|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-219 |
1.05e-119 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 339.33 E-value: 1.05e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 2 SIIELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTE 81
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 82 ERRSELGFVFQDFHLLPMLNAVENVELPSMWD--TTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINE 159
Cdd:COG1136 83 LRRRHIGFVFQFFNLLPELTALENVALPLLLAgvSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 160 PDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-219 |
8.28e-115 |
|
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: 326.37 E-value: 8.28e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEER 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPMLNAVENVELPSMWDTT--VDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPD 161
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVpkKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 162 VLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-219 |
2.24e-90 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 265.07 E-value: 2.24e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 2 SIIELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTE 81
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 82 ERRSELGFVFQDFHLLPMLNAVENVELPSMWDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPD 161
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 162 VLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-220 |
3.66e-81 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 241.50 E-value: 3.66e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGAEtvvALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEE 82
Cdd:COG2884 1 MIRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSeLGFVFQDFHLLPMLNAVENVELPsMWDTTVDRRE---RAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINE 159
Cdd:COG2884 78 RRR-IGVVFQDFRLLPDRTVYENVALP-LRVTGKSRKEirrRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906108912 160 PDVLLADEPTGNLDQETGRTILEEMTRLKETeNIAIVAITHDEQLV-QYADRVVRIVDGVIQ 220
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVdRMPKRVLELEDGRLV 216
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-217 |
7.67e-76 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 228.00 E-value: 7.67e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEE 82
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDFHLLPMLNAVENVELPSMWD--TTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEP 160
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGkkSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 161 DVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDG 217
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDG 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-212 |
6.25e-72 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 219.19 E-value: 6.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDert 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 eerrseLGFVFQDFHLLPMLNAVENVELP--SMWDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALIN 158
Cdd:COG1116 82 ------RGVVFQEPALLPWLTVLDNVALGleLRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1906108912 159 EPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVV 212
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDvDEAVFLADRVV 210
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-219 |
2.91e-71 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 217.23 E-value: 2.91e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 2 SIIELDSVVKRYESGaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTE 81
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 82 ERRsELGFVFQDFHLLPMLNAVENV---ELP--SMWDT-----TVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVA 151
Cdd:COG3638 78 LRR-RIGMIFQQFNLVPRLSVLTNVlagRLGrtSTWRSllglfPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906108912 152 IARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLV-QYADRVVRIVDGVI 219
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLArRYADRIIGLRDGRV 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-219 |
2.41e-70 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 218.02 E-value: 2.41e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEE 82
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSeLGFVFQDFHLLPMLNAVENVELP---SMWDTtVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINE 159
Cdd:COG1135 81 RRK-IGMIFQHFNLLSSRTVAENVALPleiAGVPK-AEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 160 PDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQY-ADRVVRIVDGVI 219
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGRI 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-212 |
5.50e-69 |
|
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: 210.41 E-value: 5.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDerteer 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 rseLGFVFQDFHLLPMLNAVENVELP--SMWDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPD 161
Cdd:cd03293 75 ---RGYVFQQDALLPWLTVLDNVALGleLQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1906108912 162 VLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVV 212
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDiDEAVFLADRVV 203
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-219 |
1.15e-66 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 216.51 E-value: 1.15e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 2 SIIELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTE 81
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 82 ERRSELGFVFQDFHLLPMLNAVENVELPSMWD--TTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINE 159
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAglERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 160 PDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVaITHDEQLVQYADRVVRIVDGVI 219
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII-VTHDPQVAAQAERVIEIRDGEI 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-219 |
1.22e-66 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 205.23 E-value: 1.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYesGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERteE 82
Cdd:COG1126 1 MIEIENLHKSF--GDLEV--LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDIN--K 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDFHLLPMLNAVENVELPSMWDTTVDR---RERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINE 159
Cdd:COG1126 75 LRRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKaeaEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 160 PDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHDEQLV-QYADRVVRIVDGVI 219
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAK-EGMTMVVVTHEMGFArEVADRVVFMDGGRI 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-219 |
1.74e-65 |
|
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: 202.04 E-value: 1.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEE 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRsELGFVFQDFHLLPMLNAVENVELP---SMWDTTvDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINE 159
Cdd:cd03258 81 RR-RIGMIFQHFNLLSSRTVFENVALPleiAGVPKA-EIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 160 PDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLV-QYADRVVRIVDGVI 219
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVkRICDRVAVMEKGEV 219
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-217 |
1.80e-65 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 201.32 E-value: 1.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGAEtvvALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEE 82
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVA---ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSeLGFVFQDFHLLPMLNAVENVELP---SMWDTTvDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINE 159
Cdd:TIGR02673 78 RRR-IGVVFQDFRLLPDRTVYENVALPlevRGKKER-EIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906108912 160 PDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAiTHDEQLV-QYADRVVRIVDG 217
Cdd:TIGR02673 156 PPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVA-THDLSLVdRVAHRVIILDDG 213
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
23-219 |
1.69e-63 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 196.39 E-value: 1.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEERRSeLGFVFQDFHLLPMLNA 102
Cdd:TIGR02982 21 LFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLRRR-IGYIFQAHNLLGFLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 103 VENVEL-----PSMwdTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETG 177
Cdd:TIGR02982 100 RQNVQMalelqPNL--SYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSG 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1906108912 178 RTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:TIGR02982 178 RDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-220 |
2.26e-63 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 196.58 E-value: 2.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 2 SIIELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTE 81
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 82 ERRSELGFVFQDFHLLPMLNAVENVELPSMWD--TTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINE 159
Cdd:PRK11629 84 LRNQKLGFIYQFHHLLPDFTALENVAMPLLIGkkKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 160 PDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVIQ 220
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLT 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-219 |
3.03e-63 |
|
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: 195.44 E-value: 3.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYesGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEer 83
Cdd:cd03262 1 IEIKNLHKSF--GDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINEL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPMLNAVENVELPSMWDTTVDRRE---RAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEP 160
Cdd:cd03262 75 RQKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEaeeRALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 161 DVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHDEQLVQ-YADRVVRIVDGVI 219
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAReVADRVIFMDDGRI 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-219 |
4.98e-63 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 195.86 E-value: 4.98e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEaseDERTEER 83
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINK---LKGKALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 --RSELGFVFQDFHLLPMLNAVENV---ELPSM--WDTTVDR-----RERAVDLLRRVGLGERLTHTPDELSGGQQQRVA 151
Cdd:cd03256 75 qlRRQIGMIFQQFNLIERLSVLENVlsgRLGRRstWRSLFGLfpkeeKQRALAALERVGLLDKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906108912 152 IARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLV-QYADRVVRIVDGVI 219
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
22-217 |
1.34e-62 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 194.17 E-value: 1.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEERRSELGFVFQDFHLLPMLN 101
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIILRRELIGYIFQSFNLIPHLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 102 AVENVELPSMWD--TTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRT 179
Cdd:NF038007 100 IFDNVALPLKYRgvAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNARA 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 1906108912 180 ILEEMTRLKETeNIAIVAITHDEQLVQYADRVVRIVDG 217
Cdd:NF038007 180 VLQQLKYINQK-GTTIIMVTHSDEASTYGNRIINMKDG 216
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-220 |
2.34e-62 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 198.01 E-value: 2.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTeaseDERT 80
Cdd:COG3842 3 MPALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT----GLPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 EERRseLGFVFQDFHLLPMLNAVENVELP-SMWDTT-VDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALIN 158
Cdd:COG3842 75 EKRN--VGMVFQDYALFPHLTVAENVAFGlRMRGVPkAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 159 EPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD--EQLVqYADRVVRIVDGVIQ 220
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeEALA-LADRIAVMNDGRIE 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-220 |
3.97e-62 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 193.46 E-value: 3.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 2 SIIELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTE 81
Cdd:PRK10584 5 NIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 82 ERRSELGFVFQDFHLLPMLNAVENVELPSMWDTTVDR--RERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINE 159
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRqsRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 160 PDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVIQ 220
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQ 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-219 |
1.02e-59 |
|
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: 186.94 E-value: 1.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERtEE 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR-KI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDfhllPM--LNAVENVE--------LPSMWDTTVDRRERAVDLLRRVGLGE-RLTHTPDELSGGQQQRVA 151
Cdd:cd03257 80 RRKEIQMVFQD----PMssLNPRMTIGeqiaeplrIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906108912 152 IARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQY-ADRVVRIVDGVI 219
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-220 |
3.71e-59 |
|
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: 185.03 E-value: 3.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERteer 83
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 rsELGFVFQDFHLLPMLNAVENVELP--SMWDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPD 161
Cdd:cd03259 73 --NIGMVFQDYALFPHLTVAENIAFGlkLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 162 VLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVIQ 220
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDqEEALALADRIAVMNEGRIV 210
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
21-214 |
4.42e-59 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 184.74 E-value: 4.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEERRSELGFVFQDFHLLPML 100
Cdd:TIGR03608 12 VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFALIENE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 101 NAVENVELPSMWD--TTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGR 178
Cdd:TIGR03608 92 TVEENLDLGLKYKklSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRD 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1906108912 179 TILEEMTRLKEtENIAIVAITHDEQLVQYADRVVRI 214
Cdd:TIGR03608 172 EVLDLLLELND-EGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-217 |
2.78e-58 |
|
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: 181.62 E-value: 2.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEER 83
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RseLGFVFQDFHLLPMLNAVENVELPsmwdttvdrreravdllrrvglgerlthtpdeLSGGQQQRVAIARALINEPDVL 163
Cdd:cd03229 77 R--IGMVFQDFALFPHLTVLENIALG--------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1906108912 164 LADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDG 217
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDlDEAARLADRVVVLRDG 177
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-219 |
3.55e-58 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 183.65 E-value: 3.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEE 82
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSeLGFVFQDFHLLPMLNAVENV---------ELPSMWDT-TVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAI 152
Cdd:TIGR02315 78 RRR-IGMIFQHYNLIERLTVLENVlhgrlgykpTWRSLLGRfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 153 ARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLV-QYADRVVRIVDGVI 219
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAkKYADRIVGLKAGEI 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
23-219 |
3.62e-58 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 182.32 E-value: 3.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASederTEERRSELGFVFQDFHLLPMlNA 102
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP----PPEWRRQVAYVPQEPALWGG-TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 103 VENVELPSMWDTTVDRRERAVDLLRRVGLGER-LTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTIL 181
Cdd:COG4619 91 RDNLPFPFQLRERKFDRERALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1906108912 182 EEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:COG4619 171 ELLREYLAEEGRAVLWVSHDpEQIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-219 |
1.78e-57 |
|
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: 189.34 E-value: 1.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYES-GAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTE 81
Cdd:COG1123 260 LLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 82 ERRsELGFVFQD-FH-LLPMLNAVENVELPSM---WDTTVDRRERAVDLLRRVGLGERLTH-TPDELSGGQQQRVAIARA 155
Cdd:COG1123 340 LRR-RVQMVFQDpYSsLNPRMTVGDIIAEPLRlhgLLSRAERRERVAELLERVGLPPDLADrYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906108912 156 LINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLV-QYADRVVRIVDGVI 219
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVrYIADRVAVMYDGRI 483
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-219 |
2.34e-57 |
|
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: 181.92 E-value: 2.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEAsedeRTEER 83
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRR----RRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQD----FHllPMLNAVENVELPSMWDTTVDRRERAVDLLRRVGLGER-LTHTPDELSGGQQQRVAIARALIN 158
Cdd:COG1124 78 RRRVQMVFQDpyasLH--PRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906108912 159 EPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQY-ADRVVRIVDGVI 219
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRI 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-219 |
5.49e-57 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 183.85 E-value: 5.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEER 83
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSeLGFVFQDFHLLPMLNAVENVELP---SMWDTTvDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEP 160
Cdd:PRK11153 82 RQ-IGMIFQHFNLLSSRTVFDNVALPlelAGTPKA-EIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 161 DVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLV-QYADRVVRIVDGVI 219
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVkRICDRVAVIDAGRL 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-220 |
4.25e-56 |
|
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: 178.25 E-value: 4.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYesGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEE 82
Cdd:COG1127 5 MIEVRNLTKSF--GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRsELGFVFQDFHLLPMLNAVENVELPSMWDTTVDR---RERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINE 159
Cdd:COG1127 81 RR-RIGMLFQGGALFDSLTVFENVAFPLREHTDLSEaeiRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906108912 160 PDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLV-QYADRVVRIVDGVIQ 220
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAfAIADRVAVLADGKII 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-211 |
2.18e-55 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 176.44 E-value: 2.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYesGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERteE 82
Cdd:PRK09493 1 MIEFKNVSKHF--GPTQV--LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDFHLLPMLNAVENVELPSMW---DTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINE 159
Cdd:PRK09493 75 IRQEAGMVFQQFYLFPHLTALENVMFGPLRvrgASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1906108912 160 PDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHDeqlVQYADRV 211
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHE---IGFAEKV 202
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-215 |
2.32e-54 |
|
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: 176.40 E-value: 2.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDSP--TEGVVRLEGRDVTEASEDER 79
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 80 TEERRSELGFVFQDfhllPM--LNavenvelPSMwdtTV-----------------DRRERAVDLLRRVGL---GERLTH 137
Cdd:COG0444 81 RKIRGREIQMIFQD----PMtsLN-------PVM---TVgdqiaeplrihgglskaEARERAIELLERVGLpdpERRLDR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 138 TPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQY-ADRVV---- 212
Cdd:COG0444 147 YPHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADRVAvmya 226
|
....
gi 1906108912 213 -RIV 215
Cdd:COG0444 227 gRIV 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-220 |
5.47e-54 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 176.42 E-value: 5.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERt 80
Cdd:COG3839 1 MASLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 eerrsELGFVFQDFHLLPMLNAVENVELP-SMWDTTVDRRERAVD-LLRRVGLGERLTHTPDELSGGQQQRVAIARALIN 158
Cdd:COG3839 76 -----NIAMVFQSYALYPHMTVYENIAFPlKLRKVPKAEIDRRVReAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 159 EPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDeqlvQ-----YADRVVRIVDGVIQ 220
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD----QveamtLADRIAVMNDGRIQ 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-219 |
9.71e-54 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 171.44 E-value: 9.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEAsEDERTEER 83
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDL-RGRAIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPMLNAVENVELPsMWDTTVDRRE---RAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEP 160
Cdd:cd03292 77 RRKIGVVFQDFRLLPDRNVYENVAFA-LEVTGVPPREirkRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 161 DVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAiTHDEQLVQ-YADRVVRIVDGVI 219
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA-THAKELVDtTRHRVIALERGKL 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-217 |
4.51e-53 |
|
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: 169.57 E-value: 4.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 5 ELDSVVKRYESGAEtvVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASederTEERR 84
Cdd:cd03225 1 ELKNLSFSYPDGAR--PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS----LKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 85 SELGFVFQD-FHLLPMLNAVENVE--LPSMWDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPD 161
Cdd:cd03225 75 RKVGLVFQNpDDQFFGPTVEEEVAfgLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 162 VLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHDEQLV-QYADRVVRIVDG 217
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLlELADRVIVLEDG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-219 |
1.21e-52 |
|
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: 169.05 E-value: 1.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLdSPTEGVVRLEGRDVTEASederTEE 82
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLnGLL-KPTSGEVLVDGKDITKKN----LRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQD---------------FhllpmlnAVENVELPSmwdttVDRRERAVDLLRRVGLGERLTHTPDELSGGQQ 147
Cdd:COG1122 73 LRRKVGLVFQNpddqlfaptveedvaF-------GPENLGLPR-----EEIRERVEEALELVGLEHLADRPPHELSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 148 QRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDlDLVAELADRVIVLDDGRI 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-220 |
1.75e-52 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 169.02 E-value: 1.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAetvVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEderTEER 83
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP---VELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSeLGFVFQDFHLLPMLNAVENVEL-PSM--WDTTvDRRERAVDLLRRVGLGER--LTHTPDELSGGQQQRVAIARALIN 158
Cdd:cd03295 75 RK-IGYVIQQIGLFPHMTVEENIALvPKLlkWPKE-KIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 159 EPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVIQ 220
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDiDEAFRLADRIAIMKNGEIV 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-219 |
3.03e-52 |
|
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: 169.36 E-value: 3.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 20 VVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEERRSELGFVFQDFHLLPM 99
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 100 LNAVENVELPsMWDTTVD---RRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQET 176
Cdd:cd03294 117 RTVLENVAFG-LEVQGVPraeREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1906108912 177 GRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:cd03294 196 RREMQDELLRLQAELQKTIVFITHDlDEALRLGDRIAIMKDGRL 239
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-219 |
4.68e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 167.93 E-value: 4.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLdSPTEGVVRLEGRDVTEASEderteE 82
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLlGLL-RPTSGEVRVLGEDVARDPA-----E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDFHLLPMLNAVENVE-------LPSmwdttVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARA 155
Cdd:COG1131 71 VRRRIGYVPQEPALYPDLTVRENLRffarlygLPR-----KEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906108912 156 LINEPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYlEEAERLCDRVAIIDKGRI 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-219 |
8.87e-52 |
|
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: 166.91 E-value: 8.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYesGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEER 83
Cdd:cd03261 1 IELRGLTKSF--GGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RsELGFVFQDFHLLPMLNAVENVELPSMWDTTVDR---RERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEP 160
Cdd:cd03261 77 R-RMGMLFQSGALFDSLTVFENVAFPLREHTRLSEeeiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 161 DVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQ-LVQYADRVVRIVDGVI 219
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDtAFAIADRIAVLYDGKI 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-201 |
1.20e-51 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 167.73 E-value: 1.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASedert 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 eerrSELGFVFQDFHLLPMLNAVENVEL-------PSMwdttvDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIA 153
Cdd:COG4525 76 ----ADRGVVFQKDALLPWLNVLDNVAFglrlrgvPKA-----ERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1906108912 154 RALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD 201
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-220 |
8.02e-51 |
|
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: 164.72 E-value: 8.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGaetvVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERteer 83
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 rsELGFVFQDFHLLPMLNAVENVELP-SMWDTTVD-RRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPD 161
Cdd:cd03300 73 --PVNTVFQNYALFPHLTVFENIAFGlRLKKLPKAeIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 162 VLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVIQ 220
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDqEEALTMSDRIAVMNKGKIQ 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-219 |
1.19e-50 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 167.63 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIiELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEaseDERT 80
Cdd:COG1118 1 MSI-EVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT---NLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 EERRseLGFVFQDFHLLPMLNAVENVE--LPSMWDTTVDRRERAVDLLRRV---GLGERLthtPDELSGGQQQRVAIARA 155
Cdd:COG1118 73 RERR--VGFVFQHYALFPHMTVAENIAfgLRVRPPSKAEIRARVEELLELVqleGLADRY---PSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906108912 156 LINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDqEEALELADRVVVMNQGRI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-219 |
1.68e-50 |
|
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: 171.24 E-value: 1.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGaeTVVALKDVDFHAERGEMVVVTGPSGSGKSTMLN-MIGLLDSPTE--GVVRLEGRDVTEASEder 79
Cdd:COG1123 4 LLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLALaLMGLLPHGGRisGEVLLDGRDLLELSE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 80 tEERRSELGFVFQDfhllPM--LNAV-------ENVELPSMwdTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRV 150
Cdd:COG1123 79 -ALRGRRIGMVFQD----PMtqLNPVtvgdqiaEALENLGL--SRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 151 AIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRI 221
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-220 |
2.93e-49 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 162.95 E-value: 2.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERteeR 83
Cdd:COG1125 2 IEFENVTKRYPDG---TVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSeLGFVFQDFHLLPMLNAVENVEL-PSM--WDTTvDRRERAVDLLRRVGL-----GERLthtPDELSGGQQQRVAIARA 155
Cdd:COG1125 76 RR-IGYVIQQIGLFPHMTVAENIATvPRLlgWDKE-RIRARVDELLELVGLdpeeyRDRY---PHELSGGQQQRVGVARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906108912 156 LINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVIQ 220
Cdd:COG1125 151 LAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDiDEALKLGDRIAVMREGRIV 216
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-220 |
3.99e-49 |
|
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: 159.73 E-value: 3.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERteer 83
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 rsELGFVFQDFHLLPMLNAVENVELP----SMWDTTVDRR-ERAVDLLrrvGLGERLTHTPDELSGGQQQRVAIARALIN 158
Cdd:cd03301 73 --DIAMVFQNYALYPHMTVYDNIAFGlklrKVPKDEIDERvREVAELL---QIEHLLDRKPKQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 159 EPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDE-QLVQYADRVVRIVDGVIQ 220
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQvEAMTMADRIAVMNDGQIQ 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-215 |
1.76e-48 |
|
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: 166.01 E-value: 1.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKS-TMLNMIGLLDSP---TEGVVRLEGRDVTEASE 76
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 77 DERTEERRSELGFVFQDfhllPM--LNAVENVEL----PSMWDTTVDR---RERAVDLLRRVGLGE---RLTHTPDELSG 144
Cdd:COG4172 84 RELRRIRGNRIAMIFQE----PMtsLNPLHTIGKqiaeVLRLHRGLSGaaaRARALELLERVGIPDperRLDAYPHQLSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 145 GQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLV-QYADRVV-----RIV 215
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVrRFADRVAvmrqgEIV 236
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-219 |
3.02e-48 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 158.33 E-value: 3.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLN-MIGLLdSPTEGVVRLEGRDVteaseder 79
Cdd:COG1121 4 MPAIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILGLL-PPTSGTVRLFGKPP-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 80 tEERRSELGFVFQDFHL---LPMLnaVENV-------ELPSMWDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQR 149
Cdd:COG1121 71 -RRARRRIGYVPQRAEVdwdFPIT--VRDVvlmgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 150 VAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDlGAVREYFDRVLLLNRGLV 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-217 |
2.17e-46 |
|
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: 151.00 E-value: 2.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASederTEER 83
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD----LESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPMLNAvENVelpsmwdttvdrreravdllrrvglgerlthtpdeLSGGQQQRVAIARALINEPDVL 163
Cdd:cd03228 75 RKNIAYVPQDPFLFSGTIR-ENI-----------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 164 LADEPTGNLDQETGRTILEEMTRLkeTENIAIVAITHDEQLVQYADRVVRIVDG 217
Cdd:cd03228 119 ILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-219 |
3.63e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 152.86 E-value: 3.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIiELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGR--DVTEASEDE 78
Cdd:COG4161 1 MSI-QLKNINCFYGS----HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 79 RTEERRSELGFVFQDFHLLPMLNAVEN-VELPsMW---DTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIAR 154
