|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-222 |
1.54e-132 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 371.68 E-value: 1.54e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 2 AMIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAA 81
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 FRNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGN 161
Cdd:COG1136 83 LRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495112432 162 PEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-220 |
5.55e-119 |
|
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: 337.15 E-value: 5.55e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFR 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 NKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-223 |
3.66e-91 |
|
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: 267.38 E-value: 3.66e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 2 AMIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAA 81
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 FRNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMA-AKERtrlAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRdARAR---ARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-220 |
5.76e-90 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 263.84 E-value: 5.76e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:COG2884 1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNKtLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:COG2884 78 RRR-IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQT-SRTIRFFDGR 220
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMpKRVLELEDGR 214
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-220 |
3.85e-80 |
|
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: 238.79 E-value: 3.85e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQ 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-205 |
6.12e-79 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 237.30 E-value: 6.12e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESmkdkela 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 afRNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:COG1116 78 --PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN-EE 205
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDvDE 201
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-215 |
5.00e-77 |
|
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: 230.58 E-value: 5.00e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 6 LTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNK 85
Cdd:TIGR03608 1 LKNISKKFGDKVI----LDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 86 TLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEII 165
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495112432 166 LADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQTSRTIR 215
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIE 205
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-219 |
1.45e-76 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 230.27 E-value: 1.45e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVeSMKDKELAAF 82
Cdd:COG1126 1 MIEIENLHKSFGDLEV----LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNKTlGFVFQSFHLINSLNVIDNVELPLLY-RKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGN 161
Cdd:COG1126 76 RRKV-GMVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 162 PEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDG 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-207 |
6.81e-75 |
|
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: 225.43 E-value: 6.81e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESmkdkelaafR 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 NKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEA 195
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-218 |
1.31e-74 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 225.71 E-value: 1.31e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 2 AMIKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAA 81
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 FRNKTlGFVFQSFHLINSLNVIDNVELPLLYR--------KMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVA 153
Cdd:COG3638 78 LRRRI-GMIFQQFNLVPRLSVLTNVLAGRLGRtstwrsllGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 154 IARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKqtsrtiRFFD 218
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLAR------RYAD 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-209 |
1.21e-73 |
|
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: 222.84 E-value: 1.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNKtLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:cd03258 81 RRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQ 209
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKR 206
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-202 |
1.37e-73 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 226.11 E-value: 1.37e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RnKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:COG1135 81 R-RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITH 199
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-223 |
1.88e-71 |
|
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: 217.54 E-value: 1.88e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 2 AMIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAA 81
Cdd:COG1127 4 PMIEVRNLTKSFGDRVV----LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 FRNKtLGFVFQSFHLINSLNVIDNVELPLL-YRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:COG1127 80 LRRR-IGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-220 |
2.05e-71 |
|
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: 216.35 E-value: 2.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNKtLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:TIGR02673 78 RRR-IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQTS-RTIRFFDGR 220
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAhRVIILDDGR 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-220 |
1.22e-68 |
|
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: 210.05 E-value: 1.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFR 83
Cdd:cd03261 1 IELRGLTKSFGGRTV----LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 NKTlGFVFQSFHLINSLNVIDNVELPLL-YRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:cd03261 77 RRM-GMLFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGR 220
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIAdRIAVLYDGK 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-207 |
2.06e-68 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 213.42 E-value: 2.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkelA 80
Cdd:COG3842 3 MPALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP----P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 AFRNktLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:COG3842 75 EKRN--VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEA 199
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-222 |
2.70e-67 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 218.05 E-value: 2.70e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 2 AMIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAA 81
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 FRNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGN 161
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495112432 162 PEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-207 |
2.98e-65 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 205.31 E-value: 2.98e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKEla 80
Cdd:COG3839 1 MASLELENVSKSYGGVE----ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 afRNktLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:COG3839 75 --RN--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEA 197
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-219 |
4.65e-64 |
|
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: 197.75 E-value: 4.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESmKDKELAAFR 83
Cdd:cd03262 1 IEIKNLHKSFGDFHV----LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 NKTlGFVFQSFHLINSLNVIDNVELPLLY-RKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:cd03262 76 QKV-GMVFQQFNLFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-220 |
7.60e-64 |
|
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: 197.25 E-value: 7.60e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFR 83
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 NKtLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03292 78 RK-IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQTS-RTIRFFDGR 220
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRhRVIALERGK 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-223 |
9.82e-64 |
|
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: 196.97 E-value: 9.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKElaafR 83
Cdd:cd03259 1 LELKGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 NktLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03259 73 N--IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFF-DGRQVQ 223
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMnEGRIVQ 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-220 |
2.69e-63 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 196.54 E-value: 2.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLGFVFQSFHLINSLNV 102
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 103 IDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEV 182
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 495112432 183 MELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQ 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-222 |
1.78e-62 |
|
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: 202.83 E-value: 1.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIETL-ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELA 80
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVrAVDDVSLTLRRGETLGLVGESGSGKSTLARlLLGLLR-PTSGSILFDGKDLTKLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 AFRnKTLGFVFQS-FHLIN-SLNVIDNVELPL-LYRKMAAKERTRLAKEVLERVGLSHRMRH-MPTQLSGGQCQRVAIAR 156
Cdd:COG1123 339 ELR-RRVQMVFQDpYSSLNpRMTVGDIIAEPLrLHGLLSRAERRERVAELLERVGLPPDLADrYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 157 AIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGRQV 222
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIAdRVAVMYDGRIV 484
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-220 |
2.11e-62 |
|
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: 193.88 E-value: 2.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKELAA 81
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARaILGLL-KPTSGSIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 FRNKtLGFVFQsfHLINSLN----VIDNVELPLLYRKMAAKERTRLAK--EVLERVGLSHRMRHM-PTQLSGGQCQRVAI 154
Cdd:cd03257 80 RRKE-IQMVFQ--DPMSSLNprmtIGEQIAEPLRIHGKLSKKEARKEAvlLLLVGVGLPEEVLNRyPHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 155 ARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGR 220
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIAdRVAVMYAGK 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-220 |
2.15e-62 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 194.26 E-value: 2.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 11 KIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLGFV 90
Cdd:PRK11629 13 KRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 91 FQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495112432 171 TGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGR 222
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
4-220 |
5.16e-62 |
|
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: 192.93 E-value: 5.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFR 83
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 nKTLGFVFQSFHLINSLNVIDNVELPL-LYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:TIGR02982 82 -RRIGYIFQAHNLLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:TIGR02982 161 KLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGK 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-202 |
1.10e-61 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 195.79 E-value: 1.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNKtLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:PRK11153 81 RRQ-IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-222 |
1.11e-61 |
|
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: 192.78 E-value: 1.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFR 83
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 NKTlGFVFQSFHLINSLNVIDNVELPLLYRK--------MAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIA 155
Cdd:cd03256 78 RQI-GMIFQQFNLIERLSVLENVLSGRLGRRstwrslfgLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 156 RAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQ-TSRTIRFFDGRQV 222
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
13-220 |
3.96e-60 |
|
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: 187.67 E-value: 3.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 13 YRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAafrnKTLGFVFQ 92
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----RKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 93 -SFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:cd03225 83 nPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495112432 172 GNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQ-TSRTIRFFDGR 220
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-223 |
3.17e-59 |
|
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: 187.47 E-value: 3.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 20 TLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLGFVFQSFHLINS 99
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 100 LNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMG 179
Cdd:cd03294 117 RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIR 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495112432 180 AEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFF-DGRQVQ 223
Cdd:cd03294 197 REMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMkDGRLVQ 241
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
19-222 |
3.62e-59 |
|
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: 186.00 E-value: 3.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTSVesmKDKELAAFRnKTLGFVFQ-SFHL 96
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLnGLL-KPTSGEVLVDGKDI---TKKNLRELR-RKVGLVFQnPDDQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 97 INSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDS 176
Cdd:COG1122 88 LFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495112432 177 KMGAEVMELLHKLNKEdGRTIVMVTHN-EEQAKQTSRTIRFFDGRQV 222
Cdd:COG1122 168 RGRRELLELLKRLNKE-GKTVIIVTHDlDLVAELADRVIVLDDGRIV 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-203 |
5.51e-59 |
|
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: 186.16 E-value: 5.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKelaAF 82
