVF---QSFNLLPDLTaleNVEL--PLLLAGVPKKER---RERAEELLERVGL----GDRLNHYPSE-LSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 149 GEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVskgVNAMRG--EGFGAMII--THYQRLLNYItpDVVHVMMEGRV 224
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETGKEV---MELLRElnKEAGTTIVvvTHDPELAEYA--DRIIELRDGKI 218
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-203 |
8.70e-17 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 75.92 E-value: 8.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 14 EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNpnYEVTKGEVLFDGVnilELEVDER----ARMGLFLAMQYP 89
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGL--LRPQSGAVLIDGE---PLDYSRKglleRRQRVGLVFQDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 90 SE---IPGI-TNAEFlrAAMNAGKEDDEkisVREfitKLDEKMELLNMkEEMAERyLNEGFSGGEKKRNEILQLLMLEPT 165
Cdd:TIGR01166 78 DDqlfAADVdQDVAF--GPLNLGLSEAE---VER---RVREALTAVGA-SGLRER-PTHCLSGGEKKRVAIAGAVAMRPD 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 2038778719 166 FALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITH 203
Cdd:TIGR01166 148 VLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-206 |
8.76e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 76.68 E-value: 8.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTL--SAAIMGNPnyevTKGEVLFDGVNILELEvDERARM 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLlkIVASLISP----TSGTLLFEGEDISTLK-PEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 GLFLAMQYPSeIPGIT---NAEF---LRaamnaGKEDDEKisvrefitKLDEKMELLNMKEEMAERYLNEgFSGGEKKRN 154
Cdd:PRK10247 82 QVSYCAQTPT-LFGDTvydNLIFpwqIR-----NQQPDPA--------IFLDDLERFALPDTILTKNIAE-LSGGEKQRI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2038778719 155 EILQLLMLEPTFALLDEIDSGLDIDALKVVSKgvnamrgegfgamIITHYQR 206
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESNKHNVNE-------------IIHRYVR 185
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-244 |
1.05e-16 |
|
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: 76.50 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKE--ILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMgnPNYEVTKGEVLFDGVNILELEVDE-RARM 80
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIP--RFYDVDSGRILIDGHDVRDYTLASlRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 GL-----FLAMQYPSE-----IPGITNAEFLRAAMNAGkeddekisVREFITKLDEKMEllnmkEEMAERYLNegFSGGE 150
Cdd:cd03251 79 GLvsqdvFLFNDTVAEniaygRPGATREEVEEAARAAN--------AHEFIMELPEGYD-----TVIGERGVK--LSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 151 KKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRgEGFGAMIITHyqRLLNYITPDVVHVMMEGRVVLSGGP 230
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAH--RLSTIENADRIVVLEDGKIVERGTH 220
|
250
....*....|....*
gi 2038778719 231 ElaARLEREG-YAKL 244
Cdd:cd03251 221 E--ELLAQGGvYAKL 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-228 |
1.83e-16 |
|
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: 74.66 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKE--ILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNpnYEVTKGEVLFDGVNILELEVderarmg 81
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGD--LKPQQGEITLDGVPVSDLEK------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 82 lflamqypseipgitnaeflraamnagkeddekiSVREFITKLDEKMELLN--MKEEMAERylnegFSGGEKKRNEILQL 159
Cdd:cd03247 72 ----------------------------------ALSSLISVLNQRPYLFDttLRNNLGRR-----FSGGERQRLALARI 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 160 LMLEPTFALLDEIDSGLD-IDALKVVSKGVNAMRGEGFgaMIITHYQRLLNYItpDVVHVMMEGRVVLSG 228
Cdd:cd03247 113 LLQDAPIVLLDEPTVGLDpITERQLLSLIFEVLKDKTL--IWITHHLTGIEHM--DKILFLENGKIIMQG 178
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-203 |
1.91e-16 |
|
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: 78.17 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEG-KEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNpnYEVTKGEVLFDGVNILELEVDERARMGL 82
Cdd:TIGR02868 335 LELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL--LDPLQGEVTLDGVPVSSLDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 FLAMQ---YPSEI--------PGITNAEFLRAAMNAGKEDDekisVREFITKLDEKMEllnmkeEMAERylnegFSGGEK 151
Cdd:TIGR02868 413 VCAQDahlFDTTVrenlrlarPDATDEELWAALERVGLADW----LRALPDGLDTVLG------EGGAR-----LSGGER 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2038778719 152 KRNEILQLLMLEPTFALLDEIDSGLDID-ALKVVSKGVNAMrgEGFGAMIITH 203
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAEtADELLEDLLAAL--SGRTVVLITH 528
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-177 |
2.42e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.10 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTL----SAAIMGNPNYEVtKGEVLFDGVNILELEVDE 76
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLlrvfNRLIELYPEARV-SGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 77 -RARMGLFLamQYPSEIPGITNAEFLRAAMNAGKEDDEKisvREFITKLDEKMELLNMKEEMAERyLNE---GFSGGEKK 152
Cdd:PRK14247 80 lRRRVQMVF--QIPNPIPNLSIFENVALGLKLNRLVKSK---KELQERVRWALEKAQLWDEVKDR-LDApagKLSGGQQQ 153
|
170 180
....*....|....*....|....*
gi 2038778719 153 RNEILQLLMLEPTFALLDEIDSGLD 177
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLD 178
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-203 |
3.00e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.51 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 17 EILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLFDGVNILELEVDERA-RMGLFLAMQYPSEIPGI 95
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI--NKLEEITSGDLIVDGLKVNDPKVDERLiRQEAGMVFQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 96 T---NAEF-LRAAMNAGKEDDEKISvREFITKLDekmellnmKEEMAERYLNEgFSGGEKKRNEILQLLMLEPTFALLDE 171
Cdd:PRK09493 93 TaleNVMFgPLRVRGASKEEAEKQA-RELLAKVG--------LAERAHHYPSE-LSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190
....*....|....*....|....*....|..
gi 2038778719 172 IDSGLDIDALKVVSKGVNAMRGEGFGAMIITH 203
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-223 |
7.82e-16 |
|
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: 72.99 E-value: 7.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELE---VDERARM 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG--LEEPDSGSILIDGEDLTDLEdelPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 GlfLAMQYPSEIPGITnaeflraamnagkeddekisVREFITkldekmellnmkeemaerylnEGFSGGEKKRNEILQLL 160
Cdd:cd03229 79 G--MVFQDFALFPHLT--------------------VLENIA---------------------LGLSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038778719 161 MLEPTFALLDEIDSGLD----IDALKVVSKgVNAMrgEGFGAMIITHYQRLLNYITPDVVhVMMEGR 223
Cdd:cd03229 116 AMDPDVLLLDEPTSALDpitrREVRALLKS-LQAQ--LGITVVLVTHDLDEAARLADRVV-VLRDGK 178
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-231 |
8.49e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 74.73 E-value: 8.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEI-EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLsaAIMGNPNYEVTKGEVLFDGVnilELEVDER---- 77
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTL--FLHFNGILKPTSGEVLIKGE---PIKYDKKslle 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 78 ARMGLFLAMQYP-SEIPGITNAEFLR-AAMNAGkeddekISVREFITKLDEKMELLNMkeEMAERYLNEGFSGGEKKRNE 155
Cdd:PRK13639 76 VRKTVGIVFQNPdDQLFAPTVEEDVAfGPLNLG------LSKEEVEKRVKEALKAVGM--EGFENKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038778719 156 ILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNyITPDVVHVMMEGRVVLSGGPE 231
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVP-VYADKVYVMSDGKIIKEGTPK 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-231 |
3.80e-15 |
|
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: 72.02 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAaiMGNPNYEVTKGEVLFDGVNILELEVDERARMGlf 83
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIK--MLTTLLKPTSGRATVAGHDVVREPREVRRRIG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LAMQYPSEIPGITNAEFLraAMNAGKEDDEKISVREFITKLDEKMELLNMKEEMAERYlnegfSGGEKKRNEILQLLMLE 163
Cdd:cd03265 77 IVFQDLSVDDELTGWENL--YIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTY-----SGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038778719 164 PTFALLDEIDSGLDIDALKVVSKGVNAM-RGEGFGAMIITHYQRLLNYITpDVVHVMMEGRVVLSGGPE 231
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLC-DRVAIIDHGRIIAEGTPE 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-203 |
3.92e-15 |
|
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: 71.79 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLFDGVNILELEVD---ERARM 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI--NLLEEPDSGTIIIDGLKLTDDKKNineLRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 G-------LFLAMqypSEIPGITNAefLRAAMNAGKEDDEKISvREFITK--LDEKmellnmkeemAERYLNEgFSGGEK 151
Cdd:cd03262 79 GmvfqqfnLFPHL---TVLENITLA--PIKVKGMSKAEAEERA-LELLEKvgLADK----------ADAYPAQ-LSGGQQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2038778719 152 KRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITH 203
Cdd:cd03262 142 QRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-218 |
4.15e-15 |
|
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: 70.17 E-value: 4.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVlfdgvnilelEVDERARMGLF 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG--ELEPDEGIV----------TWGSTVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 lamqypseipgitnaeflraamnagkeddekisvrefitkldekmellnmkeemaerylnEGFSGGEKKRNEILQLLMLE 163
Cdd:cd03221 69 ------------------------------------------------------------EQLSGGEKMRLALAKLLLEN 88
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2038778719 164 PTFALLDEIDSGLDIDALKVVSKGVNAMRGegfGAMIITHYQRLLNYITPDVVHV 218
Cdd:cd03221 89 PNLLLLDEPTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIEL 140
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-234 |
7.04e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.54 E-value: 7.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 16 KEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG-NPNYEVTKGEVLFDGVNIlelEVDERARMGLFLaMQYPSEIPG 94
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrSPKGVKGSGSVLLNGMPI---DAKEMRAISAYV-QQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 95 ITNAEFLR-AAMNAGKEDDEKISVREFITKLDEKMELLN-MKEEMAERYLNEGFSGGEKKRNEILQLLMLEPTFALLDEI 172
Cdd:TIGR00955 114 LTVREHLMfQAHLRMPRRVTKKEKRERVDEVLQALGLRKcANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038778719 173 DSGLD-IDALKVVS--KGVnAMRGEgfgAMIITHYQ------RLLNYITpdvvhVMMEGRVVLSGGPELAA 234
Cdd:TIGR00955 194 TSGLDsFMAYSVVQvlKGL-AQKGK---TIICTIHQpsselfELFDKII-----LMAEGRVAYLGSPDQAV 255
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-230 |
8.21e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.19 E-value: 8.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEI-EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLFDGVNIlelevdERARMG 81
Cdd:PRK13636 5 ILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNL--NGILKPSSGRILFDGKPI------DYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 82 LF-----LAMQYPSEIPGITNAEFLR----AAMNAGKEDDEkisVREFITKLDEKMELLNMKEEMaerylNEGFSGGEKK 152
Cdd:PRK13636 77 LMklresVGMVFQDPDNQLFSASVYQdvsfGAVNLKLPEDE---VRKRVDNALKRTGIEHLKDKP-----THCLSFGQKK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038778719 153 RNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGE-GFGAMIITHYQRLLNyITPDVVHVMMEGRVVLSGGP 230
Cdd:PRK13636 149 RVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVP-LYCDNVFVMKEGRVILQGNP 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-82 |
1.10e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 71.61 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 2 SVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgN------PNYEVTkGEVLFDGVNILELEVD 75
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL--NrmndliPGARVE-GEILLDGEDIYDPDVD 86
|
90
....*....|
gi 2038778719 76 ---ERARMGL 82
Cdd:COG1117 87 vveLRRRVGM 96
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-228 |
1.22e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.78 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPNyevtKGEVLFDGVNILELEVDERARM 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGivPPD----SGTLEIGGNPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 GLFLAMQYPSEIPGITNAEFLRAAMNAGKEDDEKIS--VREFITKLDekmelLNMKE---EMAERYLnegfsggekkrNE 155
Cdd:PRK15439 87 GIYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKqlLAALGCQLD-----LDSSAgslEVADRQI-----------VE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038778719 156 ILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITpDVVHVMMEGRVVLSG 228
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLA-DRISVMRDGTIALSG 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-225 |
1.44e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.79 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFdGVNIlelevderaRMGl 82
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG--ELEPDSGTVKL-GETV---------KIG- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 FLAmQYPSEI-PGITNAEFLRAAMNAGKEddekISVREFitkldekMELLNMKEEMAERYLnEGFSGGEKKRNEILQLLM 161
Cdd:COG0488 382 YFD-QHQEELdPDKTVLDELRDGAPGGTE----QEVRGY-------LGRFLFSGDDAFKPV-GVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038778719 162 LEPTFALLDEIDSGLDIDALKVVskgVNAMrgEGF-GAMI-ITHYQRLLNYITPDVVHVmMEGRVV 225
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEAL---EEAL--DDFpGTVLlVSHDRYFLDRVATRILEF-EDGGVR 508
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-256 |
1.88e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 6 IKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNpnYEVTKGEVlfdgvnilelEVDERARMGlFLA 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGE--LEPDSGEV----------SIPKGLRIG-YLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 86 mQYPSEIPGIT---------------NAEFLRAAMNAGKEDDEKISVREFITKLDEK------------MELLNMKEEMA 138
Cdd:COG0488 68 -QEPPLDDDLTvldtvldgdaelralEAELEELEAKLAEPDEDLERLAELQEEFEALggweaearaeeiLSGLGFPEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 139 ERYLNEgFSGGEKKRNEILQLLMLEPTFALLDEIDSGLDIDA---LkvvskgvnamrgEGF-----GAMI-ITHYQRLLN 209
Cdd:COG0488 147 DRPVSE-LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewL------------EEFlknypGTVLvVSHDRYFLD 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2038778719 210 yitpDVVHVMME---GRVVLSGGP--------ELAARLEREGYAKLAEELgydyKEEL 256
Cdd:COG0488 214 ----RVATRILEldrGKLTLYPGNysayleqrAERLEQEAAAYAKQQKKI----AKEE 263
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-153 |
2.12e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.50 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 5 EIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAI---MgnpnyEVTKGEVLFDGVNILELEVDERARMg 81
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIsrlL-----PPDSGEVLVDGLDVATTPSRELAKR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 82 lfLAM--QYPSEIPGITNAE---FLRAAMNAG---KEDDEKIsvrefitklDEKMELLNMkEEMAERYLNEgFSGGEKKR 153
Cdd:COG4604 77 --LAIlrQENHINSRLTVRElvaFGRFPYSKGrltAEDREII---------DEAIAYLDL-EDLADRYLDE-LSGGQRQR 143
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
16-254 |
3.63e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 70.02 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 16 KEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDE-RARMGLFLamQYP-SEIP 93
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTG--LLKPQSGEIKIDGITISKENLKEiRKKIGIIF--QNPdNQFI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 94 GITnaeflraamnagKEDD-------EKISVREFITKLDEKMELLNMKEEMAERYLNegFSGGEKKRNEILQLLMLEPTF 166
Cdd:PRK13632 98 GAT------------VEDDiafglenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQN--LSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 167 ALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMI-ITHyqRLLNYITPDVVHVMMEGRVVLSGGPE---------LAARL 236
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIsITH--DMDEAILADKVIVFSEGKLIAQGKPKeilnnkeilEKAKI 241
|
250 260
....*....|....*....|...