Cdd:COG4161 76 AIRLLRQKVGMVFQQYNLWPHLTVMENlIEAP-CKvlgLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906108912 155 ALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETEnIAIVAITHDEQLV-QYADRVVRIVDGVI 219
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTG-ITQVIVTHEVEFArKVASQVVYMEKGRI 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-219 |
7.69e-46 |
|
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: 161.16 E-value: 7.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDsPTEGVVRLEGRDVTEASederTEE 82
Cdd:COG2274 474 IELENVSFRYPGDSPPV--LDNISLTIKPGERVAIVGRSGSGKSTLLKLLlGLYE-PTSGRILIDGIDLRQID----PAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDFHLLPMlNAVENVelpSMWDTTVDRrERAVDLLRRVGLGERLTHTPD-----------ELSGGQQQRVA 151
Cdd:COG2274 547 LRRQIGVVLQDVFLFSG-TIRENI---TLGDPDATD-EEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLA 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 152 IARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKetENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-219 |
1.51e-45 |
|
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: 150.79 E-value: 1.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAetvvALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLD----SPTEGVVRLEGRDVTEasEDE 78
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLnRLNDlipgAPDEGEVLLDGKDIYD--LDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 79 RTEERRSELGFVFQDFHLLPMlNAVENVELP----SMWDTTVdRRERAVDLLRRVGLGERL---THtPDELSGGQQQRVA 151
Cdd:cd03260 75 DVLELRRRVGMVFQKPNPFPG-SIYDNVAYGlrlhGIKLKEE-LDERVEEALRKAALWDEVkdrLH-ALGLSGGQQQRLC 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906108912 152 IARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKetENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELK--KEYTIVIVTHNmQQAARVADRTAFLLNGRL 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-219 |
1.76e-45 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 158.78 E-value: 1.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDsPTEGVVRLEGRDVTEASEDERtee 82
Cdd:COG4987 334 LELEDVSFRYPGAGRPV--LDGLSLTLPPGERVAIVGPSGSGKSTLLALLlRFLD-PQSGSITLGGVDLRDLDEDDL--- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 rRSELGFVFQDFHLLpmlnavenvelpsmwDTTV------------DrrERAVDLLRRVGLGERLTHTPDEL-------- 142
Cdd:COG4987 408 -RRRIAVVPQRPHLF---------------DTTLrenlrlarpdatD--EELWAALERVGLGDWLAALPDGLdtwlgegg 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 143 ---SGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMtrLKETENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:COG4987 470 rrlSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL--LEALAGRTVLLITHRLAGLERMDRILVLEDGRI 547
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-212 |
2.43e-45 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 151.43 E-value: 2.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESgaETVVALKDVDFHAERGEMVVVTGPSGSGKSTM-LNMIGLLDsPTEGVVRLEGRDVteaSEDERTEE 82
Cdd:TIGR04520 1 IEVENVSFSYPE--SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaKLLNGLLL-PTSGKVTVDGLDT---LDEENLWE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQD---------------FHLlpmlnavENVELPS--MwdttvdrRERAVDLLRRVGLGERLTHTPDELSGG 145
Cdd:TIGR04520 75 IRKKVGMVFQNpdnqfvgatveddvaFGL-------ENLGVPReeM-------RKRVDEALKLVGMEDFRDREPHLLSGG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 146 QQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQyADRVV 212
Cdd:TIGR04520 141 QKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDmEEAVL-ADRVI 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-219 |
1.01e-44 |
|
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: 149.42 E-value: 1.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYesGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLdSPTEGVVRLEGRDVTEASederTE 81
Cdd:COG1120 1 MLEAENLSVGY--GGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALaGLL-KPSSGEVLLDGRDLASLS----RR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 82 ERRSELGFVFQDFHLLPMLNAVENVEL---P--SMWDTTVDRRERAVD-LLRRVGLGErLTHTP-DELSGGQQQRVAIAR 154
Cdd:COG1120 72 ELARRIAYVPQEPPAPFGLTVRELVALgryPhlGLFGRPSAEDREAVEeALERTGLEH-LADRPvDELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 155 ALINEPDVLLADEPTGNLD----QEtgrtILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDlahqLE----VLELLRRLARERGRTVVMVLHDlNLAARYADRLVLLKDGRI 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-212 |
1.12e-44 |
|
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: 149.42 E-value: 1.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYesGAetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERT 80
Cdd:COG0411 2 DPLLEVRGLTKRF--GG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 EerrseLGFV--FQDFHLLPMLNAVENVEL-----------------PSMWDTTVDRRERAVDLLRRVGLGERLTHTPDE 141
Cdd:COG0411 78 R-----LGIArtFQNPRLFPELTVLENVLVaaharlgrgllaallrlPRARREEREARERAEELLERVGLADRADEPAGN 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906108912 142 LSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLV-QYADRVV 212
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVmGLADRIV 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-220 |
1.52e-44 |
|
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: 148.64 E-value: 1.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIiELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERt 80
Cdd:cd03296 1 MSI-EVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 eerrsELGFVFQDFHLLPMLNAVENV----------ELPSmwdtTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRV 150
Cdd:cd03296 75 -----NVGFVFQHYALFRHMTVFDNVafglrvkprsERPP----EAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 151 AIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVIQ 220
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDqEEALEVADRVVVMNKGRIE 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-169 |
2.98e-44 |
|
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: 145.10 E-value: 2.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTeaseDERTEERRSELGFVFQDFHLLPMLNA 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT----DDERKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 103 VENVELP---SMWDTTVDRReRAVDLLRRVGLGE----RLTHTPDELSGGQQQRVAIARALINEPDVLLADEPT 169
Cdd:pfam00005 77 RENLRLGlllKGLSKREKDA-RAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-220 |
3.00e-44 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 147.59 E-value: 3.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYEsgaetvVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERteer 83
Cdd:COG3840 2 LRLDDLTYRYG------DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 rsELGFVFQDFHLLPMLNAVENVEL---PSMwDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEP 160
Cdd:COG3840 72 --PVSMLFQENNLFPHLTVAQNIGLglrPGL-KLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906108912 161 DVLLADEPTGNLD----QEtgrtILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVIQ 220
Cdd:COG3840 149 PILLLDEPFSALDpalrQE----MLDLVDELCRERGLTVLMVTHDpEDAARIADRVLLVADGRIA 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-219 |
3.87e-44 |
|
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: 145.62 E-value: 3.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGaetvVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLdSPTEGVVRLEGRDVTeasedERTEE 82
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIlGLL-KPDSGEIKVLGKDIK-----KEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDFHLLPMLNAVENVelpsmwdttvdrreravdllrrvglgerlthtpdELSGGQQQRVAIARALINEPDV 162
Cdd:cd03230 71 VKRRIGYLPEEPSLYENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 163 LLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-220 |
4.20e-44 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 147.64 E-value: 4.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTeasedeRTEER 83
Cdd:TIGR00968 1 IEIANISKRFGS----FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDAT------RVHAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPMLNAVENVE--LPSMWDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPD 161
Cdd:TIGR00968 71 DRKIGFVFQHYALFKHLTVRDNIAfgLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 162 VLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVIQ 220
Cdd:TIGR00968 151 VLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDqEEAMEVADRIVVMSNGKIE 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
23-220 |
5.87e-44 |
|
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: 147.10 E-value: 5.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERteerrsELGFVFQDFHLLPMLNA 102
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR------DISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 103 VENVE--LPSMWDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTI 180
Cdd:cd03299 89 YKNIAygLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1906108912 181 LEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDG-VIQ 220
Cdd:cd03299 169 REELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGkLIQ 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-217 |
1.84e-43 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 149.10 E-value: 1.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 25 DVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDV--TEASEDERTEERRseLGFVFQDFHLLPMLNA 102
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLPPHRRR--IGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 103 VENVELpSMWDTTVDRR----ERAVDLLrrvGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGR 178
Cdd:COG4148 95 RGNLLY-GRKRAPRAERrisfDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1906108912 179 TILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDG 217
Cdd:COG4148 171 EILPYLERLRDELDIPILYVSHSlDEVARLADHVVLLEQG 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-219 |
2.03e-43 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 152.99 E-value: 2.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAEtvvALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDsPTEGVVRLEGRDVTEASEDERtee 82
Cdd:COG4988 337 IELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLlGFLP-PYSGSILINGVDLSDLDPASW--- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 rRSELGFVFQDFHLLPMLNAvENVELPSMwDTTVDRRERAvdlLRRVGLGERLTHTPD-------E----LSGGQQQRVA 151
Cdd:COG4988 410 -RRQIAWVPQNPYLFAGTIR-ENLRLGRP-DASDEELEAA---LEAAGLDEFVAALPDgldtplgEggrgLSGGQAQRLA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 152 IARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVaITHDEQLVQYADRVVRIVDGVI 219
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVIL-ITHRLALLAQADRILVLDDGRI 549
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-217 |
2.07e-43 |
|
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: 143.15 E-value: 2.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 5 ELDSVVKRYESGaetvVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTeaseDERTEERR 84
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA----KLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 85 SELGFVFQdfhllpmlnavenvelpsmwdttvdrreravdllrrvglgerlthtpdeLSGGQQQRVAIARALINEPDVLL 164
Cdd:cd00267 73 RRIGYVPQ-------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 165 ADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHDEQLVQ-YADRVVRIVDG 217
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAElAADRVIVLKDG 156
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-201 |
2.68e-43 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 146.10 E-value: 2.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYesGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEG--------RDVTEAS 75
Cdd:COG4598 9 LEVRDLHKSF--GDLEV--LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdRDGELVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 76 EDERTEER-RSELGFVFQDFHLLPMLNAVENV-ELPsmwdTTVDRR------ERAVDLLRRVGLGERLTHTPDELSGGQQ 147
Cdd:COG4598 85 ADRRQLQRiRTRLGMVFQSFNLWSHMTVLENViEAP----VHVLGRpkaeaiERAEALLAKVGLADKRDAYPAHLSGGQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 148 QRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVaITHD 201
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLV-VTHE 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-212 |
4.55e-43 |
|
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: 144.89 E-value: 4.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYesGAetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDerteeR 83
Cdd:cd03219 1 LEVRGLTKRF--GG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-----E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFV--FQDFHLLPMLNAVENVEL------PSMWDTTVDR------RERAVDLLRRVGLGERLTHTPDELSGGQQQR 149
Cdd:cd03219 72 IARLGIGrtFQIPRLFPELTVLENVMVaaqartGSGLLLARARreereaRERAEELLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906108912 150 VAIARALINEPDVLLADEPTGNL-DQETGRTIlEEMTRLKEtENIAIVAITHDEQLV-QYADRVV 212
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLnPEETEELA-ELIRELRE-RGITVLLVEHDMDVVmSLADRVT 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-214 |
6.31e-43 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 144.11 E-value: 6.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKR---YESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEG--VVRLEGR--DVTEAS 75
Cdd:COG4778 4 LLEVENLSKTftlHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGsiLVRHDGGwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 76 EDERTEERRSELGFVFQDFHLLPMLNAVENVELPsMWDTTVDR---RERAVDLLRRVGLGERLTHT-PDELSGGQQQRVA 151
Cdd:COG4778 84 PREILALRRRTIGYVSQFLRVIPRVSALDVVAEP-LLERGVDReeaRARARELLARLNLPERLWDLpPATFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 152 IARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHDEQLV-QYADRVVRI 214
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKA-RGTAIIGIFHDEEVReAVADRVVDV 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-219 |
1.10e-42 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 144.00 E-value: 1.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIiELDSVVKRYesGAETvvALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGR--DVTEASEDE 78
Cdd:PRK11124 1 MSI-QLNGINCFY--GAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 79 RTEERRSELGFVFQDFHLLPMLNAVEN-VELPsMWDTTVDR---RERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIAR 154
Cdd:PRK11124 76 AIRELRRNVGMVFQQYNLWPHLTVQQNlIEAP-CRVLGLSKdqaLARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906108912 155 ALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETeNIAIVAITHDEQLVQ-YADRVVRIVDGVI 219
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARkTASRVVYMENGHI 219
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-212 |
7.57e-42 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 142.98 E-value: 7.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESG-AETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLdSPTEGVVRLEGRDVTeASEDERTE 81
Cdd:TIGR04521 1 IKLKNVSYIYQPGtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLnGLL-KPTSGTVTIDGRDIT-AKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 82 ERRSELGFVFQdF--HLLpmlnavenvelpsmWDTTVDR----------------RERAVDLLRRVGLGER-LTHTPDEL 142
Cdd:TIGR04521 79 DLRKKVGLVFQ-FpeHQL--------------FEETVYKdiafgpknlglseeeaEERVKEALELVGLDEEyLERSPFEL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 143 SGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVV 212
Cdd:TIGR04521 144 SGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVI 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-214 |
8.46e-42 |
|
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: 140.69 E-value: 8.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYesGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVteaseDERTEER 83
Cdd:COG4133 3 LEAENLSCRR--GERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-----RDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPMLNAVENVELPSMWDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVL 163
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 164 LADEPTGNLDQETGRTILEEMTRLKETENIAIVAiTHDEQLVQyADRVVRI 214
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLT-THQPLELA-AARVLDL 202
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-219 |
1.34e-41 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 144.41 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYEsgaeTVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERteer 83
Cdd:TIGR03265 5 LSIDNIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 rsELGFVFQDFHLLPMLNAVENVE--LPSMWDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPD 161
Cdd:TIGR03265 77 --DYGIVFQSYALFPNLTVADNIAygLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906108912 162 VLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:TIGR03265 155 LLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDqEEALSMADRIVVMNHGVI 213
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-217 |
1.42e-41 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 140.78 E-value: 1.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGAEtvvALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEE 82
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRsELGFVFQDFHLLPMLNAVENVELPSMWD--TTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEP 160
Cdd:PRK10908 78 RR-QIGMIFQDHHLLMDRTVYDNVAIPLIIAgaSGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 161 DVLLADEPTGNLDQETGRTIL---EEMTRLketeNIAIVAITHDEQLVQYAD-RVVRIVDG 217
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILrlfEEFNRV----GVTVLMATHDIGLISRRSyRMLTLSDG 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-215 |
4.35e-41 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 142.18 E-value: 4.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYE-------SGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEAS 75
Cdd:COG4608 7 LLEVRDLKKHFPvrgglfgRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 76 EDERTEERRsELGFVFQDfhllPM--LNavenvelPSMwdtTV-----------------DRRERAVDLLRRVGLG-ERL 135
Cdd:COG4608 87 GRELRPLRR-RMQMVFQD----PYasLN-------PRM---TVgdiiaeplrihglaskaERRERVAELLELVGLRpEHA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 136 THTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLD-----QetgrtILEEMTRLKETENIAIVAITHDEQLVQY-AD 209
Cdd:COG4608 152 DRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqaQ-----VLNLLEDLQDELGLTYLFISHDLSVVRHiSD 226
|
250
....*....|.
gi 1906108912 210 RVV-----RIV 215
Cdd:COG4608 227 RVAvmylgKIV 237
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
23-216 |
4.97e-41 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 138.77 E-value: 4.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLN-MIGLLDSP--TEGVVRLEGRDVTEASederTEERRseLGFVFQDFHLLPM 99
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALP----AEQRR--IGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 100 LNAVENV--ELPSMWdTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETG 177
Cdd:COG4136 91 LSVGENLafALPPTI-GRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1906108912 178 RTILE---EMTRlkeTENIAIVAITHDEQLVQYADRVVRIVD 216
Cdd:COG4136 170 AQFREfvfEQIR---QRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-217 |
8.50e-41 |
|
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: 138.75 E-value: 8.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTeerrselgfVFQDFHLLPMLNA 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 103 VENVEL------PSMwdTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQET 176
Cdd:TIGR01184 72 RENIALavdrvlPDL--SKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1906108912 177 GRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDG 217
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDvDEALLLSDRVVMLTNG 191
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-219 |
1.14e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 139.11 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYEsgAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLeGRDVTEASEDERT 80
Cdd:PRK11264 1 MSAIEVKNLVKKFH--GQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTARSLSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 EER-----RSELGFVFQDFHLLPMLNAVENV-ELPSMWDTTV--DRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAI 152
Cdd:PRK11264 76 QKGlirqlRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPkeEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 153 ARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHDEQLVQ-YADRVVRIVDGVI 219
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARdVADRAIFMDQGRI 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-220 |
7.13e-40 |
|
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: 135.89 E-value: 7.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 25 DVDFHAErGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGR--DVTEASEDERTEERRseLGFVFQDFHLLPMLNA 102
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRKKINLPPQQRK--IGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 103 VENVELPSMWDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILE 182
Cdd:cd03297 93 RENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1906108912 183 EMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVIQ 220
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDlSEAEYLADRIVVMEDGRLQ 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-202 |
7.44e-40 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 139.47 E-value: 7.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYesGAETVValKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERteer 83
Cdd:PRK11432 7 VVLKNITKRF--GSNTVI--DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 rsELGFVFQDFHLLPMLNAVENVE--LPSMWDTTVDRRER---AVDLLRRVGLGERLThtpDELSGGQQQRVAIARALIN 158
Cdd:PRK11432 79 --DICMVFQSYALFPHMSLGENVGygLKMLGVPKEERKQRvkeALELVDLAGFEDRYV---DQISGGQQQRVALARALIL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1906108912 159 EPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDE 202
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQ 197
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-220 |
7.69e-40 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 140.08 E-value: 7.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYEsgaeTVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERt 80
Cdd:PRK09452 12 SPLVELRGISKSFD----GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 eerrsELGFVFQDFHLLPMLNAVENV-------ELPSmwdttVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIA 153
Cdd:PRK09452 87 -----HVNTVFQSYALFPHMTVFENVafglrmqKTPA-----AEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 154 RALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVIQ 220
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqEEALTMSDRIVVMRDGRIE 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-219 |
3.32e-39 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 135.58 E-value: 3.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 6 LDSVVKRYesGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERteerrs 85
Cdd:PRK11247 15 LNAVSKRY--GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 86 elgFVFQDFHLLPMLNAVENVELpsmwDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLA 165
Cdd:PRK11247 85 ---LMFQDARLLPWKKVIDNVGL----GLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1906108912 166 DEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-220 |
5.46e-39 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 137.52 E-value: 5.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIiELDSVVKRYesgAETVVaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTeasedeRT 80
Cdd:PRK10851 1 MSI-EIANIKKSF---GRTQV-LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS------RL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 EERRSELGFVFQDFHLLPMLNAVENVelpSMWDTTVDRRER---------AVDLLRRVGLGERLTHTPDELSGGQQQRVA 151
Cdd:PRK10851 70 HARDRKVGFVFQHYALFRHMTVFDNI---AFGLTVLPRRERpnaaaikakVTQLLEMVQLAHLADRYPAQLSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 152 IARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVIQ 220
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDqEEAMEVADRVVVMSQGNIE 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
21-219 |
1.03e-38 |
|
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: 131.79 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLdSPTEGVVRLEGRDVTEASederTEERRSELGFVFQdfhllpm 99
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLaGLL-KPSSGEILLDGKDLASLS----PKELARKIAYVPQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 100 lnavenvelpsmwdttvdrreravdLLRRVGLGErLTHTP-DELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGR 178
Cdd:cd03214 81 -------------------------ALELLGLAH-LADRPfNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1906108912 179 TILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:cd03214 135 ELLELLRRLARERGKTVVMVLHDlNLAARYADRVILLKDGRI 176
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-217 |
1.85e-38 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 133.60 E-value: 1.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTML-NMIGLL--DSPTEGVVRLEGRDVTEASEDER-TEERRSELGFVFQDFHLL 97
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLrHLSGLItgDKSAGSHIELLGRTVQREGRLARdIRKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 98 PMLNAVENVELPSM-----WDT-----TVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADE 167
Cdd:PRK09984 99 NRLSVLENVLIGALgstpfWRTcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 168 PTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDG 217
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQG 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
21-212 |
1.54e-37 |
|
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: 129.96 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDsPTEGVVRLEGRDVteasedertEERRSELGFVFQDFHLLPM 99
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIlGLLK-PTSGSIRVFGKPL---------EKERKRIGYVPQRRSIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 100 LNA-VENVELPSMW-------DTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGN 171
Cdd:cd03235 83 FPIsVRDVVLMGLYghkglfrRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1906108912 172 LDQETGRTILEEMTRLKEtENIAIVAITHDEQLVQ-YADRVV 212
Cdd:cd03235 163 VDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLeYFDRVL 203
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
22-219 |
3.77e-37 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 129.72 E-value: 3.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTMLN----MIGLLDS-PTEGVVRLEGRDVTEASEDerTEERRSELGFVFQDFHL 96
Cdd:TIGR00972 16 ALKNINLDIPKNQVTALIGPSGCGKSTLLRslnrMNDLVPGvRIEGKVLFDGQDIYDKKID--VVELRRRVGMVFQKPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 97 LPMlNAVENVELPSMWDTTVDR---RERAVDLLRRVGLGE----RLTHTPDELSGGQQQRVAIARALINEPDVLLADEPT 169
Cdd:TIGR00972 94 FPM-SIYDNIAYGPRLHGIKDKkelDEIVEESLKKAALWDevkdRLHDSALGLSGGQQQRLCIARALAVEPEVLLLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 170 GNLDQETGRTILEEMTRLKETENIAIVaiTHD-EQLVQYADRVVRIVDGVI 219
Cdd:TIGR00972 173 SALDPIATGKIEELIQELKKKYTIVIV--THNmQQAARISDRTAFFYDGEL 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-219 |
4.57e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 136.06 E-value: 4.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAEtvvALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDsPTEGVVRLEGRDVTEASederTEE 82
Cdd:COG1132 340 IEFENVSFSYPGDRP---VLKDISLTIPPGETVALVGPSGSGKSTLVNLLlRFYD-PTSGRILIDGVDIRDLT----LES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDFHLLPMlNAVENVELpSMWDTTVDRRERAvdlLRRVGLGERLTHTPD-----------ELSGGQQQRVA 151
Cdd:COG1132 412 LRRQIGVVPQDTFLFSG-TIRENIRY-GRPDATDEEVEEA---AKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIA 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 152 IARALINEPDVLLADEPTGNLDQETGRTILEEMTRLkeTENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-211 |
1.29e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 130.47 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 15 SGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERtEERRSELGFVFQDf 94
Cdd:PRK11308 23 KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQ-KLLRQKIQIVFQN- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 95 hllPM--LNAVENV----ELPSMWDTTVD---RRERAVDLLRRVGLgeRLTHT---PDELSGGQQQRVAIARALINEPDV 162
Cdd:PRK11308 101 ---PYgsLNPRKKVgqilEEPLLINTSLSaaeRREKALAMMAKVGL--RPEHYdryPHMFSGGQRQRIAIARALMLDPDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1906108912 163 LLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQY-ADRV 211
Cdd:PRK11308 176 VVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHiADEV 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-219 |
2.42e-36 |
|
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: 125.41 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLN-MIGLLdSPTEGVVRLEGRDVTEASEDerteE 82
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARlILGLL-RPTSGRVRLDGADISQWDPN----E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDFHLLPMLNAvENVelpsmwdttvdrreravdllrrvglgerlthtpdeLSGGQQQRVAIARALINEPDV 162
Cdd:cd03246 74 LGDHVGYLPQDDELFSGSIA-ENI-----------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 163 LLADEPTGNLDQETGRTILEEMTRLKETENIAIVaITHDEQLVQYADRVVRIVDGVI 219
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAAGATRIV-IAHRPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-219 |
2.72e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.59 E-value: 2.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 2 SIIELDSVVKRYESGAETvvALKDVDFHAERGEMVVVTGPSGSGKSTML-NMIGLLDsPTEGVVRLEGRDVTEasedERT 80
Cdd:PRK13635 4 EIIRVEHISFRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAkLLNGLLL-PEAGTITVGGMVLSE----ETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 EERRSELGFVFQD---------------FHLlpmlnavENVELPSmwDTTVDRRERAvdlLRRVGLGERLTHTPDELSGG 145
Cdd:PRK13635 77 WDVRRQVGMVFQNpdnqfvgatvqddvaFGL-------ENIGVPR--EEMVERVDQA---LRQVGMEDFLNREPHRLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 146 QQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEI 218
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-214 |
3.44e-36 |
|
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: 132.80 E-value: 3.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAEtvvALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDsPTEGVVRLEGRDVTEASEDERtee 82
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP---ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLlGFVD-PTEGSIAVNGVPLADADADSW--- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 rRSELGFVFQDFHLLPMLNAvENVEL--PSMWDTTVDRRERAVDLLRRV-----GLGERLTHTPDELSGGQQQRVAIARA 155
Cdd:TIGR02857 395 -RDQIAWVPQHPFLFAGTIA-ENIRLarPDASDAEIREALERAGLDEFVaalpqGLDTPIGEGGAGLSGGQAQRLALARA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906108912 156 LINEPDVLLADEPTGNLDQETGRTILEEMTRLkeTENIAIVAITHDEQLVQYADRVVRI 214
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-220 |
4.68e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 127.39 E-value: 4.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDsvvKRYesGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVT-------- 72
Cdd:PRK10619 6 LNVIDLH---KRY--GEHEV--LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 73 -EASEDERTEERRSELGFVFQDFHLLPMLNAVENV-ELP--SMWDTTVDRRERAVDLLRRVGLGERLTHT-PDELSGGQQ 147
Cdd:PRK10619 79 lKVADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVmEAPiqVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 148 QRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHDEQLVQY-ADRVVRIVDGVIQ 220
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHvSSHVIFLHQGKIE 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-219 |
1.02e-35 |
|
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: 131.73 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 20 VVALKDVDFHAERGEMVVVTGPSGSGKSTM-LNMIGLLdsPTEGVVRLEGRDVTEASEDERTEERRsELGFVFQDfhllP 98
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGLSRRALRPLRR-RMQVVFQD----P 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 99 M--LN-------------AVENVELpsmwdTTVDRRERAVDLLRRVGLGERLTHT-PDELSGGQQQRVAIARALINEPDV 162
Cdd:COG4172 372 FgsLSprmtvgqiiaeglRVHGPGL-----SAAERRARVAEALEEVGLDPAARHRyPHEFSGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 163 LLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQY-ADRVVRIVDGVI 219
Cdd:COG4172 447 LVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKV 504
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-219 |
1.08e-35 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 128.00 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 40 GPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEasedeRTEERRSeLGFVFQDFHLLPMLNAVENVELPSMWDTT--VD 117
Cdd:TIGR01187 3 GPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN-----VPPHLRH-INMVFQSYALFPHMTVEENVAFGLKMRKVprAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 118 RRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVA 197
Cdd:TIGR01187 77 IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180
....*....|....*....|...