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK---AF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RnKTLGFVFQsfHLINSLN----VIDNVELPL-LYRKMAAKERtrlAKEVLERVGLSHRMRHM-PTQLSGGQCQRVAIAR 156
Cdd:COG1124 78 R-RRVQMVFQ--DPYASLHprhtVDRILAEPLrIHGLPDREER---IAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495112432 157 AIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHD 198
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-202 |
6.13e-59 |
|
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: 186.02 E-value: 6.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKELAa 81
Cdd:COG1120 1 MLEAENLSVGYGGRPV----LDDVSLSLPPGEVTALLGPNGSGKSTLLRaLAGLL-KPSSGEVLLDGRDLASLSRRELA- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 frnKTLGFVFQSFHLINSLNVIDNVEL---PLL--YRKMAAKERtRLAKEVLERVGLSH-RMRHMpTQLSGGQCQRVAIA 155
Cdd:COG1120 75 ---RRIAYVPQEPPAPFGLTVRELVALgryPHLglFGRPSAEDR-EAVEEALERTGLEHlADRPV-DELSGGERQRVLIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495112432 156 RAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLH 196
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-203 |
7.04e-59 |
|
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: 187.95 E-value: 7.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLDAP--SSGKIEINGTSVESMKDKEL 79
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaRAILGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 80 AAFRNKTLGFVFQSfhLINSLN----VIDNVELPLLY-RKMAAKERTRLAKEVLERVGLSHRMRHM---PTQLSGGQCQR 151
Cdd:COG0444 81 RKIRGREIQMIFQD--PMTSLNpvmtVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495112432 152 VAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHD 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-207 |
2.26e-57 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 182.37 E-value: 2.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMkdkelA 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP-----G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 AFRnktlGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:COG4525 76 ADR----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495112432 161 NPEIILADEPTGNLDSkMGAEVM-ELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:COG4525 152 DPRFLLMDEPFGALDA-LTREQMqELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-222 |
3.28e-57 |
|
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: 181.34 E-value: 3.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNKTlGFVFQSFHLINSLNVIDNVELPLLYRK--------MAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAI 154
Cdd:TIGR02315 78 RRRI-GMIFQHYNLIERLTVLENVLHGRLGYKptwrsllgRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 155 ARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQ-TSRTIRFFDGRQV 222
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEIV 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-220 |
1.95e-55 |
|
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: 174.68 E-value: 1.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMkDKELAAFR 83
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 NKTlGFVFQSFHLINSLNVIDNVELPLlyrkmaakertrlakevlervglshrmrhmptqlSGGQCQRVAIARAIVGNPE 163
Cdd:cd03229 76 RRI-GMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGR 220
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLAdRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-222 |
5.08e-55 |
|
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: 183.18 E-value: 5.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDAPS--SGKIEINGTSVESMKDKElaafRNKTLGFVFQSF- 94
Cdd:COG1123 18 DVPAVDGVSLTIAPGETVALVGESGSGKSTLALaLMGLLPHGGriSGEVLLDGRDLLELSEAL----RGRRIGMVFQDPm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 95 HLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:COG1123 94 TQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTAL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495112432 175 DSKMGAEVMELLHKLNKEDGRTIVMVTHN-EEQAKQTSRTIRFFDGRQV 222
Cdd:COG1123 174 DVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRIV 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-214 |
8.19e-55 |
|
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: 174.73 E-value: 8.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTneieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESmkdkeLAAFR 83
Cdd:cd03300 1 IELENVSKFYGG----FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN-----LPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 nKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03300 72 -RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTI 214
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRI 201
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
23-220 |
3.93e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 172.31 E-value: 3.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkeLAAFRNKtLGFVFQSFHLINSlNV 102
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRRQ-VAYVPQEPALWGG-TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 103 IDNVELPLLYRKMAAKERTrlAKEVLERVGLSHRMRHMPT-QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAE 181
Cdd:COG4619 91 RDNLPFPFQLRERKFDRER--ALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495112432 182 VMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGR 220
Cdd:COG4619 169 VEELLREYLAEEGRAVLWVSHDPEQIERVAdRVLTLEAGR 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-207 |
8.95e-54 |
|
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: 171.67 E-value: 8.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKElaafR 83
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 NktLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03301 73 D--IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEA 194
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-223 |
4.06e-53 |
|
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: 170.44 E-value: 4.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLD----APSSGKIEINGTSVESmKDKE 78
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLnRLNDlipgAPDEGEVLLDGKDIYD-LDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 79 LAAFRnKTLGFVFQSFHLINsLNVIDNVELPLLYRKMA-AKERTRLAKEVLERVGLSHRM--RHMPTQLSGGQCQRVAIA 155
Cdd:cd03260 76 VLELR-RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKlKEELDERVEEALRKAALWDEVkdRLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 156 RAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdgRTIVMVTHNEEQAKQTS-RTIRFFDGRQVQ 223
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVAdRTAFLLNGRLVE 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-203 |
7.95e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 169.86 E-value: 7.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVesmkDKELAAF 82
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRmLLGLL-RPTSGEVRVLGEDV----ARDPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RnKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:COG1131 72 R-RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHN 203
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHY 190
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-203 |
1.39e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 169.50 E-value: 1.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESmkdkel 79
Cdd:COG1121 4 MPAIELENLTVSYG----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILGLL-PPTSGTVRLFGKPPRR------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 80 aafRNKTLGFVFQSFHLINS--LNVIDNVELPLLYR----KMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVA 153
Cdd:COG1121 73 ---ARRRIGYVPQRAEVDWDfpITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495112432 154 IARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHN 203
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHD 198
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-207 |
7.52e-52 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 170.71 E-value: 7.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTneieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvesmKDkelaAFR 83
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG------RD----LFT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 NKTL-----GFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAI 158
Cdd:COG1118 69 NLPPrerrvGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495112432 159 VGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEA 197
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-223 |
8.27e-51 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 164.80 E-value: 8.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSV---ESMKDKELA 80
Cdd:COG4161 3 IQLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 AFRNKtLGFVFQSFHLINSLNVIDN-VELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIV 159
Cdd:COG4161 79 LLRQK-VGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQT-SRTIRFFDGRQVQ 223
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVaSQVVYMEKGRIIE 221
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-207 |
2.39e-50 |
|
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: 167.14 E-value: 2.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRTneieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvesmKDKELA 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGG------RDITRL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 AFRNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:TIGR03265 72 PPQKRDYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALAT 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:TIGR03265 152 SPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEA 198
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-207 |
4.40e-50 |
|
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: 161.06 E-value: 4.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 5 KLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKELAafr 83
Cdd:cd03214 1 EVENLSVGYGGRTV----LDDLSLSIEAGEIVGILGPNGAGKSTLLKtLAGLL-KPSSGEILLDGKDLASLSPKELA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 nKTLGFVFQsfhlinslnvidnvelpllyrkmaakertrlakeVLERVGLSH-RMRHMpTQLSGGQCQRVAIARAIVGNP 162
Cdd:cd03214 73 -RKIAYVPQ----------------------------------ALELLGLAHlADRPF-NELSGGERQRVLLARALAQEP 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLA 161
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-219 |
7.65e-50 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 162.57 E-value: 7.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQV----LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNKtlGFVFQSFHLINSLNVIDNVEL-PLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGN 161
Cdd:PRK09493 77 QEA--GMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 162 PEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQT-SRTIrFFDG 219
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVaSRLI-FIDK 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-223 |
8.57e-49 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 159.79 E-value: 8.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSV---ESMKDKELA 80
Cdd:PRK11124 3 IQLNGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 AFRNKtLGFVFQSFHLINSLNVIDN-VELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIV 159
Cdd:PRK11124 79 ELRRN-VGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQT-SRTIRFFDGRQVQ 223
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTaSRVVYMENGHIVE 221
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-202 |
1.13e-48 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 159.97 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 2 AMIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKD----- 76
Cdd:COG4598 7 PALEVRDLHKSFGDLEV----LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgel 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 77 -----KELAAFRNKtLGFVFQSFHLINSLNVIDNV-ELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQ 150
Cdd:COG4598 83 vpadrRQLQRIRTR-LGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495112432 151 RVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTH 202
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTH 212
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-220 |
1.03e-47 |
|
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: 157.59 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRtnEIETLALENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLDaPSSGKIEINGtsVESMKDKELAAF 82
Cdd:TIGR04520 1 IEVENVSFSYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaKLLNGLLL-PTSGKVTVDG--LDTLDEENLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNKtLGFVFQsfhliNSLN------VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIAR 156
Cdd:TIGR04520 76 RKK-VGMVFQ-----NPDNqfvgatVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495112432 157 AIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGK 213
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
3-202 |
1.60e-47 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 158.33 E-value: 1.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAaf 82
Cdd:COG1125 1 MIEFENVTKRYPDG---TVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNktLGFVFQSFHLINSLNVIDNVEL-PLLYRKMAAKERTRlAKEVLERVGLSH-RMRH-MPTQLSGGQCQRVAIARAIV 159
Cdd:COG1125 76 RR--IGYVIQQIGLFPHMTVAENIATvPRLLGWDKERIRAR-VDELLELVGLDPeEYRDrYPHELSGGQQQRVGVARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495112432 160 GNPEIILADEPTGNLD----SKMGAEVMELLHKLNKedgrTIVMVTH 202
Cdd:COG1125 153 ADPPILLMDEPFGALDpitrEQLQDELLRLQRELGK----TIVFVTH 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-220 |
2.36e-47 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 159.73 E-value: 2.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkelAAFR 83
Cdd:PRK09452 15 VELRGISKSFDGKEV----ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP----AENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 NktLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:PRK09452 87 H--VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGR 220
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSdRIVVMRDGR 222
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-222 |
4.62e-47 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 155.68 E-value: 4.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKI-----EINGTSVESMK 75
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTV----LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 76 DKELAAFRNKtLGFVFQSFHLINSLNVIDNV-ELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAI 154
Cdd:PRK11264 77 KGLIRQLRQH-VGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 155 ARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDgRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-203 |
1.76e-46 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 153.07 E-value: 1.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGtsvesmkdKELAAFRNKtLGFVFQSFHlINS- 99
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLLK-PTSGSIRVFG--------KPLEKERKR-IGYVPQRRS-IDRd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 100 --LNVIDNVELPLLYR----KMAAKERTRLAKEVLERVGLSHrMRHMP-TQLSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:cd03235 83 fpISVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSE-LADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190
....*....|....*....|....*....|.