gi 2038778719 237 EREGYAKLAEELG-----YDYKE 254
Cdd:PRK13632 242 DSPFIYKLSKKLKgidptYNEEE 264
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-228 |
4.50e-14 |
|
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: 69.44 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 14 EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDE-RARMGLFL-------- 84
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQR--FYVPENGRVLVDGHDLALADPAWlRRQVGVVLqenvlfnr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 85 --AMQYPSEIPGITNAEFLRAAMNAGKEDdekisvreFITKLDEKMELLnmkeeMAERylNEGFSGGEKKRNEILQLLML 162
Cdd:cd03252 91 siRDNIALADPGMSMERVIEAAKLAGAHD--------FISELPEGYDTI-----VGEQ--GAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038778719 163 EPTFALLDEIDSGLDIDALKVVSKGVNAMrGEGFGAMIITHyqRLLNYITPDVVHVMMEGRVVLSG 228
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDI-CAGRTVIIIAH--RLSTVKNADRIIVMEKGRIVEQG 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
4.58e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 70.22 E-value: 4.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDL-HVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLFDGVNILELEVDErAR 79
Cdd:PRK13652 1 MHLIETRDLcYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHF--NGILKPTSGSVLIRGEPITKENIRE-VR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 80 MGLFLAMQYPSEIPGITNAE--FLRAAMNAGKeDDEKISVRefitkLDEKMELLNMkEEMAERYLNEgFSGGEKKRNEIL 157
Cdd:PRK13652 78 KFVGLVFQNPDDQIFSPTVEqdIAFGPINLGL-DEETVAHR-----VSSALHMLGL-EELRDRVPHH-LSGGEKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038778719 158 QLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGE-GFGAMIITHYQRLLNYITpDVVHVMMEGRVVLSGGPE 231
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMA-DYIYVMDKGRIVAYGTVE 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-231 |
8.15e-14 |
|
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: 68.52 E-value: 8.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLhvEIEGKEI-LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERarmGL 82
Cdd:cd03299 1 LKVENL--SKDWKEFkLKNVSLEVERGDYFVILGPTGSGKSVLLETIAG--FIKPDSGKILLNGKDITNLPPEKR---DI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 FLAMQYPSEIPGIT---NAEF-LRAAMNAGKEDDEKisVREfITKLDEKMELLNMKEEMaerylnegFSGGEKKRNEILQ 158
Cdd:cd03299 74 SYVPQNYALFPHMTvykNIAYgLKKRKVDKKEIERK--VLE-IAEMLGIDHLLNRKPET--------LSGGEQQRVAIAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038778719 159 LLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGE-GFGAMIITHYQ---RLLNyitpDVVHVMMEGRVVLSGGPE 231
Cdd:cd03299 143 ALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFeeaWALA----DKVAIMLNGKLIQVGKPE 215
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-225 |
1.61e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.96 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDL--HVEIEGK--------EILK---GVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNI 69
Cdd:PRK15079 8 LLEVADLkvHFDIKDGkqwfwqppKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIG--LVKATDGEVAWLGKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 70 LELEVDER--ARMGLFLAMQYP--SEIPGITN----AEFLRAAMNAGKEDDEKISVREFITKLDEKMELLNmkeemaeRY 141
Cdd:PRK15079 86 LGMKDDEWraVRSDIQMIFQDPlaSLNPRMTIgeiiAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLIN-------RY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 142 LNEgFSGGEKKRNEILQLLMLEPTFALLDEIDSGLD--IDAlKVVSKGVNAMRGEGFGAMIITHYQRLLNYITpDVVHVM 219
Cdd:PRK15079 159 PHE-FSGGQCQRIGIARALILEPKLIICDEPVSALDvsIQA-QVVNLLQQLQREMGLSLIFIAHDLAVVKHIS-DRVLVM 235
|
....*.
gi 2038778719 220 MEGRVV 225
Cdd:PRK15079 236 YLGHAV 241
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-230 |
1.71e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.54 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVlEIKDL-HVEIEG----KEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLFDGVNILELEV- 74
Cdd:PRK13637 1 MSI-KIENLtHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHL--NGLLKPTSGKIIIDGVDITDKKVk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 75 --DERARMGlfLAMQYPS----EIPGITNAEFlrAAMNAGKEDDEkISVRefitkLDEKMELLNMK-EEMAERYLNEgFS 147
Cdd:PRK13637 78 lsDIRKKVG--LVFQYPEyqlfEETIEKDIAF--GPINLGLSEEE-IENR-----VKRAMNIVGLDyEDYKDKSPFE-LS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 148 GGEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEgFGAMIIthyqrLLNYITPDV------VHVMME 221
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKE-YNMTII-----LVSHSMEDVakladrIIVMNK 220
|
....*....
gi 2038778719 222 GRVVLSGGP 230
Cdd:PRK13637 221 GKCELQGTP 229
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-228 |
1.85e-13 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 69.30 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 16 KEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYevTKGEVLFDGVNILELEVDERARMGLFLamqyPSEI--- 92
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP--TSGSVRLDGADLKQWDRETFGKHIGYL----PQDVelf 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 93 PGITNAEFLRAAMNAgkeDDEKI-------SVREFITKLDEKMEllnmkEEMAERylNEGFSGGEKKRNEILQLLMLEPT 165
Cdd:TIGR01842 405 PGTVAENIARFGENA---DPEKIieaaklaGVHELILRLPDGYD-----TVIGPG--GATLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038778719 166 FALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYItpDVVHVMMEGRVVLSG 228
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCV--DKILVLQDGRIARFG 535
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-228 |
1.89e-13 |
|
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: 69.33 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGK-----------EILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG-NPnyevTKGEVLFDGVNIL 70
Cdd:COG4172 275 LLEARDLKVWFPIKrglfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRlIP----SEGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 71 ELevDERARMGLFLAMQ------YPS--------EIpgItnAEFLRAamnagkeDDEKISVREFITKLDEKMELLNMKEE 136
Cdd:COG4172 351 GL--SRRALRPLRRRMQvvfqdpFGSlsprmtvgQI--I--AEGLRV-------HGPGLSAAERRARVAEALEEVGLDPA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 137 MAERYLNEgFSGGEKKRNEILQLLMLEPTFALLDEIDSGLD-------IDALKvvskgvNAMRGEGFGAMIITHYQRLLN 209
Cdd:COG4172 418 ARHRYPHE-FSGGQRQRIAIARALILEPKLLVLDEPTSALDvsvqaqiLDLLR------DLQREHGLAYLFISHDLAVVR 490
|
250
....*....|....*....
gi 2038778719 210 YITPDVVhVMMEGRVVLSG 228
Cdd:COG4172 491 ALAHRVM-VMKDGKVVEQG 508
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-180 |
2.02e-13 |
|
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: 67.74 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 10 HVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNILELEVDERARMGLFLAM- 86
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGllQP----TSGEVRVAGLVPWKRRKKFLRRIGVVFGQk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 87 -QYPSEIPGITNAEFLRAAMNagkeddekISVREFITKLDEKMELLNMKEEMAE--RYLnegfSGGEKKRNEILQLLMLE 163
Cdd:cd03267 104 tQLWWDLPVIDSFYLLAAIYD--------LPPARFKKRLDELSELLDLEELLDTpvRQL----SLGQRMRAEIAAALLHE 171
|
170
....*....|....*..
gi 2038778719 164 PTFALLDEIDSGLDIDA 180
Cdd:cd03267 172 PEILFLDEPTIGLDVVA 188
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-225 |
2.13e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 67.38 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 2 SVLEIKDLH----VEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLsAAIMG---NPnyevTKGEVLFDGVNILELEV 74
Cdd:COG1136 3 PLLELRNLTksygTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTL-LNILGgldRP----TSGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 75 DERARM-----GL-FlamQYPSEIPGIT---NAEFlrAAMNAGkeddekISVREFITKLDEKMELLNMkEEMAERYLNEg 145
Cdd:COG1136 78 RELARLrrrhiGFvF---QFFNLLPELTaleNVAL--PLLLAG------VSRKERRERARELLERVGL-GDRLDHRPSQ- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 146 FSGGEKKRNEILQLLMLEPTFALLDEIDSGLD-------IDALKvvskgvNAMRGEGFGAMIITHYQRLLNYItpDVVHV 218
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDsktgeevLELLR------ELNRELGTTIVMVTHDPELAARA--DRVIR 216
|
....*..
gi 2038778719 219 MMEGRVV 225
Cdd:COG1136 217 LRDGRIV 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-228 |
2.30e-13 |
|
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: 67.01 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERARMGLFLAMQ--YPsEIPGIT 96
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAG--LLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTglYD-RLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 97 NAEFLrAAMNAGKEDdekisvrEFITKLDEKMELLNMKEEMAERylNEGFSGGEKKRNEILQLLMLEPTFALLDEIDSGL 176
Cdd:cd03266 98 NLEYF-AGLYGLKGD-------ELTARLEELADRLGMEELLDRR--VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2038778719 177 DIDALKVVSKGVNAMRGEG----FGAMIITHYQRLLnyitpDVVHVMMEGRVVLSG 228
Cdd:cd03266 168 DVMATRALREFIRQLRALGkcilFSTHIMQEVERLC-----DRVVVLHRGRVVYEG 218
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-203 |
2.45e-13 |
|
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: 69.24 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 2 SVLEIKDLHVEIEGK-EILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNpnYEVTKGEVLFDGVNILELEVDERaRM 80
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF--VDPTEGSIAVNGVPLADADADSW-RD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 GLFLAMQYPSEIPGiTNAEFLRAAMNAGKEDDekisVREFITKLDeKMELLNMKEEMAERYLNE---GFSGGEKKRNEIL 157
Cdd:TIGR02857 397 QIAWVPQHPFLFAG-TIAENIRLARPDASDAE----IREALERAG-LDEFVAALPQGLDTPIGEggaGLSGGQAQRLALA 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2038778719 158 QLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRgEGFGAMIITH 203
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTH 515
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-228 |
2.63e-13 |
|
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: 67.22 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGK----EILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNILELEVDE 76
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGleRP----TSGSVLVDGTDLTLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 77 ----RARMGL-------------FLAMQYPSEIPGITNAEFLRaamnagkeddekisvrefitKLDEKMELLNMkEEMAE 139
Cdd:cd03258 77 lrkaRRRIGMifqhfnllssrtvFENVALPLEIAGVPKAEIEE--------------------RVLELLELVGL-EDKAD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 140 RYLNEgFSGGEKKRNEILQLLMLEPTFALLDEIDSGLD------IDALkvvSKGVNAMRgeGFGAMIITHYQRLLNYITp 213
Cdd:cd03258 136 AYPAQ-LSGGQKQRVGIARALANNPKVLLCDEATSALDpettqsILAL---LRDINREL--GLTIVLITHEMEVVKRIC- 208
|
250
....*....|....*
gi 2038778719 214 DVVHVMMEGRVVLSG 228
Cdd:cd03258 209 DRVAVMEKGEVVEEG 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-224 |
2.85e-13 |
|
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: 66.09 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKE--ILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERARMG 81
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILG--LLRPTSGRVRLDGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 82 LFLaMQypseipgitnaeflraamnagkeDDE--KISVREFItkldekmellnmkeemaerylnegFSGGEKKRNEILQL 159
Cdd:cd03246 79 GYL-PQ-----------------------DDElfSGSIAENI------------------------LSGGQRQRLGLARA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038778719 160 LMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNyiTPDVVHVMMEGRV 224
Cdd:cd03246 111 LYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLA--SADRILVLEDGRV 173
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-177 |
3.12e-13 |
|
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: 66.73 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHV----EIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNIleleVDER 77
Cdd:cd03293 1 LEVRNVSKtyggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGleRP----TSGEVLVDGEPV----TGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 78 ARMGLFLamQYPSEIPGIT---NAEF-LRAAMNAGKEDDEKisVREFItkldEKMELlnmkEEMAERYLNEgFSGGEKKR 153
Cdd:cd03293 73 PDRGYVF--QQDALLPWLTvldNVALgLELQGVPKAEARER--AEELL----ELVGL----SGFENAYPHQ-LSGGMRQR 139
|
170 180
....*....|....*....|....
gi 2038778719 154 NEILQLLMLEPTFALLDEIDSGLD 177
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALD 163
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
8-228 |
3.33e-13 |
|
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: 66.55 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 8 DLHVEIEGKeiLKGVNLTLKT---GEIAAIMGPNGTGKSTLSAAIMG--NPN--YEVTKGEVLFDGVNILELEVDERaRM 80
Cdd:cd03297 1 MLCVDIEKR--LPDFTLKIDFdlnEEVTGIFGASGAGKSTLLRCIAGleKPDggTIVLNGTVLFDSRKKINLPPQQR-KI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 GlFLAMQYpSEIPGITNAEFLRAAMNAGKEDDEKISVREFItkldekmELLNMkEEMAERYLNEgFSGGEKKRNEILQLL 160
Cdd:cd03297 78 G-LVFQQY-ALFPHLNVRENLAFGLKRKRNREDRISVDELL-------DLLGL-DHLLNRYPAQ-LSGGEKQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038778719 161 MLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGE-GFGAMIITHYQRLLNYITPDVVhVMMEGRVVLSG 228
Cdd:cd03297 147 AAQPELLLLDEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIV-VMEDGRLQYIG 214
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
19-236 |
3.85e-13 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 67.80 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNILELEVDERARMGLflAMQYPSEIPGIT 96
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTllRP----TSGTARVAGYDVVREPRKVRRSIGI--VPQYASVDEDLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 97 NAEFLRaaMNAGKEDDEKISVREfitKLDEKMELLNMKEEmAERYLnEGFSGGEKKRNEILQLLMLEPTFALLDEIDSGL 176
Cdd:TIGR01188 83 GRENLE--MMGRLYGLPKDEAEE---RAEELLELFELGEA-ADRPV-GTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038778719 177 DIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITpDVVHVMMEGRVVLSGGP-ELAARL 236
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLC-DRIAIIDHGRIIAEGTPeELKRRL 215
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-90 |
4.27e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 67.62 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEIEGKE----ILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPNYEVTKGEVLFDGVNILELEV 74
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQgrvkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGitKDNWHVTADRFRWNGIDLLKLSP 80
|
90
....*....|....*....
gi 2038778719 75 DERAR-MGLFLAM--QYPS 90
Cdd:COG4170 81 RERRKiIGREIAMifQEPS 99
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-225 |
6.08e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.63 E-value: 6.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDL-----HVEIEGK----EILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNI 69
Cdd:PRK10419 1 MTLLNVSGLshhyaHGGLSGKhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGleSP----SQGNVSWRGEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 70 LELEvdeRARMGLF-----LAMQYPseiPGITN---------AEFLRAAMNAGKEDDEKisvrefitKLDEKMELLNMKE 135
Cdd:PRK10419 77 AKLN---RAQRKAFrrdiqMVFQDS---ISAVNprktvreiiREPLRHLLSLDKAERLA--------RASEMLRAVDLDD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 136 EMAERyLNEGFSGGEKKRNEILQLLMLEPTFALLDEIDSGLD-------IDALKvvskgvnAMRGE-GFGAMIITHYQRL 207
Cdd:PRK10419 143 SVLDK-RPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlqagvIRLLK-------KLQQQfGTACLFITHDLRL 214
|
250
....*....|....*...
gi 2038778719 208 LNYITPDVVhVMMEGRVV 225
Cdd:PRK10419 215 VERFCQRVM-VMDNGQIV 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-231 |
7.87e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.17 E-value: 7.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNILELEVDERA 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGtlTP----TAGTVLVAGDDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 79 RmglflamQYPSeIPGITNAEF---LRAAMNAGK-----------EDDEkisvrefiTKLDEKMELLNMkEEMAERYLNE 144
Cdd:PRK09536 77 R-------RVAS-VPQDTSLSFefdVRQVVEMGRtphrsrfdtwtETDR--------AAVERAMERTGV-AQFADRPVTS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 145 gFSGGEKKRNEILQLLMLEPTFALLDEIDSGLDID----ALKVVSKGVNamrgEGFGAMIITHYQRL-LNYItpDVVHVM 219
Cdd:PRK09536 140 -LSGGERQRVLLARALAQATPVLLLDEPTASLDINhqvrTLELVRRLVD----DGKTAVAAIHDLDLaARYC--DELVLL 212
|
250
....*....|..