gi 1906108912 198 ITHD-EQLVQYADRVVRIVDGVI 219
Cdd:TIGR01187 157 VTHDqEEAMTMSDRIAIMRKGKI 179
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-219 |
1.30e-35 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 125.17 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEasedERTEER 83
Cdd:cd03265 1 IEVENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSeLGFVFQDFHLLPMLNAVENVELPSM-----WDttvDRRERAVDLLRRVGLGE---RLTHTpdeLSGGQQQRVAIARA 155
Cdd:cd03265 73 RR-IGIVFQDLSVDDELTGWENLYIHARlygvpGA---ERRERIDELLDFVGLLEaadRLVKT---YSGGMRRRLEIARS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906108912 156 LINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYmEEAEQLCDRVAIIDHGRI 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-201 |
5.07e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 124.43 E-value: 5.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASederteerrSELGFVFQDFHLLPMLN 101
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG---------AERGVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 102 AVENV----ELPSMwdTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETG 177
Cdd:PRK11248 87 VQDNVafglQLAGV--EKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180
....*....|....*....|....
gi 1906108912 178 RTILEEMTRLKETENIAIVAITHD 201
Cdd:PRK11248 165 EQMQTLLLKLWQETGKQVLLITHD 188
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-219 |
5.80e-35 |
|
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: 123.37 E-value: 5.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 25 DVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTeerrseLGFVFQDFHLLPMLNAVE 104
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP------VSMLFQENNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 105 NVEL---PSMWDTTVDRrERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQetgrTIL 181
Cdd:cd03298 90 NVGLglsPGLKLTAEDR-QAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDP----ALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1906108912 182 EEMTRL-----KETENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:cd03298 165 AEMLDLvldlhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-219 |
1.08e-34 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 123.15 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 27 DFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTeerrseLGFVFQDFHLLPMLNAVENV 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP------VSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 107 EL---PSMwDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEE 183
Cdd:PRK10771 93 GLglnPGL-KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1906108912 184 MTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:PRK10771 172 VSQVCQERQLTLLMVSHSlEDAARIAPRSLVVADGRI 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-217 |
3.27e-34 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 124.84 E-value: 3.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 25 DVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEERRSELGFVFQDFHLLPMLNAVE 104
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 105 NVELpSMWDTTVDRR----ERAVDLLrrvGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTI 180
Cdd:TIGR02142 95 NLRY-GMKRARPSERrisfERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 1906108912 181 LEEMTRLKETENIAIVAITHDEQLVQY-ADRVVRIVDG 217
Cdd:TIGR02142 171 LPYLERLHAEFGIPILYVSHSLQEVLRlADRVVVLEDG 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-217 |
3.96e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 127.06 E-value: 3.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYeSGaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASedeRTEE 82
Cdd:COG1129 4 LLEMRGISKSF-GG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS---PRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDFHLLPMLNAVENV----ELPSMWdtTVDRRE---RAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARA 155
Cdd:COG1129 77 QAAGIAIIHQELNLVPNLSVAENIflgrEPRRGG--LIDWRAmrrRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 156 LINEPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDG 217
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRRLKA-QGVAIIYISHRlDEVFEIADRVTVLRDG 216
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-217 |
4.02e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 125.53 E-value: 4.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEERRSELGFVFQDFHLLPML 100
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 101 NAVEN----VELPSMwdTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQET 176
Cdd:PRK10070 122 TVLDNtafgMELAGI--NAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1906108912 177 GRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDG 217
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNG 241
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-219 |
7.15e-34 |
|
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: 120.55 E-value: 7.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASedertEE 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP-----AE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDFHLLPMLNAVENVE-LPSMWDTTVDRRERAVD-LLRRVGLGERLTHTPDELSGGQQQRVAIARALINEP 160
Cdd:cd03266 76 ARRRLGFVSDSTGLYDRLTARENLEyFAGLYGLKGDELTARLEeLADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 161 DVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHDEQLVQ-YADRVVRIVDGVI 219
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRA-LGKCILFSTHIMQEVErLCDRVVVLHRGRV 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-219 |
1.53e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 121.35 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGAETV--VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVteaSEDERT 80
Cdd:PRK13633 4 MIKCKNVSYKYESNEESTekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDT---SDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 EERRSELGFVFQ-------------DFHLLPmlnavENVELPSMwdttvDRRERAVDLLRRVGLGERLTHTPDELSGGQQ 147
Cdd:PRK13633 81 WDIRNKAGMVFQnpdnqivativeeDVAFGP-----ENLGIPPE-----EIRERVDESLKKVGMYEYRRHAPHLLSGGQK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906108912 148 QRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-219 |
1.56e-33 |
|
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: 121.07 E-value: 1.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 2 SIIELDSVVKRYESGA-----ETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASE 76
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGGlfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 77 DERTEERRsELGFVFQDFH--LLPMLNAVENVELPSMWDTTVD---RRERAVDLLRRVGL-GERLTHTPDELSGGQQQRV 150
Cdd:TIGR02769 81 KQRRAFRR-DVQLVFQDSPsaVNPRMTVRQIIGEPLRHLTSLDeseQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 151 AIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQY-ADRVVRIVDGVI 219
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQI 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-219 |
2.43e-33 |
|
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: 120.19 E-value: 2.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYEsgaETVVaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEG-VVRLEGRDVTEASeder 79
Cdd:COG1119 1 DPLLELRNVTVRRG---GKTI-LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGED---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 80 TEERRSELGFVFQDFHLLPMLNA-VENVELPSMWDT-------TVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVA 151
Cdd:COG1119 73 VWELRKRIGLVSPALQLRFPRDEtVLDVVLSGFFDSiglyrepTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906108912 152 IARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHvEEIPPGITHVLLLKDGRV 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-175 |
3.36e-33 |
|
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: 118.45 E-value: 3.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGaetvVALKDVDFHAERGeMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEasedeRTEER 83
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-----QPQKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPMLNAVENVE----LPSMWDTtvDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINE 159
Cdd:cd03264 71 RRRIGYLPQEFGVYPNFTVREFLDyiawLKGIPSK--EVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170
....*....|....*.
gi 1906108912 160 PDVLLADEPTGNLDQE 175
Cdd:cd03264 149 PSILIVDEPTAGLDPE 164
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
17-212 |
3.53e-33 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 119.05 E-value: 3.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 17 AETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASederTEERRSELGFVFQDfhl 96
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK----PEIYRQQVSYCAQT--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 97 lPML---NAVENVELPsmWDTTVDRRERA--VDLLRRVGLGER-LTHTPDELSGGQQQRVAIARALINEPDVLLADEPTG 170
Cdd:PRK10247 90 -PTLfgdTVYDNLIFP--WQIRNQQPDPAifLDDLERFALPDTiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1906108912 171 NLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVV 212
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-219 |
5.24e-33 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 119.79 E-value: 5.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRY-------ESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTE 73
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgKHQHQTV--LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 74 ASEDERTEERRsELGFVFQDfhllpMLNAV-------ENVELPSMWDTTVDRRERAV---DLLRRVGLG-ERLTHTPDEL 142
Cdd:PRK10419 79 LNRAQRKAFRR-DIQMVFQD-----SISAVnprktvrEIIREPLRHLLSLDKAERLArasEMLRAVDLDdSVLDKRPPQL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 143 SGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQY-ADRVVRIVDGVI 219
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQI 230
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-212 |
6.32e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.71 E-value: 6.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 2 SIIELDSVVKRYESgaETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTeaseDERTE 81
Cdd:PRK13632 6 VMIKVENVSFSYPN--SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS----KENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 82 ERRSELGFVFQD---------------FHLlpmlnavENVELPS--MWDTTVDrreravdLLRRVGLGERLTHTPDELSG 144
Cdd:PRK13632 80 EIRKKIGIIFQNpdnqfigatveddiaFGL-------ENKKVPPkkMKDIIDD-------LAKKVGMEDYLDKEPQNLSG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 145 GQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVV 212
Cdd:PRK13632 146 GQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVI 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-219 |
8.70e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 119.03 E-value: 8.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESG-AETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLdSPTEGVVRLEGRDVTEASEDERT 80
Cdd:COG1101 1 MLELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIaGSL-PPDSGSILIDGKDVTKLPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 eerrSELGFVFQDfhllPMLNAV------ENVELPSM--------WDTTVDRRERAVDLLRRVGLG--ERLTHTPDELSG 144
Cdd:COG1101 80 ----KYIGRVFQD----PMMGTApsmtieENLALAYRrgkrrglrRGLTKKRRELFRELLATLGLGleNRLDTKVGLLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906108912 145 GQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNmEQALDYGNRLIMMHEGRI 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-212 |
2.15e-32 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 120.52 E-value: 2.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYesgAETVVAlKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERt 80
Cdd:PRK11000 1 MASVTLRNVTKAY---GDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 eerrsELGFVFQDFHLLPMLNAVEN----VELPSMWDTTVDRR-ERAVDLLRrvgLGERLTHTPDELSGGQQQRVAIARA 155
Cdd:PRK11000 76 -----GVGMVFQSYALYPHLSVAENmsfgLKLAGAKKEEINQRvNQVAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRT 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 156 LINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDE-QLVQYADRVV 212
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQvEAMTLADKIV 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-216 |
2.72e-32 |
|
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: 116.38 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDsPTEGVVRLEGRDVTEASEDERTeerRSELGFVFQDFHLLPML 100
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTImGLLP-PRSGSIRFDGRDITGLPPHERA---RAGIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 101 NAVENVEL---PSMWDTTVDRRERAVDLLRRvgLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETG 177
Cdd:cd03224 91 TVEENLLLgayARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1906108912 178 RTILEEMTRLKETEnIAIVaithdeqLV-QYADRVVRIVD 216
Cdd:cd03224 169 EEIFEAIRELRDEG-VTIL-------LVeQNARFALEIAD 200
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-219 |
2.78e-32 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 116.50 E-value: 2.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 27 DFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTeerrseLGFVFQDFHLLPMLNAVENV 106
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP------VSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 107 EL---PSMwDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEE 183
Cdd:TIGR01277 92 GLglhPGL-KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1906108912 184 MTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:TIGR01277 171 VKQLCSERQRTLLMVTHHlSDARAIASQIAVVSQGKI 207
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-219 |
5.39e-32 |
|
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: 116.18 E-value: 5.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERteer 83
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPMlNAVENVelpsMWDTTVDRRERAVDLLRRVGLGERLTHTPD-----------ELSGGQQQRVAI 152
Cdd:cd03251 75 RRQIGLVSQDVFLFND-TVAENI----AYGRPGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 153 ARALINEPDVLLADEPTGNLDQETGRTILEEMTRLkeTENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERL--MKNRTTFVIAHRLSTIENADRIVVLEDGKI 214
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-219 |
1.08e-31 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 116.09 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYES-----GAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEAS 75
Cdd:COG4167 2 SALLEVRNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 76 EDERTEERRselgFVFQD--FHLLPMLNAVENVELPSMWDTTVD---RRERAVDLLRRVGL-GERLTHTPDELSGGQQQR 149
Cdd:COG4167 82 YKYRCKHIR----MIFQDpnTSLNPRLNIGQILEEPLRLNTDLTaeeREERIFATLRLVGLlPEHANFYPHMLSSGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 150 VAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQY-ADRVVRIVDGVI 219
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHiSDKVLVMHQGEV 228
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-219 |
1.54e-31 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 117.64 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYESGAEtvvALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERt 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQ---VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 eerrsELGFVFQDFHLLPMLNAVENVE----LPSMWDTTVDRR-ERAVDLLrrvGLGERLTHTPDELSGGQQQRVAIARA 155
Cdd:PRK11650 77 -----DIAMVFQNYALYPHMSVRENMAyglkIRGMPKAEIEERvAEAARIL---ELEPLLDRKPRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 156 LINEPDVLLADEPTGNLD-----------QETGRtileemtRLKETEniaiVAITHDeQL--VQYADRVVRIVDGVI 219
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDaklrvqmrleiQRLHR-------RLKTTS----LYVTHD-QVeaMTLADRVVVMNGGVA 213
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-220 |
1.72e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.27 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEERRSELGFVFQ--------- 92
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQfpehqlfee 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 93 ----DFHLLPMLNAVenvelpsmwdTTVDRRERAVDLLRRVGLGER-LTHTPDELSGGQQQRVAIARALINEPDVLLADE 167
Cdd:PRK13634 102 tvekDICFGPMNFGV----------SEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 168 PTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVIQ 220
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSmEDAARYADQIVVMHKGTVF 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
23-219 |
2.64e-31 |
|
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: 113.51 E-value: 2.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEAsederteERRSELGFVFQD--FHLLpmL 100
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK-------ERRKSIGYVMQDvdYQLF--T 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 101 NAVENVELPSMwDTTVDRRERAVDLLRRVGL-GERLTHtPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRT 179
Cdd:cd03226 87 DSVREELLLGL-KELDAGNEQAETVLKDLDLyALKERH-PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1906108912 180 ILEEMTRLKETENiAIVAITHDEQLVQ-YADRVVRIVDGVI 219
Cdd:cd03226 165 VGELIRELAAQGK-AVIVITHDYEFLAkVCDRVLLLANGAI 204
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-219 |
2.90e-31 |
|
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: 113.84 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYEsgAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDerteER 83
Cdd:cd03245 3 IEFRNVSFSYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPA----DL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLL------------------PMLNAVENVELpsmwDTTVDRRERAVDLLrrvgLGERlthtPDELSGG 145
Cdd:cd03245 77 RRNIGYVPQDVTLFygtlrdnitlgapladdeRILRAAELAGV----TDFVNKHPNGLDLQ----IGER----GRGLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 146 QQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETEniAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:cd03245 145 QRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-219 |
8.83e-31 |
|
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: 110.98 E-value: 8.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLdSPTEGVVRLEGRDVTEASedeRTEE 82
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILsGLY-KPDSGEILVDGKEVSFAS---PRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQdfhllpmlnavenvelpsmwdttvdrreravdllrrvglgerlthtpdeLSGGQQQRVAIARALINEPDV 162
Cdd:cd03216 73 RRAGIAMVYQ-------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 163 LLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRA-QGVAVIFISHRlDEVFEIADRVTVLRDGRV 160
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-220 |
9.23e-31 |
|
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: 112.60 E-value: 9.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGaeTVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEasedERTEER 83
Cdd:cd03263 1 LQIRNLTKTYKKG--TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSeLGFVFQDFHLLPMLNAVENVELPSMWD--TTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPD 161
Cdd:cd03263 75 QS-LGYCPQFDALFDELTVREHLRFYARLKglPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 162 VLLADEPTGNLDQETGRTILEemTRLKETENIAIVAITHD----EQLvqyADRVVRIVDGVIQ 220
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWD--LILEVRKGRSIILTTHSmdeaEAL---CDRIAIMSDGKLR 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-219 |
1.86e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 113.25 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGAEtvvALKDVDFHAERGEMVVVTGPSGSGKSTM-LNMIGLLDsPTEGVVRLEGRDVTEASEDerTE 81
Cdd:PRK13639 1 ILETRDLKYSYPDGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLfLHFNGILK-PTSGEVLIKGEPIKYDKKS--LL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 82 ERRSELGFVFQ-------------DFHLLPMlnaveNVELPSMwdttvDRRERAVDLLRRVGLGERLTHTPDELSGGQQQ 148
Cdd:PRK13639 75 EVRKTVGIVFQnpddqlfaptveeDVAFGPL-----NLGLSKE-----EVEKRVKEALKAVGMEGFENKPPHHLSGGQKK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906108912 149 RVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHDEQLVQ-YADRVVRIVDGVI 219
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPvYADKVYVMSDGKI 215
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-212 |
2.24e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 114.07 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKS-TMLNMIGLLDSP---TEGVVRLEGRDVTEASEDERTEERRSELGFVFQDfhll 97
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQD---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 98 PM--LNAVENVELPSMWDTTV-------DRRERAVDLLRRVGL---GERLTHTPDELSGGQQQRVAIARALINEPDVLLA 165
Cdd:PRK11022 98 PMtsLNPCYTVGFQIMEAIKVhqggnkkTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1906108912 166 DEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLV-QYADRVV 212
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVaEAAHKII 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
23-212 |
3.27e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 112.13 E-value: 3.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLdSPTEGVVRLEGRDVTEASEDERTEER-----RSELGFVFqdfhl 96
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGEL-TPSSGEVRLNGRPLAAWSPWELARRRavlpqHSSLAFPF----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 97 lpmlNAVENVEL---PSMWDTTVDRR--ERAvdlLRRVG---LGERLTHTpdeLSGGQQQRVAIARALI-------NEPD 161
Cdd:COG4559 91 ----TVEEVVALgraPHGSSAAQDRQivREA---LALVGlahLAGRSYQT---LSGGEQQRVQLARVLAqlwepvdGGPR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1906108912 162 VLLADEPTGNLD---QETGRTILEEMTRlketENIAIVAITHDEQLV-QYADRVV 212
Cdd:COG4559 161 WLFLDEPTSALDlahQHAVLRLARQLAR----RGGGVVAVLHDLNLAaQYADRIL 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-214 |
3.44e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 110.40 E-value: 3.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRlegrdvteasedeRTEERRseLGFVFQDFHL---L 97
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR-------------RAGGAR--VAYVPQRSEVpdsL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 98 PmLNAVENVEL-------PSMWDTTVDRReRAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTG 170
Cdd:NF040873 71 P-LTVRDLVAMgrwarrgLWRRLTRDDRA-AVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1906108912 171 NLDQETGRTILEEMTRLKEtENIAIVAITHDEQLVQYADRVVRI 214
Cdd:NF040873 149 GLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
22-200 |
4.18e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 111.67 E-value: 4.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTML---N-MIGLLDSP-TEGVVRLEGRDVTEASEDerTEERRSELGFVFQDFHL 96
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLrclNrMNDLIPGArVEGEILLDGEDIYDPDVD--VVELRRRVGMVFQKPNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 97 LPMlnavenvelpSMWDTTV---------DRR---ERAVDLLRRVGLGE----RLTHTPDELSGGQQQRVAIARALINEP 160
Cdd:COG1117 104 FPK----------SIYDNVAyglrlhgikSKSeldEIVEESLRKAALWDevkdRLKKSALGLSGGQQQRLCIARALAVEP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1906108912 161 DVLLADEPTGNLDQETGRTILEEMTRLKetENIAIVAITH 200
Cdd:COG1117 174 EVLLMDEPTSALDPISTAKIEELILELK--KDYTIVIVTH 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-202 |
1.39e-29 |
|
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: 114.77 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAEtvvALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDsPTEGVVRLEGRDVTEASEDERtee 82
Cdd:TIGR02868 335 LELRDLSAGYPGAPP---VLDGVSLDLPPGERVAILGPSGSGKSTLLATLaGLLD-PLQGEVTLDGVPVSSLDQDEV--- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 rRSELGFVFQDFHLLPMlNAVENVEL--PSMWDttvdrrERAVDLLRRVGLGERLTHTPD-----------ELSGGQQQR 149
Cdd:TIGR02868 408 -RRRVSVCAQDAHLFDT-TVRENLRLarPDATD------EELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 150 VAIARALINEPDVLLADEPTGNLDQETGRTILEEMtrLKETENIAIVAITHDE 202
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-219 |
2.10e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 110.64 E-value: 2.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAE-TVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEE 82
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQdfhlLPMLNAVE-NVEL-----PSMWDTTVDR-RERAVDLLRRVGLGER-LTHTPDELSGGQQQRVAIAR 154
Cdd:PRK13646 83 VRKRIGMVFQ----FPESQLFEdTVEReiifgPKNFKMNLDEvKNYAHRLLMDLGFSRDvMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906108912 155 ALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSI 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-216 |
2.78e-29 |
|
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: 108.92 E-value: 2.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYesGAetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDsPTEGVVRLEGRDVTEAsedeR 79
Cdd:COG0410 1 MPMLEVENLHAGY--GG--IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAIsGLLP-PRSGSIRFDGEDITGL----P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 80 TEER-RSELGFVFQDFHLLPMLNAVENVELPSM----WDTTVDRRERAVDLLRRvgLGERLTHTPDELSGGQQQRVAIAR 154
Cdd:COG0410 72 PHRIaRLGIGYVPEGRRIFPSLTVEENLLLGAYarrdRAEVRADLERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 155 ALINEPDVLLADEPT-G---NLDQETGRTIleemTRLKEtENIAIVaithdeqLV-QYADRVVRIVD 216
Cdd:COG0410 150 ALMSRPKLLLLDEPSlGlapLIVEEIFEII----RRLNR-EGVTIL-------LVeQNARFALEIAD 204
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-219 |
8.50e-29 |
|
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: 112.89 E-value: 8.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYesGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVteasEDERTEER 83
Cdd:TIGR02203 331 VEFRNVTFRY--PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL----ADYTLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPMLNAvENVELPSMWDTTVDRRERAV------DLLRRVGLGerlTHTP-----DELSGGQQQRVAI 152
Cdd:TIGR02203 405 RRQVALVSQDVVLFNDTIA-NNIAYGRTEQADRAEIERALaaayaqDFVDKLPLG---LDTPigengVLLSGGQRQRLAI 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 153 ARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAitHDEQLVQYADRVVRIVDGVI 219
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIA--HRLSTIEKADRIVVMDDGRI 545
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
23-212 |
1.01e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 108.32 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLdSPTEGVVRLEGRDVTEASEDERTEER-----RSELGFVFqdfhl 96
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGEL-SPDSGEVRLNGRPLADWSPAELARRRavlpqHSSLSFPF----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 97 lpmlNAVENVELPSM-WDTTVDRRERAVD-LLRRVG---LGERLTHTpdeLSGGQQQRVAIARALI------NEPDVLLA 165
Cdd:PRK13548 92 ----TVEEVVAMGRApHGLSRAEDDALVAaALAQVDlahLAGRDYPQ---LSGGEQQRVQLARVLAqlwepdGPPRWLLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 166 DEPTGNLD---QETGRTILEEMTRlkeTENIAIVAITHDEQL-VQYADRVV 212
Cdd:PRK13548 165 DEPTSALDlahQHHVLRLARQLAH---ERGLAVIVVLHDLNLaARYADRIV 212
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-219 |
3.03e-28 |
|
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: 106.16 E-value: 3.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEdertEER 83
Cdd:cd03254 3 IEFENVNFSYDEK---KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISR----KSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPMlNAVENVEL--PSMWDTTVDRRERAV---DLLRRV--GLGERLTHTPDELSGGQQQRVAIARAL 156
Cdd:cd03254 76 RSMIGVVLQDTFLFSG-TIMENIRLgrPNATDEEVIEAAKEAgahDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 157 INEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAitHDEQLVQYADRVVRIVDGVI 219
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIA--HRLSTIKNADKILVLDDGKI 215
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-219 |
3.24e-28 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 111.50 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYeSGAETVvALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASederTEER 83
Cdd:TIGR03375 464 IEFRNVSFAY-PGQETP-ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQID----PADL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLpmLNAV-ENVEL--PSMWDttvdrrERAVDLLRRVGLGERLTHTPD-----------ELSGGQQQR 149
Cdd:TIGR03375 538 RRNIGYVPQDPRLF--YGTLrDNIALgaPYADD------EEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQA 609
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 150 VAIARALINEPDVLLADEPTGNLDQETGRTILEemtRLKE-TENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:TIGR03375 610 VALARALLRDPPILLLDEPTSAMDNRSEERFKD---RLKRwLAGKTLVLVTHRTSLLDLVDRIIVMDNGRI 677
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-212 |
3.36e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.50 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYesGAetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLdSPTEGVVRLEGRDVT-----EAse 76
Cdd:COG3845 5 ALELRGITKRF--GG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILyGLY-QPDSGEILIDGKPVRirsprDA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 77 derteeRRSELGFVFQDFHLLPMLNAVENVEL--PSMWDTTVDR---RERAVDLLRRVGLGERLTHTPDELSGGQQQRVA 151
Cdd:COG3845 78 ------IALGIGMVHQHFMLVPNLTVAENIVLglEPTKGGRLDRkaaRARIRELSERYGLDVDPDAKVEDLSVGEQQRVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 152 IARALINEPDVLLADEPTGNL-DQETgRTILEEMTRLKEtENIAIVAITH--DEQLvQYADRVV 212
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLtPQEA-DELFEILRRLAA-EGKSIIFITHklREVM-AIADRVT 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
8.69e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.99 E-value: 8.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 2 SIIELDSVVKRYESgaETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTeaseDERTE 81
Cdd:PRK13648 6 SIIVFKNVSFQYQS--DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT----DDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 82 ERRSELGFVFQD---------------FHLlpmlnavENVELPsmwdtTVDRRERAVDLLRRVGLGERLTHTPDELSGGQ 146
Cdd:PRK13648 80 KLRKHIGIVFQNpdnqfvgsivkydvaFGL-------ENHAVP-----YDEMHRRVSEALKQVDMLERADYEPNALSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 147 QQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
23-200 |
1.06e-27 |
|
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: 103.78 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDSP-TEGVVRLEGRDVTEasedertEERRSELGFVFQDFHLLPML 100
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLgVSGEVLINGRPLDK-------RSFRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 101 NAVENVELPSmwdttvdrreravdLLRRvglgerlthtpdeLSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTI 180
Cdd:cd03213 98 TVRETLMFAA--------------KLRG-------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180
....*....|....*....|
gi 1906108912 181 LEEMTRLKETeNIAIVAITH 200
Cdd:cd03213 151 MSLLRRLADT-GRTIICSIH 169
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-220 |
1.15e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 109.45 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYeSGAETVVaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLdSPTEGVVRLEGRDVTEASEDERtee 82
Cdd:COG4618 331 LSVENLTVVP-PGSKRPI-LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVW-PPTAGSVRLDGADLSQWDREEL--- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 rRSELGFVFQDfhllpmlnavenVELpsmWDTTV---------DRRERAVDLLRRVGLGERLTHTPD-----------EL 142
Cdd:COG4618 405 -GRHIGYLPQD------------VEL---FDGTIaeniarfgdADPEKVVAAAKLAGVHEMILRLPDgydtrigeggaRL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 143 SGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHDEQLVQYADRVVRIVDGVIQ 220
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKA-RGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-212 |
1.43e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.07 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEERRSELGFVFQdfhlLPMLNA 102
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQ----FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 103 VENVEL------PSMWDTTVDR-RERAVDLLRRVGLGERL-THTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQ 174
Cdd:PRK13641 99 FENTVLkdvefgPKNFGFSEDEaKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 1906108912 175 EtGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVV 212
Cdd:PRK13641 179 E-GRKEMMQLFKDYQKAGHTVILVTHNmDDVAEYADDVL 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-219 |
1.72e-27 |
|
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: 103.90 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYEsgaeTVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASederteer 83
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPMLNAVENV----ELPSMwdTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINE 159
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLvylaQLKGL--KKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 160 PDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHDEQLVQ-YADRVVRIVDGVI 219
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEeLCDRVLLLNKGRA 206
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-219 |
2.28e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.20 E-value: 2.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGAEtvvALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEdertEE 82
Cdd:PRK13647 4 IIEVEDLHFRYKDGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENE----KW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDfhllpmlnAVENVELPSMWD-----------TTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVA 151
Cdd:PRK13647 77 VRSKVGLVFQD--------PDDQVFSSTVWDdvafgpvnmglDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906108912 152 IARALINEPDVLLADEPTGNLD---QETGRTILEEMTRLKETeniaIVAITHDEQL-VQYADRVVRIVDGVI 219
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKT----VIVATHDVDLaAEWADQVIVLKEGRV 216
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
25-219 |
2.29e-27 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 103.99 E-value: 2.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 25 DVDFHAERGEMVVVTGPSGSGKS-TMLNMIGLLDS---PTEGVVRLEGRDVTEASEderteeRRSELGFVFQDfhllPM- 99
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSlTCLAILGLLPPgltQTSGEILLDGRPLLPLSI------RGRHIATIMQN----PRt 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 100 -LNAVENVE------LPSMWDTTVDRRERAVDLLRRVGL--GERLTHT-PDELSGGQQQRVAIARALINEPDVLLADEPT 169
Cdd:TIGR02770 74 aFNPLFTMGnhaietLRSLGKLSKQARALILEALEAVGLpdPEEVLKKyPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 170 GNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQY-ADRVVRIVDGVI 219
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARiADEVAVMDDGRI 204
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-219 |
2.65e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 105.07 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGAEtvvALKDVDFHAERGEMVVVTGPSGSGKSTM-LNMIGLLdSPTEGVVRLEGRDVTEASedeRTE 81
Cdd:PRK13644 1 MIRLENVSYSYPDGTP---ALENINLVIKKGEYIGIIGKNGSGKSTLaLHLNGLL-RPQKGKVLVSGIDTGDFS---KLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 82 ERRSELGFVFQDFHLLPMLNAVE--------NVELPSmwdttVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIA 153
Cdd:PRK13644 74 GIRKLVGIVFQNPETQFVGRTVEedlafgpeNLCLPP-----IEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906108912 154 RALINEPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
20-210 |
2.75e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 105.96 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 20 VVALKDVDFHAERGEMVVVTGPSGSGKS-TMLNMIGLLDSP--TEGVVRLEGRDVTEASEDERTEERRSELGFVFQDfhl 96
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKELNKLRAEQISMIFQD--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 97 lPM--LNAVENVELPSMWDTTVDRR-------ERAVDLLRRVGLGE---RLTHTPDELSGGQQQRVAIARALINEPDVLL 164
Cdd:PRK09473 106 -PMtsLNPYMRVGEQLMEVLMLHKGmskaeafEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1906108912 165 ADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD---------EQLVQYADR 210
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlgvvagicdKVLVMYAGR 239
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-219 |
3.55e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 105.17 E-value: 3.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVV-ALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRD-----VTEASED 77
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 78 ERTE---------------ERRSELGFVFQ--DFHLLP-------MLNAVenvelpSMWDTTVDRRERAVDLLRRVGLGE 133
Cdd:PRK13651 83 VLEKlviqktrfkkikkikEIRRRVGVVFQfaEYQLFEqtiekdiIFGPV------SMGVSKEEAKKRAAKYIELVGLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 134 R-LTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRV 211
Cdd:PRK13651 157 SyLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDlDNVLEWTKRT 235
|
....*...