gi 495112432 173 NLDSKMGAEVMELLHKLNKEdGRTIVMVTHN 203
Cdd:cd03235 162 GVDPKTQEDIYELLRELRRE-GMTILVVTHD 191
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-223 |
2.11e-46 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 153.37 E-value: 2.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYrtneiETLALeNVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVE---------S 73
Cdd:COG3840 1 MLRLDDLTYRY-----GDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTalppaerpvS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 74 MkdkelaafrnktlgfVFQSFHLINSLNVIDNVEL---PLLyrKMAAKERTRLAkEVLERVGLSHRMRHMPTQLSGGQCQ 150
Cdd:COG3840 75 M---------------LFQENNLFPHLTVAQNIGLglrPGL--KLTAEQRAQVE-QALERVGLAGLLDRLPGQLSGGQRQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495112432 151 RVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQ-TSRTIRFFDGRQVQ 223
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAA 210
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-220 |
2.20e-46 |
|
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: 154.53 E-value: 2.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTN-EIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTSVESMKDKELAA 81
Cdd:TIGR04521 1 IKLKNVSYIYQPGtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLnGLL-KPTSGTVTIDGRDITAKKKKKLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 FRnKTLGFVFQsF--HLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHM-PTQLSGGQCQRVAIARAI 158
Cdd:TIGR04521 80 LR-KKVGLVFQ-FpeHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERsPFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495112432 159 VGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN-EEQAKQTSRTIRFFDGR 220
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGK 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-207 |
4.28e-46 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 156.01 E-value: 4.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDkelaafR 83
Cdd:PRK10851 3 IEIANIKKSFGRTQV----LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 NKTLGFVFQSFHLINSLNVIDNVE-----LPLLYRKMAAKERTRLAKeVLERVGLSHRMRHMPTQLSGGQCQRVAIARAI 158
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIAfgltvLPRRERPNAAAIKAKVTQ-LLEMVQLAHLADRYPAQLSGGQKQRVALARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495112432 159 VGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEA 200
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-207 |
4.77e-46 |
|
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: 152.49 E-value: 4.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKElaafRNktLGFVFQSFHLINSLN 101
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE----RN--VGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPLLYRKMAAK----ERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSK 177
Cdd:cd03296 91 VFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190
....*....|....*....|....*....|
gi 495112432 178 MGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:cd03296 171 VRKELRRWLRRLHDELHVTTVFVTHDQEEA 200
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-223 |
1.31e-45 |
|
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: 151.68 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEIetlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELaafR 83
Cdd:cd03295 1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 NKtLGFVFQSFHLINSLNVIDNVEL-PLLYRKMAAKERTRlAKEVLERVGL--SHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:cd03295 75 RK-IGYVIQQIGLFPHMTVEENIALvPKLLKWPKEKIRER-ADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA-KQTSRTIRFFDGRQVQ 223
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAfRLADRIAIMKNGEIVQ 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
22-223 |
1.33e-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: 159.16 E-value: 1.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELAAfrnkTLGFVFQSFHLINSl 100
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLAlLLRFLD-PQSGSITLGGVDLRDLDEDDLRR----RIAVVPQRPHLFDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVelpLLYRKMAAKERtrlAKEVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADE 169
Cdd:COG4987 424 TLRENL---RLARPDATDEE---LWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDE 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495112432 170 PTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:COG4987 498 PTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVLEDGRIVE 549
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
3-223 |
3.84e-44 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 151.00 E-value: 3.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTneietLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvesmKDKELAAF 82
Cdd:NF040840 1 MIRIENLSKDWKE-----FKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDG------KDITNLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:NF040840 70 EKRGIAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGRQVQ 223
Cdd:NF040840 150 KLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLAdRVGIMLNGRLSQ 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-220 |
1.06e-43 |
|
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: 144.45 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELAaf 82
Cdd:cd03228 1 IEFKNVSFSYPGRP--KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKlLLRLYD-PTSGEILIDGVDLRDLDLESLR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 rnKTLGFVFQSFHLINSlNVIDNVelpllyrkmaakertrlakevlervglshrmrhmptqLSGGQCQRVAIARAIVGNP 162
Cdd:cd03228 76 --KNIAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLnkEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-223 |
2.05e-43 |
|
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: 145.94 E-value: 2.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEietlaLENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKElaaf 82
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLEtIAGFI-KPDSGKILLNGKDITNLPPEK---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNKtlGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:cd03299 71 RDI--SYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGRQVQ 223
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALAdKVAIMLNGKLIQ 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
19-223 |
2.46e-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: 2.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELAafrnKTLGFVFQSFHLI 97
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNlLLGFLP-PYSGSILINGVDLSDLDPASWR----RQIAWVPQNPYLF 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 98 NSlNVIDNVelpLLYRKMAAKERTRlakEVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIIL 166
Cdd:COG4988 424 AG-TIRENL---RLGRPDASDEELE---AALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLL 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 167 ADEPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:COG4988 497 LDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRIVE 551
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-203 |
5.94e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 147.19 E-value: 5.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELAAFRnKTLGFVFQ-SFhliNS 99
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRlLLRLEE-PTSGEILFDGQDITGLSGRELRPLR-RRMQMVFQdPY---AS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 100 LN----VIDNVELPLLYRKMA-AKERTRLAKEVLERVGL--SHRMRHmPTQLSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:COG4608 108 LNprmtVGDIIAEPLRIHGLAsKAERRERVAELLELVGLrpEHADRY-PHEFSGGQRQRIGIARALALNPKLIVCDEPVS 186
|
170 180 190
....*....|....*....|....*....|.
gi 495112432 173 NLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:COG4608 187 ALDVSIQAQVLNLLEDLQDELGLTYLFISHD 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-223 |
7.39e-43 |
|
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: 153.07 E-value: 7.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINkiYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMkdkELAAF 82
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKlLLGLYE-PTSGRILIDGIDLRQI---DPASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNKtLGFVFQSFHLINSlNVIDNVelpLLYRKMAAKERtrlAKEVLERVGLSHRMRHMP-----------TQLSGGQCQR 151
Cdd:COG2274 548 RRQ-IGVVLQDVFLFSG-TIRENI---TLGDPDATDEE---IIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495112432 152 VAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIVE 689
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-209 |
7.62e-43 |
|
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: 142.15 E-value: 7.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVesmkDKELAAF 82
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKiILGLL-KPDSGEIKVLGKDI----KKEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNKtLGFVFQSFHLINSLNVIDNVELpllyrkmaakertrlakevlervglshrmrhmptqlSGGQCQRVAIARAIVGNP 162
Cdd:cd03230 72 KRR-IGYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDP 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQ 209
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAER 160
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
22-203 |
9.20e-43 |
|
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: 144.80 E-value: 9.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKELAAfrnktLGFV--FQSFHLIN 98
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNlITGFY-RPTSGRILFDGRDITGLPPHRIAR-----LGIArtFQNPRLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 SLNVIDNVELPLLYR-------------KMAAKER--TRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:COG0411 93 ELTVLENVLVAAHARlgrgllaallrlpRARREEReaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:COG0411 173 LLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHD 212
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-207 |
1.12e-42 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 144.46 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMkdkelAAFRnktlGFVFQSFHLINSLN 101
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP-----GAER----GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAE 181
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|....*.
gi 495112432 182 VMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-171 |
1.18e-42 |
|
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: 141.25 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGtsvESMKDKELAAFRnKTLGFVFQSFHLINSLN 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKlIAGLLS-PTEGTILLDG---QDLTDDERKSLR-KEIGYVFQDPQLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495112432 102 VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSH----RMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-220 |
1.79e-42 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 143.09 E-value: 1.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEietLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:PRK10908 1 MIRFEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RnKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:PRK10908 78 R-RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQ-AKQTSRTIRFFDGR 220
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLiSRRSYRMLTLSDGH 214
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-207 |
1.33e-41 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 144.79 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRTNEIEtlalENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvESMKDKELA 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVIS----KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMNDVPPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 afrNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:PRK11000 74 ---ERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEA 197
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-203 |
6.53e-41 |
|
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: 139.49 E-value: 6.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKELAAfrnktLGFV--FQSFHLIN 98
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNlISGFL-RPTSGSVLFDGEDITGLPPHEIAR-----LGIGrtFQIPRLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 SLNVIDNVELPLLYRK-------MAAKERTRL---AKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILAD 168
Cdd:cd03219 89 ELTVLENVMVAAQARTgsglllaRARREEREArerAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190
....*....|....*....|....*....|....*
gi 495112432 169 EPTGNLDSKMGAEVMELLHKLNkEDGRTIVMVTHN 203
Cdd:cd03219 169 EPAAGLNPEETEELAELIRELR-ERGITVLLVEHD 202
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-220 |
7.07e-41 |
|
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: 136.61 E-value: 7.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 5 KLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAafrn 84
Cdd:cd00267 1 EIENLSFRYGGRTA----LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 85 KTLGFVFQsfhlinslnvidnvelpllyrkmaakertrlakevlervglshrmrhmptqLSGGQCQRVAIARAIVGNPEI 164
Cdd:cd00267 73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 165 ILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQ-TSRTIRFFDGR 220
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-207 |
1.21e-40 |
|
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: 138.37 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSV-ESMKDKELaafrnktlgfVFQSFHLINSLN 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItEPGPDRMV----------VFQNYSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPL--LYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMG 179
Cdd:TIGR01184 71 VRENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180
....*....|....*....|....*...
gi 495112432 180 AEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTHDVDEA 178
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-220 |
1.93e-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: 137.43 E-value: 1.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDV---IKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTS-VESMKDKELAAFRNKtLGFVFQSFHLIN 98
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlFDSRKKINLPPQQRK-IGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 SLNVIDNVELPLlyRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKM 178
Cdd:cd03297 89 HLNVRENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495112432 179 GAEVMELLHKLNKEDGRTIVMVTHN-EEQAKQTSRTIRFFDGR 220
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDlSEAEYLADRIVVMEDGR 209
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-220 |
6.49e-40 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 137.48 E-value: 6.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLL---NIMGLL--DAPSSGKIEINGTSVESmKDKELAAFRnKTLGFVFQS 93
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLrclNRMNDLipGARVEGEILLDGEDIYD-PDVDVVELR-RRVGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 94 ---FhlinSLNVIDNVELPLlyRKMAAKERTRLAKEV---LERVGL----SHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:COG1117 101 pnpF----PKSIYDNVAYGL--RLHGIKSKSELDEIVeesLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLnKEDgRTIVMVTHNEEQAKQTS-RTIRFFDGR 220
Cdd:COG1117 175 VLLMDEPTSALDPISTAKIEELILEL-KKD-YTIVIVTHNMQQAARVSdYTAFFYLGE 230
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-223 |
1.40e-39 |
|
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: 138.40 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 38 IMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVEsmkdkeLAAFRNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAA 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT------NVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 118 KERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSK----MGAEVMELLHKLnked 193
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlrdqMQLELKTIQEQL---- 150
|
170 180 190
....*....|....*....|....*....|.
gi 495112432 194 GRTIVMVTHNEEQAKQTS-RTIRFFDGRQVQ 223
Cdd:TIGR01187 151 GITFVFVTHDQEEAMTMSdRIAIMRKGKIAQ 181
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-207 |
1.98e-39 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 136.35 E-value: 1.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 6 LTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIeINGTSvesmkdkELAAFRNK 85
Cdd:PRK11247 15 LNAVSKRYGERTV----LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTA-------PLAEARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 86 TLgFVFQSFHLINSLNVIDNVELPLlyrkmAAKERTRlAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEII 165
Cdd:PRK11247 83 TR-LMFQDARLLPWKKVIDNVGLGL-----KGQWRDA-ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495112432 166 LADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEA 197
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-203 |
7.51e-39 |
|
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: 140.20 E-value: 7.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLdaPSSGKIEINGTSVESMKDKELAAFRNKtLGFVFQS-FhliNS 99
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGLSRRALRPLRRR-MQVVFQDpF---GS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 100 LN----VIDNVELPL--LYRKMAAKERTRLAKEVLERVGLSHRMRH-MPTQLSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:COG4172 375 LSprmtVGQIIAEGLrvHGPGLSAAERRARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
170 180 190
....*....|....*....|....*....|.