gi 2038778719 220 MEGRVVLSGGPE 231
Cdd:PRK09536 213 ADGRVRAAGPPA 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-216 |
8.07e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.75 E-value: 8.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 16 KEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEVTKGEVLFDGVNIlelevderarmglflamqyPSEIPGI 95
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQF-------------------GREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 96 TNAeflraamnaGKEDDekisvrefitkLDEKMELLNMKEemaeryLNEGF---------SGGEKKRNEILQLLMLEPTF 166
Cdd:COG2401 104 DAI---------GRKGD-----------FKDAVELLNAVG------LSDAVlwlrrfkelSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2038778719 167 ALLDEIDSGLDIDALKVVSKGV-NAMRGEGFGAMIITHYQRLLNYITPDVV 216
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLqKLARRAGITLVVATHHYDVIDDLQPDLL 208
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-244 |
8.84e-13 |
|
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: 67.43 E-value: 8.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 15 GKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgnPN-YEVTKGEVLFDGVNILELEVDE-RARMGL---------- 82
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLI---PRfYEPDSGQILLDGHDLADYTLASlRRQVALvsqdvvlfnd 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 --FLAMQYpSEIPGITNAEFLRAAMNAgkeddekiSVREFITKLDEKMEllnmkEEMAERYLNegFSGGEKKRNEILQLL 160
Cdd:TIGR02203 421 tiANNIAY-GRTEQADRAEIERALAAA--------YAQDFVDKLPLGLD-----TPIGENGVL--LSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 161 MLEPTFALLDEIDSGLDIDALKVVSKGVNAMRgEGFGAMIITHyqRLLNYITPDVVHVMMEGRVVLSGG-PELaarLERE 239
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLM-QGRTTLVIAH--RLSTIEKADRIVVMDDGRIVERGThNEL---LARN 558
|
....*.
gi 2038778719 240 G-YAKL 244
Cdd:TIGR02203 559 GlYAQL 564
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-228 |
9.35e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 67.44 E-value: 9.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 16 KEILKGVNLTLKTGEIAAIMGPNGTGKSTLsAAIMGNpNYEVTKGEVLFDGVNILELE---------------------V 74
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTV-AALLQN-LYQPTGGQVLLDGVPLVQYDhhylhrqvalvgqepvlfsgsV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 75 DERARMGLflaMQYPSEipgitnaEFLRAAMNAGKEDDEKISVREFITKLDEKMELLnmkeemaerylnegfSGGEKKRN 154
Cdd:TIGR00958 572 RENIAYGL---TDTPDE-------EIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQL---------------SGGQKQRI 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038778719 155 EILQLLMLEPTFALLDEIDSGLDIDALKVVSkgvNAMRGEGFGAMIITHyqRLLNYITPDVVHVMMEGRVVLSG 228
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDAECEQLLQ---ESRSRASRTVLLIAH--RLSTVERADQILVLKKGSVVEMG 695
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-249 |
1.09e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.18 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPNyevtKGEVLFDGVnilELEVDERA-- 78
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGllRPQ----KGAVLWQGK---PLDYSKRGll 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 79 --RMGLFLAMQYPSEIPGITN--AEFLRAAMNAGKEDDEkISVRefitkLDEKMELLNmkeemAERYLNEG---FSGGEK 151
Cdd:PRK13638 74 alRQQVATVFQDPEQQIFYTDidSDIAFSLRNLGVPEAE-ITRR-----VDEALTLVD-----AQHFRHQPiqcLSHGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 152 KRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLnYITPDVVHVMMEGRVVLSGGP- 230
Cdd:PRK13638 143 KRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLI-YEISDAVYVLRQGQILTHGAPg 221
|
250 260
....*....|....*....|....*..
gi 2038778719 231 ELAAR---LEREGYA-----KLAEELG 249
Cdd:PRK13638 222 EVFACteaMEQAGLTqpwlvKLHTQLG 248
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-231 |
1.11e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.16 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 14 EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPNyevtKGEVLFDGVNILELEVDERARMGLFLAMQYP-S 90
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGllRPQ----KGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPeT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 91 EIPGITNAEFLraAMNAGKEDDEKISVREFItkldeKMELLNMKEEMAERYLNEGFSGGEKKRNEILQLLMLEPTFALLD 170
Cdd:PRK13644 89 QFVGRTVEEDL--AFGPENLCLPPIEIRKRV-----DRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038778719 171 EIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNyiTPDVVHVMMEGRVVLSGGPE 231
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELH--DADRIIVMDRGKIVLEGEPE 220
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-228 |
1.37e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 64.59 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 15 GKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGN-PNYEVTKGEVLFDGVNILElevderarmglfLAMQYPSEIp 93
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtEGNVSVEGDIHYNGIPYKE------------FAEKYPGEI- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 94 gitnaeflraAMNAgkEDDEKIS---VRE---FITKLDekmellnmkeemAERYLnEGFSGGEKKRNEILQLLMLEPTFA 167
Cdd:cd03233 86 ----------IYVS--EEDVHFPtltVREtldFALRCK------------GNEFV-RGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038778719 168 LLDEIDSGLD----IDALKVVSKGVNAMRgegfGAMIITHYQ---RLlnYITPDVVHVMMEGRVVLSG 228
Cdd:cd03233 141 CWDNSTRGLDsstaLEILKCIRTMADVLK----TTTFVSLYQasdEI--YDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-177 |
1.69e-12 |
|
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: 64.95 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPnyEVTKGEVLFDGVNILELEVDERARMGLF 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFE--TPTSGEILLDGKDITNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 lamQYPSEIPGIT---NAEF-LRAAmnagkeddeKISVREFITKLDEKMELLNMkEEMAERYLNEgFSGGEKKRNEILQL 159
Cdd:cd03300 79 ---QNYALFPHLTvfeNIAFgLRLK---------KLPKAEIKERVAEALDLVQL-EGYANRKPSQ-LSGGQQQRVAIARA 144
|
170
....*....|....*...
gi 2038778719 160 LMLEPTFALLDEIDSGLD 177
Cdd:cd03300 145 LVNEPKVLLLDEPLGALD 162
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
12-230 |
1.85e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.49 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 12 EIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLFDGVNILELE--VDERARMGlfLAMQYP 89
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHM--NALLIPSEGKVYVDGLDTSDEEnlWDIRNKAG--MVFQNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 90 SE--IPGITNAEFLRAAMNAGKEDDEkisVREfitKLDEKMELLNMKEemAERYLNEGFSGGEKKRNEILQLLMLEPTFA 167
Cdd:PRK13633 95 DNqiVATIVEEDVAFGPENLGIPPEE---IRE---RVDESLKKVGMYE--YRRHAPHLLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038778719 168 LLDEIDSGLDIDALKVVSKGVNAMRGE-GFGAMIITHYQRllNYITPDVVHVMMEGRVVLSGGP 230
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYME--EAVEADRIIVMDSGKVVMEGTP 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-224 |
2.11e-12 |
|
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: 64.80 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 18 ILKGVNLTLKTGEIAAIMGPNGTGKSTLsAAIMGNpNYEVTKGEVLFDGVNILELEvDERARMGLFLAMQYP-------- 89
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTV-VALLEN-FYQPQGGQVLLDGKPISQYE-HKYLHSKVSLVGQEPvlfarslq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 90 SEIP-GITNAEFLR---AAMNAGKEDDEKISVREFITKLDEKMELLnmkeemaerylnegfSGGEKKRNEILQLLMLEPT 165
Cdd:cd03248 106 DNIAyGLQSCSFECvkeAAQKAHAHSFISELASGYDTEVGEKGSQL---------------SGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038778719 166 FALLDEIDSGLDIDALKVVSKgvnAMRG--EGFGAMIITHyqRLLNYITPDVVHVMMEGRV 224
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQ---ALYDwpERRTVLVIAH--RLSTVERADQILVLDGGRI 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-231 |
4.98e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.88 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAI--MGNPnyevTKGEVLFDGVNILELEVDERARMG 81
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFarLLTP----QSGTVFLGDKPISMLSSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 82 LFLAMQYPSeiP-GITNAEFL---RAAMNA--GK--EDDEKIsvrefITKLDEKMELlnmkEEMAERYLNEgFSGGEKKR 153
Cdd:PRK11231 79 ALLPQHHLT--PeGITVRELVaygRSPWLSlwGRlsAEDNAR-----VNQAMEQTRI----NHLADRRLTD-LSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 154 NEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYqrlLN----YItpDVVHVMMEGRVVLSGG 229
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHD---LNqasrYC--DHLVVLANGHVMAQGT 221
|
..
gi 2038778719 230 PE 231
Cdd:PRK11231 222 PE 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-225 |
9.06e-12 |
|
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: 62.66 E-value: 9.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERarmGLF 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAG--LEEPTSGRIYIGGRDVTDLPPKDR---DIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LAMQYPSEIPGITNAEFLRAAMNAGKEDDEKISVRefitkLDEKMELLNMkEEMAERYLNEgFSGGEKKRNEILQLLMLE 163
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDER-----VREVAELLQI-EHLLDRKPKQ-LSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038778719 164 PTFALLDEIDSGLDIdALKVvskgvnAMRGEgfgamiITHYQRLLN----YITPDVVHVM-MEGRVV 225
Cdd:cd03301 149 PKVFLMDEPLSNLDA-KLRV------QMRAE------LKRLQQRLGtttiYVTHDQVEAMtMADRIA 202
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-177 |
9.73e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 63.32 E-value: 9.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAA----IMGNPNYEVtKGEVLFDGVNILELEVDE 76
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrlLELNEEARV-EGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 77 -RARMGLFLAMQYPSEIPGITNAEFLRAAMNAGKEDDEKisvrefiTKLDEKMELLNMK----EEMAERyLNE---GFSG 148
Cdd:PRK14267 81 iEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSK-------KELDERVEWALKKaalwDEVKDR-LNDypsNLSG 152
|
170 180
....*....|....*....|....*....
gi 2038778719 149 GEKKRNEILQLLMLEPTFALLDEIDSGLD 177
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANID 181
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-242 |
1.04e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.52 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 6 IKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEVTKGEVLFDGVNILELEVderARMGlFLA 85
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQIL---KRTG-FVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 86 mQYPSEIPGITNAE------FLRAAMNAGKedDEKISVREFITkldEKMELLNMKEEMAERYLNEGFSGGEKKRNEILQL 159
Cdd:PLN03211 147 -QDDILYPHLTVREtlvfcsLLRLPKSLTK--QEKILVAESVI---SELGLTKCENTIIGNSFIRGISGGERKRVSIAHE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 160 LMLEPTFALLDEIDSGLD-IDALKVVSK-GVNAMRGEgfgaMIIT--HYQRLLNYITPDVVHVMMEGRVVLSG-GPELAA 234
Cdd:PLN03211 221 MLINPSLLILDEPTSGLDaTAAYRLVLTlGSLAQKGK----TIVTsmHQPSSRVYQMFDSVLVLSEGRCLFFGkGSDAMA 296
|
....*...
gi 2038778719 235 RLEREGYA 242
Cdd:PLN03211 297 YFESVGFS 304
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-230 |
1.23e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 63.22 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLFDGVNILELEVDE-----RARMGLflAMQYPS--- 90
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLL--NGLHVPTQGSVRVDDTLITSTSKNKdikqiRKKVGL--VFQFPEsql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 91 -EIPGITNAEFLRAAMNAGKEDDEKISvrefitklDEKMELLNMKEEMAERYLNEgFSGGEKKRNEILQLLMLEPTFALL 169
Cdd:PRK13649 99 fEETVLKDVAFGPQNFGVSQEEAEALA--------REKLALVGISESLFEKNPFE-LSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038778719 170 DEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITH-YQRLLNYitPDVVHVMMEGRVVLSGGP 230
Cdd:PRK13649 170 DEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlMDDVANY--ADFVYVLEKGKLVLSGKP 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-177 |
1.38e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 63.70 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpnYEV-TKGEVLFDGVNILELEVDERARMG 81
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG---FEQpTAGQIMLDGVDLSHVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 82 LFlamQYPSEIPGITNAEFLRAAMnagKEDdeKISVREFITKLDEKMELLNMkEEMAERYLNEgFSGGEKKRNEILQLLM 161
Cdd:PRK11607 96 MF---QSYALFPHMTVEQNIAFGL---KQD--KLPKAEIASRVNEMLGLVHM-QEFAKRKPHQ-LSGGQRQRVALARSLA 165
|
170
....*....|....*.
gi 2038778719 162 LEPTFALLDEIDSGLD 177
Cdd:PRK11607 166 KRPKLLLLDEPMGALD 181
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-180 |
1.66e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.67 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEI-EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYevTKGEVlfdgvnilelEVDERARMgL 82
Cdd:COG4178 363 LALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPY--GSGRI----------ARPAGARV-L 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 FL-------------AMQYPSEIPGITNAEfLRAAMnagkeddEKISVREFITKLDEkmellnmkeemaERYLNEGFSGG 149
Cdd:COG4178 430 FLpqrpylplgtlreALLYPATAEAFSDAE-LREAL-------EAVGLGHLAERLDE------------EADWDQVLSLG 489
|
170 180 190
....*....|....*....|....*....|.
gi 2038778719 150 EKKRNEILQLLMLEPTFALLDEIDSGLDIDA 180
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEEN 520
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
5-177 |
1.69e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.58 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 5 EIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMgnPNYEVTKGEVLFDGVNILELEVDE-RARmgLF 83
Cdd:PRK10789 317 NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQ--RHFDVSEGDIRFHDIPLTKLQLDSwRSR--LA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LAMQYP--------SEI----PGITNAEFLRAAMNAgkeddekiSVREFITKLDEKMEllnmkEEMAERYLNegFSGGEK 151
Cdd:PRK10789 393 VVSQTPflfsdtvaNNIalgrPDATQQEIEHVARLA--------SVHDDILRLPQGYD-----TEVGERGVM--LSGGQK 457
|
170 180
....*....|....*....|....*.
gi 2038778719 152 KRNEILQLLMLEPTFALLDEIDSGLD 177
Cdd:PRK10789 458 QRISIARALLLNAEILILDDALSAVD 483
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-231 |
1.92e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 62.31 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERARMGLF 83
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTG--FYKPTGGTILLRGQHIEGLPGHQIARMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LAMQYPSEIPGITNAEFLRAA----MNAG------KEDDEKISVREFITKLDEKMELLNMKeEMAERYLNEgFSGGEKKR 153
Cdd:PRK11300 84 RTFQHVRLFREMTVIENLLVAqhqqLKTGlfsgllKTPAFRRAESEALDRAATWLERVGLL-EHANRQAGN-LAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 154 NEILQLLMLEPTFALLDEIDSGL------DIDALkvvskgVNAMRGE-GFGAMIITHYQRLLNYITpDVVHVMMEGRVVL 226
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLnpketkELDEL------IAELRNEhNVTVLLIEHDMKLVMGIS-DRIYVVNQGTPLA 234
|
....*
gi 2038778719 227 SGGPE 231
Cdd:PRK11300 235 NGTPE 239
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-245 |
1.96e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.44 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLFDGVNI--LELEVDERARMGLFL-AMQYPSEI--- 92
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLL--QRVFDPQSGRILIDGTDIrtVTRASLRRNIAVVFQdAGLFNRSIedn 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 93 -----PGITNAEFLRAAMNAGKEDdekisvreFITKLDEKMELLnmkeeMAERylNEGFSGGEKKRNEILQLLMLEPTFA 167
Cdd:PRK13657 429 irvgrPDATDEEMRAAAERAQAHD--------FIERKPDGYDTV-----VGER--GRQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038778719 168 LLDEIDSGLDIDALKVVSKGVNAMRgEGFGAMIITHyqRLLNYITPDVVHVMMEGRVVLSGG-PELAARLERegYAKLA 245
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDELM-KGRTTFIIAH--RLSTVRNADRILVFDNGRVVESGSfDELVARGGR--FAALL 567
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-231 |
2.00e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.18 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVlEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYevTKGEVLFDGVNILELEVDERaRM 80
Cdd:PRK10851 1 MSI-EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ--TSGHIRFHGTDVSRLHARDR-KV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 G-------LFLAMQYPSEIP-GITnaeflraaMNAGKEDDEKISVREFITKLDEKMELlnmkEEMAERYLNEgFSGGEKK 152
Cdd:PRK10851 77 GfvfqhyaLFRHMTVFDNIAfGLT--------VLPRRERPNAAAIKAKVTQLLEMVQL----AHLADRYPAQ-LSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 153 RNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGE-GFGAMIITHYQRLLNYITPDVVhVMMEGRVVLSGGPE 231
Cdd:PRK10851 144 RVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVV-VMSQGNIEQAGTPD 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-89 |
2.50e-11 |
|
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: 60.52 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERARMGLF 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSG--LYKPDSGEILVDGKEVSFASPRDARRAGIA 78
|
....*.