gi 1906108912 212 VRIVDGVI 219
Cdd:PRK13651 236 IFFKDGKI 243
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-220 |
4.12e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.43 E-value: 4.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYESGAETVVaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEasedERT 80
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE----ENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 EERRSELGFVFQD---------------FHLlpmlnavENVELPSmwdttVDRRERAVDLLRRVGLGERLTHTPDELSGG 145
Cdd:PRK13650 77 WDIRHKIGMVFQNpdnqfvgatveddvaFGL-------ENKGIPH-----EEMKERVNEALELVGMQDFKEREPARLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906108912 146 QQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVIQ 220
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVE 219
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
40-217 |
4.67e-27 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 105.73 E-value: 4.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 40 GPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDER--TEERRseLGFVFQDFHLLPMLNAVENVELpSMWDTTVD 117
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIClpPEKRR--IGYVFQDARLFPHYKVRGNLRY-GMAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 118 RRERAVDLLrrvGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVA 197
Cdd:PRK11144 108 QFDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILY 184
|
170 180
....*....|....*....|..
gi 1906108912 198 ITH--DEqLVQYADRVVRIVDG 217
Cdd:PRK11144 185 VSHslDE-ILRLADRVVVLEQG 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-217 |
5.93e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 104.42 E-value: 5.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDsPTEGVVRLEGRDVTEasEDERT- 80
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIIlGILA-PDSGEVLWDGEPLDP--EDRRRi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 ----EERRselgfvfqdfhLLPMLNAVENV----ELPSMwdTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAI 152
Cdd:COG4152 74 gylpEERG-----------LYPKMKVGEQLvylaRLKGL--SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906108912 153 ARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHDEQLVQ-YADRVVRIVDG 217
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEeLCDRIVIINKG 205
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-211 |
1.60e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 102.23 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLL-----DSPTEGVVRLEGRDVTeaSEDERTEERRSELGFVFQDFHLL 97
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIY--SPDVDPIEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 98 PMLNAVENVELPSMWDTTVDRR----ERAVDLLRRVGLGE----RLTHTPDELSGGQQQRVAIARALINEPDVLLADEPT 169
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLVKSKkeldERVEWALKKAALWDevkdRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1906108912 170 GNLDQETGRTILEEMTRLKetENIAIVAITHD-EQLVQYADRV 211
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELK--KEYTIVLVTHSpAQAARVSDYV 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-219 |
2.39e-26 |
|
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: 101.46 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAEtVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASederTEER 83
Cdd:cd03249 1 IEFKNVSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN----LRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPMLNAvENVELpSMWDTTVDRRERAVdllRRVGLGERLTHTPD-----------ELSGGQQQRVAI 152
Cdd:cd03249 76 RSQIGLVSQEPVLFDGTIA-ENIRY-GKPDATDEEVEEAA---KKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 153 ARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKetENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRNADLIAVLQNGQV 215
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-217 |
2.41e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 105.66 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRL-EGRDVTeasederteerrselgFVFQDFHLlPMLN 101
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL----------------FLPQRPYL-PLGT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 102 AVENVELPSMwDTTVDRrERAVDLLRRVGLG---ERL---THTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQE 175
Cdd:COG4178 442 LREALLYPAT-AEAFSD-AELREALEAVGLGhlaERLdeeADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1906108912 176 TGRTILEemtRLKET-ENIAIVAITHDEQLVQYADRVVRIVDG 217
Cdd:COG4178 520 NEAALYQ---LLREElPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-219 |
2.99e-26 |
|
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: 101.41 E-value: 2.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYesGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASederTEER 83
Cdd:cd03252 1 ITFEHVRFRY--KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD----PAWL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDfHLLPMLNAVENVELPsmwDTTVDRrERAVDLLRRVGLGERLTHTPD-----------ELSGGQQQRVAI 152
Cdd:cd03252 75 RRQVGVVLQE-NVLFNRSIRDNIALA---DPGMSM-ERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 153 ARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAitHDEQLVQYADRVVRIVDGVI 219
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIA--HRLSTVKNADRIIVMEKGRI 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
21-201 |
3.48e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 101.54 E-value: 3.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGR-----DVTEASEDERTEERRSELGFVFQDFH 95
Cdd:PRK11701 20 KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRLLRTEWGFVHQHPR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 96 --LLPMLNAVENVELPSM---WDTTVDRRERAVDLLRRVGLG-ERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPT 169
Cdd:PRK11701 100 dgLRMQVSAGGNIGERLMavgARHYGDIRATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPT 179
|
170 180 190
....*....|....*....|....*....|..
gi 1906108912 170 GNLDQETGRTILEEMTRLKETENIAIVAITHD 201
Cdd:PRK11701 180 GGLDVSVQARLLDLLRGLVRELGLAVVIVTHD 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-219 |
5.02e-26 |
|
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: 104.88 E-value: 5.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGAETVV-ALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRL----EGRDVTEASED 77
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 78 ERTEERRSeLGFVFQDFHLLPMLNAVEN------VELPSMWdttvdRRERAVDLLRRVGLGER-----LTHTPDELSGGQ 146
Cdd:TIGR03269 359 GRGRAKRY-IGILHQEYDLYPHRTVLDNlteaigLELPDEL-----ARMKAVITLKMVGFDEEkaeeiLDKYPDELSEGE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 147 QQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLV-QYADRVVRIVDGVI 219
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKI 506
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
22-203 |
7.12e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.99 E-value: 7.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTeerrseLGFVFQDFHLLPMLN 101
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP------INMMFQSYALFPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 102 AVENVELPSMWD--TTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRT 179
Cdd:PRK11607 108 VEQNIAFGLKQDklPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
|
170 180
....*....|....*....|....
gi 1906108912 180 ILEEMTRLKETENIAIVAITHDEQ 203
Cdd:PRK11607 188 MQLEVVDILERVGVTCVMVTHDQE 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-219 |
8.51e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 104.14 E-value: 8.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERteer 83
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPV--LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLpmlNAV--ENVELPSmwDTTVDrrERAVDLLRRVGLgERLTHTPD-----------ELSGGQQQRV 150
Cdd:PRK11160 413 RQAISVVSQRVHLF---SATlrDNLLLAA--PNASD--EALIEVLQQVGL-EKLLEDDKglnawlgeggrQLSGGEQRRL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906108912 151 AIARALINEPDVLLADEPTGNLDQETGRTILEEMtrLKETENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELL--AEHAQNKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-217 |
9.19e-26 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 98.27 E-value: 9.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERteeRRSELGFVFQDFH---LLP 98
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA---IRAGIAYVPEDRKregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 99 MLNAVENVELPSMwdttvdrreravdllrrvglgerlthtpdeLSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGR 178
Cdd:cd03215 92 DLSVAENIALSSL------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1906108912 179 TILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDG 217
Cdd:cd03215 142 EIYRLIRELAD-AGKAVLLISSElDELLGLCDRILVMYEG 180
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-219 |
9.62e-26 |
|
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: 98.54 E-value: 9.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDsPTEGVVRLEGRDVTEASEderteERRSELGFVFQDFHLlpm 99
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLtGDLK-PQQGEITLDGVPVSDLEK-----ALSSLISVLNQRPYL--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 100 lnavenvelpsmWDTTVdrreravdllrRVGLGERLthtpdelSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRT 179
Cdd:cd03247 87 ------------FDTTL-----------RNNLGRRF-------SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1906108912 180 ILEEMtrLKETENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:cd03247 137 LLSLI--FEVLKDKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-212 |
1.02e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.02 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 8 SVVKRYESGAETVValKDVDFHAERGEMVVVTGPSGSGKS-TMLNMIGLLDSP----TEGVVRLEGRDVTEASEDERTEE 82
Cdd:PRK15134 12 SVAFRQQQTVRTVV--NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDfhllPM--LNAVENVELP---------SMwdttvdRRERA----VDLLRRVGL---GERLTHTPDELSG 144
Cdd:PRK15134 90 RGNKIAMIFQE----PMvsLNPLHTLEKQlyevlslhrGM------RREAArgeiLNCLDRVGIrqaAKRLTDYPHQLSG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906108912 145 GQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLV-QYADRVV 212
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVrKLADRVA 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-200 |
1.06e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 99.18 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGrdvtEASEDERTEERRSELGfvFQDFhLLPML 100
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG----GDIDDPDVAEACHYLG--HRNA-MKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 101 NAVENVELpsmWDTTVDRRERAVD-LLRRVGLGeRLTHTP-DELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGR 178
Cdd:PRK13539 89 TVAENLEF---WAAFLGGEELDIAaALEAVGLA-PLAHLPfGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|..
gi 1906108912 179 TILEEMTRLKETENIAIVAiTH 200
Cdd:PRK13539 165 LFAELIRAHLAQGGIVIAA-TH 185
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
22-212 |
1.07e-25 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 99.52 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTMLN-MIGLLDsPTEGVVRLEGRDVTEASEDERTeerRSELGFVFQDFHLLPML 100
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKtLMGLLP-VKSGSIRLDGEDITKLPPHERA---RAGIAYVPQGREIFPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 101 NAVENVELPSmwdTTVDRRERAVD-------------LLRRVGLgerlthtpdeLSGGQQQRVAIARALINEPDVLLADE 167
Cdd:TIGR03410 91 TVEENLLTGL---AALPRRSRKIPdeiyelfpvlkemLGRRGGD----------LSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 168 PT-G---NLDQETGRTIleemTRLKETENIAIVAIthdEQLV----QYADRVV 212
Cdd:TIGR03410 158 PTeGiqpSIIKDIGRVI----RRLRAEGGMAILLV---EQYLdfarELADRYY 203
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-219 |
1.08e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 99.99 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLL-----DSPTEGVVRLEGRDVTEASederTEERRSELGFVFQDFHLL 97
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD----VIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 98 PMLNAVENVELPSMWDTTVDRR----ERAVDLLRRVGLGE----RLTHTPDELSGGQQQRVAIARALINEPDVLLADEPT 169
Cdd:PRK14247 95 PNLSIFENVALGLKLNRLVKSKkelqERVRWALEKAQLWDevkdRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 170 GNLDQETGRTILEEMTRLKetENIAIVAITH-DEQLVQYADRVVRIVDGVI 219
Cdd:PRK14247 175 ANLDPENTAKIESLFLELK--KDMTIVLVTHfPQQAARISDYVAFLYKGQI 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-219 |
2.99e-25 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 102.57 E-value: 2.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDS--PTEGVV----------------- 64
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 65 -------------RLEGRDVTEASEDERTEERRsELGFVFQ-DFHLLPMLNAVENV--ELPSMWDTTVDRRERAVDLLRR 128
Cdd:TIGR03269 77 kvgepcpvcggtlEPEEVDFWNLSDKLRRRIRK-RIAIMLQrTFALYGDDTVLDNVleALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 129 VGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITH-DEQLVQY 207
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwPEVIEDL 235
|
250
....*....|..
gi 1906108912 208 ADRVVRIVDGVI 219
Cdd:TIGR03269 236 SDKAIWLENGEI 247
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-219 |
4.78e-25 |
|
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: 98.07 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETvvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERteer 83
Cdd:cd03253 1 IEFENVTFAYDPGRPV---LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDfhlLPMLNAV--ENVEL--PSMWDTTVDRRERAVDLLRRVG---------LGERLThtpdELSGGQQQRV 150
Cdd:cd03253 74 RRAIGVVPQD---TVLFNDTigYNIRYgrPDATDEEVIEAAKAAQIHDKIMrfpdgydtiVGERGL----KLSGGEKQRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906108912 151 AIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLkeTENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-217 |
4.94e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.58 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTE--ERRSELGFVFQDFHLLPML 100
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDaiKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 101 NAVENVELPSMWDTTVDRRERAV---DLLRRVGLG----ERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLD 173
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKKiveECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1906108912 174 QETGRTILEEMTRLKetENIAIVAITHD-EQLVQYADRVVRIVDG 217
Cdd:PRK14246 186 IVNSQAIEKLITELK--NEIAIVIVSHNpQQVARVADYVAFLYNG 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-220 |
7.31e-25 |
|
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: 97.40 E-value: 7.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 18 ETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTeasedERTEERRSELGFVF-QDFHL 96
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPW-----KRRKKFLRRIGVVFgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 97 ---LP------MLNAVENVElPSMWDTTVDRRERAVDLlrrvglgERLTHTP-DELSGGQQQRVAIARALINEPDVLLAD 166
Cdd:cd03267 107 wwdLPvidsfyLLAAIYDLP-PARFKKRLDELSELLDL-------EELLDTPvRQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 167 EPTGNLD---QETGRTILEEMTRLKETeniAIVAITHDEQLV-QYADRVVRIVDGVIQ 220
Cdd:cd03267 179 EPTIGLDvvaQENIRNFLKEYNRERGT---TVLLTSHYMKDIeALARRVLVIDKGRLL 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
23-219 |
7.98e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 100.30 E-value: 7.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVteASEDERTEERRseLGFVFQDFHLLPMLNA 102
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV--EALSARAASRR--VASVPQDTSLSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 103 VENVEL-----PSMWDTTVDRRERAVD-LLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQET 176
Cdd:PRK09536 95 RQVVEMgrtphRSRFDTWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1906108912 177 GRTILEEMTRLKETENIAIVAItHDEQL-VQYADRVVRIVDGVI 219
Cdd:PRK09536 175 QVRTLELVRRLVDDGKTAVAAI-HDLDLaARYCDELVLLADGRV 217
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
4-220 |
9.92e-25 |
|
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: 101.27 E-value: 9.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEAseDERTEER 83
Cdd:TIGR01842 317 LSVENVTIVPPGGKKPT--LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQW--DRETFGK 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RseLGFVFQDFHLLPMLNAvENVelpSMWDTTVDRrERAVDLLRRVGLGERLTHTPD-----------ELSGGQQQRVAI 152
Cdd:TIGR01842 393 H--IGYLPQDVELFPGTVA-ENI---ARFGENADP-EKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIAL 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 153 ARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVaITHDEQLVQYADRVVRIVDGVIQ 220
Cdd:TIGR01842 466 ARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVV-ITHRPSLLGCVDKILVLQDGRIA 532
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-211 |
1.50e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 98.63 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 17 AETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLN-MIGLLDSpTEGVVRLEGRDVTEASEDERtEERRSELGFVFQDfh 95
Cdd:PRK15079 31 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARaIIGLVKA-TDGEVAWLGKDLLGMKDDEW-RAVRSDIQMIFQD-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 96 LLPMLNAVENVE----------LPSMWDTTVDRRERAvdLLRRVGLGERLTHT-PDELSGGQQQRVAIARALINEPDVLL 164
Cdd:PRK15079 107 PLASLNPRMTIGeiiaeplrtyHPKLSRQEVKDRVKA--MMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1906108912 165 ADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQY-ADRV 211
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRV 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-212 |
1.58e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.81 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEasEDERTEERRSELGFVFQ--DFHLLP 98
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD--KKVKLSDIRKKVGLVFQypEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 99 mlnavENVE---------LPSMWDTTVDRRERAVDLlrrVGLG--ERLTHTPDELSGGQQQRVAIARALINEPDVLLADE 167
Cdd:PRK13637 99 -----ETIEkdiafgpinLGLSEEEIENRVKRAMNI---VGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1906108912 168 PTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVV 212
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSmEDVAKLADRII 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-220 |
1.92e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.14 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYesGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLdSPTEGVVRLeGRDVteasederte 81
Cdd:COG0488 315 VLELEGLSKSY--GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGEL-EPDSGTVKL-GETV---------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 82 errsELGFVFQDFHLLPM-LNAVENvelpsMWDTTVDRRERAV-DLLRRVGL-GERLtHTP-DELSGGQQQRVAIARALI 157
Cdd:COG0488 379 ----KIGYFDQHQEELDPdKTVLDE-----LRDGAPGGTEQEVrGYLGRFLFsGDDA-FKPvGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 158 NEPDVLLADEPTGNLDQETgRTILEEMtrLKETENiAIVAITHDEQLVQ-YADRVVRIVDGVIQ 220
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIET-LEALEEA--LDDFPG-TVLLVSHDRYFLDrVATRILEFEDGGVR 508
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-211 |
2.11e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.51 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAE-TVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEE 82
Cdd:PRK13649 3 INLQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQdfhlLPMLNAVENVEL------PSMWDTTVDRRER-AVDLLRRVGLGERL-THTPDELSGGQQQRVAIAR 154
Cdd:PRK13649 83 IRKKVGLVFQ----FPESQLFEETVLkdvafgPQNFGVSQEEAEAlAREKLALVGISESLfEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 155 ALINEPDVLLADEPTGNLDQEtGRTilEEMTRLKE--TENIAIVAITH-DEQLVQYADRV 211
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPK-GRK--ELMTLFKKlhQSGMTIVLVTHlMDDVANYADFV 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-206 |
4.61e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.39 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTM-LNMIGLLDSptEGVVRLEGRDVTEASEDERTEERRsELGFVFQDFH--LL 97
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTgLALLRLINS--QGEIWFDGQPLHNLNRRQLLPVRH-RIQVVFQDPNssLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 98 PMLNAVE------NVELPSMwdTTVDRRERAVDLLRRVGLGERLTHT-PDELSGGQQQRVAIARALINEPDVLLADEPTG 170
Cdd:PRK15134 377 PRLNVLQiieeglRVHQPTL--SAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190
....*....|....*....|....*....|....*.