gi 495112432 173 NLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:COG4172 455 ALDVSVQAQILDLLRDLQREHGLAYLFISHD 485
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-222 |
1.78e-38 |
|
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: 132.23 E-value: 1.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 28 LDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKElaafrnKTLGFVFQSFHLINSLNVIDNVE 107
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 108 LPLLYR-KMAAKERTRLAKeVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELL 186
Cdd:cd03298 93 LGLSPGlKLTAEDRQAIEV-ALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 495112432 187 HKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFD-GRQV 222
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDnGRIA 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
23-216 |
3.30e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 131.45 E-value: 3.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDAP--SSGKIEINGTSVESMKdkelAAFRNktLGFVFQSFHLINS 99
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALP----AEQRR--IGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 100 LNVIDNveLPL-LYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKM 178
Cdd:COG4136 91 LSVGEN--LAFaLPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 495112432 179 GAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRF 216
Cdd:COG4136 169 RAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-217 |
4.44e-38 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 132.79 E-value: 4.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDK--ELAA 81
Cdd:PRK10619 6 LNVIDLHKRYGEHEV----LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 FRNKTL-------GFVFQSFHLINSLNVIDNV-ELPLLYRKMAAKERTRLAKEVLERVGLSHRMR-HMPTQLSGGQCQRV 152
Cdd:PRK10619 82 ADKNQLrllrtrlTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 153 AIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRFF 217
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFL 225
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-219 |
9.58e-38 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 132.06 E-value: 9.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLL--DAPSSGKIEINGTSV--ESMKDK 77
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLrHLSGLItgDKSAGSHIELLGRTVqrEGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 78 ELAAFRNKTlGFVFQSFHLINSLNVIDNVELPLL---------YRKMAAKERTRlAKEVLERVGLSHRMRHMPTQLSGGQ 148
Cdd:PRK09984 80 DIRKSRANT-GYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKQR-ALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 149 CQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTI-------RFFDG 219
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIvalrqghVFYDG 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-202 |
1.03e-37 |
|
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: 130.29 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 2 AMIKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVesmkDKELAA 81
Cdd:COG4133 1 MMLEAENLSCRRG----ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 FRnKTLGFVFQSFHLINSLNVIDNVELpllYRKMAAKERTRLA-KEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:COG4133 73 YR-RRLAYLGHADGLKPELTVRENLRF---WAALYGLRADREAiDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLS 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTH 189
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-203 |
1.25e-37 |
|
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: 130.63 E-value: 1.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKELAAfrnKTLGFVFQSFHLINSL 100
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMGLL-PPRSGSIRFDGRDITGLPPHERAR---AGIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVELPLLYRKMAAKERTRlaKEVLERV-GLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMG 179
Cdd:cd03224 91 TVEENLLLGAYARRRAKRKARL--ERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIV 168
|
170 180
....*....|....*....|....
gi 495112432 180 AEVMELLHKLNKEdGRTIVMVTHN 203
Cdd:cd03224 169 EEIFEAIRELRDE-GVTILLVEQN 191
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-202 |
1.56e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 133.82 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKEla 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 afRNktLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:PRK11650 76 --RD--IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495112432 161 NPEIILADEPTGNLDSKMGAEvMEL-LHKLNKEDGRTIVMVTH 202
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAKLRVQ-MRLeIQRLHRRLKTTSLYVTH 193
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-202 |
1.80e-37 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 130.97 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAaf 82
Cdd:COG4604 1 MIEIKNVSKRYGGKVV----LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 rnKTLGFVFQSFHLINSLNVIDNVEL---PllYRKmaakerTRLAKE-------VLERVGLSH-RMRHMpTQLSGGQCQR 151
Cdd:COG4604 75 --KRLAILRQENHINSRLTVRELVAFgrfP--YSK------GRLTAEdreiideAIAYLDLEDlADRYL-DELSGGQRQR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495112432 152 VAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLH 194
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-203 |
3.51e-37 |
|
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: 135.97 E-value: 3.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 13 YRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKS-TLLNIMGLLDAPS---SGKIEINGTSVESMKDKELAAFRNKTLG 88
Cdd:COG4172 16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDLLGLSERELRRIRGNRIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 89 FVFQ---SfhlinSLNVIDNV-----ELPLLYRKMAAKERTRLAKEVLERVGLSH---RMRHMPTQLSGGQCQRVAIARA 157
Cdd:COG4172 96 MIFQepmT-----SLNPLHTIgkqiaEVLRLHRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQRVMIAMA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495112432 158 IVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:COG4172 171 LANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD 216
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-220 |
6.32e-37 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 128.93 E-value: 6.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYrtneiETLALEnVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvesmKDKELAAF 82
Cdd:PRK10771 1 MLKLTDITWLY-----HHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG------QDHTTTPP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNKTLGFVFQSFHLINSLNVIDNVEL---PLLyrKMAAKERTRLaKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIV 159
Cdd:PRK10771 69 SRRPVSMLFQENNLFSHLTVAQNIGLglnPGL--KLNAAQREKL-HAIARQMGIEDLLARLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN-EEQAKQTSRTIRFFDGR 220
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSlEDAARIAPRSLVVADGR 207
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-222 |
6.89e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 130.21 E-value: 6.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNE--IETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDkeLA 80
Cdd:PRK13633 4 MIKCKNVSYKYESNEesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--LW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 AFRNKTlGFVFQsfhliNSLNVI------DNVELPLLYRKMAAKE-RTRLaKEVLERVGLSHRMRHMPTQLSGGQCQRVA 153
Cdd:PRK13633 82 DIRNKA-GMVFQ-----NPDNQIvativeEDVAFGPENLGIPPEEiRERV-DESLKKVGMYEYRRHAPHLLSGGQKQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 154 IARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-203 |
1.63e-36 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 129.11 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 24 ENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRnKTLGFVFQSFHLINSLNVI 103
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDMNVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 104 DNVELPLlyrkmaaKERTRLAKEV--------LERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEP-TGNL 174
Cdd:PRK11831 103 DNVAYPL-------REHTQLPAPLlhstvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPfVGQD 175
|
170 180
....*....|....*....|....*....
gi 495112432 175 DSKMGAEVmELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK11831 176 PITMGVLV-KLISELNSALGVTCVVVSHD 203
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-220 |
2.57e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 128.28 E-value: 2.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEI-ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKEla 80
Cdd:COG1101 1 MLELKNLSKTFNPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNaIAGSL-PPDSGSILIDGKDVTKLPEYK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 afRNKTLGFVFQsfhliN-------SLNVIDNveLPLLYRKMAA--------KERTRLAKEVLERV--GLSHRMrHMPT- 142
Cdd:COG1101 78 --RAKYIGRVFQ-----DpmmgtapSMTIEEN--LALAYRRGKRrglrrgltKKRRELFRELLATLglGLENRL-DTKVg 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 143 QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA-KQTSRTIRFFDGR 220
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQAlDYGNRLIMMHEGR 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
22-223 |
2.61e-36 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 131.11 E-value: 2.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKElaafrnKTLGFVFQSFHLINSLN 101
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ------RPINMMFQSYALFPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSK---- 177
Cdd:PRK11607 108 VEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdr 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495112432 178 MGAEVMELLHKLnkedGRTIVMVTHNEEQAKQTSRTIRFFD-GRQVQ 223
Cdd:PRK11607 188 MQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNrGKFVQ 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-202 |
3.04e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 133.75 E-value: 3.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKdkeLAAFRNKtLGFVFQSFHLI 97
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNlLLRFYD-PTSGRILIDGVDIRDLT---LESLRRQ-IGVVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 98 nSLNVIDNVelpLLYRKMAAKERtrlAKEVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIIL 166
Cdd:COG1132 427 -SGTIRENI---RYGRPDATDEE---VEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190
....*....|....*....|....*....|....*.
gi 495112432 167 ADEPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTH 202
Cdd:COG1132 500 LDEATSALDTETEALIQEALERLMK--GRTTIVIAH 533
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
22-204 |
3.08e-36 |
|
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: 133.25 E-value: 3.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELAAfrnkTLGFVFQSFHLINSl 100
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLAtLAGLLD-PLQGEVTLDGVPVSSLDQDEVRR----RVSVCAQDAHLFDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVelpLLYRKMAAKERtrlAKEVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADE 169
Cdd:TIGR02868 424 TVRENL---RLARPDATDEE---LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|....*
gi 495112432 170 PTGNLDSKMGAEVMELLhkLNKEDGRTIVMVTHNE 204
Cdd:TIGR02868 498 PTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-214 |
4.13e-36 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 129.84 E-value: 4.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 6 LTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESmkdkelAAFRNK 85
Cdd:PRK11432 9 LKNITKRFGSNTV----IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 86 TLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEII 165
Cdd:PRK11432 79 DICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495112432 166 LADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTI 214
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTV 207
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-202 |
7.06e-36 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 125.77 E-value: 7.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRtneiETLALENVNLDVIKGEFVsIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKelaaFR 83
Cdd:cd03264 1 LQLENLTKRYG----KKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 nKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEdgRTIVMVTH 202
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTH 187
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-222 |
1.12e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 126.64 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 2 AMIKLTGINkiYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELaa 81
Cdd:PRK13632 6 VMIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 fRNKtLGFVFQsfhliNSLN------VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIA 155
Cdd:PRK13632 82 -RKK-IGIIFQ-----NPDNqfigatVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 156 RAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-222 |
1.14e-35 |
|
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: 125.06 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 9 INKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNI-MGLLDaPSSGKIEINGtsvESMKDKElaafRNKTL 87
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKIlAGLIK-ESSGSILLNG---KPIKAKE----RRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 88 GFVFQS--FHLINslnviDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEII 165
Cdd:cd03226 74 GYVMQDvdYQLFT-----DSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 166 LADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEE-QAKQTSRTIRFFDGRQV 222
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEfLAKVCDRVLLLANGAIV 205
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-203 |
1.51e-35 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 125.74 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDaPSSGKIEINGTSVEsmkdKELAA 81
Cdd:COG4555 1 MIEVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLaGLLK-PDSGSILIDGEDVR----KEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 FRNKtLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLShRMRHMPTQ-LSGGQCQRVAIARAIVG 160
Cdd:COG4555 72 ARRQ-IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLE-EFLDRRVGeLSTGMKKKVALARALVH 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHN 203
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHI 191
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-209 |
2.59e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 126.29 E-value: 2.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKD-KELAAFRNKtLGFVFQsF--H 95
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnKKLKPLRKK-VGIVFQ-FpeH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 96 LINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMR-HMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:PRK13634 97 QLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLaRSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190
....*....|....*....|....*....|....*
gi 495112432 175 DSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQ 209
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAAR 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-207 |
3.39e-35 |
|
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: 124.71 E-value: 3.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYrtNEIEtlALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKEL 79
Cdd:COG0410 1 MPMLEVENLHAGY--GGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLL-PPRSGSIRFDGEDITGLPPHRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 80 AAfrnKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAkEVLE---RvgLSHRMRHMPTQLSGGQCQRVAIAR 156
Cdd:COG0410 76 AR---LGIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLE-RVYElfpR--LKERRRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495112432 157 AIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQA 207
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFA 199
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-203 |
3.50e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.58 E-value: 3.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 20 TLALENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLDaPSSGKIEINGTSVESMKdKELAAFRnKTLGFVFQ-SFHLI 97
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLfLHFNGILK-PTSGEVLIKGEPIKYDK-KSLLEVR-KTVGIVFQnPDDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 98 NSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSK 177
Cdd:PRK13639 92 FAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180
....*....|....*....|....*.