gi 2038778719 84 LAMQYP 89
Cdd:cd03216 79 MVYQLS 84
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-231 |
2.64e-11 |
|
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: 61.59 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVlEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNILELEVDERa 78
Cdd:cd03296 1 MSI-EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGleRP----DSGTILFGGEDATDVPVQER- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 79 rmGLFLAMQYPSEIPGIT---NAEF-LRAamnagkeddEKISVREFITKLDEK-MELLNMK--EEMAERYLNEgFSGGEK 151
Cdd:cd03296 75 --NVGFVFQHYALFRHMTvfdNVAFgLRV---------KPRSERPPEAEIRAKvHELLKLVqlDWLADRYPAQ-LSGGQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 152 KRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGE-GFGAMIITHYQRLLNYITPDVVhVMMEGRVVLSGGP 230
Cdd:cd03296 143 QRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVV-VMNKGRIEQVGTP 221
|
.
gi 2038778719 231 E 231
Cdd:cd03296 222 D 222
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-228 |
3.68e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 61.64 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 2 SVLEIKDLHVEIEGkEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPNYEVTKGEVLFDGVNILelevderar 79
Cdd:PRK10418 3 QQIELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGilPAGVRQTAGRVLLDGKPVA--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 80 mglflamqyPSEIPGITNAEFL---RAAMN---------------AGKEDDEKisvrefitKLDEKMEL--LNMKEEMAE 139
Cdd:PRK10418 73 ---------PCALRGRKIATIMqnpRSAFNplhtmhtharetclaLGKPADDA--------TLTAALEAvgLENAARVLK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 140 RYLNEgFSGGEKKRNEILQLLMLEPTFALLDEIDSGLDIDA-LKVVSKGVNAMRGEGFGAMIITH----YQRLlnyitPD 214
Cdd:PRK10418 136 LYPFE-MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAqARILDLLESIVQKRALGMLLVTHdmgvVARL-----AD 209
|
250
....*....|....
gi 2038778719 215 VVHVMMEGRVVLSG 228
Cdd:PRK10418 210 DVAVMSHGRIVEQG 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-228 |
5.40e-11 |
|
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: 60.37 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVD-------E 76
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG--IILPDSGEVLFDGKPLDIAARNrigylpeE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 77 RarmGLFLAMQYpseipgITNAEFLRAAMNAGKEDdekisVREFITKLDEKMELlnmkEEMAERYLNEgFSGGEKKRNEI 156
Cdd:cd03269 79 R---GLYPKMKV------IDQLVYLAQLKGLKKEE-----ARRRIDEWLERLEL----SEYANKRVEE-LSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038778719 157 LQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITPDVVhVMMEGRVVLSG 228
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVL-LLNKGRAVLYG 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-82 |
5.81e-11 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 62.01 E-value: 5.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEIEG----KEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPNYEVTKGEVLFDGVNILELev 74
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRllPDPAAHPSGSILFDGQDLLGL-- 81
|
....*...
gi 2038778719 75 DERARMGL 82
Cdd:COG4172 82 SERELRRI 89
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-228 |
6.15e-11 |
|
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: 60.20 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 24 LTLKTGEIAAIMGPNGTGKSTLSAAIMGnpnYEV-TKGEVLFDGVNILELEVDERARMGLFlamQYPSEIPGITNAEFLR 102
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAG---FETpQSGRVLINGVDVTAAPPADRPVSMLF---QENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 103 AAMNAG----KEDDEKISVREFITKLDEKMellnmkeemaeRYLNEGFSGGEKKRNEILQLLMLEPTFALLDE----IDS 174
Cdd:cd03298 93 LGLSPGlkltAEDRQAIEVALARVGLAGLE-----------KRLPGELSGGERQRVALARVLVRDKPVLLLDEpfaaLDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2038778719 175 GLDIDALKVVSKgvnAMRGEGFGAMIITHYQRLLNYITPDVVHVmMEGRVVLSG 228
Cdd:cd03298 162 ALRAEMLDLVLD---LHAETKMTVLMVTHQPEDAKRLAQRVVFL-DNGRIAAQG 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-228 |
8.78e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.45 E-value: 8.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEV------TKGEVLFDGVNILELE-VD 75
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL--NRLIEIydskikVDGKVLYFGKDIFQIDaIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 76 ERARMGlfLAMQYPSEIPGITNAEFLRAAMNAGKEDDEkisvREFITKLDEKMELLNMKEEMAERyLN---EGFSGGEKK 152
Cdd:PRK14246 88 LRKEVG--MVFQQPNPFPHLSIYDNIAYPLKSHGIKEK----REIKKIVEECLRKVGLWKEVYDR-LNspaSQLSGGQQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038778719 153 RNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEgFGAMIITHYQRLLNYITpDVVHVMMEGRVVLSG 228
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVA-DYVAFLYNGELVEWG 234
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-178 |
1.03e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 60.24 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEvtkGEVLFDGVNILELEVDERARMGLFLAMQYPSeIPGITNA 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ---GEILLNGRPLSDWSAAELARHRAYLSQQQSP-PFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 99 EFLRAAMNAGKEDDEKISVREFIT---KLDEKMellnmkeemaERYLNEgFSGGEKKRNEI----LQL---LMLEPTFAL 168
Cdd:COG4138 88 QYLALHQPAGASSEAVEQLLAQLAealGLEDKL----------SRPLTQ-LSGGEWQRVRLaavlLQVwptINPEGQLLL 156
|
170
....*....|
gi 2038778719 169 LDEIDSGLDI 178
Cdd:COG4138 157 LDEPMNSLDV 166
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-235 |
1.16e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 60.13 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEI-EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLFDGVNILELEVDE-RARM 80
Cdd:PRK13647 4 IIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHL--NGIYLPQRGRVKVMGREVNAENEKWvRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 GlfLAMQYPSEipgitnaeflrAAMNAGKEDD-------EKISVREFITKLDEKMELLNMKE--EMAERYLnegfSGGEK 151
Cdd:PRK13647 82 G--LVFQDPDD-----------QVFSSTVWDDvafgpvnMGLDKDEVERRVEEALKAVRMWDfrDKPPYHL----SYGQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 152 KRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITpDVVHVMMEGRVVLSGGPE 231
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWA-DQVIVLKEGRVLAEGDKS 223
|
....
gi 2038778719 232 LAAR 235
Cdd:PRK13647 224 LLTD 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-203 |
1.20e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 60.15 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTL--SAAIMGNPNYEVTK-GEVLFDGVNILE----LE 73
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrCINLLEQPEAGTIRvGDITIDTARSLSqqkgLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 74 VDERARMG-------LF---LAMQYPSEIPGITNAEFLRAAMNAGkeddekisvREFITKLDekmelLNMKEEMAERYLn 143
Cdd:PRK11264 81 RQLRQHVGfvfqnfnLFphrTVLENIIEGPVIVKGEPKEEATARA---------RELLAKVG-----LAGKETSYPRRL- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 144 egfSGGEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITH 203
Cdd:PRK11264 146 ---SGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-231 |
2.32e-10 |
|
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: 60.20 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 21 GVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLF----DGVNILELEVDERARMGLFLAM--QYPSEIPG 94
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG--VLEPTSGEVNVrvgdEWVDMTKPGPDGRGRAKRYIGIlhQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 95 ITNAEFLRAAMnaGKEDDEKISVREFITKL-----DEKmellnMKEEMAERYLNEgFSGGEKKRNEILQLLMLEPTFALL 169
Cdd:TIGR03269 380 RTVLDNLTEAI--GLELPDELARMKAVITLkmvgfDEE-----KAEEILDKYPDE-LSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038778719 170 DEIDSGLD-IDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITpDVVHVMMEGRVVLSGGPE 231
Cdd:TIGR03269 452 DEPTGTMDpITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVC-DRAALMRDGKIVKIGDPE 513
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-203 |
2.41e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 58.01 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 14 EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG---------------NPNYEVTKGEVlfdgVNILELEVDERA 78
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGvlrptsgtvrraggaRVAYVPQRSEV----PDSLPLTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 79 RMGLFlamqypseipgitnAEflRAAMNAGKEDDEKIsvrefitkLDEKMELLNMkEEMAERYLNEgFSGGEKKRNEILQ 158
Cdd:NF040873 79 AMGRW--------------AR--RGLWRRLTRDDRAA--------VDDALERVGL-ADLAGRQLGE-LSGGQRQRALLAQ 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2038778719 159 LLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITH 203
Cdd:NF040873 133 GLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTH 177
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
23-77 |
3.21e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 58.61 E-value: 3.21e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2038778719 23 NLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpnYE-VTKGEVLFDGVNILELEVDER 77
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAG---FLpPDSGRILWNGQDLTALPPAER 71
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-177 |
3.34e-10 |
|
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: 58.63 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNILELEVDeraRMGLFlamQYPSEIPGIT 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlaQP----TSGGVILEGKQITEPGPD---RMVVF---QNYSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 97 NAEFLRAAMNAGKEDDEKISVREFItklDEKMELLNMKEEmAERYLNEgFSGGEKKRNEILQLLMLEPTFALLDEIDSGL 176
Cdd:TIGR01184 71 VRENIALAVDRVLPDLSKSERRAIV---EEHIALVGLTEA-ADKRPGQ-LSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
.
gi 2038778719 177 D 177
Cdd:TIGR01184 146 D 146
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
18-229 |
3.61e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 59.27 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 18 ILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPnyEVTKGEVLFDGVNILELEVDERarmGLFLAMQYPSEIPGITN 97
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLE--DITSGDLFIGEKRMNDVPPAER---GVGMVFQSYALYPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 98 AEFLRAAMNAGKEDDEKISVRefitkLDEKMELLNMkEEMAERyLNEGFSGGEKKRNEILQLLMLEPTFALLDEIDSGLD 177
Cdd:PRK11000 93 AENMSFGLKLAGAKKEEINQR-----VNQVAEVLQL-AHLLDR-KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2038778719 178 IdALKVvskgvnAMRGEgfgamiITHYQRLLN----YITPDVVHVMM--EGRVVLSGG 229
Cdd:PRK11000 166 A-ALRV------QMRIE------ISRLHKRLGrtmiYVTHDQVEAMTlaDKIVVLDAG 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-240 |
3.83e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 58.87 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 2 SVLEIKDLHVEIEGKE--ILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNILELEV-DE 76
Cdd:PRK13635 4 EIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGllLP----EAGTITVGGMVLSEETVwDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 77 RARMGlfLAMQYPseipgitNAEFLRAAMnagkEDD-----EKISV--REFITKLDEKMELLNMkEEMAERYLNEgFSGG 149
Cdd:PRK13635 80 RRQVG--MVFQNP-------DNQFVGATV----QDDvafglENIGVprEEMVERVDQALRQVGM-EDFLNREPHR-LSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 150 EKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMI-ITHyqRLLNYITPDVVHVMMEGRVVLSG 228
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLsITH--DLDEAAQADRVIVMNKGEILEEG 222
|
250
....*....|....*.
gi 2038778719 229 GPE----LAARLEREG 240
Cdd:PRK13635 223 TPEeifkSGHMLQEIG 238
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-230 |
4.03e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.98 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 22 VNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLFDGVNILELEVDER---ARMGLFLAMQYPS----EIPG 94
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHL--NGLLQPTEGKVTVGDIVVSSTSKQKEikpVRKKVGVVFQFPEsqlfEETV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 95 ITNAEFLRAAMNAGKEDDEKISVrefitkldEKMELLNMKEEMAERYLNEgFSGGEKKRNEILQLLMLEPTFALLDEIDS 174
Cdd:PRK13643 103 LKDVAFGPQNFGIPKEKAEKIAA--------EKLEMVGLADEFWEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2038778719 175 GLDIDALKVVSKGVNAMRGEGFGAMIITHyqrLLNYIT--PDVVHVMMEGRVVLSGGP 230
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVTH---LMDDVAdyADYVYLLEKGHIISCGTP 228
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-178 |
6.18e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 58.26 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 6 IKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLsAAIMGNpNYEVTKGEVLFDGVNILELEVDERARMGLFLA 85
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTL-LKMLGR-HQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 86 MQYPSEiPGITNAEFLR--------AAMNAGKEDDEKIsvrefitklDEKMELLNMKeEMAERyLNEGFSGGEKKRNEIL 157
Cdd:PRK10575 92 QQLPAA-EGMTVRELVAigrypwhgALGRFGAADREKV---------EEAISLVGLK-PLAHR-LVDSLSGGERQRAWIA 159
|
170 180
....*....|....*....|.
gi 2038778719 158 QLLMLEPTFALLDEIDSGLDI 178
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDI 180
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-207 |
6.56e-10 |
|
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: 57.12 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGvnilelEVDERARMG 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGlsPP----LAGRVLLNG------GPLDFQRDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 82 LFLAMQYPSEIPGIT-------NAEFLRAAmnagkEDDEKIsvrefITKLDEKMelLNMKEEMAERYLnegfSGGEKKRN 154
Cdd:cd03231 71 IARGLLYLGHAPGIKttlsvleNLRFWHAD-----HSDEQV-----EEALARVG--LNGFEDRPVAQL----SAGQQRRV 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2038778719 155 EILQLLMLEPTFALLDEIDSGLDIDAlkvVSKGVNAMRG--EGFGAMIITHYQRL 207
Cdd:cd03231 135 ALARLLLSGRPLWILDEPTTALDKAG---VARFAEAMAGhcARGGMVVLTTHQDL 186
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-230 |
9.18e-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: 57.12 E-value: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHV--EIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDE-RARM 80
Cdd:cd03244 3 IEFKNVSLryRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFR--LVELSSGSILIDGVDISKIGLHDlRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 GLFLamQYPSEIPGiTnaefLRAAMNA-GKEDDEKI-------SVREFITKLDEKmelLNMKEEMAerylNEGFSGGEKk 152
Cdd:cd03244 81 SIIP--QDPVLFSG-T----IRSNLDPfGEYSDEELwqalervGLKEFVESLPGG---LDTVVEEG----GENLSVGQR- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 153 rneilQLLML------EPTFALLDEIDSGLDIDALKVVSKgvnAMRGEGFGAMIITHYQRLLNYITPDVVHVMMEGRVVL 226
Cdd:cd03244 146 -----QLLCLarallrKSKILVLDEATASVDPETDALIQK---TIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVE 217
|
....
gi 2038778719 227 SGGP 230
Cdd:cd03244 218 FDSP 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-82 |
1.02e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.11 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIE-GKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERARMG 81
Cdd:COG3845 257 VLEVENLSVRDDrGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAG--LRPPASGSIRLDGEDITGLSPRERRRLG 334
|
.
gi 2038778719 82 L 82
Cdd:COG3845 335 V 335
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-231 |
1.05e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.29 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLFDGVNIlELEVDERARMGLF 83
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI--NFLEKPSEGSIVVNGQTI-NLVRDKDGQLKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LAMQYpseipgitnaEFLRAAMNAGKeddEKISVREFITKLDEKME----LLNMKE----EMAERYLNE----------- 144
Cdd:PRK10619 83 DKNQL----------RLLRTRLTMVF---QHFNLWSHMTVLENVMEapiqVLGLSKqearERAVKYLAKvgideraqgky 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 145 --GFSGGEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITPDVVhVMMEG 222
Cdd:PRK10619 150 pvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVI-FLHQG 228
|
....*....