gi 1906108912 171 NLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQ 206
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVR 490
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-219 |
4.86e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.54 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYesGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTeeR 83
Cdd:COG4604 2 IEIKNVSKRY--GGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA--K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RseLGFVFQDFHLLPMLNAVENVE----------LpsmwdTTVDRR--ERAVDLLRRVGLGERLThtpDELSGGQQQRVA 151
Cdd:COG4604 76 R--LAILRQENHINSRLTVRELVAfgrfpyskgrL-----TAEDREiiDEAIAYLDLEDLADRYL---DELSGGQRQRAF 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906108912 152 IARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDiNFASCYADHIVAMKDGRV 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-168 |
6.05e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 95.10 E-value: 6.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYesGAETVValKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLdSPTEGVVRLEGRDVTEASEDER 79
Cdd:COG1137 1 MMTLEAENLVKSY--GKRTVV--KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIvGLV-KPDSGRIFLDGEDITHLPMHKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 80 TeerRSELGF------VFQDfhllpmLNAVENV----ELPSMwdTTVDRRERAVDLLRRVGLgERLTHTP-DELSGGQQQ 148
Cdd:COG1137 76 A---RLGIGYlpqeasIFRK------LTVEDNIlavlELRKL--SKKEREERLEELLEEFGI-THLRKSKaYSLSGGERR 143
|
170 180
....*....|....*....|
gi 1906108912 149 RVAIARALINEPDVLLADEP 168
Cdd:COG1137 144 RVEIARALATNPKFILLDEP 163
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-219 |
8.74e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.64 E-value: 8.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 2 SIIELDSVVKRYESGAETvvALKDVDFHAERGEMVVVTGPSGSGKST---MLNMIGLLDSPTEGVVRLEGRDVTEasedE 78
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTA----K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 79 RTEERRSELGFVFQDFHLLPMLNAVENVELPSMWDTTVDRRE--RAV-DLLRRVGLGERLTHTPDELSGGQQQRVAIARA 155
Cdd:PRK13640 78 TVWDIREKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEmiKIVrDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 156 LINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-219 |
9.28e-24 |
|
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: 93.82 E-value: 9.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYesGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTeasedeRTEER 83
Cdd:cd03268 1 LKTNDLTKTY--GKKRV--LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ------KNIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPMLNAVENVELpsmWDTTVDRRERAVD-LLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDV 162
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRL---LARLLGIRKKRIDeVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 163 LLADEPTGNLDQEtGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:cd03268 148 LILDEPTNGLDPD-GIKELRELILSLRDQGITVLISSHLlSEIQKVADRIGIINKGKL 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-216 |
1.25e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 6 LDSVVKRYesGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGR--------DVTEASED 77
Cdd:COG0488 1 LENLSKSF--GGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlrigylpqEPPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 78 ---ERTEERRSELGFVFQDFHLLPMLNAVENVELPSMWDTTVDRRE--------RAVDLLRRVGLGERLTHTP-DELSGG 145
Cdd:COG0488 77 tvlDTVLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEAlggweaeaRAEEILSGLGFPEEDLDRPvSELSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 146 QQQRVAIARALINEPDVLLADEPTGNLDQEtgrTI--LEEMtrLKETENiAIVAITHDEQLVqyaDRVV-RIVD 216
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLE---SIewLEEF--LKNYPG-TVLVVSHDRYFL---DRVAtRILE 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-219 |
2.06e-23 |
|
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: 93.76 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYesGAETVValKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERteeR 83
Cdd:cd03218 1 LRAENLSKRY--GKRKVV--NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKR---A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPMLNAVENVE--LPSMWDTTVDRRERAVDLLRRVGLgERLTHTP-DELSGGQQQRVAIARALINEP 160
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENILavLEIRGLSKKEREEKLEELLEEFHI-THLRKSKaSSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 161 DVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNvRETLSITDRAYIIYEGKV 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
22-217 |
2.11e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.07 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTML---NMIGLL--DSPTEGVVRLEGRDVTEASEDerTEERRSELGFVFQDFHL 96
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLnpEVTITGSIVYNGHNIYSPRTD--TVDLRKEIGMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 97 LPMlNAVENV---------ELPSMWDTTVDRRERAVDLLRRVGlgERLTHTPDELSGGQQQRVAIARALINEPDVLLADE 167
Cdd:PRK14239 98 FPM-SIYENVvyglrlkgiKDKQVLDEAVEKSLKGASIWDEVK--DRLHDSALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 168 PTGNLDQETGRTILEEMTRLKETENIAIVaiTHD-EQLVQYADRVVRIVDG 217
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGLKDDYTMLLV--TRSmQQASRISDRTGFFLDG 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-217 |
2.65e-23 |
|
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: 92.53 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 14 ESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLN-MIGLLDsPTEGVVRLEGRdvteasederteerrseLGFVFQ 92
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELE-KLSGSVSVPGS-----------------IAYVSQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 93 dfhlLP-MLNA--VENVELPSMWDTtvDRRERAVDL--LRR----------VGLGER-LThtpdeLSGGQQQRVAIARAL 156
Cdd:cd03250 74 ----EPwIQNGtiRENILFGKPFDE--ERYEKVIKAcaLEPdleilpdgdlTEIGEKgIN-----LSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 157 INEPDVLLADEPTGNLDQETGRTILEE--MTRLKetENIAIVAITHDEQLVQYADRVVRIVDG 217
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIFENciLGLLL--NNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
21-217 |
2.92e-23 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 93.74 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRD-----VTEASEDERTEERRSELGFVFQDFH 95
Cdd:TIGR02323 17 KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERRRLMRTEWGFVHQNPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 96 --LLPMLNAVENVELPSMwdTTVDR-----RERAVDLLRRVGLGE-RLTHTPDELSGGQQQRVAIARALINEPDVLLADE 167
Cdd:TIGR02323 97 dgLRMRVSAGANIGERLM--AIGARhygniRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 168 PTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQ-YADRVVRIVDG 217
Cdd:TIGR02323 175 PTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQG 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
14-219 |
3.81e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 94.92 E-value: 3.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 14 ESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLE----GRDVTEASEDERTEER------ 83
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITNPYSKkiknfk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 --RSELGFVFQ--DFHLLPmlnavENVELPSMWD------TTVDRRERAVDLLRRVGLGER-LTHTPDELSGGQQQRVAI 152
Cdd:PRK13631 113 elRRRVSMVFQfpEYQLFK-----DTIEKDIMFGpvalgvKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAI 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 153 ARALINEPDVLLADEPTGNLDQETGRtileEMTRL---KETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEH----EMMQLildAKANNKTVFVITHTmEHVLEVADEVIVMDKGKI 254
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-198 |
4.71e-23 |
|
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: 92.72 E-value: 4.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 19 TVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDSP--TEGVVRLEGRDVTEAsederteERRSELGFVFQDFH 95
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGgtTSGQILFNGQPRKPD-------QFQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 96 LLPMLNAVE------NVELPSMWDTTVDRRERAVDLLRRVGLgERLTHTPDE-LSGGQQQRVAIARALINEPDVLLADEP 168
Cdd:cd03234 92 LLPGLTVREtltytaILRLPRKSSDAIRKKRVEDVLLRDLAL-TRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190
....*....|....*....|....*....|
gi 1906108912 169 TGNLDQETGRTILEEMTRLKETENIAIVAI 198
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTI 200
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-219 |
5.10e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.03 E-value: 5.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEERRSELGFVFQdfhlLPMLN 101
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQ----FPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 102 AVENVEL------PSMWDTTVDRRER-AVDLLRRVGLGERL-THTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLD 173
Cdd:PRK13643 97 LFEETVLkdvafgPQNFGIPKEKAEKiAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1906108912 174 QETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-219 |
6.01e-23 |
|
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: 91.43 E-value: 6.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLD-SPTEGVVRLEGRDVTEASEDERTeerRSELGFVFQdfhllpml 100
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImGHPKyEVTEGEILFKGEDITDLPPEERA---RLGIFLAFQ-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 101 navENVELPSMwdttvdrreRAVDLLRRVGLGerlthtpdeLSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTI 180
Cdd:cd03217 85 ---YPPEIPGV---------KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1906108912 181 LEEMTRLKEtENIAIVAITHDEQLVQY--ADRVVRIVDGVI 219
Cdd:cd03217 144 AEVINKLRE-EGKSVLIITHYQRLLDYikPDRVHVLYDGRI 183
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-198 |
8.33e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.88 E-value: 8.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPteGVVRLEGRDVTEASEDERTEERRSelGFVFQDFHLLPMLNA 102
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLLNGMPIDAKEMRAIS--AYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 103 VENVELPSMW-----DTTVDRRERAVDLLRRVGLG---ERLTHTPDE---LSGGQQQRVAIARALINEPDVLLADEPTGN 171
Cdd:TIGR00955 117 REHLMFQAHLrmprrVTKKEKRERVDEVLQALGLRkcaNTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180
....*....|....*....|....*..
gi 1906108912 172 LDQETGRTILEEMTRLKETENIAIVAI 198
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGKTIICTI 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-205 |
8.90e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.94 E-value: 8.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYESGAEtvvALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEasedERT 80
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKE---ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK----ENI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 EERRSELGFVFQDFHLLPMLNAVE--------NVELPsmwDTTVDRRERAVdlLRRVGLGERLTHTPDELSGGQQQRVAI 152
Cdd:PRK13652 74 REVRKFVGLVFQNPDDQIFSPTVEqdiafgpiNLGLD---EETVAHRVSSA--LHMLGLEELRDRVPHHLSGGEKKRVAI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 153 ARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLV 205
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLV 201
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-187 |
8.99e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.33 E-value: 8.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 2 SIIELDSVVKRYesGAETVValKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEasedeRTE 81
Cdd:PRK13537 6 APIDFRNVEKRY--GDKLVV--DGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-----RAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 82 ERRSELGFVFQDFHLLPMLNAVENVELPSMW--DTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINE 159
Cdd:PRK13537 77 HARQRVGVVPQFDNLDPDFTVRENLLVFGRYfgLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180
....*....|....*....|....*...
gi 1906108912 160 PDVLLADEPTGNLDQETGRTILEEMTRL 187
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSL 184
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-219 |
1.02e-22 |
|
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: 89.43 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGaetvVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLeGRDVTeasederteer 83
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 rseLGFVFQdfhllpmlnavenvelpsmwdttvdrreravdllrrvglgerlthtpdeLSGGQQQRVAIARALINEPDVL 163
Cdd:cd03221 65 ---IGYFEQ-------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1906108912 164 LADEPTGNLDQETgRTILEEMtrLKETENiAIVAITHDEQLVQyadrvvRIVDGVI 219
Cdd:cd03221 93 LLDEPTNHLDLES-IEALEEA--LKEYPG-TVILVSHDRYFLD------QVATKII 138
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
12-212 |
7.89e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 90.23 E-value: 7.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 12 RYESG---AETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEERRselg 88
Cdd:PRK15112 15 RYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIR---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 89 FVFQD--FHLLPMLNAVENVELPSMWDTTVD---RRERAVDLLRRVGL-GERLTHTPDELSGGQQQRVAIARALINEPDV 162
Cdd:PRK15112 91 MIFQDpsTSLNPRQRISQILDFPLRLNTDLEpeqREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906108912 163 LLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITH---------DEQLVQYADRVV 212
Cdd:PRK15112 171 IIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQhlgmmkhisDQVLVMHQGEVV 229
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-219 |
8.71e-22 |
|
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: 92.55 E-value: 8.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYES-GAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTeaseDERTEE 82
Cdd:COG4615 328 LELRGVTYRYPGeDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT----ADNREA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDFHLLPMLNAVENVELPsmwdttvdrrERAVDLLRRVGLGERLTHTPD-----ELSGGQQQRVAIARALI 157
Cdd:COG4615 404 YRQLFSAVFSDFHLFDRLLGLDGEADP----------ARARELLERLELDHKVSVEDGrfsttDLSQGQRKRLALLVALL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 158 NEPDVLLADEPTGnlDQETG------RTILEEMTRLKETeniaIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:COG4615 474 EDRPILVFDEWAA--DQDPEfrrvfyTELLPELKARGKT----VIAISHDDRYFDLADRVLKMDYGKL 535
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-219 |
8.79e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.77 E-value: 8.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYEsGAETVvALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVteasEDERTEER 83
Cdd:PRK11176 342 IEFRNVTFTYP-GKEVP-ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL----RDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPMLNAvENVELPSMWDTTVDRRERAVDLLRRVGLGERLTHTPDE--------LSGGQQQRVAIARA 155
Cdd:PRK11176 416 RNQVALVSQNVHLFNDTIA-NNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIARA 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 156 LINEPDVLLADEPTGNLDQETGRTILEEMTRLKetENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTIEKADEILVVEDGEI 556
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-219 |
1.01e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 89.36 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLD-SPTEGVVRLEGRDVTEASEDERTeerRSELGFVFQ-------- 92
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmGHPKyEVTSGSILLDGEDILELSPDERA---RAGIFLAFQypveipgv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 93 ---DFhLLPMLNAVENVELPSMwdttvDRRERAVDLLRRVGLGERLTHTP--DELSGGQQQRVAIARALINEPDVLLADE 167
Cdd:COG0396 93 svsNF-LRTALNARRGEELSAR-----EFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 168 PTGNLDQETGRTILEEMTRLKETENiAIVAITHDEQLVQY--ADRVVRIVDGVI 219
Cdd:COG0396 167 TDSGLDIDALRIVAEGVNKLRSPDR-GILIITHYQRILDYikPDFVHVLVDGRI 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-219 |
1.56e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.00 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDER--------TEERRSElGfvfqd 93
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAiragiayvPEDRKGE-G----- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 94 fhLLPMLNAVENVELPSMWDTT----VDR---RERAVDLLRRVGLgeRlTHTPD----ELSGGQQQRVAIARALINEPDV 162
Cdd:COG1129 341 --LVLDLSIRENITLASLDRLSrgglLDRrreRALAEEYIKRLRI--K-TPSPEqpvgNLSGGNQQKVVLAKWLATDPKV 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 163 LLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:COG1129 416 LILDEPTRGIDVGAKAEIYRLIRELAA-EGKAVIVISSElPELLGLSDRILVMREGRI 472
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-220 |
3.15e-21 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 91.19 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAetvVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTeaseDERTEER 83
Cdd:PRK10522 323 LELRNVTFAYQDNG---FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT----AEQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPMLNAVENVELPSmwdttvdrrERAVDLLRRVGLGERLTH-----TPDELSGGQQQRVAIARALIN 158
Cdd:PRK10522 396 RKLFSAVFTDFHLFDQLLGPEGKPANP---------ALVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906108912 159 EPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVIQ 220
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLS 528
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-206 |
3.34e-21 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 87.03 E-value: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEasedeRTEERRSELGFVFQDFHLLPML 100
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-----QRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 101 NAVENVelpSMWDTTVDRRERAV-DLLRRVGLGErLTHTP-DELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGR 178
Cdd:TIGR01189 89 SALENL---HFWAAIHGGAQRTIeDALAAVGLTG-FEDLPaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|....*...
gi 1906108912 179 TILEEMTRLKETENIAIVAITHDEQLVQ 206
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLTTHQDLGLVE 192
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-216 |
4.30e-21 |
|
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: 85.67 E-value: 4.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDSPTEGVVRLEGRDVTeasederteerrselgFVFQdfhllpmln 101
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALaGLWPWGSGRIGMPEGEDLL----------------FLPQ--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 102 avenveLPSMWDTTvdrreravdlLRrvglgERLTHtP--DELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRT 179
Cdd:cd03223 72 ------RPYLPLGT----------LR-----EQLIY-PwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180 190
....*....|....*....|....*....|....*..
gi 1906108912 180 ILeemtRLKETENIAIVAITHDEQLVQYADRVVRIVD 216
Cdd:cd03223 130 LY----QLLKELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-217 |
5.55e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.37 E-value: 5.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGAEtvvALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDerTEE 82
Cdd:PRK13636 5 ILKVEELNYNYSDGTH---ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKG--LMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQD-FHLLPMLNAVE-------NVELPSMwdttvDRRERAVDLLRRVGLgERLTHTPDE-LSGGQQQRVAIA 153
Cdd:PRK13636 80 LRESVGMVFQDpDNQLFSASVYQdvsfgavNLKLPED-----EVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906108912 154 RALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQ-YADRVVRIVDG 217
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEG 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-217 |
8.52e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 87.35 E-value: 8.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEasedeRTEERRSELGFV--FQDFHLLPM 99
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG-----LPGHQIARMGVVrtFQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 100 LNAVENVE-----------LPSMWDTTVDRR------ERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDV 162
Cdd:PRK11300 95 MTVIENLLvaqhqqlktglFSGLLKTPAFRRaesealDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 163 LLADEPTGNLD-QETgRTILEEMTRLKETENIAIVAITHDEQLVQ-YADRVVRIVDG 217
Cdd:PRK11300 175 LMLDEPAAGLNpKET-KELDELIAELRNEHNVTVLLIEHDMKLVMgISDRIYVVNQG 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-214 |
1.01e-20 |
|
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: 86.01 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 14 ESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVteaseDERTEERRSELGFVFQD 93
Cdd:cd03231 9 ERDGRAL--FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-----DFQRDSIARGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 94 FHLLPMLNAVENVElpsmWDTTVDRRERAVDLLRRVGLGErLTHTP-DELSGGQQQRVAIARALINEPDVLLADEPTGNL 172
Cdd:cd03231 82 PGIKTTLSVLENLR----FWHADHSDEQVEEALARVGLNG-FEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1906108912 173 DQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRI 214
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-220 |
1.04e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.67 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MS-IIELDSVVKRY------------------ESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTE 61
Cdd:COG1134 1 MSsMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 62 GVVRLEGrdvteasederteeRRS---ELGFVFQdfhllPMLNAVENVELPS----MWDTTVDRRERAVdllrrV---GL 131
Cdd:COG1134 81 GRVEVNG--------------RVSallELGAGFH-----PELTGRENIYLNGrllgLSRKEIDEKFDEI-----VefaEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 132 GERLtHTP-DELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHDEQLV-QYAD 209
Cdd:COG1134 137 GDFI-DQPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRE-SGRTVIFVSHSMGAVrRLCD 214
|
250
....*....|.
gi 1906108912 210 RVVRIVDGVIQ 220
Cdd:COG1134 215 RAIWLEKGRLV 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-220 |
1.33e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.40 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTE-----------ASEDERTEERRS---ELG 88
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydhhylhrqvaLVGQEPVLFSGSvreNIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 89 FVFQDFHLLPMLNAVENV-------ELPSMWDTTVdrreravdllrrvglGERLThtpdELSGGQQQRVAIARALINEPD 161
Cdd:TIGR00958 577 YGLTDTPDEEIMAAAKAAnahdfimEFPNGYDTEV---------------GEKGS----QLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906108912 162 VLLADEPTGNLDQETGRTILEEMTRLKETeniaIVAITHDEQLVQYADRVVRIVDGVIQ 220
Cdd:TIGR00958 638 VLILDEATSALDAECEQLLQESRSRASRT----VLLIAHRLSTVERADQILVLKKGSVV 692
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-211 |
1.47e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 87.65 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 19 TVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDSP---TEGVVRLEGRDVTEASEDERTEERRSELGFVFQD- 93
Cdd:COG4170 19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcGITKDNwhvTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQEp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 94 -FHLLPMLNAVENVE--LPS------MWDTTVDRRERAVDLLRRVGLGER---LTHTPDELSGGQQQRVAIARALINEPD 161
Cdd:COG4170 99 sSCLDPSAKIGDQLIeaIPSwtfkgkWWQRFKWRKKRAIELLHRVGIKDHkdiMNSYPHELTEGECQKVMIAMAIANQPR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 162 VLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRV 211
Cdd:COG4170 179 LLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDlESISQWADTI 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-219 |
1.53e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 89.11 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAEtvvALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEG---RDVTEASedert 80
Cdd:COG5265 358 VRFENVSFGYDPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDVTQAS----- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 eeRRSELGFVFQD---F---------------------------HLLPMLNAvenveLPSMWDTTVdrreravdllrrvg 130
Cdd:COG5265 430 --LRAAIGIVPQDtvlFndtiayniaygrpdaseeeveaaaraaQIHDFIES-----LPDGYDTRV-------------- 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 131 lGER-LthtpdELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLkeTENIAIVAITHDEQLVQYAD 209
Cdd:COG5265 489 -GERgL-----KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV--ARGRTTLVIAHRLSTIVDAD 560
|
250
....*....|
gi 1906108912 210 RVVRIVDGVI 219
Cdd:COG5265 561 EILVLEAGRI 570
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-219 |
1.56e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 89.13 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLdsPTEGVVRLEGrdvTEASEDERTEERRsELGFVFQDFHLLPM 99
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALlGFL--PYQGSLKING---IELRELDPESWRK-HLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 100 lNAVENVEL--PSMWDTTVD---RRERAVDLLRRVGLGerLTHTPDE----LSGGQQQRVAIARALINEPDVLLADEPTG 170
Cdd:PRK11174 438 -TLRDNVLLgnPDASDEQLQqalENAWVSEFLPLLPQG--LDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1906108912 171 NLDQETGRTILEEMTrlKETENIAIVAITHD-EQLVQYaDRVVRIVDGVI 219
Cdd:PRK11174 515 SLDAHSEQLVMQALN--AASRRQTTLMVTHQlEDLAQW-DQIWVMQDGQI 561
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-219 |
1.75e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 87.45 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRY-----ESGA------------ETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLdSPTEGVV 64
Cdd:COG4586 1 IIEVENLSKTYrvyekEPGLkgalkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtGIL-VPTSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 65 RLEGRDVTEasedERTEERRsELGFVF-QDFHLLPMLNAVENVEL-PSMWDTTVDRRERAVDLLRRV-GLGErLTHTP-D 140
Cdd:COG4586 80 RVLGYVPFK----RRKEFAR-RIGVVFgQRSQLWWDLPAIDSFRLlKAIYRIPDAEYKKRLDELVELlDLGE-LLDTPvR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 141 ELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD----EQLvqyADRVVRIVD 216
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDmddiEAL---CDRVIVIDH 230
|
...
gi 1906108912 217 GVI 219
Cdd:COG4586 231 GRI 233
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-219 |
1.80e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.69 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGAEtVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEasedERTEE 82
Cdd:PRK13642 4 ILEVENLVFKYEKESD-VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA----ENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDFHLLPMLNAVENVELPSMWDTTVDRRE---RAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINE 159
Cdd:PRK13642 79 LRRKIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEmikRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 160 PDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-212 |
6.73e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 87.32 E-value: 6.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEG---RDVTEASEderteeRRSeLGFVFQDfhllP 98
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVTRASL------RRN-IAVVFQD----A 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 99 ML---NAVENVEL--PSMWDTTVDR---RERAVDLLRRVGL------GERlthtPDELSGGQQQRVAIARALINEPDVLL 164
Cdd:PRK13657 419 GLfnrSIEDNIRVgrPDATDEEMRAaaeRAQAHDFIERKPDgydtvvGER----GRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 165 ADEPTGNLDQETGRTI---LEEMTRLKETENIAivaitHDEQLVQYADRVV 212
Cdd:PRK13657 495 LDEATSALDVETEAKVkaaLDELMKGRTTFIIA-----HRLSTVRNADRIL 540
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-219 |
1.69e-19 |
|
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: 86.33 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAEtvvALKDVDFHAERGEMVVVTGPSGSGKSTMLN-MIGLLDsPTEGVVRLEGRDVTEASedeRTEE 82
Cdd:TIGR01193 474 IVINDVSYSYGYGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKlLVGFFQ-ARSGEILLNGFSLKDID---RHTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSeLGFVFQDfhllPMLNA---VENVELPSMWDTTVDRRERAVDLLR--------RVGLGERLTHTPDELSGGQQQRVA 151
Cdd:TIGR01193 547 RQF-INYLPQE----PYIFSgsiLENLLLGAKENVSQDEIWAACEIAEikddienmPLGYQTELSEEGSSISGGQKQRIA 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 152 IARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETeniAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-219 |
2.42e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.97 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLdsPTEGVVRLEGRDVTEASEDERTEER-----RSELGF---VFQ- 92
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLL--PGQGEILLNGRPLSDWSAAELARHRaylsqQQSPPFampVFQy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 93 -DFHLLPMLNAVENVELPSMwdttvdrreravdLLRRVGLGERLTHTPDELSGGQQQRVAIARAL------IN-EPDVLL 164
Cdd:COG4138 90 lALHQPAGASSEAVEQLLAQ-------------LAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906108912 165 ADEPTGNLD---QETGRTILEEMTRLketeNIAIVAITHDEQL-VQYADRVVRIVDGVI 219
Cdd:COG4138 157 LDEPMNSLDvaqQAALDRLLRELCQQ----GITVVMSSHDLNHtLRHADRVWLLKQGKL 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
21-211 |
4.21e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.91 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVvRLEGRDVTEASE--DERTE--ERRSELGFVFQDFHL 96
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGF-RVEGKVTFHGKNlyAPDVDpvEVRRRIGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 97 LPMlNAVENVEL-PSMWDTTVDRRERAVDLLRRVGL----GERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGN 171
Cdd:PRK14243 103 FPK-SIYDNIAYgARINGYKGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1906108912 172 LDQETGRTILEEMTRLKETENIAIVaiTHDeqlVQYADRV 211
Cdd:PRK14243 182 LDPISTLRIEELMHELKEQYTIIIV--THN---MQQAARV 216
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-219 |
4.47e-19 |
|
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: 81.77 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASederTEER 83
Cdd:cd03244 3 IEFKNVSLRYRPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG----LHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLP-----------------MLNAVENVELPSMWDTTVDrreravdllrrvGLGERLTHTPDELSGGQ 146
Cdd:cd03244 77 RSRISIIPQDPVLFSgtirsnldpfgeysdeeLWQALERVGLKEFVESLPG------------GLDTVVEEGGENLSVGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 147 QQRVAIARALINEPDVLLADEPTGNLDQETGRTILEE-MTRLKeteNIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPETDALIQKTiREAFK---DCTVLTIAHRLDTIIDSDRILVLDKGRV 215
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-219 |
9.10e-19 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 81.36 E-value: 9.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGAETVVaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTeaseDERTEE 82
Cdd:cd03248 11 IVKFQNVTFAYPTRPDTLV-LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS----QYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDfhllPMLNA---VENVELpSMWDTTVDRRERAVDLLRRVGLGERLTHTPDE--------LSGGQQQRVA 151
Cdd:cd03248 86 LHSKVSLVGQE----PVLFArslQDNIAY-GLQSCSFECVKEAAQKAHAHSFISELASGYDTevgekgsqLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 152 IARALINEPDVLLADEPTGNLDQETGRTIleEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQV--QQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-217 |
9.91e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.07 E-value: 9.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 20 VVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVteaseDERTEERRSELGF--VFQDFHLL 97
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINY-----NKLDHKLAAQLGIgiIYQELSVI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 98 PMLNAVENV---ELPS--MWDTTV----DRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEP 168
Cdd:PRK09700 93 DELTVLENLyigRHLTkkVCGVNIidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1906108912 169 TGNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDG 217
Cdd:PRK09700 173 TSSLTNKEVDYLFLIMNQLRK-EGTAIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-219 |
1.09e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 81.04 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESG------------------AETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVR 65
Cdd:cd03220 1 IELENVSKSYPTYkggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 66 LEGRDVTEAsederteerrsELGFVFQdfhllPMLNAVENVELPSMWD--TTVDRRERAVDLLRRVGLGERLtHTP-DEL 142
Cdd:cd03220 81 VRGRVSSLL-----------GLGGGFN-----PELTGRENIYLNGRLLglSRKEIDEKIDEIIEFSELGDFI-DLPvKTY 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 143 SGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAiTHDEQLV-QYADRVVRIVDGVI 219
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILV-SHDPSSIkRLCDRALVLEKGKI 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-217 |
1.17e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.75 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 12 RYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKS-TMLNMIGLLD------SPTEGVVRLEGRDVTEASEDERTEERR 84
Cdd:PRK10261 21 AFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEqagglvQCDKMLLRRRSRQVIELSEQSAAQMRH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 85 ---SELGFVFQDfhllPM--LNAV--------ENVELPSMWDTTVDRRE--RAVDLLRRVGLGERLTHTPDELSGGQQQR 149
Cdd:PRK10261 101 vrgADMAMIFQE----PMtsLNPVftvgeqiaESIRLHQGASREEAMVEakRMLDQVRIPEAQTILSRYPHQLSGGMRQR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906108912 150 VAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLV-QYADRVVRIVDG 217
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQG 245
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
23-205 |
2.46e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.54 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVrlegrdvteasedERTEERRseLGFVFQDFHLLPMLNA 102
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGKLR--IGYVPQKLYLDTTLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 103 veNVELPSMWDTTVdRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILE 182
Cdd:PRK09544 85 --TVNRFLRLRPGT-KKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170 180
....*....|....*....|...