gi 495112432 178 MGAEVMELLHKLNKEdGRTIVMVTHN 203
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHD 196
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-220 |
3.92e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.51 E-value: 3.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 13 YRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLLdAPSSGKIEINGT--SVESMKDkelaaFRNKtLGF 89
Cdd:PRK13635 13 FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAkLLNGLL-LPEAGTITVGGMvlSEETVWD-----VRRQ-VGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 90 VFQsfhliNSLN------VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:PRK13635 86 VFQ-----NPDNqfvgatVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGE 217
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-222 |
4.05e-35 |
|
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: 125.30 E-value: 4.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 2 AMIKLTGINKIYRTNEI-----ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKD 76
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGGLfgakqRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 77 KELAAFRnKTLGFVFQSfhLINSLNVIDNVEL----PLL-YRKMAAKERTRLAKEVLERVGL-SHRMRHMPTQLSGGQCQ 150
Cdd:TIGR02769 81 KQRRAFR-RDVQLVFQD--SPSAVNPRMTVRQiigePLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495112432 151 RVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-222 |
4.97e-35 |
|
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: 124.43 E-value: 4.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGK-IEI-----NGTSVESM 74
Cdd:COG1119 1 DPLLELRNVTVRRGGKTI----LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLfgerrGGEDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 75 KdkelaafrnKTLGFVFQSFHL-----INSLNVI-----DNVELpllYRKMAAKERTRlAKEVLERVGLSHRMRHMPTQL 144
Cdd:COG1119 77 R---------KRIGLVSPALQLrfprdETVLDVVlsgffDSIGL---YREPTDEQRER-ARELLELLGLAHLADRPFGTL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 145 SGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN-EEQAKQTSRTIRFFDGRQV 222
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHvEEIPPGITHVLLLKDGRVV 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-202 |
2.19e-34 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 125.60 E-value: 2.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 25 NVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTS-VESMKDKELAAFRNKtLGFVFQSFHLINSLNVI 103
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlQDSARGIFLPPHRRR-IGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 104 DNvelpLLY--RKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAE 181
Cdd:COG4148 96 GN----LLYgrKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180
....*....|....*....|.
gi 495112432 182 VMELLHKLNKEDGRTIVMVTH 202
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSH 192
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-220 |
7.79e-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: 124.07 E-value: 7.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 26 VNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSV-ESMKDKELAAFRNKtLGFVFQSFHLINSLNVID 104
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfDSRKGIFLPPEKRR-IGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 105 NvelpLLY--RKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEV 182
Cdd:TIGR02142 95 N----LRYgmKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 495112432 183 MELLHKLNKEDGRTIVMVTHN-EEQAKQTSRTIRFFDGR 220
Cdd:TIGR02142 171 LPYLERLHAEFGIPILYVSHSlQEVLRLADRVVVLEDGR 209
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-203 |
9.11e-34 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 121.72 E-value: 9.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRTNEIETLA-----LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMK 75
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLSGKHqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 76 DKELAAFRnKTLGFVFQ-SFHLINSLNVI-DNVELPLLY-RKMAAKERTRLAKEVLERVGL--SHRMRhMPTQLSGGQCQ 150
Cdd:PRK10419 81 RAQRKAFR-RDIQMVFQdSISAVNPRKTVrEIIREPLRHlLSLDKAERLARASEMLRAVDLddSVLDK-RPPQLSGGQLQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495112432 151 RVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHD 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-205 |
1.02e-33 |
|
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: 120.62 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 2 AMIKLTGINK---IYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLL-----NIMglldaPSSGKIEIN--GTSV 71
Cdd:COG4778 3 TLLEVENLSKtftLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLkciygNYL-----PDSGSILVRhdGGWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 72 E--SMKDKELAAFRNKTLGFVFQsFhlinsLNVI------DNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHM-PT 142
Cdd:COG4778 78 DlaQASPREILALRRRTIGYVSQ-F-----LRVIprvsalDVVAEPLLERGVDREEARARARELLARLNLPERLWDLpPA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495112432 143 QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEE 205
Cdd:COG4778 152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEE 213
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
4-222 |
1.12e-33 |
|
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: 119.97 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEIEtlalenVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESmkdkeLAAFR 83
Cdd:TIGR01277 1 LALDKVRYEYEHLPME------FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG-----LAPYQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 nKTLGFVFQSFHLINSLNVIDNVEL---PLLyrKMAAKERTRLaKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:TIGR01277 70 -RPVSMLFQENNLFAHLTVRQNIGLglhPGL--KLNAEQQEKV-VDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:TIGR01277 146 PNPILLLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-222 |
1.63e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 123.99 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 20 TLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLGFVFQSFHLINS 99
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 100 LNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMG 179
Cdd:PRK10070 121 MTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495112432 180 AEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-220 |
2.53e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 121.73 E-value: 2.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIY-RTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEI---------NGTSVES 73
Cdd:PRK13651 3 IKVKNIVKIFnKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 74 MKDK---ELAAFRN--------KTLGFVFQ--SFHLINSLNVIDNVELPLLY--RKMAAKERtrlAKEVLERVGLSHR-M 137
Cdd:PRK13651 83 VLEKlviQKTRFKKikkikeirRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMgvSKEEAKKR---AAKYIELVGLDESyL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 138 RHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQA-KQTSRTIRF 216
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVlEWTKRTIFF 238
|
....
gi 495112432 217 FDGR 220
Cdd:PRK13651 239 KDGK 242
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-203 |
5.37e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 121.22 E-value: 5.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVeSMKDKELAAFRNKTLGFVFQSFHliNSLN 101
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL-LKADPEAQKLLRQKIQIVFQNPY--GSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 ----VIDNVELPLLYR-KMAAKERTRLAKEVLERVGL----SHRMRHMptqLSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:PRK11308 107 prkkVGQILEEPLLINtSLSAAERREKALAMMAKVGLrpehYDRYPHM---FSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190
....*....|....*....|....*....|.
gi 495112432 173 NLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK11308 184 ALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-207 |
7.16e-33 |
|
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: 117.99 E-value: 7.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNI-MGLLDaPSSGKIEINGTSVESMKDKelaAF 82
Cdd:cd03263 1 LQIRNLTKTYKKGT--KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMlTGELR-PTSGTAYINGYSIRTDRKA---AR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNktLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:cd03263 75 QS--LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQA 207
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEA 195
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
23-218 |
7.87e-33 |
|
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: 117.27 E-value: 7.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNI-MGLLDAPS-SGKIEINGTSVEsmkdkeLAAFRnKTLGFVFQSFHLINSL 100
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNAlAGRRTGLGvSGEVLINGRPLD------KRSFR-KIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVElpllyrkMAAKERtrlakevlervglshrmrhmptQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGA 180
Cdd:cd03213 98 TVRETLM-------FAAKLR----------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 495112432 181 EVMELLHKLNKeDGRTIVMVTHneeqakQTSRTI-RFFD 218
Cdd:cd03213 149 QVMSLLRRLAD-TGRTIICSIH------QPSSEIfELFD 180
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
23-202 |
1.66e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 118.34 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTSVESMKDKELAafrnKTLGFVFQSFHLINSLN 101
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGEL-SPDSGEVRLNGRPLADWSPAELA----RRRAVLPQHSSLSFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSH-RMRHMPtQLSGGQCQRVAIARAIV------GNPEIILADEPTGNL 174
Cdd:PRK13548 93 VEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHlAGRDYP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSAL 171
|
170 180
....*....|....*....|....*...