gi 2038778719 223 RVVLSGGPE 231
Cdd:PRK10619 229 KIEEEGAPE 237
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-230 |
1.67e-09 |
|
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: 56.36 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKE--ILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNILELEVDERAR 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGelRP----TSGTAYINGYSIRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 80 MGlfLAMQYPSEIPGITNAEFLR-AAMNAGKEDDEKISVREFITkldEKMELLNMKEEMAERYlnegfSGGEKKRneiLQ 158
Cdd:cd03263 77 LG--YCPQFDALFDELTVREHLRfYARLKGLPKSEIKEEVELLL---RVLGLTDKANKRARTL-----SGGMKRK---LS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038778719 159 L---LMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEgfGAMIIT-HYQRLLNYITpDVVHVMMEGRVVLSGGP 230
Cdd:cd03263 144 LaiaLIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKG--RSIILTtHSMDEAEALC-DRIAIMSDGKLRCIGSP 216
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-203 |
1.80e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.48 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 22 VNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEvtkGEVLFDGVNILELEVDERARMGLFLAMQYPSeIPGITNAEFL 101
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS---GSIQFAGQPLEAWSAAELARHRAYLSQQQTP-PFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 102 RAAMNAGKEDDEKISVrefitkLDEKMELLNMKEEMaERYLNEgFSGGEKKR----NEILQL---LMLEPTFALLDEIDS 174
Cdd:PRK03695 91 TLHQPDKTRTEAVASA------LNEVAEALGLDDKL-GRSVNQ-LSGGEWQRvrlaAVVLQVwpdINPAGQLLLLDEPMN 162
|
170 180
....*....|....*....|....*....
gi 2038778719 175 GLDIDALKVVSKGVNAMRGEGFGAMIITH 203
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCQQGIAVVMSSH 191
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-228 |
2.19e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.90 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAI--MGNPnyevTKGEVLFDGVNILELEVDERA--RMGLFLAMQ--YPSEI 92
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLtmIETP----TGGELYYQGQDLLKADPEAQKllRQKIQIVFQnpYGSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 93 P----GITNAEFLraAMNAgkeddeKISVREFITKLDEKMELLNMKEEMAERYLNEgFSGGEKKRNEILQLLMLEPTFAL 168
Cdd:PRK11308 107 PrkkvGQILEEPL--LINT------SLSAAERREKALAMMAKVGLRPEHYDRYPHM-FSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038778719 169 LDEIDSGLDIdalKVVSKGVNAM----RGEGFGAMIITHYQRLLNYITPDVVhVMMEGRVVLSG 228
Cdd:PRK11308 178 ADEPVSALDV---SVQAQVLNLMmdlqQELGLSYVFISHDLSVVEHIADEVM-VMYLGRCVEKG 237
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-177 |
2.55e-09 |
|
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: 56.11 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 22 VNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLFDGVNILELEVDE-----RARM-------GLFLAM--- 86
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCI--NRLIEPTSGKVLIDGQDIAAMSRKElrelrRKKIsmvfqsfALLPHRtvl 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 87 ---QYPSEIPGITNAEFLRAAMnagkeddekisvrefitkldEKMELLNMkEEMAERYLNEgFSGGEKKRNEILQLLMLE 163
Cdd:cd03294 121 envAFGLEVQGVPRAEREERAA--------------------EALELVGL-EGWEHKYPDE-LSGGMQQRVGLARALAVD 178
|
170
....*....|....
gi 2038778719 164 PTFALLDEIDSGLD 177
Cdd:cd03294 179 PDILLMDEAFSALD 192
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-231 |
2.78e-09 |
|
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: 57.12 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEVTKGEVLFD------------------ 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 66 -----GVNILELEVD-------ERARMGLFLAMQYPSEIPGITNAEFLRAAMNAGKEddEKISVREFITKLDEKMELLNM 133
Cdd:TIGR03269 81 pcpvcGGTLEPEEVDfwnlsdkLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEE--IGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 134 KEEMAerYLNEGFSGGEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGV-NAMRGEGFGAMIITHYQRLLNYIT 212
Cdd:TIGR03269 159 SHRIT--HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeEAVKASGISMVLTSHWPEVIEDLS 236
|
250
....*....|....*....
gi 2038778719 213 PDVVhVMMEGRVVLSGGPE 231
Cdd:TIGR03269 237 DKAI-WLENGEIKEEGTPD 254
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-177 |
3.37e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.49 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPnyEVTKGEVLFDGVNILELEVDERARM 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFE--TPDSGRIMLDGQDITHVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 GLFlamQYPSEIPGITNAEFLRAAMNAGKEDDEKISVRefitkldeKMELLNMK--EEMAERYLNEgFSGGEKKRNEILQ 158
Cdd:PRK09452 90 TVF---QSYALFPHMTVFENVAFGLRMQKTPAAEITPR--------VMEALRMVqlEEFAQRKPHQ-LSGGQQQRVAIAR 157
|
170
....*....|....*....
gi 2038778719 159 LLMLEPTFALLDEIDSGLD 177
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALD 176
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-228 |
3.94e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 56.39 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHV-EIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEvtkGEVLFDGVNILELEVdERARMGL 82
Cdd:PRK11174 350 IEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ---GSLKINGIELRELDP-ESWRKHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 FLAMQYPSEIPGITNAEFLRAAMNAgkeDDEKIS-------VREFITKLDEKMELlnmkeEMAERylNEGFSGGEKKRNE 155
Cdd:PRK11174 426 SWVGQNPQLPHGTLRDNVLLGNPDA---SDEQLQqalenawVSEFLPLLPQGLDT-----PIGDQ--AAGLSVGQAQRLA 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038778719 156 ILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVN-AMRGEgfGAMIITH-YQRLLNYitpDVVHVMMEGRVVLSG 228
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNaASRRQ--TTLMVTHqLEDLAQW---DQIWVMQDGQIVQQG 565
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-223 |
4.71e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.89 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEIEGKE----ILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPNYEVTkGEVLFDGVNILELEV 74
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDgdvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllAANGRIG-GSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 75 DERARM-GLFLAM--QYP--SEIPGITNAEFLRAAMNAGKEDDEKISVREFITKLDE-KMELLNMKEEMaerYLNEgFSG 148
Cdd:PRK09473 89 KELNKLrAEQISMifQDPmtSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAvKMPEARKRMKM---YPHE-FSG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038778719 149 GEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMI-ITHYQRLLNYITpDVVHVMMEGR 223
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGIC-DKVLVMYAGR 239
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-219 |
5.00e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.33 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 25 TLKTGEIAAIMGPNGTGKST----LSAAIM---GNPNYEVTKGEVL--FDGVNI---LELEVDERARMglflAM--QYPS 90
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTalkiLSGELKpnlGDYDEEPSWDEVLkrFRGTELqdyFKKLANGEIKV----AHkpQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 91 EIPgitnaEFLRaamnaGKeddekisVREFITKLDEKM------ELLNMKEEMaERYLNEgFSGGEKKRNEILQLLMLEP 164
Cdd:COG1245 171 LIP-----KVFK-----GT-------VRELLEKVDERGkldelaEKLGLENIL-DRDISE-LSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2038778719 165 TFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITpDVVHVM 219
Cdd:COG1245 232 DFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLA-DYVHIL 285
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
15-228 |
5.17e-09 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 56.29 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 15 GKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNpnYEVTKGEVLFDGVNILELEVDERARMGLFLAmQYPSEIPG 94
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGF--FQARSGEILLNGFSLKDIDRHTLRQFINYLP-QEPYIFSG 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 95 iTNAEFLRAAMNAGKEDDEKISVREF--ITKLDEKMELlNMKEEMAERylNEGFSGGEKKRNEILQLLMLEPTFALLDEI 172
Cdd:TIGR01193 563 -SILENLLLGAKENVSQDEIWAACEIaeIKDDIENMPL-GYQTELSEE--GSSISGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2038778719 173 DSGLD-IDALKVVSKGVNAMRgegfgAMIITHYQRLLNYITPDVVHVMMEGRVVLSG 228
Cdd:TIGR01193 639 TSNLDtITEKKIVNNLLNLQD-----KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQG 690
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-177 |
5.65e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.87 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKE-----------ILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNyevTKGEVLFDGVNILE 71
Cdd:PRK15134 275 LLDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN---SQGEIWFDGQPLHN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 72 LEVDE----RARMGLFLAMQYPSEIPGITN----AEFLR---AAMNAGKEDDEKISVrefitkldekMELLNMKEEMAER 140
Cdd:PRK15134 352 LNRRQllpvRHRIQVVFQDPNSSLNPRLNVlqiiEEGLRvhqPTLSAAQREQQVIAV----------MEEVGLDPETRHR 421
|
170 180 190
....*....|....*....|....*....|....*..
gi 2038778719 141 YLNEgFSGGEKKRNEILQLLMLEPTFALLDEIDSGLD 177
Cdd:PRK15134 422 YPAE-FSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-230 |
5.99e-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: 54.34 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEI--EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMgnPNYEVTKGEVLFDGVNILELEVdERARMG 81
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALF--RFLEAEEGKIEIDGIDISTIPL-EDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 82 LFLAMQYPSEIPGItnaefLRAAMNA-GKEDDEKIsvrefitkldekMELLNMKEEmaerylNEGFSGGEKKRNEILQLL 160
Cdd:cd03369 84 LTIIPQDPTLFSGT-----IRSNLDPfDEYSDEEI------------YGALRVSEG------GLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 161 MLEPTFALLDEIDSGLDIDALKVVSKGVnamRGEGFGAMIITHYQRLLNYITPDVVHVMMEGRVVLSGGP 230
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTI---REEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-228 |
6.05e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERARMGLFLAMQYPSEIPGITNA 98
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG--IHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 99 EflraAMNAGKEDDEK------ISVREFITKLDEKMELLNMKEEMAERYLNEGFSggEKKRNEILQLLMLEPTFALLDEI 172
Cdd:PRK09700 99 E----NLYIGRHLTKKvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSIS--HKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2038778719 173 DSGL---DIDALKVVskgVNAMRGEGFGAMIITHYQRLLNYITpDVVHVMMEGRVVLSG 228
Cdd:PRK09700 173 TSSLtnkEVDYLFLI---MNQLRKEGTAIVYISHKLAEIRRIC-DRYTVMKDGSSVCSG 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-203 |
7.49e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.89 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 17 EILKGVNLTLKTGEIAAIMGPNGTGKSTLsAAIMGNPNyEVTKGEVLFDGVNILELEVDERARMGL----FLAMQYP--S 90
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTL-MNILGCLD-KPTSGTYRVAGQDVATLDADALAQLRRehfgFIFQRYHllS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 91 EIPGITNAEFlrAAMNAGKEDDEKIS-VREFITKLDekmellnmkeeMAER--YLNEGFSGGEKKRNEILQLLMLEPTFA 167
Cdd:PRK10535 100 HLTAAQNVEV--PAVYAGLERKQRLLrAQELLQRLG-----------LEDRveYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 2038778719 168 LLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITH 203
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-203 |
8.09e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.66 E-value: 8.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAI--MGNPNYEV-TKGEVLFDGVNILELEVD-ERAR 79
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEVrVEGRVEFFNQNIYERRVNlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 80 MGLFLAMQYPSEIPGITNAEFLRAAMNAGKEddEKISVREFITKLDEKMELLN-MKEEMAERYLNegFSGGEKKRNEILQ 158
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGVKIVGWR--PKLEIDDIVESALKDADLWDeIKHKIHKSALD--LSGGQQQRLCIAR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2038778719 159 LLMLEPTFALLDEIDSGLD-IDALKVVSKGVNAMRGEGFGAMIITH 203
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDpIASMKVESLIQSLRLRSELTMVIVSH 209
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-235 |
8.15e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.49 E-value: 8.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 14 EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEvDERARMGLFLAMQYPseip 93
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG--YYPLTEGEIRLDGRPLSSLS-HSVLRQGVAMVQQDP---- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 94 gITNAEFLRAAMNAGKEDDEkisvrEFITKLDEKMELLNMKEEMAE----RYLNEG--FSGGEKKRNEILQLLMLEPTFA 167
Cdd:PRK10790 425 -VVLADTFLANVTLGRDISE-----EQVWQALETVQLAELARSLPDglytPLGEQGnnLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038778719 168 LLDE----IDSGLDidalKVVSKGVNAMRgEGFGAMIITHyqRLLNYITPDVVHVMMEGRVVLSGGPE--LAAR 235
Cdd:PRK10790 499 ILDEatanIDSGTE----QAIQQALAAVR-EHTTLVVIAH--RLSTIVEADTILVLHRGQAVEQGTHQqlLAAQ 565
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
12-248 |
8.53e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.94 E-value: 8.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 12 EIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLfdgvnilelevDERarmglflAMQYPSE 91
Cdd:PTZ00243 669 ELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS--QFEISEGRVW-----------AER-------SIAYVPQ 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 92 IPGITNAEFLRAAMNAGKEDDEKI--SVRefITKLDEKMELLN--MKEEMAERYLNegFSGGEKKRNEILQLLMLEPTFA 167
Cdd:PTZ00243 729 QAWIMNATVRGNILFFDEEDAARLadAVR--VSQLEADLAQLGggLETEIGEKGVN--LSGGQKARVSLARAVYANRDVY 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 168 LLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYitPDVVHVMMEGRVVLSGgpELAARLEREGYAKLAEE 247
Cdd:PTZ00243 805 LLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPR--ADYVVALGDGRVEFSG--SSADFMRTSLYATLAAE 880
|
.
gi 2038778719 248 L 248
Cdd:PTZ00243 881 L 881
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-238 |
9.33e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 54.74 E-value: 9.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDL---HVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEV-DE 76
Cdd:PRK13650 2 SNIIEVKNLtfkYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDG--LLEAESGQIIIDGDLLTEENVwDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 77 RARMGlfLAMQYPseipgitNAEFLRAAMnagkEDD-------EKISVREFITKLDEKMELLNM---KEEMAERylnegF 146
Cdd:PRK13650 80 RHKIG--MVFQNP-------DNQFVGATV----EDDvafglenKGIPHEEMKERVNEALELVGMqdfKEREPAR-----L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 147 SGGEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGE-GFGAMIITHyqRLLNYITPDVVHVMMEGRVV 225
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITH--DLDEVALSDRVLVMKNGQVE 219
|
250
....*....|....
gi 2038778719 226 LSGGP-ELAARLER 238
Cdd:PRK13650 220 STSTPrELFSRGND 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-66 |
1.06e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.02 E-value: 1.06e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDG 66
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSG--VYQPDSGEILLDG 65
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-231 |
1.53e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 16 KEILKGVNLTLKTGEIAAIMGPNGTGKSTL--SAAIMGNPnyevTKGEVLFDGVNILELEVDERARMGLFLAMQypSEIP 93
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLlrTLSRLMTP----AHGHVWLDGEHIQHYASKEVARRIGLLAQN--ATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 94 GITNAEFLRAamnAGKEDDEKISVRefITKLDEKMELLNMK----EEMAERYLNEgFSGGEKKRNEILQLLMLEPTFALL 169
Cdd:PRK10253 94 GDITVQELVA---RGRYPHQPLFTR--WRKEDEEAVTKAMQatgiTHLADQSVDT-LSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038778719 170 DEIDSGLD----IDALKVVSKgVNamRGEGFGAMIITHYqrlLNYITPDVVHV--MMEGRVVLSGGPE 231
Cdd:PRK10253 168 DEPTTWLDishqIDLLELLSE-LN--REKGYTLAAVLHD---LNQACRYASHLiaLREGKIVAQGAPK 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-219 |
3.20e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 25 TLKTGEIAAIMGPNGTGKST----LSAAIM---GNPNYEVTKGEVL--FDGV---NILELEVDERARMGlfLAMQYPSEI 92
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTavkiLSGELIpnlGDYEEEPSWDEVLkrFRGTelqNYFKKLYNGEIKVV--HKPQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 93 PGITnaeflraamnagkeddeKISVREFITKLDEK------MELLNMkEEMAERYLNEgFSGGEKKRNEILQLLMLEPTF 166
Cdd:PRK13409 173 PKVF-----------------KGKVRELLKKVDERgkldevVERLGL-ENILDRDISE-LSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2038778719 167 ALLDEIDSGLDIDALKVVSKGVNAMrGEGFGAMIITHYQRLLNYITpDVVHVM 219
Cdd:PRK13409 234 YFFDEPTSYLDIRQRLNVARLIREL-AEGKYVLVVEHDLAVLDYLA-DNVHIA 284
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
11-66 |
4.17e-08 |
|
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: 52.09 E-value: 4.17e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2038778719 11 VEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDG 66
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG--ELEKLSGSVSVPG 66
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
16-66 |
4.28e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 52.39 E-value: 4.28e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2038778719 16 KEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDG 66
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG--ILEPTSGRVEVNG 87
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-225 |
7.06e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEI----EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG---NPNYEVTKGEVLFDGVNIleLE 73
Cdd:PRK15134 3 QPLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRllpSPPVVYPSGDIRFHGESL--LH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 74 VDERARMGLF---LAMQYpsEIPGITnaefLRAAMNAGKEDDEKISVREFITKLDEKMELLNMKEEM----AERYLNE-- 144
Cdd:PRK15134 81 ASEQTLRGVRgnkIAMIF--QEPMVS----LNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVgirqAAKRLTDyp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 145 -GFSGGEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGE-GFGAMIITHYQRLLNYITpDVVHVMMEG 222
Cdd:PRK15134 155 hQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLA-DRVAVMQNG 233
|
...