gi 1906108912 183 EMTRLKETENIAIVAITHDEQLV 205
Cdd:PRK09544 162 LIDQLRRELDCAVLMVSHDLHLV 184
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-211 |
3.18e-18 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 81.39 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDSP---TEGVVRLEGRDVTEASE 76
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcGVTKDNwrvTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 77 DERTEERRSELGFVFQDfhllPM--LNAVENVELPSM------------WDTTVDRRERAVDLLRRVGLGER---LTHTP 139
Cdd:PRK15093 81 RERRKLVGHNVSMIFQE----PQscLDPSERVGRQLMqnipgwtykgrwWQRFGWRKRRAIELLHRVGIKDHkdaMRSFP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 140 DELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLV-QYADRV 211
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLsQWADKI 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-209 |
3.86e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.08 E-value: 3.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 10 VKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLdSPTEGVVRLEGRdvTEASEDERTEER------ 83
Cdd:PRK14258 10 VNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGR--VEFFNQNIYERRvnlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPML---NAVENVEL----PSM-WDTTVDRRERAVDLLRRVGlgERLTHTPDELSGGQQQRVAIARA 155
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSvydNVAYGVKIvgwrPKLeIDDIVESALKDADLWDEIK--HKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1906108912 156 LINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHD-EQLVQYAD 209
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNlHQVSRLSD 219
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-213 |
5.17e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.23 E-value: 5.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMI--GLLDSPTEGVVRLegrdvteasederteerrselgfvfQDFHLLPML 100
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDV-------------------------PDNQFGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 101 NAVENVelPSMWDTTVdrrerAVDLLRRVGLGERLTH--TPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGR 178
Cdd:COG2401 101 SLIDAI--GRKGDFKD-----AVELLNAVGLSDAVLWlrRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1906108912 179 TILEEMTRLKETENIAIVAITHDEQLVQY--ADRVVR 213
Cdd:COG2401 174 RVARNLQKLARRAGITLVVATHHYDVIDDlqPDLLIF 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-217 |
5.60e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.14 E-value: 5.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 38 VTGPSGSGKSTMLNMIGLLDSPTEGV-----VRLEGRDVTEASEderTEERRSELGFVFQDFHLLPMlNAVENVELPSMW 112
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRD---VLEFRRRVGMLFQRPNPFPM-SIMDNVLAGVRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 113 DTTVDRRE-RAVDLLRRVGLG------ERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMT 185
Cdd:PRK14271 128 HKLVPRKEfRGVAQARLTEVGlwdavkDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR 207
|
170 180 190
....*....|....*....|....*....|...
gi 1906108912 186 RLkeTENIAIVAITHD-EQLVQYADRVVRIVDG 217
Cdd:PRK14271 208 SL--ADRLTVIIVTHNlAQAARISDRAALFFDG 238
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-168 |
1.76e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.15 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 25 DVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASedertEERRSELGFVfqdFHLL---PMLN 101
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-----DEYHQDLLYL---GHQPgikTELT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 102 AVENVELpSMWDTTVDRRERAVDLLRRVGLGER---LTHTpdeLSGGQQQRVAIARALINEPDVLLADEP 168
Cdd:PRK13538 91 ALENLRF-YQRLHGPGDDEALWEALAQVGLAGFedvPVRQ---LSAGQQRRVALARLWLTRAPLWILDEP 156
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-219 |
3.50e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.13 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDSPTEGVVRLEGRDVTEASEDERTEERRSELGFVFQ--DFHLLP 98
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTnGLIISETGQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 99 mlNAVENVELPSMWDTTVDRRE---RAVDLLRRVGLGER-LTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQ 174
Cdd:PRK13645 106 --ETIEKDIAFGPVNLGENKQEaykKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1906108912 175 ETGRTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:PRK13645 184 KGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKV 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
25-201 |
3.83e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.50 E-value: 3.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 25 DVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEdERTEERRSELGFVFQDFHLLPMLNAVE 104
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSR-SRLYTVRKRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 105 NVELP---------SMWDTTVDRReravdlLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQE 175
Cdd:PRK11831 104 NVAYPlrehtqlpaPLLHSTVMMK------LEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPI 177
|
170 180
....*....|....*....|....*.
gi 1906108912 176 TGRTILEEMTRLKETENIAIVAITHD 201
Cdd:PRK11831 178 TMGVLVKLISELNSALGVTCVVVSHD 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-169 |
4.95e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.01 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDsPTEGVVRLEGRDVteaseDERTEERRSELGFVFQDFHLLPM 99
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLtGLLP-ASEGEAWLFGQPV-----DAGDIATRRRVGYMSQAFSLYGE 353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906108912 100 LNAVENVELPS-MWDTTVDRRERAVD-LLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPT 169
Cdd:NF033858 354 LTVRQNLELHArLFHLPAAEIAARVAeMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-187 |
1.35e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.79 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYesGAETVValKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEasedeRTEER 83
Cdd:PRK13536 42 IDLAGVSKSY--GDKAVV--NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-----RARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHLLPMLNAVENVELPSMWDTTVDRRERAV--DLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPD 161
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVipSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180
....*....|....*....|....*.
gi 1906108912 162 VLLADEPTGNLDQETGRTILEEMTRL 187
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSL 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-211 |
1.72e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.76 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAEtVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEG----RDVT------- 72
Cdd:PTZ00265 383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINlkwwrsk 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 73 -----------------------------EASEDERTEE----------RRSELGFVFQDFHLlpMLNAVENVELPSMWD 113
Cdd:PTZ00265 462 igvvsqdpllfsnsiknnikyslyslkdlEALSNYYNEDgndsqenknkRNSCRAKCAGDLND--MSNTTDSNELIEMRK 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 114 T--TVDRRErAVDLLRRVGLGERLTHTPDE-----------LSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTI 180
Cdd:PTZ00265 540 NyqTIKDSE-VVDVSKKVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260 270
....*....|....*....|....*....|.
gi 1906108912 181 LEEMTRLKETENIAIVAITHDEQLVQYADRV 211
Cdd:PTZ00265 619 QKTINNLKGNENRITIIIAHRLSTIRYANTI 649
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-219 |
2.11e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.99 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 20 VVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERteeRRSELGFVFQDFH---L 96
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER---RRLGVAYIPEDRLgrgL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 97 LPMLNAVENVELPSMWDTTVDR---------RERAVDLLRRVGLGERLTHTP-DELSGGQQQRVAIARALINEPDVLLAD 166
Cdd:COG3845 348 VPDMSVAENLILGRYRRPPFSRggfldrkaiRAFAEELIEEFDVRTPGPDTPaRSLSGGNQQKVILARELSRDPKLLIAA 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 167 EPTGNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:COG3845 428 QPTRGLDVGAIEFIHQRLLELRD-AGAAVLLISEDlDEILALSDRIAVMYEGRI 480
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
33-219 |
2.73e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.41 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 33 GEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTeeRRseLGFVFQDFHLLPMLNAVENV---ELP 109
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--RR--IGLLAQNATTPGDITVQELVargRYP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 110 SMWDTTVDRRE--RAVD-LLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTR 186
Cdd:PRK10253 109 HQPLFTRWRKEdeEAVTkAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSE 188
|
170 180 190
....*....|....*....|....*....|....
gi 1906108912 187 LKETENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:PRK10253 189 LNREKGYTLAAVLHDlNQACRYASHLIALREGKI 222
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-219 |
2.75e-16 |
|
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: 73.99 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASederTEER 83
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP----LEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDfhllPMLnavenveLPSMWDTTVDRRERAVDLLRRVGLgeRLTHTPDELSGGQQQRVAIARALINEPDVL 163
Cdd:cd03369 81 RSSLTIIPQD----PTL-------FSGTIRSNLDPFDEYSDEEIYGAL--RVSEGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 164 LADEPTGNLDQET----GRTILEEMTrlketeNIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:cd03369 148 VLDEATASIDYATdaliQKTIREEFT------NSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-216 |
4.51e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.14 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIG---LLDsptEG---------VVRLEG---RDVTEASEDeRTEERRSEL 87
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLD---DGriiyeqdliVARLQQdppRNVEGTVYD-FVAEGIEEQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 88 GFVFQDFHLLPMLNAVEnvelPSmwDTTVDRRERAVDLLRRVGLG----------ERLTHTPD----ELSGGQQQRVAIA 153
Cdd:PRK11147 95 AEYLKRYHDISHLVETD----PS--EKNLNELAKLQEQLDHHNLWqlenrinevlAQLGLDPDaalsSLSGGWLRKAALG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906108912 154 RALINEPDVLLADEPTGNLDQEtgrTI--LEEMtrLKETENiAIVAITHDEQLVQyaDRVVRIVD 216
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIE---TIewLEGF--LKTFQG-SIIFISHDRSFIR--NMATRIVD 225
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-210 |
4.96e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.15 E-value: 4.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEAsedERT 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 EERRSELGFVFQDFHLLPMLNAVENVELPSMW---DTTVDRRERAVDLLRRvgLGERLTHTPDELSGGQQQRVAIARALI 157
Cdd:PRK11614 76 KIMREAVAIVPEGRRVFSRMTVEENLAMGGFFaerDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 158 NEPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADR 210
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNaNQALKLADR 206
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
22-197 |
9.60e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 75.13 E-value: 9.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTeaseDERTEERRSELGFVFQdfhlLPML- 100
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT----KLQLDSWRSRLAVVSQ----TPFLf 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 101 --NAVENVEL--PsmwDTTVDRRERAV-------DLLR-----RVGLGERLTHtpdeLSGGQQQRVAIARALINEPDVLL 164
Cdd:PRK10789 402 sdTVANNIALgrP---DATQQEIEHVArlasvhdDILRlpqgyDTEVGERGVM----LSGGQKQRISIARALLLNAEILI 474
|
170 180 190
....*....|....*....|....*....|...
gi 1906108912 165 ADEPTGNLDQETGRTILEEMTRLKETENIAIVA 197
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGEGRTVIISA 507
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-219 |
1.14e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.20 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 19 TVVALKDVDFHAERGEMVVVTGPSGSGKStmLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEERRSELGFVFQD----F 94
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQNprsaF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 95 HLLPMLNAVENVELPSMWDTTVDRRERAVdlLRRVGLGER---LTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGN 171
Cdd:PRK10418 93 NPLHTMHTHARETCLALGKPADDATLTAA--LEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1906108912 172 LDQETGRTILEEMTRLKETENIAIVAITHDEQLV-QYADRVVRIVDGVI 219
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRALGMLLVTHDMGVVaRLADDVAVMSHGRI 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-206 |
4.01e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.35 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 20 VVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASeDERTEERRSELGFVFQDFHllPM 99
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS-PGKLQALRRDIQFIFQDPY--AS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 100 LNAVENVELPSMWDTTVDR-------RERAVDLLRRVGL-GERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGN 171
Cdd:PRK10261 414 LDPRQTVGDSIMEPLRVHGllpgkaaAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190
....*....|....*....|....*....|....*
gi 1906108912 172 LDQETGRTILEEMTRLKETENIAIVAITHDEQLVQ 206
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVE 528
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
16-217 |
4.29e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.58 E-value: 4.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 16 GAETVValKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEdeRTEERRseLGFVFQDfH 95
Cdd:PRK11231 13 GTKRIL--NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS--RQLARR--LALLPQH-H 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 96 LLPMLNAV-ENVEL---P--SMWD--TTVDRR--ERAVDLLRRVGLGERLThtpDELSGGQQQRVAIARALINEPDVLLA 165
Cdd:PRK11231 86 LTPEGITVrELVAYgrsPwlSLWGrlSAEDNArvNQAMEQTRINHLADRRL---TDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 166 DEPTGNLDQETGRTILEEMTRLKeTENIAIVAITHD-EQLVQYADRVVRIVDG 217
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELN-TQGKTVVTVLHDlNQASRYCDHLVVLANG 214
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-214 |
4.82e-15 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 70.04 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGlldsPTEGVVRLEGrdvteasederTEERRSELGFVFqdfhllpmln 101
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLIS-----------FLPKFSRNKLIF---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 102 avenvelpsmwdttVDRRERAVDllrrVGLG----ERLTHTpdeLSGGQQQRVAIARALINEPD--VLLADEPTGNLDQE 175
Cdd:cd03238 65 --------------IDQLQFLID----VGLGyltlGQKLST---LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190
....*....|....*....|....*....|....*....
gi 1906108912 176 TGRTILEEMTRLKETENIAIVaITHDEQLVQYADRVVRI 214
Cdd:cd03238 124 DINQLLEVIKGLIDLGNTVIL-IEHNLDVLSSADWIIDF 161
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-219 |
6.46e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.78 E-value: 6.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYeSGaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEAsederTEE 82
Cdd:PRK15439 11 LLCARSISKQY-SG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL-----TPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELG--FVFQDFHLLPMLNAVENV--ELPSmwdtTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALIN 158
Cdd:PRK15439 82 KAHQLGiyLVPQEPLLFPNLSVKENIlfGLPK----RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906108912 159 EPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKlPEIRQLADRISVMRDGTI 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-200 |
1.08e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.25 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEderT 80
Cdd:PRK11288 2 SPYLSFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST---T 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 EERRSELGFVFQDFHLLPMLNAVENV---ELPSMWDtTVDRRE---RAVDLLRRvgLGERLT-HTP-DELSGGQQQRVAI 152
Cdd:PRK11288 75 AALAAGVAIIYQELHLVPEMTVAENLylgQLPHKGG-IVNRRLlnyEAREQLEH--LGVDIDpDTPlKYLSIGQRQMVEI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1906108912 153 ARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITH 200
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRA-EGRVILYVSH 198
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
23-214 |
1.39e-14 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 69.98 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTML---------------------NMIGLLDSPTegVVRLEGRDVTEASEDERTE 81
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPD--VDSIEGLSPAIAIDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 82 ER-RSELGFVFQDFHLLPMLNAVENVelpsmwdttvdrRERaVDLLRRVGLGE-RLTHTPDELSGGQQQRVAIARALINE 159
Cdd:cd03270 89 RNpRSTVGTVTEIYDYLRLLFARVGI------------RER-LGFLVDVGLGYlTLSRSAPTLSGGEAQRIRLATQIGSG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 160 PDVLL--ADEPTGNLDQETGRTILEEMTRLKETENIAIVaITHDEQLVQYADRVVRI 214
Cdd:cd03270 156 LTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLV-VEHDEDTIRAADHVIDI 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
9-217 |
2.26e-14 |
|
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: 69.28 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 9 VVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTML-NMIGLLDSpTEGVVRLEGRDVTEASEDERTEERRSEL 87
Cdd:cd03290 3 VTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNKNESEPSFEATRSRNRYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 88 GFVFQDFHLLpmlNAV--ENVELPSMWDTtvdRRERAV----------DLL---RRVGLGERLTHtpdeLSGGQQQRVAI 152
Cdd:cd03290 82 AYAAQKPWLL---NATveENITFGSPFNK---QRYKAVtdacslqpdiDLLpfgDQTEIGERGIN----LSGGQRQRICV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906108912 153 ARALINEPDVLLADEPTGNLDQETGRTILEE-MTRLKETENIAIVAITHDEQLVQYADRVVRIVDG 217
Cdd:cd03290 152 ARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-217 |
2.31e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.97 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYeSGaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDSPT-EGVVRLEGRDVteASEDERT 80
Cdd:NF040905 1 ILEMRGITKTF-PG---VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsGVYPHGSyEGEILFDGEVC--RFKDIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 EERRselGFVF--QDFHLLPMLNAVENVEL---PSM-----WDTTvdrRERAVDLLRRVGLGERLTHTPDELSGGQQQRV 150
Cdd:NF040905 75 SEAL---GIVIihQELALIPYLSIAENIFLgneRAKrgvidWNET---NRRARELLAKVGLDESPDTLVTDIGVGKQQLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 151 AIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDG 217
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKlNEIRRVADSITVLRDG 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-218 |
3.15e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 28 FHAERGEMVVVTGPSGSGKSTMLNMI-GLLdsPTEGVVRLEGRDVTEASEDERTeERRSELG------FVFQDFHLLPMl 100
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMaGLL--PGSGSIQFAGQPLEAWSAAELA-RHRAYLSqqqtppFAMPVFQYLTL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 101 navenvELPSMwdTTVDRRERAVDLL-RRVGLGERLTHTPDELSGGQQQRVAIARAL------IN-EPDVLLADEPTGNL 172
Cdd:PRK03695 93 ------HQPDK--TRTEAVASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpdINpAGQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1906108912 173 D--QETG-RTILEEMTRLketeNIAIVAITHD-EQLVQYADRVVRIVDGV 218
Cdd:PRK03695 165 DvaQQAAlDRLLSELCQQ----GIAVVMSSHDlNHTLRHADRVWLLKQGK 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
38-201 |
3.17e-14 |
|
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: 70.73 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 38 VTGPSGSGKSTMLNMIGLLDSPTEGVVRL----------------EGRDVTEASED---------ERTEERRSELGFVFQ 92
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPqpgikvgylpqepqldPTKTVRENVEEgvaeikdalDRFNEISAKYAEPDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 93 DFHLLpmlnAVENVELPSMWDT----TVDRR-ERAVDLLRRVGLGERLTHtpdeLSGGQQQRVAIARALINEPDVLLADE 167
Cdd:TIGR03719 116 DFDKL----AAEQAELQEIIDAadawDLDSQlEIAMDALRCPPWDADVTK----LSGGERRRVALCRLLLSKPDMLLLDE 187
|
170 180 190
....*....|....*....|....*....|....
gi 1906108912 168 PTGNLDQETgRTILEEMtrLKETENiAIVAITHD 201
Cdd:TIGR03719 188 PTNHLDAES-VAWLERH--LQEYPG-TVVAVTHD 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-217 |
5.13e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDSPT-EGVVRLEGRDVTeASEDERT 80
Cdd:PRK13549 5 LLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsGVYPHGTyEGEIIFEGEELQ-ASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 EerRSELGFVFQDFHLLPMLNAVENVELPSM--------WDTTVdrrERAVDLLRRVGLGERlTHTP-DELSGGQQQRVA 151
Cdd:PRK13549 80 E--RAGIAIIHQELALVKELSVLENIFLGNEitpggimdYDAMY---LRAQKLLAQLKLDIN-PATPvGNLGLGQQQLVE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 152 IARALINEPDVLLADEPTGNL-DQETgRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDG 217
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASLtESET-AVLLDIIRDLKA-HGIACIYISHKlNEVKAISDTICVIRDG 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-218 |
5.38e-14 |
|
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: 70.32 E-value: 5.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDsPTEGVVRLEGRdvteasederteerrseLGFVFQDFHLLPMlN 101
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMImGELE-PSEGKIKHSGR-----------------ISFSPQTSWIMPG-T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 102 AVENVELPSMWDttvDRRERAVdlLRRVGLGERLTHTPDE-----------LSGGQQQRVAIARALINEPDVLLADEPTG 170
Cdd:TIGR01271 503 IKDNIIFGLSYD---EYRYTSV--IKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1906108912 171 NLDQETGRTILEEMTrLKETENIAIVAITHDEQLVQYADRVVRIVDGV 218
Cdd:TIGR01271 578 HLDVVTEKEIFESCL-CKLMSNKTRILVTSKLEHLKKADKILLLHEGV 624
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-219 |
1.11e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 24 KDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDER--------TEERRsELGFvFQDFH 95
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAvkkgmayiTESRR-DNGF-FPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 96 L---LPMLNAVENVELPSMWDTTVDRRERAVDLLRRVGLGER---LTHTPDELSGGQQQRVAIARALINEPDVLLADEPT 169
Cdd:PRK09700 358 IaqnMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKchsVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1906108912 170 GNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
33-217 |
1.23e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.89 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 33 GEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVteASEDERTEERrsELGFVFQDfhlLPMLNAVENVELPSM- 111
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL--ESWSSKAFAR--KVAYLPQQ---LPAAEGMTVRELVAIg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 112 ---WDTTVDR-----RERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEE 183
Cdd:PRK10575 110 rypWHGALGRfgaadREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLAL 189
|
170 180 190
....*....|....*....|....*....|....*
gi 1906108912 184 MTRLKETENIAIVAITHDEQL-VQYADRVVRIVDG 217
Cdd:PRK10575 190 VHRLSQERGLTVIAVLHDINMaARYCDYLVALRGG 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-212 |
1.75e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 68.66 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 32 RGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLegrDVT--------EASEDERTEErrselgfvfqdfhllpMLNAV 103
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE---DLKisykpqyiSPDYDGTVEE----------------FLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 104 ENVELPSMWDTTvdrreravDLLRRVGLgERLTHTP-DELSGGQQQRVAIARALINEPDVLLADEPTGNLDQE----TGR 178
Cdd:COG1245 426 NTDDFGSSYYKT--------EIIKPLGL-EKLLDKNvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAK 496
|
170 180 190
....*....|....*....|....*....|....*
gi 1906108912 179 TIleemTRLKETENIAIVAITHDEQLVQY-ADRVV 212
Cdd:COG1245 497 AI----RRFAENRGKTAMVVDHDIYLIDYiSDRLM 527
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-217 |
1.78e-13 |
|
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: 67.57 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDsPTEGVVRLEGRdvteasederteerrseLGFVFQDFHLLPMlN 101
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLIlGELE-PSEGKIKHSGR-----------------ISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 102 AVENVELPSMWDttvDRRERAVdlLRRVGLGERLTHTPDE-----------LSGGQQQRVAIARALINEPDVLLADEPTG 170
Cdd:cd03291 114 IKENIIFGVSYD---EYRYKSV--VKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1906108912 171 NLDQETGRTILEEMTrLKETENIAIVAITHDEQLVQYADRVVRIVDG 217
Cdd:cd03291 189 YLDVFTEKEIFESCV-CKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-217 |
2.66e-13 |
|
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: 67.93 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESgaetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDSPT-EGVVRLEGRDVtEASEDERT 80
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILsGVYPHGTwDGEIYWSGSPL-KASNIRDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 EerRSELGFVFQDFHLLPMLNAVENV------ELPSMWDTTVDRRERAVDLLRRVGL-GERLTHTPDELSGGQQQRVAIA 153
Cdd:TIGR02633 76 E--RAGIVIIHQELTLVPELSVAENIflgneiTLPGGRMAYNAMYLRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906108912 154 RALINEPDVLLADEPTGNL-DQETgrTILEEMTRLKETENIAIVAITHD-EQLVQYADRVVRIVDG 217
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLtEKET--EILLDIIRDLKAHGVACVYISHKlNEVKAVCDTICVIRDG 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-212 |
2.69e-13 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 66.66 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 32 RGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVT------EASEDERTEERRSElgfVFQDFHLLPMLNAveN 105
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyiKADYEGTVRDLLSS---ITKDFYTHPYFKT--E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 106 VELPSMWDTTVDRRERavdllrrvglgerlthtpdELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMT 185
Cdd:cd03237 99 IAKPLQIEQILDREVP-------------------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
170 180
....*....|....*....|....*...