gi 495112432 175 DSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:PRK13548 172 DLAHQHHVLRLARQLAHERGLAVIVVLH 199
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-203 |
1.73e-32 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 118.40 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRTN-------EIEtlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVES 73
Cdd:COG4167 2 SALLEVRNLSKTFKYRtglfrrqQFE--AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 74 MKDKelaaFRNKTLGFVFQsfHLINSLNVIDNV----ELPL-LYRKMAAKERTRLAKEVLERVGL----SHRMRHMptqL 144
Cdd:COG4167 80 GDYK----YRCKHIRMIFQ--DPNTSLNPRLNIgqilEEPLrLNTDLTAEEREERIFATLRLVGLlpehANFYPHM---L 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 145 SGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:COG4167 151 SSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQH 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-202 |
2.95e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.05 E-value: 2.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRTneieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVEsmkdkela 80
Cdd:COG1129 2 EPLLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 aFRN----KTLG--FVFQSFHLINSLNVIDNVELPLLYRKMAA---KERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQR 151
Cdd:COG1129 70 -FRSprdaQAAGiaIIHQELNLVPNLSVAENIFLGREPRRGGLidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495112432 152 VAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISH 198
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-220 |
3.12e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 118.23 E-value: 3.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNE-IETLALENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLLDaPSSGKIEINGTSVESMKDKeLAA 81
Cdd:PRK13637 3 IKIENLTHIYMEGTpFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIqHLNGLLK-PTSGKIIIDGVDITDKKVK-LSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 FRnKTLGFVFQ-SFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSH-RMRHM-PTQLSGGQCQRVAIARAI 158
Cdd:PRK13637 81 IR-KKVGLVFQyPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYeDYKDKsPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495112432 159 VGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN-EEQAKQTSRTIRFFDGR 220
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSmEDVAKLADRIIVMNKGK 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-203 |
4.03e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 118.01 E-value: 4.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRT-NEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVES-MKDKELAA 81
Cdd:PRK13641 3 IKFENVDYIYSPgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 FRNK-TLGFVFQSFHLINSlNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHR-MRHMPTQLSGGQCQRVAIARAIV 159
Cdd:PRK13641 83 LRKKvSLVFQFPEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHN 203
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHN 204
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
13-221 |
5.26e-32 |
|
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: 114.62 E-value: 5.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 13 YRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTSVESMKDKELAAFrnktLGFVF 91
Cdd:cd03246 8 FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLIlGLL-RPTSGRVRLDGADISQWDPNELGDH----VGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 92 QSFHLInSLNVIDNVelpllyrkmaakertrlakevlervglshrmrhmptqLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:cd03246 83 QDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495112432 172 GNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQ 221
Cdd:cd03246 125 SHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-222 |
8.39e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.17 E-value: 8.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLL-----DAPSSGKIEINGTSVESMKDKELaafrNKTLGFVFQSFHLI 97
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEL----RRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 98 NSLNVIDNVELPLLYRKMAA--KERTRLAKEVLERVGL----SHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:PRK14247 95 PNLSIFENVALGLKLNRLVKskKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495112432 172 GNLDSKMGAEVMELLHKLNKEdgRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-223 |
1.85e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 116.42 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRT-NEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLLDaPSSGKIEINGTSVES-MKDKELA 80
Cdd:PRK13646 3 IRFDNVSYTYQKgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIqNINALLK-PTTGTVTVDDITITHkTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 AFRnKTLGFVFQsfhLINSLNVIDNVELPLLYR----KMAAKERTRLAKEVLERVGLSHR-MRHMPTQLSGGQCQRVAIA 155
Cdd:PRK13646 82 PVR-KRIGMVFQ---FPESQLFEDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDvMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 156 RAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN-EEQAKQTSRTIRFFDGRQVQ 223
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIVS 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-216 |
1.88e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 115.32 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLL-----DAPSSGKIEINGTSVESMKDKE 78
Cdd:PRK14267 5 IETVNLRVYYGSNHV----IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 79 LAAfrNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAA--KERTRLAKEVLERVGL----SHRMRHMPTQLSGGQCQRV 152
Cdd:PRK14267 81 IEV--RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKskKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495112432 153 AIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdgRTIVMVTHNEEQAKQTSRTIRF 216
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAF 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-202 |
4.41e-31 |
|
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: 113.86 E-value: 4.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVesmKDKELAAFRNKtLGFVFQSFHLIN 98
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV---RDYTLASLRRQ-IGLVSQDVFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 slnviDNVELPLLYRKMAAKE-------RTRLAKEVLERV--GLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADE 169
Cdd:cd03251 90 -----DTVAENIAYGRPGATReeveeaaRAANAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190
....*....|....*....|....*....|...
gi 495112432 170 PTGNLDSKMGAEVMELLHKLNKedGRTIVMVTH 202
Cdd:cd03251 165 ATSALDTESERLVQAALERLMK--NRTTFVIAH 195
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
23-202 |
6.82e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 114.06 E-value: 6.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTSVESMKDKELAAFR-----NKTLGFVFqsfhl 96
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGEL-TPSSGEVRLNGRPLAAWSPWELARRRavlpqHSSLAFPF----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 97 inslNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSH-RMRHMPTqLSGGQCQRVAIARAIV-------GNPEIILAD 168
Cdd:COG4559 91 ----TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHlAGRSYQT-LSGGEQQRVQLARVLAqlwepvdGGPRWLFLD 165
|
170 180 190
....*....|....*....|....*....|....
gi 495112432 169 EPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTH 202
Cdd:COG4559 166 EPTSALDLAHQHAVLRLARQLARR-GGGVVAVLH 198
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-223 |
8.86e-31 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 115.57 E-value: 8.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDApSSGKIEINGTSVESMKDKELAAFRnKTLGFVFQSfhLINSL 100
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARaIIGLVKA-TDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQD--PLASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 N----VIDNVELPL--LYRKMAAKERTRLAKEVLERVGLSHRM--RHmPTQLSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:PRK15079 112 NprmtIGEIIAEPLrtYHPKLSRQEVKDRVKAMMLKVGLLPNLinRY-PHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495112432 173 NLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGRQVQ 223
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISdRVLVMYLGHAVE 242
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-202 |
1.04e-30 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 112.31 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVesmkdkelaafr 83
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 nktlgfvfqsFHLINSLNVIDN-VELPLLYRKMAAKERTRLA-----------KEVLERVGLSHRMRHMPTQLSGGQCQR 151
Cdd:cd03268 65 ----------QKNIEALRRIGAlIEAPGFYPNLTARENLRLLarllgirkkriDEVLDVVGLKDSAKKKVKGFSLGMKQR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495112432 152 VAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTH 202
Cdd:cd03268 135 LGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSH 184
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-222 |
1.37e-30 |
|
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: 110.60 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTSVESMKDKElaAF 82
Cdd:cd03216 1 LELRGITKRFG----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILsGLY-KPDSGEILVDGKEVSFASPRD--AR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNKtLGFVFQsfhlinslnvidnvelpllyrkmaakertrlakevlervglshrmrhmptqLSGGQCQRVAIARAIVGNP 162
Cdd:cd03216 74 RAG-IAMVYQ---------------------------------------------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTI---RffDGRQV 222
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVtvlR--DGRVV 161
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-216 |
1.43e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.17 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGtsvesmkdkelaafrNKTLGFVFQSFHLINSL 100
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKvLAGVL-RPTSGTVRRAG---------------GARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 --NVIDNVELPL-----LYRKMAAKERTRLAkEVLERVGLsHRMRHMPTQ-LSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:NF040873 71 plTVRDLVAMGRwarrgLWRRLTRDDRAAVD-DALERVGL-ADLAGRQLGeLSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495112432 173 NLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRF 216
Cdd:NF040873 149 GLDAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCVLL 191
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
22-215 |
1.62e-30 |
|
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: 117.39 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKdkelAAFRNKTLGFVFQSFHLINSl 100
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNlLLGFVD-PTEGSIAVNGVPLADAD----ADSWRDQIAWVPQHPFLFAG- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVelpLLYRKMAAKERTRlakEVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADE 169
Cdd:TIGR02857 411 TIAENI---RLARPDASDAEIR---EALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDE 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495112432 170 PTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIR 215
Cdd:TIGR02857 485 PTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVV 528
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
22-202 |
2.43e-30 |
|
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: 111.93 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELaafRNKtLGFVFQSFHLINSl 100
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINlLMRFYD-PQKGQILIDGIDIRDISRKSL---RSM-IGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVelpLLYRKMAAKERTrlaKEVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADE 169
Cdd:cd03254 92 TIMENI---RLGRPNATDEEV---IEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190
....*....|....*....|....*....|...
gi 495112432 170 PTGNLDSKMGAEVMELLHKLNKedGRTIVMVTH 202
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMK--GRTSIIIAH 196
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-203 |
4.47e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 112.63 E-value: 4.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 20 TLALENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLLDaPSSGKIEINGTSVESMKdKELAAFRnKTLGFVFQS-FHLI 97
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFqNLNGILK-PSSGRILFDGKPIDYSR-KGLMKLR-ESVGMVFQDpDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 98 NSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHrMRHMPTQ-LSGGQCQRVAIARAIVGNPEIILADEPTGNLDS 176
Cdd:PRK13636 96 FSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180
....*....|....*....|....*..
gi 495112432 177 KMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK13636 175 MGVSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-222 |
6.20e-30 |
|
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: 110.37 E-value: 6.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 13 YRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELaafrNKTLGFVF 91
Cdd:cd03245 10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKlLAGLYK-PTSGSVLLDGTDIRQLDPADL----RRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 92 QSFHLINSlNVIDNVELPLLY----RKMAAKERTRLAKEVLER-VGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIIL 166
Cdd:cd03245 85 QDVTLFYG-TLRDNITLGAPLaddeRILRAAELAGVTDFVNKHpNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 167 ADEPTGNLDskMGAEvMELLHKLNKE-DGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:cd03245 164 LDEPTSAMD--MNSE-ERLKERLRQLlGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-202 |
6.89e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 112.15 E-value: 6.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRT-NEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESM-KDKELAA 81
Cdd:PRK13649 3 INLQNVSYTYQAgTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 FRnKTLGFVFQ-SFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHM-PTQLSGGQCQRVAIARAIV 159
Cdd:PRK13649 83 IR-KKVGLVFQfPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNkEDGRTIVMVTH 202
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTH 203
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
19-209 |
1.04e-29 |
|
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: 109.77 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVEsmkdKELAAFRnKTLGFVFQSFHLIN 98
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVR-RRIGIVFQDLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 SLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKM 178
Cdd:cd03265 87 ELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190
....*....|....*....|....*....|.
gi 495112432 179 GAEVMELLHKLNKEDGRTIVMVTHNEEQAKQ 209
Cdd:cd03265 167 RAHVWEYIEKLKEEFGMTILLTTHYMEEAEQ 197
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-202 |
1.07e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 111.75 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNE-IETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESM-KDKELA 80
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTsKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 AFRNKtLGFVFQ--SFHLINSlNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRM-RHMPTQLSGGQCQRVAIARA 157
Cdd:PRK13643 81 PVRKK-VGVVFQfpESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495112432 158 IVGNPEIILADEPTGNLDSKMGAEVMELLHKLNkEDGRTIVMVTH 202
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTH 202
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-207 |
2.22e-29 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 108.99 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkeLAAF 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP---AEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNktLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:cd03266 78 RR--LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQA 207
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEV 199
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
23-203 |
6.63e-29 |
|
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: 108.09 E-value: 6.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvESMKDKELAAFRnKTLGFVFQSFHLINslnv 102
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG---QDIREVTLDSLR-RAIGVVPQDTVLFN---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 103 iDNVELPLLYRKMAAKErtrlaKEVLE--RVGLSH-RMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILAD 168
Cdd:cd03253 89 -DTIGYNIRYGRPDATD-----EEVIEaaKAAQIHdKIMRFPdgydtivgergLKLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190
....*....|....*....|....*....|....*
gi 495112432 169 EPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHN 203
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSK--GRTTIVIAHR 195
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
23-207 |
9.02e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 108.56 E-value: 9.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAafrnKTLGFVFQSfHLI-NSLN 101
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----RRLALLPQH-HLTpEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVE------LPlLYRKMAAKERTRLAKeVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLD 175
Cdd:PRK11231 93 VRELVAygrspwLS-LWGRLSAEDNARVNQ-AMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
170 180 190
....*....|....*....|....*....|..