gi 2038778719 223 RVV 225
Cdd:PRK15134 234 RCV 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-177 |
8.26e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 52.00 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGK----EILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgnpNY--EVTKGEVLFDGVNILELE---- 73
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI----NLleRPTSGSVLVDGVDLTALSerel 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 74 VDERARMGL-F----LAMQ--------YPSEIPGITNAEflRAAmnagkeddekisvrefitKLDEKMELLNMkEEMAER 140
Cdd:COG1135 78 RAARRKIGMiFqhfnLLSSrtvaenvaLPLEIAGVPKAE--IRK------------------RVAELLELVGL-SDKADA 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 2038778719 141 YLNEgFSGGEKKRNEILQLLMLEPTFALLDEIDSGLD 177
Cdd:COG1135 137 YPSQ-LSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-72 |
8.68e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.69 E-value: 8.68e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038778719 1 MSVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGN--PNyevtKGEVLFDGVNILEL 72
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQiaPD----HGEILFDGENIPAM 74
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-230 |
8.68e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.02 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKE---ILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEV-DERA 78
Cdd:PRK13642 4 ILEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDG--LFEEFEGKVKIDGELLTAENVwNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 79 RMGlfLAMQYP-SEIPGITNAEFLRAAMnagkeDDEKISVREFITKLDEKMELLNMKEEMAERYLNegFSGGEKKRNEIL 157
Cdd:PRK13642 82 KIG--MVFQNPdNQFVGATVEDDVAFGM-----ENQGIPREEMIKRVDEALLAVNMLDFKTREPAR--LSGGQKQRVAVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038778719 158 QLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRgEGFGAMIITHYQRLLNYITPDVVHVMMEGRVVLSGGP 230
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIK-EKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAP 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-241 |
1.13e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 51.03 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPnyEVTKGEVLFDGVNILELEVDERARM 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDP--RATSGRIVFDGKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 GLFLAMQYPSEIPGITNAEFLraAMNAGKEDDEkisvrEFITKLDEKMELL-NMKEEMAERylNEGFSGGEKKRNEILQL 159
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENL--AMGGFFAERD-----QFQERIKWVYELFpRLHERRIQR--AGTMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 160 LMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGfgaMIITHYQRLLNYI--TPDVVHVMMEGRVVL--SGGPELAAR 235
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQG---MTIFLVEQNANQAlkLADRGYVLENGHVVLedTGDALLANE 228
|
....*.
gi 2038778719 236 LEREGY 241
Cdd:PRK11614 229 AVRSAY 234
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
21-228 |
1.19e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.47 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 21 GVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNpnYEVTKGEVLFDG-----VNILELEVDER---ARMGLFLAMQYPsei 92
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSAR--LAPDAGEVHYRMrdgqlRDLYALSEAERrrlLRTEWGFVHQHP--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 93 pgitnAEFLRAAMNAGKEDDEK---ISVREFITKLDEKMELLNMKEEMAERY--LNEGFSGGEKKRNEILQLLMLEPTFA 167
Cdd:PRK11701 99 -----RDGLRMQVSAGGNIGERlmaVGARHYGDIRATAGDWLERVEIDAARIddLPTTFSGGMQQRLQIARNLVTHPRLV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038778719 168 LLDEIDSGLDidalkvVSkgVNA-----MRG----EGFGAMIITH---YQRLLnyitPDVVHVMMEGRVVLSG 228
Cdd:PRK11701 174 FMDEPTGGLD------VS--VQArlldlLRGlvreLGLAVVIVTHdlaVARLL----AHRLLVMKQGRVVESG 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-203 |
1.24e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDG--VNILelevDERARMGLFLAM--QYPSEIPG 94
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYG--LYQPDSGEILIDGkpVRIR----SPRDAIALGIGMvhQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 95 ITNAEflraamN--AGKEDdekisVREFITKLDEKMELLnmkEEMAERYlneGF-----------SGGEKKRNEILQLLM 161
Cdd:COG3845 95 LTVAE------NivLGLEP-----TKGGRLDRKAARARI---RELSERY---GLdvdpdakvedlSVGEQQRVEILKALY 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2038778719 162 LEPTFALLDEIDSGL---DIDALKVVskgVNAMRGEGFGAMIITH 203
Cdd:COG3845 158 RGARILILDEPTAVLtpqEADELFEI---LRRLAAEGKSIIFITH 199
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
15-231 |
1.33e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 51.76 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 15 GKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEVTKgevlfdgVNILELEVDER---ARMGLFLAMQYPSE 91
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGK-------ITVLGVPVPARarlARARIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 92 IPGITNAEFLRA-----AMNAGKEDDEKISVREFI---TKLDEKMELLnmkeemaerylnegfSGGEKKRNEILQLLMLE 163
Cdd:PRK13536 126 DLEFTVRENLLVfgryfGMSTREIEAVIPSLLEFArleSKADARVSDL---------------SGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038778719 164 PTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHY----QRLLnyitpDVVHVMMEGRVVLSGGPE 231
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFmeeaERLC-----DRLCVLEAGRKIAEGRPH 257
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-177 |
1.46e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.86 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 15 GKEILKGVNLTLKTGEIAAIMGPNGTGKSTLsAAIMGNPNYEVTkGEVLF-DGVNI----LELEVDER--ARMGLFLAMQ 87
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTL-LRIMAGVDKDFN-GEARPqPGIKVgylpQEPQLDPTktVRENVEEGVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 88 ypsEIPGITnAEFLRAAMNAGKEDDEKISVREFITKLDEKMEL-----LNMKEEMAERYLN--------EGFSGGEKKRN 154
Cdd:TIGR03719 95 ---EIKDAL-DRFNEISAKYAEPDADFDKLAAEQAELQEIIDAadawdLDSQLEIAMDALRcppwdadvTKLSGGERRRV 170
|
170 180
....*....|....*....|...
gi 2038778719 155 EILQLLMLEPTFALLDEIDSGLD 177
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
14-203 |
1.50e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.97 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 14 EGK---EILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNILELEVDERARM---GLFLA 85
Cdd:PRK11629 17 EGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGldTP----TSGDVIFNGQPMSKLSSAAKAELrnqKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 86 MQYPSEIPGITNAEFLRAAMNAGKEDDEKISVREFitkldEKMELLNMKEEMAERylNEGFSGGEKKRNEILQLLMLEPT 165
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMPLLIGKKKPAEINSRAL-----EMLAAVGLEHRANHR--PSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2038778719 166 FALLDEIDSGLDI---DALKVVSKGVNAMRGEGFgaMIITH 203
Cdd:PRK11629 166 LVLADEPTGNLDArnaDSIFQLLGELNRLQGTAF--LVVTH 204
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-207 |
1.65e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.33 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEvtKGEVLFDGVNIlelEVDERARMGL 82
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE--KGEILFERQSI---KKDLCTYQKQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 FLAMQYPSEI-PGIT---NAEFLRAAMNAGKEDDEKISVREFITKLDEKMELLnmkeemaerylnegfSGGEKKRNEILQ 158
Cdd:PRK13540 76 LCFVGHRSGInPYLTlreNCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLL---------------SSGQKRQVALLR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2038778719 159 LLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGfGAMIITHYQRL 207
Cdd:PRK13540 141 LWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKG-GAVLLTSHQDL 188
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-80 |
1.88e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.96 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEIEGKE----ILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPNYEVTKGEVLFDGVNILELEV 74
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDgwvkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtKDNWRVTADRMRFDDIDLLRLSP 80
|
....*.
gi 2038778719 75 DERARM 80
Cdd:PRK15093 81 RERRKL 86
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
5-188 |
1.91e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.77 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 5 EIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEVTKGEVLFDGvniLELEVDERARMGLFL 84
Cdd:PLN03140 882 EMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISG---FPKKQETFARISGYC 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 85 AmQYPSEIPGITNAE------FLRAAMNAGKEddEKISvreFITKLDEKMELLNMKEEMAERYLNEGFSGGEKKRNEILQ 158
Cdd:PLN03140 959 E-QNDIHSPQVTVREsliysaFLRLPKEVSKE--EKMM---FVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAV 1032
|
170 180 190
....*....|....*....|....*....|
gi 2038778719 159 LLMLEPTFALLDEIDSGLDIDALKVVSKGV 188
Cdd:PLN03140 1033 ELVANPSIIFMDEPTSGLDARAAAIVMRTV 1062
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
2.17e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.52 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 2 SVLEIKDLHVEIEGKE--ILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPnyEVTKGEVLFDGVNILELEVDE-RA 78
Cdd:PRK13648 6 SIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIE--KVKSGEIFYNNQAITDDNFEKlRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 79 RMGLFLamQYPSEipgitnaEFLRAAMN---AGKEDDEKISVREFITKLDEKMELLNMKEEmaERYLNEGFSGGEKKRNE 155
Cdd:PRK13648 84 HIGIVF--QNPDN-------QFVGSIVKydvAFGLENHAVPYDEMHRRVSEALKQVDMLER--ADYEPNALSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038778719 156 ILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMI-ITHyqRLLNYITPDVVHVMMEGRVVLSGGPE 231
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIIsITH--DLSEAMEADHVIVMNKGTVYKEGTPT 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-238 |
2.54e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 50.27 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 15 GKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEvlfdgVNILELEVDERARMGLFLAMQYPSEI-- 92
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMG--FVRLASGK-----ISILGQPTRQALQKNLVAYVPQSEEVdw 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 93 --PGIT----------NAEFLRAAmnagKEDDEKIsvrefitkLDEKMELLNMkEEMAERYLNEgFSGGEKKRNEILQLL 160
Cdd:PRK15056 92 sfPVLVedvvmmgrygHMGWLRRA----KKRDRQI--------VTAALARVDM-VEFRHRQIGE-LSGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 161 MLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYqrlLNYITPDVVH-VMMEGRVVLSGGPE---LAARL 236
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN---LGSVTEFCDYtVMVKGTVLASGPTEttfTAENL 234
|
..
gi 2038778719 237 ER 238
Cdd:PRK15056 235 EL 236
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-224 |
2.89e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNpnYEVTKGEVLFDG----------------VNILElevdERARMGL 82
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGA--LPRTSGYVTLDGhevvtrspqdglangiVYISE----DRKRDGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 FLAMQYpSEIPGITNAEFLRAAMNAGKEDDEKISVREFItkldekmELLNMKEEMAERYLNEgFSGGEKKRNEILQLLML 162
Cdd:PRK10762 342 VLGMSV-KENMSLTALRYFSRAGGSLKHADEQQAVSDFI-------RLFNIKTPSMEQAIGL-LSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038778719 163 EPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGamIIthyqrLLNYITPDV------VHVMMEGRV 224
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLS--II-----LVSSEMPEVlgmsdrILVMHEGRI 473
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-78 |
3.19e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 49.49 E-value: 3.19e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERA 78
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAG--LLPPAAGTIKLDGGDIDDPDVAEAC 75
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-231 |
3.58e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 50.18 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 16 KEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG------NPNYEVTkgevlFDGVNILELEV-DERARMGlfLAMQY 88
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddNPNSKIT-----VDGITLTAKTVwDIREKVG--IVFQN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 89 PseipgitNAEFLRAAMnagkEDD-------EKISVREFITKLDEKMELLNMKEEMAERYLNegFSGGEKKRNEILQLLM 161
Cdd:PRK13640 93 P-------DNQFVGATV----GDDvafglenRAVPRPEMIKIVRDVLADVGMLDYIDSEPAN--LSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038778719 162 LEPTFALLDEIDSGLDIDA----LKVVSKgvnAMRGEGFGAMIITHyqRLLNYITPDVVHVMMEGRVVLSGGPE 231
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGkeqiLKLIRK---LKKKNNLTVISITH--DIDEANMADQVLVLDDGKLLAQGSPV 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-231 |
4.16e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 49.71 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 8 DLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLsAAIMGNPNYEVT----KGEVLFDGVNILELE--VDERARMG 81
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTF-LRTLNRMNDKVSgyrySGDVLLGGRSIFNYRdvLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 82 LFLamQYPSEIPGITNAEFLraamnAGKEDDEKISVREFITKLDEKMELLNMKEEMAERYLNEGF--SGGEKKRNEILQL 159
Cdd:PRK14271 105 MLF--QRPNPFPMSIMDNVL-----AGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFrlSGGQQQLLCLART 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038778719 160 LMLEPTFALLDEIDSGLDIDALKVVSKGVNAMrGEGFGAMIITHYQRLLNYITpDVVHVMMEGRVVLSGGPE 231
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARIS-DRAALFFDGRLVEEGPTE 247
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-121 |
5.51e-07 |
|
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: 49.07 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 10 HVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVlfdgvnilelEVDERARMGLFLAMQYP 89
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAG--IYPPDSGTV----------TVRGRVSSLLGLGGGFN 96
|
90 100 110
....*....|....*....|....*....|...
gi 2038778719 90 SEIPGITNAEFLRAAMNA-GKEDDEKIsvrEFI 121
Cdd:cd03220 97 PELTGRENIYLNGRLLGLsRKEIDEKI---DEI 126
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-177 |
6.04e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 49.31 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEvtKGEVLFDGVNIlELEVDERArmglf 83
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ--HGSITLDGKPV-EGPGAERG----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LAMQYPSEIPG---ITNAEFLRAAMNAGKEDDEKISvREFITKLDekmellnmKEEMAERYLNEgFSGGEKKRNEILQLL 160
Cdd:PRK11248 74 VVFQNEGLLPWrnvQDNVAFGLQLAGVEKMQRLEIA-HQMLKKVG--------LEGAEKRYIWQ-LSGGQRQRVGIARAL 143
|
170
....*....|....*..
gi 2038778719 161 MLEPTFALLDEIDSGLD 177
Cdd:PRK11248 144 AANPQLLLLDEPFGALD 160
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-231 |
6.31e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEI--EGKEI--LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIM---GNPNYEVTKGEVLFDGVN--ILELE 73
Cdd:PRK10261 12 VLAVENLNIAFmqEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMrllEQAGGLVQCDKMLLRRRSrqVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 74 VDERARM----GLFLAMQY--------PSEIPGITNAEFLRAAMNAGKEDdekiSVREFITKLDEKMelLNMKEEMAERY 141
Cdd:PRK10261 92 EQSAAQMrhvrGADMAMIFqepmtslnPVFTVGEQIAESIRLHQGASREE----AMVEAKRMLDQVR--IPEAQTILSRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 142 LNEgFSGGEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGE-GFGAMIITHYQRLLNYITpDVVHVMM 220
Cdd:PRK10261 166 PHQ-LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIA-DRVLVMY 243
|
250
....*....|.