gi 1906108912 186 RLKETENIAIVAITHDEQLVQY-ADRVV 212
Cdd:cd03237 160 RFAENNEKTAFVVEHDIIMIDYlADRLI 187
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
38-201 |
3.82e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 38 VTGPSGSGKSTMLNMIGLLDSPTEGVVRL----------------EGRDVTEASED---------ERTEERRSELGFVFQ 92
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPapgikvgylpqepqldPEKTVRENVEEgvaevkaalDRFNEIYAAYAEPDA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 93 DFHLLpmlnAVENVELPSM------WDttVDRR-ERAVDLLRRVGLGERLTHtpdeLSGGQQQRVAIARALINEPDVLLA 165
Cdd:PRK11819 118 DFDAL----AAEQGELQEIidaadaWD--LDSQlEIAMDALRCPPWDAKVTK----LSGGERRRVALCRLLLEKPDMLLL 187
|
170 180 190
....*....|....*....|....*....|....*.
gi 1906108912 166 DEPTGNLDQETgRTILEEMtrLKETENiAIVAITHD 201
Cdd:PRK11819 188 DEPTNHLDAES-VAWLEQF--LHDYPG-TVVAVTHD 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-212 |
3.99e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.53 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 32 RGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVrleGRDVT--------EASEDERTEERrseLGFVFQDFHllpmlnav 103
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELKisykpqyiKPDYDGTVEDL---LRSITDDLG-------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 104 envelPSMWDTtvdrreravDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQE----TGRT 179
Cdd:PRK13409 430 -----SSYYKS---------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKA 495
|
170 180 190
....*....|....*....|....*....|....
gi 1906108912 180 IleemTRLKETENIAIVAITHDEQLVQY-ADRVV 212
Cdd:PRK13409 496 I----RRIAEEREATALVVDHDIYMIDYiSDRLM 525
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-212 |
5.30e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.36 E-value: 5.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESgAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGL---LDSPTEGVVRLEGRDVTEASEDERT 80
Cdd:PTZ00265 1166 IEIMDVNFRYIS-RPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydLKNDHHIVFKNEHTNDMTNEQDYQG 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 EERRS------------------ELGFVFQ-------------DFHLLPMLNAVENV-ELPSMWDTTV------DRRERA 122
Cdd:PTZ00265 1245 DEEQNvgmknvnefsltkeggsgEDSTVFKnsgkilldgvdicDYNLKDLRNLFSIVsQEPMLFNMSIyenikfGKEDAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 123 VDLLRRV----GLGERLTHTPDE-----------LSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRL 187
Cdd:PTZ00265 1325 REDVKRAckfaAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
250 260
....*....|....*....|....*
gi 1906108912 188 KETENIAIVAITHDEQLVQYADRVV 212
Cdd:PTZ00265 1405 KDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-216 |
7.34e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 66.67 E-value: 7.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAetvVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEdertEER 83
Cdd:PRK10790 341 IDIDNVSFAYRDDN---LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH----SVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDfhllPMLNA---VENVEL------PSMWDT--TVdrreRAVDLLRRV--GLGERLTHTPDELSGGQQQRV 150
Cdd:PRK10790 414 RQGVAMVQQD----PVVLAdtfLANVTLgrdiseEQVWQAleTV----QLAELARSLpdGLYTPLGEQGNNLSVGQKQLL 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906108912 151 AIARALINEPDVLLADEPTGNLDQETGRTILEemtrlketeniAIVAITHDEQLVQYADRVVRIVD 216
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQ-----------ALAAVREHTTLVVIAHRLSTIVE 540
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
26-184 |
7.97e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.87 E-value: 7.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 26 VDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEAsEDERTEERRSELGFVFQD------FHLLPM 99
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG-DRSRFMAYLGHLPGLKADlstlenLHFLCG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 100 LNAVENVELPSMWDTTVDRRERAVDLLRrvglgerlthtpdELSGGQQQRVAIARALINEPDVLLADEPTGNLDQEtGRT 179
Cdd:PRK13543 109 LHGRRAKQMPGSALAIVGLAGYEDTLVR-------------QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-GIT 174
|
....*
gi 1906108912 180 ILEEM 184
Cdd:PRK13543 175 LVNRM 179
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-217 |
8.83e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.96 E-value: 8.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 8 SVVKRYESGAETVVALKDVDFHaeRGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVtEASEDERteerRSEL 87
Cdd:TIGR01257 933 NLVKIFEPSGRPAVDRLNITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAV----RQSL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 88 GFVFQDFHLLPMLNAVENVELPSM-----WDTTVDRRERavdLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDV 162
Cdd:TIGR01257 1006 GMCPQHNILFHHLTVAEHILFYAQlkgrsWEEAQLEMEA---MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1906108912 163 LLADEPTGNLDQETGRTILEEMTRLKETENIaIVAITHDEQLVQYADRVVRIVDG 217
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLLKYRSGRTI-IMSTHHMDEADLLGDRIAIISQG 1136
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
23-207 |
9.35e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.43 E-value: 9.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGllDSP----TEGVVRLEGRDVTEASEDErteerRSELG--FVFQ---- 92
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHPaykiLEGDILFKGESILDLEPEE-----RAHLGifLAFQypie 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 93 -------DFhllpmLNAVENVELPSMWDTTVDR---RERAVDLLRRVGLGER-LTHTPDE-LSGGQQQRVAIARALINEP 160
Cdd:CHL00131 96 ipgvsnaDF-----LRLAYNSKRKFQGLPELDPlefLEIINEKLKLVGMDPSfLSRNVNEgFSGGEKKRNEILQMALLDS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1906108912 161 DVLLADEPTGNLDQETGRTILEEMTRLKETENiAIVAITHDEQLVQY 207
Cdd:CHL00131 171 ELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQRLLDY 216
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-217 |
1.48e-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: 63.82 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYESGAETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGlldSPTEGVVRLEGrDVTEASE--DE 78
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA---NRTEGNVSVEG-DIHYNGIpyKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 79 RTEERRSELGFVFQDFHLLPMLNAVEnvelpsmwdtTVD--RRERAVDLLRRVglgerlthtpdelSGGQQQRVAIARAL 156
Cdd:cd03233 77 FAEKYPGEIIYVSEEDVHFPTLTVRE----------TLDfaLRCKGNEFVRGI-------------SGGERKRVSIAEAL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 157 INEPDVLLADEPTGNLDQETGRTI---LEEMTRLKETENIAIVAITHDEQLVQYaDRVVRIVDG 217
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTALEIlkcIRTMADVLKTTTFVSLYQASDEIYDLF-DKVLVLYEG 196
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
135-214 |
2.07e-12 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 63.40 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 135 LTHTPDELSGGQQQ------RVAIARALINEPDVLLADEPTGNLDQETGRTILEE-MTRLKETENIAIVAITHDEQLVQY 207
Cdd:cd03240 109 LLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEiIEERKSQKNFQLIVITHDEELVDA 188
|
....*..
gi 1906108912 208 ADRVVRI 214
Cdd:cd03240 189 ADHIYRV 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-219 |
3.40e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.69 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 24 KDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEerrseLGFVFqdfhlLPMLNAV 103
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLA-----RGLVY-----LPEDRQS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 104 E--NVELPSMWDT---TVDR--------RERAVDLLRRVGLGERLTHtPDE----LSGGQQQRVAIARALINEPDVLLAD 166
Cdd:PRK15439 350 SglYLDAPLAWNVcalTHNRrgfwikpaRENAVLERYRRALNIKFNH-AEQaartLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1906108912 167 EPTGNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAA-QNVAVLFISSDlEEIEQMADRVLVMHQGEI 481
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-201 |
4.01e-12 |
|
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: 64.57 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGaetvVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLeGRDVTEASEDERtee 82
Cdd:TIGR03719 322 VIEAENLTKAFGDK----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQS--- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 rRSELG---FVFQDF-----HLLpmlnaVENVELPSmwdttvdrreRA---------VDLLRRVGlgerlthtpdELSGG 145
Cdd:TIGR03719 394 -RDALDpnkTVWEEIsggldIIK-----LGKREIPS----------RAyvgrfnfkgSDQQKKVG----------QLSGG 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1906108912 146 QQQRVAIARALINEPDVLLADEPTGNLDQETGRTiLEEMtrLKETENIAIVaITHD 201
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRA-LEEA--LLNFAGCAVV-ISHD 499
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-219 |
1.09e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.36 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 30 AERGEMVVVTGPSGSGKSTMLNMIG--LLDSPTEGVVRLEGRDVTEASEdERTeerrselGFVFQDFHLLPMLNAVENVE 107
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAgrIQGNNFTGTILANNRKPTKQIL-KRT-------GFVTQDDILYPHLTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 108 LPSM--WDTTVDRRER---AVDLLRRVGL--------GERLTHTpdeLSGGQQQRVAIARALINEPDVLLADEPTGNLDQ 174
Cdd:PLN03211 163 FCSLlrLPKSLTKQEKilvAESVISELGLtkcentiiGNSFIRG---ISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1906108912 175 ETGRTILEEMTRLKEtENIAIVAITHdeqlvQYADRVVRIVDGVI 219
Cdd:PLN03211 240 TAAYRLVLTLGSLAQ-KGKTIVTSMH-----QPSSRVYQMFDSVL 278
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-209 |
2.34e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.73 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVteaseDERTEERRSELGFVFQDFHLLPMLNA 102
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-----KKDLCTYQKQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 103 VENVelpsMWDTTVDRRERAVD-LLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQetgRTIL 181
Cdd:PRK13540 92 RENC----LYDIHFSPGAVGITeLCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE---LSLL 164
|
170 180 190
....*....|....*....|....*....|
gi 1906108912 182 EEMTRLKE--TENIAIVAITHDEQLVQYAD 209
Cdd:PRK13540 165 TIITKIQEhrAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-217 |
3.01e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 20 VVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEerrSELGFVFQDFHLLPM 99
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQE---AGIGIIHQELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 100 LNAVENVELPSMWDTTVDR------RERAVDLLRRVGLgerlTHTPD----ELSGGQQQRVAIARALINEPDVLLADEPT 169
Cdd:PRK10762 94 LTIAENIFLGREFVNRFGRidwkkmYAEADKLLARLNL----RFSSDklvgELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1906108912 170 GNL-DQETgRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDG 217
Cdd:PRK10762 170 DALtDTET-ESLFRVIRELKS-QGRGIVYISHRlKEIFEICDDVTVFRDG 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-198 |
6.38e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 6.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDS---PTEGVVRLEGrdvteASEDERTEERRSELGFVFQ-DFHlL 97
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIaSNTDGfhiGVEGVITYDG-----ITPEEIKKHYRGDVVYNAEtDVH-F 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 98 PMLNAVENVELPSMWDTT------VDRRERA---VDLLRRVgLGerLTHTPDE---------LSGGQQQRVAIARALINE 159
Cdd:TIGR00956 151 PHLTVGETLDFAARCKTPqnrpdgVSREEYAkhiADVYMAT-YG--LSHTRNTkvgndfvrgVSGGERKRVSIAEASLGG 227
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1906108912 160 PDVLLADEPTGNLDQETGrtiLEEMTRLKETENI----AIVAI 198
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATA---LEFIRALKTSANIldttPLVAI 267
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-214 |
6.43e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.28 E-value: 6.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAetvVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIglldsptEGVVRLEGRDVTEASEDERTEER 83
Cdd:PRK15056 7 IVVNDVTVTWRNGH---TALRDASFTVPGGSIAALVGVNGSGKSTLFKAL-------MGFVRLASGKISILGQPTRQALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDFHL---LPMLnaVENV-------ELPSMWDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIA 153
Cdd:PRK15056 77 KNLVAYVPQSEEVdwsFPVL--VEDVvmmgrygHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 154 RALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQLVQYADRVVRI 214
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-205 |
7.04e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.41 E-value: 7.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 12 RYESgaETVVALKDVDF--HAERGemvvVTGPSGSGKSTM-LNMIGLLdSPTEGVVRLEGRDVTEASEDerTEERRSELG 88
Cdd:PRK13638 10 RYQD--EPVLKGLNLDFslSPVTG----LVGANGCGKSTLfMNLSGLL-RPQKGAVLWQGKPLDYSKRG--LLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 89 FVFQDFHLLPMLNAVENVELPSMWDTTVDRRE--RAVDLLRRVGLGERLTHTPDE-LSGGQQQRVAIARALINEPDVLLA 165
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEitRRVDEALTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1906108912 166 DEPTGNLDqETGRTILEEMTRLKETENIAIVAITHDEQLV 205
Cdd:PRK13638 161 DEPTAGLD-PAGRTQMIAIIRRIVAQGNHVIISSHDIDLI 199
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-220 |
7.96e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.91 E-value: 7.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLN-MIGLLDSPTEGVVRLEGrdvteasederTEERRSELGFVFqdfhllpmlN 101
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-----------TVAYVPQVSWIF---------N 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 102 AV--ENVELPSMWDTtvDRRERAVDL--LRR----------VGLGERLTHtpdeLSGGQQQRVAIARALINEPDVLLADE 167
Cdd:PLN03130 693 ATvrDNILFGSPFDP--ERYERAIDVtaLQHdldllpggdlTEIGERGVN----ISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 168 PTGNLDQETGRTILEEMTRlKETENIAIVAITHDEQLVQYADRVVRIVDGVIQ 220
Cdd:PLN03130 767 PLSALDAHVGRQVFDKCIK-DELRGKTRVLVTNQLHFLSQVDRIILVHEGMIK 818
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-173 |
8.32e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.52 E-value: 8.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 1 MSIIELDSVVKRYEsgAETVValKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERT 80
Cdd:PRK10895 1 MATLTAKNLAKAYK--GRRVV--EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 81 eerRSELGFVFQDFHLLPMLNAVENVE--LPSMWDTTVDRRE-RAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALI 157
Cdd:PRK10895 77 ---RRGIGYLPQEASIFRRLSVYDNLMavLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170
....*....|....*.
gi 1906108912 158 NEPDVLLADEPTGNLD 173
Cdd:PRK10895 154 ANPKFILLDEPFAGVD 169
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-169 |
8.67e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.91 E-value: 8.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYesGAetVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEE 82
Cdd:NF033858 1 VARLEGVSHRY--GK--TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RrseLGFVFQDF--HLLPMLNAVENVE-------LPSmwdttVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIA 153
Cdd:NF033858 77 R---IAYMPQGLgkNLYPTLSVFENLDffgrlfgQDA-----AERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLC 148
|
170
....*....|....*.
gi 1906108912 154 RALINEPDVLLADEPT 169
Cdd:NF033858 149 CALIHDPDLLILDEPT 164
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-220 |
1.51e-10 |
|
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: 60.34 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTM-LNMIGLLDSpTEGVVRLEGRDVTEASederTEE 82
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLV--LRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINES-AEGEIIIDGLNIAKIG----LHD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDfhllPML-NAVENVELPSMWDTTVDRRERAVDLLRRVG----LGERLTHTPDE----LSGGQQQRVAIA 153
Cdd:TIGR00957 1358 LRFKITIIPQD----PVLfSGSLRMNLDPFSQYSDEEVWWALELAHLKTfvsaLPDKLDHECAEggenLSVGQRQLVCLA 1433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 154 RALINEPDVLLADEPTGNLDQETGRTIleEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVIQ 220
Cdd:TIGR00957 1434 RALLRKTKILVLDEATAAVDLETDNLI--QSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVA 1498
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-219 |
2.47e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIG--LLDSPTEGVVRLEGrDVT------EASEDERTEERRSEL----- 87
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdLTGGGAPRGARVTG-DVTlngeplAAIDAPRLARLRAVLpqaaq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 88 -GFVFQDFHLLpMLNAVENVELPSmwDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARAL---------I 157
Cdd:PRK13547 94 pAFAFSAREIV-LLGRYPHARRAG--ALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 158 NEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIVAITHDEQL-VQYADRVVRIVDGVI 219
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLaARHADRIAMLADGAI 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-201 |
4.36e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 31 ERGEMVVVTGPSGSGKSTMLNMI-GLLdsptegVVRLeGRDVTEASEDERTEE-RRSELGFVFQDF-------------- 94
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILsGEL------IPNL-GDYEEEPSWDEVLKRfRGTELQNYFKKLyngeikvvhkpqyv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 95 HLLPML---NAVENVElpsmwdtTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGN 171
Cdd:PRK13409 170 DLIPKVfkgKVRELLK-------KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190
....*....|....*....|....*....|....
gi 1906108912 172 LDqetgrtILEEMT--RL--KETENIAIVAITHD 201
Cdd:PRK13409 243 LD------IRQRLNvaRLirELAEGKYVLVVEHD 270
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-217 |
4.60e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.90 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 18 ETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVrlegrdvteasederteERRSELGFVFQDFHLL 97
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------------DRNGEVSVIAISAGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 98 PMLNAVENVELP--SMWDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQE 175
Cdd:PRK13546 98 GQLTGIENIEFKmlCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1906108912 176 TGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDG 217
Cdd:PRK13546 178 FAQKCLDKIYEFKE-QNKTIFFVSHNlGQVRQFCTKIAWIEGG 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-173 |
4.65e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGaetvVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GllDSPtEGV---VRLEGRdvtEASEDER 79
Cdd:PRK10938 261 IVLNNGVVSYNDR----PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItG--DHP-QGYsndLTLFGR---RRGSGET 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 80 TEERRSELGFVFQDFHLLPMLNA-VENVELPSMWDT------TVDR-RERAVDLLRRVGLGERLTHTP-DELSGGQQQRV 150
Cdd:PRK10938 331 IWDIKKHIGYVSSSLHLDYRVSTsVRNVILSGFFDSigiyqaVSDRqQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLA 410
|
170 180
....*....|....*....|...
gi 1906108912 151 AIARALINEPDVLLADEPTGNLD 173
Cdd:PRK10938 411 LIVRALVKHPTLLILDEPLQGLD 433
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
25-214 |
5.06e-10 |
|
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: 56.21 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 25 DVDFHAERgeMVVVTGPSGSGKSTMLNMIGLL---DSPTEGVVRLEGRDVTEASederteerrSELGFVFqdfhllpmln 101
Cdd:cd03227 15 DVTFGEGS--LTIITGPNGSGKSTILDAIGLAlggAQSATRRRSGVKAGCIVAA---------VSAELIF---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 102 avenvelpsmwdttvdrreravdllrrvglgerlthTPDELSGGQQQRVAIARAL----INEPDVLLADEPTGNLDQETG 177
Cdd:cd03227 74 ------------------------------------TRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDG 117
|
170 180 190
....*....|....*....|....*....|....*..
gi 1906108912 178 RTILEEMTRLKETENIAIVaITHDEQLVQYADRVVRI 214
Cdd:cd03227 118 QALAEAILEHLVKGAQVIV-ITHLPELAELADKLIHI 153
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-201 |
7.34e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 7.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 3 IIELDSVVKRYESGaetvVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLeGRDVT--------EA 74
Cdd:PRK11819 324 VIEAENLSKSFGDR----LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKlayvdqsrDA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 75 SEDERTeerrselgfVFQDFHL-LPMLNaVENVELPSmwdttvdrreRA---------VDLLRRVGlgerlthtpdELSG 144
Cdd:PRK11819 399 LDPNKT---------VWEEISGgLDIIK-VGNREIPS----------RAyvgrfnfkgGDQQKKVG----------VLSG 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 145 GQQQRVAIARALINEPDVLLADEPTGNLDQETGRTiLEEMtrLKETENIAIVaITHD 201
Cdd:PRK11819 449 GERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRA-LEEA--LLEFPGCAVV-ISHD 501
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-173 |
7.70e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 7.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDSpTEGVVRLEGRDVTEASEDER--------TEERRSElGFVFQd 93
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPR-TSGYVTLDGHEVVTRSPQDGlangivyiSEDRKRD-GLVLG- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 94 fhllpmLNAVENVELPSM------WDTTVDRRER-AVDllRRVGLGERLTHTPDE----LSGGQQQRVAIARALINEPDV 162
Cdd:PRK10762 345 ------MSVKENMSLTALryfsraGGSLKHADEQqAVS--DFIRLFNIKTPSMEQaiglLSGGNQQKVAIARGLMTRPKV 416
|
170
....*....|.
gi 1906108912 163 LLADEPTGNLD 173
Cdd:PRK10762 417 LILDEPTRGVD 427
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-219 |
1.01e-09 |
|
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: 57.65 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLN-MIGLLDSpTEGVVRLEGrDVTEASEDE--RTEERRSELGF---------- 89
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKG-SVAYVPQQAwiQNDSLRENILFgkalnekyyq 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 90 -VFQDFHLLPMLNAvenveLPSMwdttvDRREravdllrrvgLGERLTHtpdeLSGGQQQRVAIARALINEPDVLLADEP 168
Cdd:TIGR00957 732 qVLEACALLPDLEI-----LPSG-----DRTE----------IGEKGVN----LSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1906108912 169 TGNLDQETGRTILEEMTRLKET-ENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:TIGR00957 788 LSAVDAHVGKHIFEHVIGPEGVlKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-219 |
1.90e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGaetvVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLegrdvteaSEDerteer 83
Cdd:PRK15064 320 LEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW--------SEN------ 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 rSELGFVFQDfHLLPMLNAVENVELPSMWdttvdRRERAVDLLRRVGLGeRLTHTPDE-------LSGGQQQRVAIARAL 156
Cdd:PRK15064 382 -ANIGYYAQD-HAYDFENDLTLFDWMSQW-----RQEGDDEQAVRGTLG-RLLFSQDDikksvkvLSGGEKGRMLFGKLM 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906108912 157 INEPDVLLADEPTGNLDQEtgrTIleemtrlkETENIA-------IVAITHDEQLVQ-YADRVVRIV-DGVI 219
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDME---SI--------ESLNMAlekyegtLIFVSHDREFVSsLATRIIEITpDGVV 514
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-220 |
3.17e-09 |
|
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: 53.92 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 32 RGEMVVVTGPSGSGKSTMLNMI-GLLDSPTEGVVRLEGRDVTEASEDERteerrselgfvfqdfhllpmlnavenvelps 110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQL------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 111 mwdttvdrreravdllrrvgLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEE-----MT 185
Cdd:smart00382 50 --------------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLL 109
|
170 180 190
....*....|....*....|....*....|....*
gi 1906108912 186 RLKETENIAIVAITHDEQLVQyADRVVRIVDGVIQ 220
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLG-PALLRRRFDRRIV 143
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-183 |
3.50e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASedeRTEER 83
Cdd:PLN03232 1235 IKFEDVHLRYRPGLPPV--LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSeLGFVFQD---------FHLLPMLNAVEnvelPSMWDTTvdRRERAVDLLRR--VGLGERLTHTPDELSGGQQQRVAI 152
Cdd:PLN03232 1310 RV-LSIIPQSpvlfsgtvrFNIDPFSEHND----ADLWEAL--ERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSL 1382
|
170 180 190
....*....|....*....|....*....|....*
gi 1906108912 153 ARALINEPDVLLADEPTGNLDQETG----RTILEE 183
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVRTDsliqRTIREE 1417
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-220 |
4.10e-09 |
|
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: 55.60 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 25 DVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDSPTEGVVRLEGRDVTEASEDERTE-------ERRSELGFVfqdfhl 96
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAQAIRagiamvpEDRKRHGIV------ 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 97 lPMLNAVENVELPSMWDTTVDRRERAVDLLRRVGLG-ERL---THTPD----ELSGGQQQRVAIARALINEPDVLLADEP 168
Cdd:TIGR02633 352 -PILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAiQRLkvkTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 169 TGNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDGVIQ 220
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSElAEVLGLSDRVLVIGEGKLK 482
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-219 |
5.84e-09 |
|
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: 54.53 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTM----LNMIGLLDspteGVVRLEGRDVTEASeder 79
Cdd:cd03288 20 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLP---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 80 TEERRSELGFVFQDfhllPML-NAVENVELPSMWDTTVDRRERAVDL--LRRV------GLGERLTHTPDELSGGQQQRV 150
Cdd:cd03288 90 LHTLRSRLSIILQD----PILfSGSIRFNLDPECKCTDDRLWEALEIaqLKNMvkslpgGLDAVVTEGGENFSVGQRQLF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 151 AIARALINEPDVLLADEPTGNLDQETgRTILEE--MTRLKETeniAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:cd03288 166 CLARAFVRKSSILIMDEATASIDMAT-ENILQKvvMTAFADR---TVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-200 |
8.15e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.90 E-value: 8.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDerteerrselgfvfqdfHLLPMLN 101
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISS-----------------GLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 102 AVENVELPS--MWDTTVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRT 179
Cdd:PRK13545 102 GIENIELKGlmMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180
....*....|....*....|.
gi 1906108912 180 ILEEMTRLKEtENIAIVAITH 200
Cdd:PRK13545 182 CLDKMNEFKE-QGKTIFFISH 201
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
23-190 |
1.75e-08 |
|
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: 52.25 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGL--LDSPTEGVVRLEGRdvteasedERTEERRSELGFVFQ-DFHlLPM 99
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGR--------PLDKNFQRSTGYVEQqDVH-SPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 100 LNAVENVELPSmwdttvdrreravdLLRrvglgerlthtpdELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRT 179
Cdd:cd03232 94 LTVREALRFSA--------------LLR-------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170
....*....|.