gi 495112432 176 SKMGAEVMELLHKLNKEdGRTIVMVTHNEEQA 207
Cdd:PRK11231 171 INHQVELMRLMRELNTQ-GKTVVTVLHDLNQA 201
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-203 |
9.32e-29 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 107.63 E-value: 9.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAfr 83
Cdd:cd03218 1 LRAENLSKRYGKRKV----VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRAR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 nKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03218 75 -LGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHN 203
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHN 192
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-214 |
2.12e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 106.72 E-value: 2.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 13 YRTNEieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKelaAFRnKTLGFVFQ 92
Cdd:PRK10247 15 YLAGD--AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---IYR-QQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 93 SFHLINSlNVIDNVELPLLYRKMAAkERTRLAKEvLERVGLSHRMRHMP-TQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:PRK10247 89 TPTLFGD-TVYDNLIFPWQIRNQQP-DPAIFLDD-LERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495112432 172 GNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTI 214
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
22-219 |
4.18e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 106.78 E-value: 4.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLL---NIMGLL--DAPSSGKIEINGTSVESMKdKELAAFRnKTLGFVFQS--- 93
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLnpEVTITGSIVYNGHNIYSPR-TDTVDLR-KEIGMVFQQpnp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 94 FHLINSLNVIDNVELPLLYRKM---AAKERTRLAKEVLERVglSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:PRK14239 98 FPMSIYENVVYGLRLKGIKDKQvldEAVEKSLKGASIWDEV--KDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495112432 171 TGNLDSKMGAEVMELLHKLnkEDGRTIVMVTHNEEQAKQTS-RTIRFFDG 219
Cdd:PRK14239 176 TSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISdRTGFFLDG 223
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-203 |
4.80e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 110.68 E-value: 4.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNimgLLD---APSSGKIEINGTSVESMKDKELAAfrnkTLGFVFQSFHLIN 98
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQ---LLTrawDPQQGEILLNGQPIADYSEAALRQ----AISVVSQRVHLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 -SLNviDNVelpllyrKMAAKERT--RLAkEVLERVGLSH----------------RmrhmptQLSGGQCQRVAIARAIV 159
Cdd:PRK11160 428 aTLR--DNL-------LLAAPNASdeALI-EVLQQVGLEKlleddkglnawlgeggR------QLSGGEQRRLGIARALL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHN 203
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHR 533
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-202 |
6.67e-28 |
|
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: 110.28 E-value: 6.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDA--PSSGKIEIN-----------------------GTSVESMK- 75
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverpskvgepcpvcGGTLEPEEv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 76 ------DKELAAFRnKTLGFVFQ-SFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQ 148
Cdd:TIGR03269 95 dfwnlsDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495112432 149 CQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-202 |
1.07e-27 |
|
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: 105.31 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTllnIMGLLD---APSSGKIEINGtsvESMKDKELAAFRNKtLGFVFQSFH 95
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLErfyDPTSGEILLDG---VDIRDLNLRWLRSQ-IGLVSQEPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 96 LINSlNVIDNVELPLLYRKMAAKERTRLAKEVLERV-GLSHRMRHM----PTQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:cd03249 88 LFDG-TIAENIRYGKPDATDEEVEEAAKKANIHDFImSLPDGYDTLvgerGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190
....*....|....*....|....*....|..
gi 495112432 171 TGNLDSKMGAEVMELLHKLNKedGRTIVMVTH 202
Cdd:cd03249 167 TSALDAESEKLVQEALDRAMK--GRTTIVIAH 196
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-219 |
1.24e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.60 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELaafrNKTLGFVFQS--FHL 96
Cdd:PRK13648 21 ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL----RKHIGIVFQNpdNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 97 INSLNVIDnVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDS 176
Cdd:PRK13648 97 VGSIVKYD-VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495112432 177 KMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKG 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-203 |
1.71e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 106.73 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKS-TLLNIMGLLdaPSSGKIE----INGTSVESMKDKELAAFRNKTLGFVFQSfhL 96
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLL--AANGRIGgsatFNGREILNLPEKELNKLRAEQISMIFQD--P 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 97 INSLNVIDNV-----ELPLLYRKMAAKERTRLAKEVLERVGLSH---RMRHMPTQLSGGQCQRVAIARAIVGNPEIILAD 168
Cdd:PRK09473 107 MTSLNPYMRVgeqlmEVLMLHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190
....*....|....*....|....*....|....*
gi 495112432 169 EPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 221
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
19-211 |
1.81e-27 |
|
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: 104.14 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELAAfrnKTLGFVFQSFHLI 97
Cdd:TIGR03410 12 QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKtLMGLLP-VKSGSIRLDGEDITKLPPHERAR---AGIAYVPQGREIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 98 NSLNVIDNVELPLLYRKMAAKErtrLAKEVLERVGLSHRMRHMPT-QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDS 176
Cdd:TIGR03410 88 PRLTVEENLLTGLAALPRRSRK---IPDEIYELFPVLKEMLGRRGgDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190
....*....|....*....|....*....|....*
gi 495112432 177 KMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS 211
Cdd:TIGR03410 165 SIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELA 199
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-203 |
3.35e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 108.25 E-value: 3.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 13 YRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKS-TLLNIMGLLDAPS----SGKIEINGTSVESMKDKELAAFRNKTL 87
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGVRGNKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 88 GFVFQsfHLINSLNVIDNVELPL-----LYRKMAAKERTRLAKEVLERVGLSH---RMRHMPTQLSGGQCQRVAIARAIV 159
Cdd:PRK15134 95 AMIFQ--EPMVSLNPLHTLEKQLyevlsLHRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLSGGERQRVMIAMALL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHN 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-223 |
3.92e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 104.36 E-value: 3.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDK-ELAAFR-NKTLGFVFQSFHLINSL 100
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIfQIDAIKlRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVELPLLYRKMAAK-ERTRLAKEVLERVGL----SHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLD 175
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495112432 176 SKMGAEVMELLHKLNKEdgRTIVMVTHNEEQAKQTSRTIRF-FDGRQVQ 223
Cdd:PRK14246 186 IVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFlYNGELVE 232
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-203 |
3.99e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 105.59 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKS-TLLNIMGLLDAP---SSGKIEINGTSVESMKDKELAAFRNKTLGFVFQSfhLI 97
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQD--PM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 98 NSLNVIDNVElpllYRKMAA---------KERTRLAKEVLERVGL---SHRMRHMPTQLSGGQCQRVAIARAIVGNPEII 165
Cdd:PRK11022 100 TSLNPCYTVG----FQIMEAikvhqggnkKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 495112432 166 LADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENMALVLITHD 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-202 |
4.34e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.81 E-value: 4.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTneieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNI-MGLLdAPSSGKIEINGTSVE--SMKDkel 79
Cdd:COG3845 5 ALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKIlYGLY-QPDSGEILIDGKPVRirSPRD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 80 aAFRNKtLGFVFQSFHLINSLNVIDNV-----ELPLLYRKMaAKERTRLaKEVLERVGLS---HRMRHmptQLSGGQCQR 151
Cdd:COG3845 77 -AIALG-IGMVHQHFMLVPNLTVAENIvlglePTKGGRLDR-KAARARI-RELSERYGLDvdpDAKVE---DLSVGEQQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495112432 152 VAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITH 199
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-222 |
5.87e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 104.30 E-value: 5.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLdAPSSGKIEINGtsVESMKDKELAA 81
Cdd:PRK13644 1 MIRLENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLaLHLNGLL-RPQKGKVLVSG--IDTGDFSKLQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 FRnKTLGFVFQSfhlINSLNVIDNVELPLLYRK----MAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARA 157
Cdd:PRK13644 75 IR-KLVGIVFQN---PETQFVGRTVEEDLAFGPenlcLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 158 IVGNPEIILADEPTGNLDSKMGAEVMELLHKLNkEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
19-202 |
7.63e-27 |
|
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: 107.64 E-value: 7.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFrnktLGFVFQSFHLIN 98
Cdd:TIGR03375 477 ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRN----IGYVPQDPRLFY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 -SLNviDNvelpLLYRKMAAKERTRLakEVLERVGLSHRMRHMPT-----------QLSGGQCQRVAIARAIVGNPEIIL 166
Cdd:TIGR03375 553 gTLR--DN----IALGAPYADDEEIL--RAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILL 624
|
170 180 190
....*....|....*....|....*....|....*..