gi 2038778719 221 EGRVVLSGGPE 231
Cdd:PRK10261 244 QGEAVETGSVE 254
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
19-171 |
8.99e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.59 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDE-RArmgLFLAMqypseipgITN 97
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTG--LYQPQSGEILLDGKPVTAEQPEDyRK---LFSAV--------FTD 405
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038778719 98 AE-FLRAAMNAGKEDDEKIsvrefitkLDEKMELLNMKEEMAE---RYLNEGFSGGEKKRNEILQLLMLEPTFALLDE 171
Cdd:PRK10522 406 FHlFDQLLGPEGKPANPAL--------VEKWLERLKMAHKLELedgRISNLKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-177 |
9.55e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 49.26 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLFDGVNILEL---EVDERARMGLFLAMQYPSEIPGI 95
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLL--NRLIEPTRGQVLIDGVDIAKIsdaELREVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 96 T---NAEF-LRAAMNAGKEDDEKisvrefitKLDEKMELlnMKEEMAERYLNEgFSGGEKKRNEILQLLMLEPTFALLDE 171
Cdd:PRK10070 122 TvldNTAFgMELAGINAEERREK--------ALDALRQV--GLENYAHSYPDE-LSGGMRQRVGLARALAINPDILLMDE 190
|
....*.
gi 2038778719 172 IDSGLD 177
Cdd:PRK10070 191 AFSALD 196
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-115 |
9.62e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 48.26 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG-NPNYEvtkGEVLFDGVNILELEvDERARMG 81
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGlARPDA---GEVLWQGEPIRRQR-DEYHQDL 76
|
90 100 110
....*....|....*....|....*....|....*....
gi 2038778719 82 LFLAMQypseiPGI----TNAEFLRAAMN-AGKEDDEKI 115
Cdd:PRK13538 77 LYLGHQ-----PGIktelTALENLRFYQRlHGPGDDEAL 110
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-225 |
1.12e-06 |
|
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: 49.05 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEVTKGEVLFDGVNILELEVDERARMGL 82
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 FLAMQYPSEIPGITNAE--FL--RAAMNAGKEDDEkisvrEFITKLDEKMELLNMKEEMAERYLNEgFSGGEKKRNEILQ 158
Cdd:TIGR02633 81 VIIHQELTLVPELSVAEniFLgnEITLPGGRMAYN-----AMYLRAKNLLRELQLDADNVTRPVGD-YGGGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038778719 159 LLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITpDVVHVMMEGRVV 225
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVC-DTICVIRDGQHV 220
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-218 |
1.13e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 6 IKDLHVE-----IEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTL-----SAAIMGNP-NYEV--TKGEVLFDGVNILEL 72
Cdd:PLN03073 175 IKDIHMEnfsisVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFlrymaMHAIDGIPkNCQIlhVEQEVVGDDTTALQC 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 73 EVD---ERARM----GLFLAMQYPSEIPGITNAeflraAMNAGKEDDEKISVREFITKLDEKMEL--------------- 130
Cdd:PLN03073 255 VLNtdiERTQLleeeAQLVAQQRELEFETETGK-----GKGANKDGVDKDAVSQRLEEIYKRLELidaytaearaasila 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 131 -LNMKEEMAERYLNEgFSGGEKKRNEILQLLMLEPTFALLDEIDSGLDIDAL----KVVSKGVNAMrgegfgaMIITHYQ 205
Cdd:PLN03073 330 gLSFTPEMQVKATKT-FSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVlwleTYLLKWPKTF-------IVVSHAR 401
|
250
....*....|...
gi 2038778719 206 RLLNYITPDVVHV 218
Cdd:PLN03073 402 EFLNTVVTDILHL 414
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-244 |
1.35e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.86 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEGKEI--LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLFDGVNILELEVdERARMG 81
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLL--TRFYDIDEGEILLDGHDLRDYTL-ASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 82 LFLAMQ--------------YPSEiPGITNAEFLRAAMNAgkeddekiSVREFITKLDEKMELLnMKEEMAErylnegFS 147
Cdd:PRK11176 419 VALVSQnvhlfndtianniaYART-EQYSREQIEEAARMA--------YAMDFINKMDNGLDTV-IGENGVL------LS 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 148 GGEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGfGAMIITHyqRLLNYITPDVVHVMMEGRVVLS 227
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAH--RLSTIEKADEILVVEDGEIVER 559
|
250
....*....|....*...
gi 2038778719 228 GGPelAARLEREG-YAKL 244
Cdd:PRK11176 560 GTH--AELLAQNGvYAQL 575
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
54-188 |
2.26e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.49 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 54 NYEVTK--GEVLFDGVNILELEVdeRARMGLFLAMqypSEIPGITNAEfLRAAMNAGKEDDEKISVREF--ITKLDEKME 129
Cdd:PTZ00265 1269 DSTVFKnsGKILLDGVDICDYNL--KDLRNLFSIV---SQEPMLFNMS-IYENIKFGKEDATREDVKRAckFAAIDEFIE 1342
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2038778719 130 LLNMKEEMAERYLNEGFSGGEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGV 188
Cdd:PTZ00265 1343 SLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-203 |
2.69e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.47 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAI--MGN--PNYEVtKGEVLFDGVNILELEVDE-- 76
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDliPGFRV-EGKVTFHGKNLYAPDVDPve 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 77 -RARMGlfLAMQYPSEIP-GITNAEFLRAAMNAGKED-DEKI--SVREFITkLDEkmellnMKEEMAERYLNegFSGGEK 151
Cdd:PRK14243 89 vRRRIG--MVFQKPNPFPkSIYDNIAYGARINGYKGDmDELVerSLRQAAL-WDE------VKDKLKQSGLS--LSGGQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2038778719 152 KRNEILQLLMLEPTFALLDEIDSGLD-IDALKVvsKGVNAMRGEGFGAMIITH 203
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDpISTLRI--EELMHELKEQYTIIIVTH 208
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
17-210 |
2.99e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 17 EILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLF-DGVNILELEVDE-RARMGL------------ 82
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLI--ERLYDPTEGDIIInDSHNLKDINLKWwRSKIGVvsqdpllfsnsi 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 ---------------FLAMQYPSE-------------------------IPGITNAEFLRAAMNAGKEDD-------EKI 115
Cdd:PTZ00265 477 knnikyslyslkdleALSNYYNEDgndsqenknkrnscrakcagdlndmSNTTDSNELIEMRKNYQTIKDsevvdvsKKV 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 116 SVREFITKLDEKMELLNMKEEmaerylnEGFSGGEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRG-E 194
Cdd:PTZ00265 557 LIHDFVSALPDKYETLVGSNA-------SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnE 629
|
250
....*....|....*.
gi 2038778719 195 GFGAMIITHYQRLLNY 210
Cdd:PTZ00265 630 NRITIIIAHRLSTIRY 645
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-230 |
3.30e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 47.11 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 2 SVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPNyevtKGEVLFDGVNILELEVDERAR 79
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGltHPD----AGSISLCGEPVPSRARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 80 MGlfLAMQYPSEIPGITNAEFLRA-----AMNAGkeddekiSVREFITKLDEKMELlnmkEEMAERYLNEgFSGGEKKRN 154
Cdd:PRK13537 82 VG--VVPQFDNLDPDFTVRENLLVfgryfGLSAA-------AARALVPPLLEFAKL----ENKADAKVGE-LSGGMKRRL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 155 EILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHY----QRLLNYITpdvvhVMMEGRVVLSGGP 230
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFmeeaERLCDRLC-----VIEEGRKIAEGAP 222
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-177 |
3.74e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEI----EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEV-TKGEVLfdgVNILELEVDER 77
Cdd:TIGR00956 759 IFHWRNLTYEVkikkEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGViTGGDRL---VNGRPLDSSFQ 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 78 ARMGlfLAMQYPSEIPGITNAEFLR--AAMNAGKEddekISVREFITKLDEKMELLNMkEEMAERYL---NEGFSGGEKK 152
Cdd:TIGR00956 836 RSIG--YVQQQDLHLPTSTVRESLRfsAYLRQPKS----VSKSEKMEYVEEVIKLLEM-ESYADAVVgvpGEGLNVEQRK 908
|
170 180
....*....|....*....|....*.
gi 2038778719 153 RNEILQLLMLEPTFAL-LDEIDSGLD 177
Cdd:TIGR00956 909 RLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-81 |
4.22e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 47.03 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVnilELEVDERARM 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGilAP----DSGEVLWDGE---PLDPEDRRRI 73
|
.
gi 2038778719 81 G 81
Cdd:COG4152 74 G 74
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-228 |
4.22e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.54 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 22 VNLTLKTGEIAAIMGPNGTGKSTLSAAIMgnPNYEVTKGEVLFDGVNILELEVDE----RARMGLFLAMQYPSEIP---- 93
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALL--RLVESQGGEIIFNGQRIDTLSPGKlqalRRDIQFIFQDPYASLDPrqtv 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 94 GITNAEFLRA-AMNAGKEDDEKISvrefitkldEKMELLNMKEEMAERYLNEgFSGGEKKRNEILQLLMLEPTFALLDEI 172
Cdd:PRK10261 421 GDSIMEPLRVhGLLPGKAAAARVA---------WLLERVGLLPEHAWRYPHE-FSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2038778719 173 DSGLDIDAL-KVVSKGVNAMRGEGFGAMIITHYQRLLNYITPDVVhVMMEGRVVLSG 228
Cdd:PRK10261 491 VSALDVSIRgQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVA-VMYLGQIVEIG 546
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-230 |
5.32e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.54 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKST---LSAAIMGNPNYEVTKGEVLFDGvNILELEVDERARMGLFLAMQYPSE--IP 93
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTmiqLTNGLIISETGQTIVGDYAIPA-NLKKIKEVKRLRKEIGLVFQFPEYqlFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 94 GITNAEFLRAAMNAGKEDDEKISvrefitKLDEKMELLNMKEEMAERYLNEgFSGGEKKRNEILQLLMLEPTFALLDEID 173
Cdd:PRK13645 106 ETIEKDIAFGPVNLGENKQEAYK------KVPELLKLVQLPEDYVKRSPFE-LSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2038778719 174 SGLDIDALK-VVSKGVNAMRGEGFGAMIITHYQRLLNYITPDVVhVMMEGRVVLSGGP 230
Cdd:PRK13645 179 GGLDPKGEEdFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVI-VMHEGKVISIGSP 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-77 |
5.41e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.76 E-value: 5.41e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038778719 1 MSVLEIKDLHVEIEGK-EILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPnyEVTKGEVLFDGVNILELEVDER 77
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLE--RITSGEIWIGGRVVNELEPADR 76
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-178 |
5.50e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEVTKGEVLFDGVNILELEVDERARMGL 82
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEELQASNIRDTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 FLAMQYPSEIPGITNAE--FL-RAAMNAGKEDDEKISVRefitkLDEKMELLNMKEEMAERYLNEGfsGGEKKRNEI--- 156
Cdd:PRK13549 85 AIIHQELALVKELSVLEniFLgNEITPGGIMDYDAMYLR-----AQKLLAQLKLDINPATPVGNLG--LGQQQLVEIaka 157
|
170 180
....*....|....*....|....*...
gi 2038778719 157 ----LQLLML-EPTFALLD-EIDSGLDI 178
Cdd:PRK13549 158 lnkqARLLILdEPTASLTEsETAVLLDI 185
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-245 |
9.34e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 45.49 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVL-EIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVlfdgvnilelEVDERAR 79
Cdd:PRK09544 1 MTSLvSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLG--LVAPDEGVI----------KRNGKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 80 MG-----LFLAMQYPseipgITNAEFLRAAMNAGKEDDekisvrefitkldekmeLLNMKEEMAERYLN---EGFSGGEK 151
Cdd:PRK09544 69 IGyvpqkLYLDTTLP-----LTVNRFLRLRPGTKKEDI-----------------LPALKRVQAGHLIDapmQKLSGGET 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 152 KRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGE-GFGAMIITHYQRLLNYITPDVV----HVMMEGRV-V 225
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLclnhHICCSGTPeV 206
|
250 260
....*....|....*....|
gi 2038778719 226 LSGGPELAARLEREGYAKLA 245
Cdd:PRK09544 207 VSLHPEFISMFGPRGAEQLG 226
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-62 |
9.98e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 9.98e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2038778719 4 LEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEV 62
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG--ELEPDSGTV 376
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-231 |
1.05e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 45.78 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLFdGVNILELEVDE------RARMGLflAMQYPS-- 90
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHL--NGLLQPTSGTVTI-GERVITAGKKNkklkplRKKVGI--VFQFPEhq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 91 --EIPGITNAEFlrAAMNAG-KEDDEKISVREFItkldekmELLNMKEEMAERYLNEgFSGGEKKRNEILQLLMLEPTFA 167
Cdd:PRK13634 98 lfEETVEKDICF--GPMNFGvSEEDAKQKAREMI-------ELVGLPEELLARSPFE-LSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038778719 168 LLDEIDSGLDidalkvvSKGVNAM--------RGEGFGAMIITH-YQRLLNYitPDVVHVMMEGRVVLSGGPE 231
Cdd:PRK13634 168 VLDEPTAGLD-------PKGRKEMmemfyklhKEKGLTTVLVTHsMEDAARY--ADQIVVMHKGTVFLQGTPR 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
17-228 |
1.16e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 45.39 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 17 EILKGVNLTLKTGEIAAIMGPNGTGKSTL-------------SAAIMGNP-NYEVTKGEVlfdgvNILELevdeRARMGL 82
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLlrvlnllemprsgTLNIAGNHfDFSKTPSDK-----AIREL----RRNVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 83 FLaMQY---------------PSEIPGITNAEFLRAAMnagkeddekisvrefitKLDEKMELlnmkEEMAERY-LNegF 146
Cdd:PRK11124 87 VF-QQYnlwphltvqqnlieaPCRVLGLSKDQALARAE-----------------KLLERLRL----KPYADRFpLH--L 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 147 SGGEKKRNEILQLLMLEPTFALLDEIDSGLD--IDAlKVVSKgVNAMRGEGFGAMIITHYQRLLNYITPDVVHvMMEGRV 224
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDpeITA-QIVSI-IRELAETGITQVIVTHEVEVARKTASRVVY-MENGHI 219
|
....
gi 2038778719 225 VLSG 228
Cdd:PRK11124 220 VEQG 223
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
15-79 |
1.38e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 45.56 E-value: 1.38e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038778719 15 GKEI--LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLFDGVNILELEVDE--RAR 79
Cdd:PRK11153 15 GRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCI--NLLERPTSGRVLVDGQDLTALSEKElrKAR 81
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-241 |
1.50e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.50 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 1 MSVLEIKDLHVEI-EGKEILKGVN---LTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNY--EVTKGEVLFDGVNILELEV 74
Cdd:PRK11022 1 MALLNVDKLSVHFgDESAPFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYpgRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 75 DERARM-GLFLAMQY--------PSEIPGITNAEFLRAAMNAGKEddekisvrefiTKLDEKMELLNM-----KEEMAER 140
Cdd:PRK11022 81 KERRNLvGAEVAMIFqdpmtslnPCYTVGFQIMEAIKVHQGGNKK-----------TRRQRAIDLLNQvgipdPASRLDV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 141 YLNEgFSGGEKKRNEILQLLMLEPTFALLDEIDSGLD--IDAlKVVSKGVNAMRGEGFGAMIITHYQRLLNYITPDVVhV 218
Cdd:PRK11022 150 YPHQ-LSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtIQA-QIIELLLELQQKENMALVLITHDLALVAEAAHKII-V 226
|
250 260
....*....|....*....|...