gi 1906108912 180 ILEEMTRLKET 190
Cdd:cd03232 147 IVRFLKKLADS 157
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-183 |
1.78e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.97 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASederTEER 83
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPV--LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG----LMDL 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQD---------FHLLPmLNAVENVELpsmWDTTvdrrERA--VDLLRR--VGLGERLTHTPDELSGGQQQRV 150
Cdd:PLN03130 1312 RKVLGIIPQApvlfsgtvrFNLDP-FNEHNDADL---WESL----ERAhlKDVIRRnsLGLDAEVSEAGENFSVGQRQLL 1383
|
170 180 190
....*....|....*....|....*....|....*..
gi 1906108912 151 AIARALINEPDVLLADEPTGNLDQETG----RTILEE 183
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVDVRTDaliqKTIREE 1420
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-180 |
1.84e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.15 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 12 RYESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSpTEGVVRLEGrdvteASEDERT-EERRSELGFV 90
Cdd:TIGR01271 1226 KYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG-----VSWNSVTlQTWRKAFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 91 FQDFHLLP-----MLNAVENVELPSMWDTTvdrreravdllRRVGLGERLTHTPDE-----------LSGGQQQRVAIAR 154
Cdd:TIGR01271 1298 PQKVFIFSgtfrkNLDPYEQWSDEEIWKVA-----------EEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLAR 1366
|
170 180
....*....|....*....|....*.
gi 1906108912 155 ALINEPDVLLADEPTGNLDQETGRTI 180
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQII 1392
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-216 |
2.38e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 22 ALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDER--------TEERRSELGFVFQD 93
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAinhgfalvTEERRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 94 FHLLPMLNAVENVElpSMWDTTVDRRERA-----VDLLRRVGLGERlTHTpDELSGGQQQRVAIARALINEPDVLLADEP 168
Cdd:PRK10982 343 IGFNSLISNIRNYK--NKVGLLDNSRMKSdtqwvIDSMRVKTPGHR-TQI-GSLSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 169 TGNLDQETGRTILEEMTRL-KETENIAIVA--------IThDEQLVQYADRVVRIVD 216
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAELaKKDKGIIIISsempellgIT-DRILVMSNGLVAGIVD 474
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-220 |
2.96e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLN-MIGLLDSPTEGVVRLEGrdvteasederTEERRSELGFVFqdfhllpmlN 101
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-----------SVAYVPQVSWIF---------N 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 102 AV--ENVELPSMWDTtvDRRERAVDLLR------------RVGLGERLTHtpdeLSGGQQQRVAIARALINEPDVLLADE 167
Cdd:PLN03232 693 ATvrENILFGSDFES--ERYWRAIDVTAlqhdldllpgrdLTEIGERGVN----ISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 168 PTGNLDQETGRTILEEMTRlKETENIAIVAITHDEQLVQYADRVVRIVDGVIQ 220
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLMDRIILVSEGMIK 818
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
121-201 |
4.89e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 121 RAVDLLRRVGLGERLTHTP-DELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETeniaIVAIT 199
Cdd:PRK15064 134 RAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNST----MIIIS 209
|
..
gi 1906108912 200 HD 201
Cdd:PRK15064 210 HD 211
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
117-219 |
6.25e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.04 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 117 DRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIV 196
Cdd:NF000106 120 DARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLL 199
|
90 100
....*....|....*....|....*....
gi 1906108912 197 AITHDEQLVQYA------DRVVRIVDGVI 219
Cdd:NF000106 200 TTQYMEEAEQLAheltviDRGRVIADGKV 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-220 |
6.83e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNmiGLLDSptegvvrlegrdvTEASEDERTEERrsELGFVFQDFHLLpml 100
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQ--SLLSQ-------------FEISEGRVWAER--SIAYVPQQAWIM--- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 101 NAV--ENVELpsmwdTTVDRRERAVDLLRRVGLGERLTHTPD-----------ELSGGQQQRVAIARALINEPDVLLADE 167
Cdd:PTZ00243 734 NATvrGNILF-----FDEEDAARLADAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1906108912 168 PTGNLDQETGRTILEEMTRLKETENIAIVAiTHDEQLVQYADRVVRIVDGVIQ 220
Cdd:PTZ00243 809 PLSALDAHVGERVVEECFLGALAGKTRVLA-THQVHVVPRADYVVALGDGRVE 860
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-200 |
7.99e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 17 AETVVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMigLLDSPTEGVVRLEGRDVTEASEDErTEERRSelGFVFQ-DFH 95
Cdd:TIGR00956 773 KEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNV--LAERVTTGVITGGDRLVNGRPLDS-SFQRSI--GYVQQqDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 96 lLPMLNAVENVE------LPSmwdtTVDRRER------AVDLLRRVGLGERLTHTPDE-LSGGQQQRVAIARALINEPDV 162
Cdd:TIGR00956 848 -LPTSTVRESLRfsaylrQPK----SVSKSEKmeyveeVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKL 922
|
170 180 190
....*....|....*....|....*....|....*....
gi 1906108912 163 LL-ADEPTGNLDQETGRTILEEMTRLKETENiAIVAITH 200
Cdd:TIGR00956 923 LLfLDEPTSGLDSQTAWSICKLMRKLADHGQ-AILCTIH 960
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-173 |
1.07e-07 |
|
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: 51.71 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 31 ERGEMVVVTGPSGSGKSTMLNMIGlldspteGVVR--LeGRDVTEASEDERTEE-RRSELGFVFQDFhllpmlnaVEN-- 105
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS-------GELKpnL-GDYDEEPSWDEVLKRfRGTELQDYFKKL--------ANGei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 106 --------VEL-PSMWDTTV-------DRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPT 169
Cdd:COG1245 161 kvahkpqyVDLiPKVFKGTVrellekvDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
....
gi 1906108912 170 GNLD 173
Cdd:COG1245 241 SYLD 244
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-218 |
1.87e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.06 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 33 GEMVVVTGPSGSGKSTMLNMIGLLDSPTEGvvrlegRDVTEASEDERTEE-RRSELgfvfQDFhLLPMLNA-------VE 104
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLG------KFDDPPDWDEILDEfRGSEL----QNY-FTKLLEGdvkvivkPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 105 NVEL-PSMWDTTV-------DRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQET 176
Cdd:cd03236 95 YVDLiPKAVKGKVgellkkkDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1906108912 177 GRTILEEMTRLKETENiAIVAITHDEQLVQYADRVVRIVDGV 218
Cdd:cd03236 175 RLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLYGE 215
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
23-207 |
3.48e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.40 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTM-LNMIGLLD-SPTEGVVRLEGRDVTEASEDERTEE-------RRSELGFVFQD 93
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREDyEVTGGTVEFKGKDLLELSPEDRAGEgifmafqYPVEIPGVSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 94 FHLLPMLNAVenvelpsmwdttvdRRERAVDLLRRVGLGE------RLTHTPDEL---------SGGQQQRVAIARALIN 158
Cdd:PRK09580 97 FFLQTALNAV--------------RSYRGQEPLDRFDFQDlmeekiALLKMPEDLltrsvnvgfSGGEKKRNDILQMAVL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1906108912 159 EPDVLLADEPTGNLDQETGRTILEEMTRLKEtENIAIVAITHDEQLVQY 207
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRD-GKRSFIIVTHYQRILDY 210
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-219 |
8.59e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.75 E-value: 8.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 26 VDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTE-------ERRSELGFVfqdfhllP 98
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRagimlcpEDRKAEGII-------P 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 99 MLNAVENVELP-----SMWDTTVDRRERAVDLLRRVGLGERLTHTPDE----LSGGQQQRVAIARALINEPDVLLADEPT 169
Cdd:PRK11288 345 VHSVADNINISarrhhLRAGCLINNRWEAENADRFIRSLNIKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1906108912 170 GNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDGVI 219
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDlPEVLGVADRIVVMREGRI 474
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-207 |
8.73e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.98 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLdSPTEGvvrleGRdvteasedeRTEERRSELGFVFQDFHllpML 100
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYG-----GR---------LTKPAKGKLFYVPQRPY---MT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 101 NAV--ENVELPsmwDTTVDRRERAV---------------DLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVL 163
Cdd:TIGR00954 528 LGTlrDQIIYP---DSSEDMKRRGLsdkdleqildnvqltHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1906108912 164 LADEPTG--NLDQEtgrtilEEMTRLKETENIAIVAITHDEQLVQY 207
Cdd:TIGR00954 605 ILDECTSavSVDVE------GYMYRLCREFGITLFSVSHRKSLWKY 644
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
31-217 |
1.74e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.41 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 31 ERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEgvvrlegrdvteasederteerrselgfvfqdfhllpmlnavENVELPS 110
Cdd:cd03222 23 KEGEVIGIVGPNGTGKTTAVKILAGQLIPNG------------------------------------------DNDEWDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 111 MwdtTVDRRERAVDLlrrvglgerlthtpdelSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKET 190
Cdd:cd03222 61 I---TPVYKPQYIDL-----------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180
....*....|....*....|....*..
gi 1906108912 191 ENIAIVAITHDEQLVQYADRVVRIVDG 217
Cdd:cd03222 121 GKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-220 |
1.94e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 25 DVDFHAERGEMVVVTGPSGSGKSTMLNMI-GLLDSPTEGVVRLEGRDVTEASEDERTeerRSELGFVFQD---FHLLPML 100
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNPQQAI---AQGIAMVPEDrkrDGIVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 101 NAVENVELPSMWD----TTVDRRERAVDLLRRVglgERL---THTPD----ELSGGQQQRVAIARALINEPDVLLADEPT 169
Cdd:PRK13549 357 GVGKNITLAALDRftggSRIDDAAELKTILESI---QRLkvkTASPElaiaRLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1906108912 170 GNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDGVIQ 220
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQLVQ-QGVAIIVISSElPEVLGLSDRVLVMHEGKLK 484
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
119-214 |
2.24e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.70 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 119 RERaVDLLRRVGLGE-RLTHTPDELSGGQQQRVAIAR----ALINEPDVLlaDEPTGNLDQETGRTILEEMTRLKETENI 193
Cdd:TIGR00630 466 RER-LGFLIDVGLDYlSLSRAAGTLSGGEAQRIRLATqigsGLTGVLYVL--DEPSIGLHQRDNRRLINTLKRLRDLGNT 542
|
90 100
....*....|....*....|.
gi 1906108912 194 AIVaITHDEQLVQYADRVVRI 214
Cdd:TIGR00630 543 LIV-VEHDEDTIRAADYVIDI 562
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-205 |
2.43e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 21 VALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRlegrdvteasedeRTEERRSElgfVFQDFHllpml 100
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-------------RSAKVRMA---VFSQHH----- 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 101 naVENVELPS--------MWDTTVDRRERAvdLLRRVGLGERLTHTPD-ELSGGQQQRVAIARALINEPDVLLADEPTGN 171
Cdd:PLN03073 582 --VDGLDLSSnpllymmrCFPGVPEQKLRA--HLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNH 657
|
170 180 190
....*....|....*....|....*....|....
gi 1906108912 172 LDQETGRTILEEMTRLKEteniAIVAITHDEQLV 205
Cdd:PLN03073 658 LDLDAVEALIQGLVLFQG----GVLMVSHDEHLI 687
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
140-214 |
2.50e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 2.50e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 140 DELSGGQQQRVAIARALINEPD--VLLADEPTGNLDQETGRTILEEMTRLKETENiAIVAITHDEQLVQYADRVVRI 214
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMISLADRIIDI 550
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
35-208 |
2.61e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.40 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 35 MVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASederteerRSELGFVFQDFHLLPMLNAVENVElpsMWDT 114
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--------KPYCTYIGHNLGLKLEMTVFENLK---FWSE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 115 TVDRRERAVDLLRRVGLGERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETgRTILEEMTRLKETENIA 194
Cdd:PRK13541 97 IYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN-RDLLNNLIVMKANSGGI 175
|
170
....*....|....
gi 1906108912 195 IVAITHDEQLVQYA 208
Cdd:PRK13541 176 VLLSSHLESSIKSA 189
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
135-173 |
2.76e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 2.76e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1906108912 135 LTHTPD-------ELSGGQQQRVAIARALINEPDVLLADEPTGNLD 173
Cdd:PLN03073 331 LSFTPEmqvkatkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-214 |
3.81e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 142 LSGGQQQ------RVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTR-LKETENIAIVaiTHDEQLVQYADRVVRI 214
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERyLRKIPQVIIV--SHDEELKDAADYVIRV 866
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
119-173 |
7.60e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 7.60e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1906108912 119 RERAVDLLRrvGLG---ERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLD 173
Cdd:PRK10636 126 RSRAASLLH--GLGfsnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-180 |
9.06e-06 |
|
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: 45.23 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLN-MIGLLDspTEGVVRLEGRDVTEASederTEE 82
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLN--TEGDIQIDGVSWNSVP----LQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 83 RRSELGFVFQDFHLLPMlNAVENVELPSMWDTtvdrrERAVDLLRRVGLGERLTHTPDE-----------LSGGQQQRVA 151
Cdd:cd03289 75 WRKAFGVIPQKVFIFSG-TFRKNLDPYGKWSD-----EEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMC 148
|
170 180
....*....|....*....|....*....
gi 1906108912 152 IARALINEPDVLLADEPTGNLDQETGRTI 180
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDPITYQVI 177
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-169 |
1.26e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.17 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKsTMLNM----------IGlldspteGVVRLEGRDVTEASEDER--------TEERR 84
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGR-TELAMsvfgrsygrnIS-------GTVFKDGKEVDVSTVSDAidaglayvTEDRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 85 sELGFVFQDfhllpmlNAVENVELPSMwdTTVDRReRAVDLLRRVGLGERL-----THTPD------ELSGGQQQRVAIA 153
Cdd:NF040905 348 -GYGLNLID-------DIKRNITLANL--GKVSRR-GVIDENEEIKVAEEYrkkmnIKTPSvfqkvgNLSGGNQQKVVLS 416
|
170
....*....|....*.
gi 1906108912 154 RALINEPDVLLADEPT 169
Cdd:NF040905 417 KWLFTDPDVLILDEPT 432
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
23-48 |
1.56e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.02 E-value: 1.56e-05
10 20
....*....|....*....|....*.
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKST 48
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSS 41
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-184 |
1.58e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.94 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 13 YESGAETVValKDVDFHAERGEMVVVTGPSGSGKSTMLN-MIGLLDsPTEGVVRLeGRDVTEASEDERTEErrselgfvf 91
Cdd:PRK11147 327 YQIDGKQLV--KDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQ-ADSGRIHC-GTKLEVAYFDQHRAE--------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 92 qdfhLLPMLNAVENVElPSMWDTTVDRRERAVdllrrVG-LGERLTH-----TP-DELSGGQQQRVAIARALINEPDVLL 164
Cdd:PRK11147 394 ----LDPEKTVMDNLA-EGKQEVMVNGRPRHV-----LGyLQDFLFHpkramTPvKALSGGERNRLLLARLFLKPSNLLI 463
|
170 180
....*....|....*....|
gi 1906108912 165 ADEPTGNLDQETgRTILEEM 184
Cdd:PRK11147 464 LDEPTNDLDVET-LELLEEL 482
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-219 |
4.02e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 4 IELDSVVKRYESGAETVvaLKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVteASEDERteER 83
Cdd:PTZ00243 1309 LVFEGVQMRYREGLPLV--LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI--GAYGLR--EL 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 84 RSELGFVFQDfhllPML---NAVENVElPSMWDTT--VDRRERAVDLLRRV-----GLGERLTHTPDELSGGQQQRVAIA 153
Cdd:PTZ00243 1383 RRQFSMIPQD----PVLfdgTVRQNVD-PFLEASSaeVWAALELVGLRERVaseseGIDSRVLEGGSNYSVGQRQLMCMA 1457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 154 RALINE-PDVLLADEPTGNLDQETGRTIleEMTRLKETENIAIVAITHDEQLVQYADRVVRIVDGVI 219
Cdd:PTZ00243 1458 RALLKKgSGFILMDEATANIDPALDRQI--QATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAV 1522
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
23-53 |
5.88e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 5.88e-05
10 20 30
....*....|....*....|....*....|.
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMI 53
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNDI 651
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
27-56 |
6.45e-05 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 42.24 E-value: 6.45e-05
10 20 30
....*....|....*....|....*....|
gi 1906108912 27 DFHAERGEMVVVTGPSGSGKSTMLNMIGLL 56
Cdd:cd03243 23 DINLGSGRLLLITGPNMGGKSTYLRSIGLA 52
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
23-53 |
6.90e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.14 E-value: 6.90e-05
10 20 30
....*....|....*....|....*....|.
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMI 53
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLINET 655
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
23-53 |
7.57e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.08 E-value: 7.57e-05
10 20 30
....*....|....*....|....*....|.
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLNMI 53
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDT 654
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-220 |
1.15e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 42.69 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 33 GEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDerteerrselgfVFQDFHLLPMLNAVENVeLPSMW 112
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD------------VHQNMGYCPQFDAIDDL-LTGRE 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 113 DTTVDRRERAVDL----------LRRVGL---GERLTHTpdeLSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRT 179
Cdd:TIGR01257 2032 HLYLYARLRGVPAeeiekvanwsIQSLGLslyADRLAGT---YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1906108912 180 ILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDGVIQ 220
Cdd:TIGR01257 2109 LWNTIVSIIR-EGRAVVLTSHSmEECEALCTRLAIMVKGAFQ 2149
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-217 |
1.16e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 20 VVALKDVDFHAERGEMVVVTGPSGSGKSTMLNMIGLLDSPTEGVVRLEGRDVTEASEDERTEERRSelgFVFQDFHLLPM 99
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGIS---MVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 100 LNAVEN------------VELPSMW-DTTVDRRERAVDLLRRVGLGErlthtpdeLSGGQQQRVAIARALINEPDVLLAD 166
Cdd:PRK10982 88 RSVMDNmwlgryptkgmfVDQDKMYrDTKAIFDELDIDIDPRAKVAT--------LSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1906108912 167 EPTGNLDQETGRTILEEMTRLKEtENIAIVAITHD-EQLVQYADRVVRIVDG 217
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKE-RGCGIVYISHKmEEIFQLCDEITILRDG 210
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
120-212 |
3.41e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 120 ERAVDLLRRVGLGE-RLTHTPDELSGGQQQRVAIARAL---INEPDVLLADEPTGNLDQETGRTILEEMTRLKETENIAI 195
Cdd:TIGR00630 807 SRKLQTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVV 886
|
90
....*....|....*..
gi 1906108912 196 VaITHDEQLVQYADRVV 212
Cdd:TIGR00630 887 V-IEHNLDVIKTADYII 902
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
23-49 |
4.05e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 4.05e-04
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
40-206 |
4.77e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.54 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 40 GPSGSGKSTMLNMIGLLDSPTEGVVRLEgrdvteasederteeRRSELGFVFQdfHLLPMLNAVENV--ELPSMWDTTVD 117
Cdd:PRK10636 345 GRNGAGKSTLIKLLAGELAPVSGEIGLA---------------KGIKLGYFAQ--HQLEFLRADESPlqHLARLAPQELE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 118 RRERavDLLRRVGL-GERLTHTPDELSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLKEteniAIV 196
Cdd:PRK10636 408 QKLR--DYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALV 481
|
170
....*....|
gi 1906108912 197 AITHDEQLVQ 206
Cdd:PRK10636 482 VVSHDRHLLR 491
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
121-212 |
6.71e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.52 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 121 RAVDLLRRVGLGE-RLTHTPDELSGGQQQRVAIARALINE---PDVLLADEPTGNLDQETGRTILEEMTRLKETENIAIV 196
Cdd:cd03271 148 RKLQTLCDVGLGYiKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVV 227
|
90
....*....|....*.
gi 1906108912 197 aITHDEQLVQYADRVV 212
Cdd:cd03271 228 -IEHNLDVIKCADWII 242
|
|
| Twinkle_C |
cd01122 |
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid ... |
5-99 |
7.08e-04 |
|
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid localization, also known as C10orf2, PEO1, SCA8, ATXN8, IOSCA, PEOA3 or SANDO) is a homohexameric DNA helicases which unwinds short stretches of double-stranded DNA in the 5' to 3' direction and, along with mitochondrial single-stranded DNA binding protein and mtDNA polymerase gamma, is thought to play a key role in mtDNA replication. Mutations in the human gene cause infantile onset spinocerebellar ataxia (IOSCA) and progressive external ophthalmoplegia (PEO) and are also associated with several mitochondrial depletion syndromes. This group also contains viral GP4-like and related bacterial helicases.
Pssm-ID: 410867 Cd Length: 266 Bit Score: 39.53 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 5 ELDSVVKRYESGAETVVALKDVDFHA--------ERGEMVVVTGPSGSGKSTMLNMIGlLDSPTEGV-----------VR 65
Cdd:cd01122 7 DLRELVYEELLNSEQVAGVQWKRFPSlnkllkghRRGELTIFTGPTGSGKTTFLSEYS-LDLCMQGVntlwgsfeiknVR 85
|
90 100 110
....*....|....*....|....*....|....
gi 1906108912 66 LEGRDVTEASEDeRTEERRSELGFVFQDFHLLPM 99
Cdd:cd01122 86 LAKTMLTQFAGK-NLEDNLREFDEWADKFELLPM 118
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
23-48 |
7.13e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 7.13e-04
10 20
....*....|....*....|....*.
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKST 48
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSS 41
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
142-198 |
7.42e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.00 E-value: 7.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1906108912 142 LSGGQQQRVAIARALINEPDVLLADEPTGNLDQETGRTILEEMTRLkETENIAIVAI 198
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASL-HQSGITLVLV 191
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
23-51 |
7.63e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.52 E-value: 7.63e-04
10 20
....*....|....*....|....*....
gi 1906108912 23 LKDVDFHAERGEMVVVTGPSGSGKSTMLN 51
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN 39
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
119-214 |
2.35e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906108912 119 RERaVDLLRRVGLG----ERLTHTpdeLSGGQQQRV----AIARALINepdVL--LaDEPTGNLDQ-ETGRtILEEMTRL 187
Cdd:COG0178 463 RSR-LGFLVDVGLDyltlDRSAGT---LSGGEAQRIrlatQIGSGLVG---VLyvL-DEPSIGLHQrDNDR-LIETLKRL 533
|
90 100
....*....|....*....|....*..
gi 1906108912 188 KETENIAIVaITHDEQLVQYADRVVRI 214
Cdd:COG0178 534 RDLGNTVIV-VEHDEDTIRAADYIIDI 559
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
140-209 |
2.55e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.34 E-value: 2.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906108912 140 DELSGGQQQ------RVAIARALINEPDVLLADEPTGNLDQETgRTILEEMTR--LKETENI-AIVAITHDEQLVQYAD 209
Cdd:PRK01156 800 DSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDR-RTNLKDIIEysLKDSSDIpQVIMISHHRELLSVAD 877
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
29-53 |
3.40e-03 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 37.76 E-value: 3.40e-03
10 20
....*....|....*....|....*....
gi 1906108912 29 HAERGeMVVVTGPSGSGKST----MLNMI 53
Cdd:COG2805 122 ELPRG-LVLVTGPTGSGKSTtlaaMIDYI 149
|
|
| PulE-GspE-like |
cd01129 |
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ... |
35-67 |
6.06e-03 |
|
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II secretory pathway, the main terminal branch of the general secretory pathway (GSP). PulE is a cytoplasmic protein of the GSP, which contains an ATP binding site and a tetracysteine motif. This subgroup also includes PilB, a type IV pilus assembly ATPase, DotB, an ATPase of the type IVb secretion system, also known as the dot/icm system, Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ, and HofB.
Pssm-ID: 410873 [Multi-domain] Cd Length: 159 Bit Score: 35.92 E-value: 6.06e-03
10 20 30
....*....|....*....|....*....|....
gi 1906108912 35 MVVVTGPSGSGKSTML-NMIGLLDSPTEGVVRLE 67
Cdd:cd01129 13 LILVTGPTGSGKTTTLyAMLRELNGPERNIITIE 46
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
25-60 |
6.14e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.11 E-value: 6.14e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1906108912 25 DVDFHAERGEMVVVTGPSGSGKSTMLN-MIGLLDSPT 60
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTLLDaIQTLLVPAK 50
|
|
| PilT |
cd01131 |
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ... |
29-58 |
7.11e-03 |
|
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein responsible for the retraction of type IV pili, likely by pili disassembly. This retraction provides the force required for travel of bacteria in low water environments by a mechanism known as twitching motility.
Pssm-ID: 410875 [Multi-domain] Cd Length: 223 Bit Score: 36.36 E-value: 7.11e-03
10 20 30
....*....|....*....|....*....|.
gi 1906108912 29 HAERGeMVVVTGPSGSGKSTML-NMIGLLDS 58
Cdd:cd01131 18 LKPRG-LVLVTGPTGSGKSTTLaAMIDYINE 47
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
32-53 |
8.09e-03 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 35.81 E-value: 8.09e-03
|
| |