gi 2038778719 219 MMEGRVVLSGGPELAARLEREGY 241
Cdd:PRK11022 227 MYAGQVVETGKAHDIFRAPRHPY 249
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-219 |
1.51e-05 |
|
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: 45.05 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 27 KTGEIAAIMGPNGTGKSTLSAAIMGN--PNYEVTKGEVLFDGV----------NILELEVDERARMglFLAMQYPSEIPg 94
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKlkPNLGKFDDPPDWDEIldefrgselqNYFTKLLEGDVKV--IVKPQYVDLIP- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 95 itnaeflRAAMNAGKEDDEKISVREFITKLDEKMELlnmkEEMAERYLNEgFSGGEKKRNEILQLLMLEPTFALLDEIDS 174
Cdd:cd03236 101 -------KAVKGKVGELLKKKDERGKLDELVDQLEL----RHVLDRNIDQ-LSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2038778719 175 GLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITpDVVHVM 219
Cdd:cd03236 169 YLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLS-DYIHCL 212
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-45 |
1.78e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 1.78e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTL 45
Cdd:PRK11147 319 VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTL 361
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-66 |
2.01e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.17 E-value: 2.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG---NPNYEvtkGEVLFDG 66
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvypHGSYE---GEILFDG 64
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-230 |
2.30e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.43 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGN------PNYEVTKGEVLFDGVNILELEVDE 76
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggaPRGARVTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 77 RARMGLFLAMQ----YP---SEIPGITNAEFLRAAMNAGKEDDEKIsvrefitklDEKMELLNmKEEMAERYLNEgFSGG 149
Cdd:PRK13547 81 LARLRAVLPQAaqpaFAfsaREIVLLGRYPHARRAGALTHRDGEIA---------WQALALAG-ATALVGRDVTT-LSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 150 EKKRNEILQLL---------MLEPTFALLDEIDSGLDIDALKVVSKGVNAM-RGEGFGAMIITHYQRLLNYiTPDVVHVM 219
Cdd:PRK13547 150 ELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAAR-HADRIAML 228
|
250
....*....|.
gi 2038778719 220 MEGRVVLSGGP 230
Cdd:PRK13547 229 ADGAIVAHGAP 239
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-229 |
2.40e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 44.40 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 17 EILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGvniLELEV------DERARMgLFlamQYPS 90
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAG--MIEPTSGELLIDD---HPLHFgdysyrSQRIRM-IF---QDPS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 91 -------EIPGITNAEfLRAAMNAGKEDDEKisvrefitKLDEKMELLNMKEEMAErYLNEGFSGGEKKRNEILQLLMLE 163
Cdd:PRK15112 98 tslnprqRISQILDFP-LRLNTDLEPEQREK--------QIIETLRQVGLLPDHAS-YYPHMLAPGQKQRLGLARALILR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 164 PTFALLDEIDSGLDidaLKVVSKGVNAM----RGEGFGAMIITHYQRLLNYITpDVVHVMMEGRVVLSGG 229
Cdd:PRK15112 168 PKVIIADEALASLD---MSMRSQLINLMlelqEKQGISYIYVTQHLGMMKHIS-DQVLVMHQGEVVERGS 233
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-69 |
2.93e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 2.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2038778719 12 EIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNI 69
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFG--IYQKDSGSILFQGKEI 62
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-177 |
3.15e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 43.39 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 2 SVLEIKDLHVEIEG----KEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNYEVTKGEVLFDGvniLELEVDER 77
Cdd:cd03232 2 SVLTWKNLNYTVPVkggkRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILING---RPLDKNFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 78 ARMGlfLAMQYPSEIPGITnaeflraamnagkeddekisVREfitkldekmellnmkeemAERY--LNEGFSGGEKKRNE 155
Cdd:cd03232 79 RSTG--YVEQQDVHSPNLT--------------------VRE------------------ALRFsaLLRGLSVEQRKRLT 118
|
170 180
....*....|....*....|..
gi 2038778719 156 ILQLLMLEPTFALLDEIDSGLD 177
Cdd:cd03232 119 IGVELAAKPSILFLDEPTSGLD 140
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-67 |
6.94e-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: 43.63 E-value: 6.94e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2038778719 22 VNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGV 67
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTG--LYRPESGEILLDGQ 394
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
15-181 |
8.23e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 42.55 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 15 GKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNILELEVDERARMGLFLAMQYPSEI 92
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGieRP----SAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 93 PGITNAEFLRAAMN---AGKEDDEkisVREFITKLDEKMELLNMKEEMAERylnegFSGGEKKRNEILQLLMLEPTFALL 169
Cdd:PRK10908 90 LLMDRTVYDNVAIPliiAGASGDD---IRRRVSAALDKVGLLDKAKNFPIQ-----LSGGEQQRVGIARAVVNKPAVLLA 161
|
170
....*....|..
gi 2038778719 170 DEIDSGLDiDAL 181
Cdd:PRK10908 162 DEPTGNLD-DAL 172
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-231 |
9.41e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.59 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 4 LEIKDLHVEIEG--KEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDE-RARM 80
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFR--MVDIFDGKIVIDGIDISKLPLHTlRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 81 GLFLamQYPSEIPGITNAEFlraamnagkeDDEKISVREFITKLDEKMELLNMKEEMA---ERYLNEG---FSGGEKKRN 154
Cdd:cd03288 98 SIIL--QDPILFSGSIRFNL----------DPECKCTDDRLWEALEIAQLKNMVKSLPgglDAVVTEGgenFSVGQRQLF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038778719 155 EILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEgfgAMIITHYQRLLNYITPDVVHVMMEGRVVLSGGPE 231
Cdd:cd03288 166 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD---RTVVTIAHRVSTILDADLVLVLSRGILVECDTPE 239
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-231 |
1.05e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 42.51 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAImgNPNYEVTKGEVLFDGVNIlELEVDERA----RMGLFLAMQYPS---- 90
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHF--NALLKPSSGTITIAGYHI-TPETGNKNlkklRKKVSLVFQFPEaqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 91 EIPGITNAEFlrAAMNAGKEDDE-KISVREFITKLdekmellNMKEEMAERYLNEgFSGGEKKRNEILQLLMLEPTFALL 169
Cdd:PRK13641 100 ENTVLKDVEF--GPKNFGFSEDEaKEKALKWLKKV-------GLSEDLISKSPFE-LSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038778719 170 DEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLNYITPDVVhVMMEGRVVLSGGPE 231
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVL-VLEHGKLIKHASPK 230
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-178 |
1.06e-04 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 42.32 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILElEVDERARMGLFLAMQYPSEIPGITNA 98
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKVHWSNKNESE-PSFEATRSRNRYSVAYAAQKPWLLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 99 EFLRAAMNAGKEDDEKISVREFITKLDEKMELLNM--KEEMAERYLNegFSGGEKKRNEILQLLMLEPTFALLDEIDSGL 176
Cdd:cd03290 94 TVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFgdQTEIGERGIN--LSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
..
gi 2038778719 177 DI 178
Cdd:cd03290 172 DI 173
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-210 |
1.09e-04 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 41.76 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 14 EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNpnYEVTKGEVlfdgvnilelevderarmglflamqypsEIP 93
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL--WPWGSGRI----------------------------GMP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 94 GITNAEFL--RAAMNAGkeddekiSVREFITKLDEKMellnmkeemaerylnegFSGGEKKRNEILQLLMLEPTFALLDE 171
Cdd:cd03223 62 EGEDLLFLpqRPYLPLG-------TLREQLIYPWDDV-----------------LSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|....*....
gi 2038778719 172 IDSGLDIDALKVVskgVNAMRGEGFGAMIITHYQRLLNY 210
Cdd:cd03223 118 ATSALDEESEDRL---YQLLKELGITVISVGHRPSLWKF 153
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
147-209 |
1.22e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.58 E-value: 1.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038778719 147 SGGEKKRNE---ILQLLMLEP-TFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITHYQRLLN 209
Cdd:cd03227 79 SGGEKELSAlalILALASLKPrPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAE 145
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-177 |
2.15e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.27 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 16 KEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpnyevtkgevlfdgvnilELEVDERARMGLFLAMQYPSEIPGI 95
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-------------------ELSHAETSSVVIRGSVAYVPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 96 TNAEFLRAAMNAGKEDDEKISVREFITKLDEKMELLNMKE--EMAERYLNegFSGGEKKRNEILQLLMLEPTFALLDEID 173
Cdd:PLN03232 691 FNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDltEIGERGVN--ISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
....
gi 2038778719 174 SGLD 177
Cdd:PLN03232 769 SALD 772
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-235 |
2.16e-04 |
|
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: 42.24 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 18 ILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMgnPNYEVTKGEVLFDGVNILELEVDErARMGLFLAMQYPSEIPGItn 97
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLF--RINESAEGEIIIDGLNIAKIGLHD-LRFKITIIPQDPVLFSGS-- 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 98 aefLRAAMNA-GKEDDEKI-------SVREFITKLDEKMEllnmkEEMAERylNEGFSGGEKKRNEILQLLMLEPTFALL 169
Cdd:TIGR00957 1376 ---LRMNLDPfSQYSDEEVwwalelaHLKTFVSALPDKLD-----HECAEG--GENLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038778719 170 DEIDSGLDIDALKVVSkgvNAMRGEGFGAMIITHYQRLLNYITPDVVHVMMEGRVVLSGGPE--LAAR 235
Cdd:TIGR00957 1446 DEATAAVDLETDNLIQ---STIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSnlLQQR 1510
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-67 |
2.45e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.82 E-value: 2.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038778719 1 MSVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGV 67
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSG--NYQPDAGSILIDGQ 66
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-203 |
2.60e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 41.61 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 19 LKGVNLTLKTGEIAAIMGPNGTGKST----LSAAIMgnPnyevTKGEVLFDGVNILELEVDERARMGLFLAMQYPSEIPG 94
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTfiehLNALLL--P----DTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKTRFKK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 95 ITNAEFLR---------AAMNAGKEDDEK----------ISVREFITKLDEKMELLNMKEEMAERYLNEgFSGGEKKRNE 155
Cdd:PRK13651 97 IKKIKEIRrrvgvvfqfAEYQLFEQTIEKdiifgpvsmgVSKEEAKKRAAKYIELVGLDESYLQRSPFE-LSGGQKRRVA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2038778719 156 ILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITH 203
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
145-230 |
3.01e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 41.37 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 145 GFSGGEKKRNEILQLLMLEPTFALLDEIDSGLDIDALKVVSKGVNAMRGEGFGAMIITH-YQRLLNyiTPDVVHVMMEGR 223
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHtMEHVLE--VADEVIVMDKGK 253
|
....*..
gi 2038778719 224 VVLSGGP 230
Cdd:PRK13631 254 ILKTGTP 260
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-204 |
3.07e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 41.23 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 16 KEILKGVNLTLKTGEIAAIMGPNGTGKST----LSAAIMgnPnyevTKGEVLFDGVNILELEVDERARMG--------LF 83
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTtikmLTGILV--P----TSGEVRVLGYVPFKRRKEFARRIGvvfgqrsqLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 84 LamqypsEIPGITNAEFLRAAMnagkeddeKISVREFITKLDEKMELLNMKEEMAE--RYLnegfSGGEKKRNEILQLLM 161
Cdd:COG4586 109 W------DLPAIDSFRLLKAIY--------RIPDAEYKKRLDELVELLDLGELLDTpvRQL----SLGQRMRCELAAALL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2038778719 162 LEPTFALLDEIDSGLDidalkVVSKgvNAMRG------EGFGAMII--THY 204
Cdd:COG4586 171 HRPKILFLDEPTIGLD-----VVSK--EAIREflkeynRERGTTILltSHD 214
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-51 |
4.27e-04 |
|
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: 41.07 E-value: 4.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG 51
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG 370
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-224 |
5.51e-04 |
|
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: 40.96 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 22 VNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYE-VTKGEVLFDGVNILELEVDERARMGLFLamqypseIPGITNAEF 100
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFG--AYPgKFEGNVFINGKPVDIRNPAQAIRAGIAM-------VPEDRKRHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 101 LRAAMNAGKedDEKISVRE---FITKLDEKMELLNMKEEMAERYLNE--------GFSGGEKKRNEILQLLMLEPTFALL 169
Cdd:TIGR02633 350 IVPILGVGK--NITLSVLKsfcFKMRIDAAAELQIIGSAIQRLKVKTaspflpigRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2038778719 170 DEIDSGLDIDALKVVSKGVNAMRGEGFGAMII-THYQRLLNyiTPDVVHVMMEGRV 224
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVsSELAEVLG--LSDRVLVIGEGKL 481
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-45 |
6.00e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 40.38 E-value: 6.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2038778719 2 SVLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTL 45
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTL 46
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-177 |
6.30e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 40.15 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 18 ILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPnyEVTKGEVLFDGVNILELEVDERARM---GLFLAMQYPSEIPG 94
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLD--DGSSGEVSLVGQPLHQMDEEARAKLrakHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 95 ITNAEF--LRAAMNAGKEDDEKISVREFITKLDEKMELLNMKEEMaerylnegfSGGEKKRNEILQLLMLEPTFALLDEI 172
Cdd:PRK10584 103 LNALENveLPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQL---------SGGEQQRVALARAFNGRPDVLFADEP 173
|
....*
gi 2038778719 173 DSGLD 177
Cdd:PRK10584 174 TGNLD 178
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-68 |
1.30e-03 |
|
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: 39.45 E-value: 1.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038778719 4 LEIKDLHVEI--EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNyevTKGEVLFDGVN 68
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN---TEGDIQIDGVS 66
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-177 |
1.70e-03 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 38.79 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 23 NLTLKTGEIAAIMGPNGTGKSTLSAAIMG--NPnyevTKGEVLFDGVNILELEVDERARMGLFlamQYPSEIPGITNAEF 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGflTP----ASGSLTLNGQDHTTTPPSRRPVSMLF---QENNLFSHLTVAQN 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038778719 101 LRAAMNAG-KEDDEKisvREFITKLDEKMELlnmkEEMAERyLNEGFSGGEKKRNEILQLLMLEPTFALLDEIDSGLD 177
Cdd:PRK10771 92 IGLGLNPGlKLNAAQ---REKLHAIARQMGI----EDLLAR-LPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-52 |
1.94e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.23 E-value: 1.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2038778719 5 EIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGN 52
Cdd:PRK10938 262 VLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD 309
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-51 |
2.14e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.95 E-value: 2.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2038778719 3 VLEIKDLHVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG 51
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITG 372
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-111 |
2.59e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.35 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 28 TGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDGVNILELEVDERARMGLFLAMQYPSEipGITNAEFLRAAMNA 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAR--ELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS--GELRLRLALALARK 76
|
....
gi 2038778719 108 GKED 111
Cdd:smart00382 77 LKPD 80
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-171 |
3.26e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.56 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 15 GKEILKGVNLTLKTGEIAAIMGPNGTGKSTLsAAIMG--NPNYEvtkGE-VLFDGVNI--LELE--------VDERARMG 81
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTL-LRIMAgvDKEFE---GEaRPAPGIKVgyLPQEpqldpektVRENVEEG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038778719 82 LflamqypSEIPGITnAEFLRAAMNAGKEDDEKISVREFITKLDEKMEL-----LNMKEEMAERYLN--------EGFSG 148
Cdd:PRK11819 95 V-------AEVKAAL-DRFNEIYAAYAEPDADFDALAAEQGELQEIIDAadawdLDSQLEIAMDALRcppwdakvTKLSG 166
|
170 180
....*....|....*....|...
gi 2038778719 149 GEKKRNEILQLLMLEPTFALLDE 171
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDE 189
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-66 |
4.31e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 38.08 E-value: 4.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038778719 3 VLEIKDLHVeiegKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGnpNYEVTKGEVLFDG 66
Cdd:COG1129 256 VLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFG--ADPADSGEIRLDG 313
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
10-51 |
4.92e-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: 37.53 E-value: 4.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2038778719 10 HVEIEGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG 51
Cdd:cd03291 44 NLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILG 85
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-68 |
5.45e-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: 37.97 E-value: 5.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038778719 4 LEIKDLHVEI--EGKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMGNPNyevTKGEVLFDGVN 68
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS---TEGEIQIDGVS 1281
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-51 |
6.45e-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: 37.97 E-value: 6.45e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2038778719 15 GKEILKGVNLTLKTGEIAAIMGPNGTGKSTLSAAIMG 51
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG 474
|
|
| |