gi 495112432 167 ADEPTGNLDskMGAEvMELLHKLNKE-DGRTIVMVTH 202
Cdd:TIGR03375 625 LDEPTSAMD--NRSE-ERFKDRLKRWlAGKTLVLVTH 658
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
24-222 |
1.00e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 103.14 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 24 ENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAafrnKTLGFVFQSFHLINSLNVI 103
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 104 DNV------ELPLLYRkmAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSK 177
Cdd:PRK10253 100 ELVargrypHQPLFTR--WRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495112432 178 MGAEVMELLHKLNKEDGRTIVMVTHNEEQA-KQTSRTIRFFDGRQV 222
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDLNQAcRYASHLIALREGKIV 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-222 |
3.07e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.12 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 20 TLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELaafRNKtLGFVFQS-FHLIN 98
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---RSK-VGLVFQDpDDQVF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 SLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKM 178
Cdd:PRK13647 94 SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495112432 179 GAEVMELLHKLNKEdGRTIVMVTHNEEQAKQ-TSRTIRFFDGRQV 222
Cdd:PRK13647 174 QETLMEILDRLHNQ-GKTVIVATHDVDLAAEwADQVIVLKEGRVL 217
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
4-223 |
5.27e-26 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 105.21 E-value: 5.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEIETLAleNVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELaafr 83
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVLS--NLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWL---- 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 NKTLGFVFQSFHLINSlNVIDNVELPllyRKMAAKERTRLAKEVLERVGLSHRMRHMPTQ--------LSGGQCQRVAIA 155
Cdd:TIGR01846 530 RRQMGVVLQENVLFSR-SIRDNIALC---NPGAPFEHVIHAAKLAGAHDFISELPQGYNTevgekganLSGGQRQRIAIA 605
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 156 RAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:TIGR01846 606 RALVGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRACDRIIVLEKGQIAE 671
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
21-220 |
7.05e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 101.01 E-value: 7.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 21 LALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLD-----APSSGKIEINGTSVESmKDKELAAFRNKtLGFVFQSFH 95
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlipgFRVEGKVTFHGKNLYA-PDVDPVEVRRR-IGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 96 LInSLNVIDNVEL------------PLLYRKMAAKERTRLAKEVLERVGLShrmrhmptqLSGGQCQRVAIARAIVGNPE 163
Cdd:PRK14243 102 PF-PKSIYDNIAYgaringykgdmdELVERSLRQAALWDEVKDKLKQSGLS---------LSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLnKEDgRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:PRK14243 172 VILMDEPCSALDPISTLRIEELMHEL-KEQ-YTIIIVTHNMQQAARVSDMTAFFNVE 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
33-218 |
1.07e-25 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 104.36 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 33 GEFVSIMGPSGCGKSTLLNIMGLLDAPS---SGKIEINGTSVESMKDKELAAFrnktlgfVFQSFHLINSLNVIDN---- 105
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISAY-------VQQDDLFIPTLTVREHlmfq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 106 --VELPllyRKMAAKERTRLAKEVLERVGLS----------HRMRhmptQLSGGQCQRVAIARAIVGNPEIILADEPTGN 173
Cdd:TIGR00955 124 ahLRMP---RRVTKKEKRERVDEVLQALGLRkcantrigvpGRVK----GLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495112432 174 LDSKMGAEVMELLHKL-NKedGRTIVMVTHneeqaKQTSRTIRFFD 218
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLaQK--GKTIICTIH-----QPSSELFELFD 235
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
17-202 |
1.87e-25 |
|
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: 97.77 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 17 EIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKelaafRNKTLGFVFQSFH 95
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQlLTGDLK-PQQGEITLDGVPVSDLEKA-----LSSLISVLNQRPY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 96 LINSlnvidnvelpllyrkmaakertrlakEVLERVGlshrmrhmpTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLD 175
Cdd:cd03247 86 LFDT--------------------------TLRNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180
....*....|....*....|....*..
gi 495112432 176 SKMGAEVMELLHKLNKEdgRTIVMVTH 202
Cdd:cd03247 131 PITERQLLSLIFEVLKD--KTLIWITH 155
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-202 |
3.22e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.45 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 6 LTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINgtsvesmkdkelaafRNK 85
Cdd:COG0488 1 LENLSKSFGGRPL----LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 86 TLGFVFQSFHLINSLNVIDNV------------ELPLLYRKMAAKER-----TRL---------------AKEVLERVGL 133
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVldgdaelraleaELEELEAKLAEPDEdlerlAELqeefealggweaearAEEILSGLGF 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495112432 134 SHRMRHMP-TQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDskmgAEVMELLHK-LNKEDGrTIVMVTH 202
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEfLKNYPG-TVLVVSH 207
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
22-220 |
5.25e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.10 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKST---LLNIMGLLDAPSSGKIEINGTSVESmkdKELAAFRNKtLGFVFQsfhliN 98
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTA---KTVWDIREK-VGIVFQ-----N 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 SLN------VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:PRK13640 93 PDNqfvgatVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495112432 173 NLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:PRK13640 173 MLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGK 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-222 |
5.92e-25 |
|
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: 97.35 E-value: 5.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLLdAPSSGKIEINGTSVEsmkdkelAAF 82
Cdd:cd03269 1 LEVENVTKRFGRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIrMILGII-LPDSGEVLFDGKPLD-------IAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNKtLGFVFQSFHLINSLNVIDNvelpLLY----RKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAI 158
Cdd:cd03269 69 RNR-IGYLPEERGLYPKMKVIDQ----LVYlaqlKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 159 VGNPEIILADEPTGNLDSkMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQ-TSRTIRFFDGRQV 222
Cdd:cd03269 144 IHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
9-203 |
8.21e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 101.86 E-value: 8.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 9 INKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRnKTLG 88
Cdd:PRK10261 330 LNRVTR----EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 89 FVFQSFH--LINSLNVIDNVELPL-LYRKMAAKERTRLAKEVLERVGL--SHRMRHmPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:PRK10261 405 FIFQDPYasLDPRQTVGDSIMEPLrVHGLLPGKAAAARVAWLLERVGLlpEHAWRY-PHEFSGGQRQRICIARALALNPK 483
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHD 523
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-203 |
9.47e-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: 9.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNE-----IETL------------ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEI 66
Cdd:cd03267 1 IEVSNLSKSYRVYSkepglIGSLkslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 67 NGTSVESMKDKELaafrnKTLGFVF-QSFHLINSLNVIDNVEL-PLLYRKMAAKERTRLAK--EVLErvgLSHRMRHMPT 142
Cdd:cd03267 81 AGLVPWKRRKKFL-----RRIGVVFgQKTQLWWDLPVIDSFYLlAAIYDLPPARFKKRLDElsELLD---LEELLDTPVR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495112432 143 QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:cd03267 153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHY 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-203 |
1.04e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 101.32 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLdaPSSGKIEINGTSVESMKDKELAAFRNKtLGFVFQSFHliNSL 100
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTgLALLRLI--NSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQDPN--SSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVE------LPLLYRKMAAKERTRLAKEVLERVGLSHRMRH-MPTQLSGGQCQRVAIARAIVGNPEIILADEPTGN 173
Cdd:PRK15134 376 NPRLNVLqiieegLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190
....*....|....*....|....*....|
gi 495112432 174 LDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-218 |
1.67e-24 |
|
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: 96.57 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 21 LALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDAPS--SGKIEINGtsVESMKDKELaafrnKTLGFVFQSFHLI 97
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDaISGRVEGGGttSGQILFNG--QPRKPDQFQ-----KCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 98 NSLNV------IDNVELPllyRKMAAKERT-RLAKEVLERVGLShRMRHMP-TQLSGGQCQRVAIARAIVGNPEIILADE 169
Cdd:cd03234 94 PGLTVretltyTAILRLP---RKSSDAIRKkRVEDVLLRDLALT-RIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495112432 170 PTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHneeqaKQTSRTIRFFD 218
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARR-NRIVILTIH-----QPRSDLFRLFD 212
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-203 |
1.79e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.98 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 21 LALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAafrNKTLGFVFQSFHLINSL 100
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA---RMGVVRTFQHVRLFREM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDN--------VELPLL--------YRKmAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEI 164
Cdd:PRK11300 96 TVIENllvaqhqqLKTGLFsgllktpaFRR-AESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 495112432 165 ILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-170 |
2.02e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 96.64 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESmkdkeL 79
Cdd:COG1137 1 MMTLEAENLVKSYGKRTV----VKDVSLEVNQGEIVGLLGPNGAGKTTTFYmIVGLV-KPDSGRIFLDGEDITH-----L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 80 AAFRNKTLGF--------VFQSfhlinsLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQR 151
Cdd:COG1137 71 PMHKRARLGIgylpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRR 144
|
170
....*....|....*....
gi 495112432 152 VAIARAIVGNPEIILADEP 170
Cdd:COG1137 145 VEIARALATNPKFILLDEP 163
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-220 |
2.89e-24 |
|
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: 95.23 E-value: 2.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 16 NEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTsvesmkdkelaafrnktLGFVFQSF 94
Cdd:cd03250 14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELE-KLSGSVSVPGS-----------------IAYVSQEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 95 HLINSlNVIDNVelpLLYRKMAaKERTrlaKEVLERVGLSHRMRHMP----TQ-------LSGGQCQRVAIARAIVGNPE 163
Cdd:cd03250 76 WIQNG-TIRENI---LFGKPFD-EERY---EKVIKACALEPDLEILPdgdlTEigekginLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 164 IILADEPTGNLDSKMGAEVME--LLHKLnkEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIFEncILGLL--LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-223 |
3.27e-24 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 96.02 E-value: 3.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMkdkELAAFR 83
Cdd:cd03252 1 ITFEHVRFRYKPDG--PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 nKTLGFVFQSFHLINSlNVIDNVELPllyRKMAAKERTrlaKEVLERVGLSHRMRHMP-----------TQLSGGQCQRV 152
Cdd:cd03252 76 -RQVGVVLQENVLFNR-SIRDNIALA---DPGMSMERV---IEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495112432 153 AIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNkeDGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-223 |
3.92e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 96.70 E-value: 3.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSG-----KIEINGTSVESMKDkeLAAFRNKtLGFVFQSFHLI 97
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRD--VLEFRRR-VGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 98 nSLNVIDNVELPLLYRKMAAKERTR-LAKEVLERVGL----SHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:PRK14271 114 -PMSIMDNVLAGVRAHKLVPRKEFRgVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495112432 173 NLDSKMGAEVMELLHKLnkEDGRTIVMVTHNEEQAKQTS-RTIRFFDGRQVQ 223
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISdRAALFFDGRLVE 242
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-223 |
7.43e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 98.76 E-value: 7.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 20 TLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdaPSSGKIEINGtsVEsMKDKELAAFRnKTLGFVFQSFHLIN 98
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKING--IE-LRELDPESWR-KHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 SlNVIDNVelpLLYRKMAAKERTRLA------KEVLERV--GLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:PRK11174 437 G-TLRDNV---LLGNPDASDEQLQQAlenawvSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495112432 171 TGNLDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:PRK11174 513 TASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQWDQIWVMQDGQIVQ 563
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-220 |
1.16e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.57 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRTNEiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvESMKDKELA 80
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQ-EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 AFRNKtLGFVFQsfhliNSLN------VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAI 154
Cdd:PRK13650 78 DIRHK-IGMVFQ-----NPDNqfvgatVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495112432 155 ARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQ 217
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-207 |
2.59e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.79 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLLdAPSSGKIEINGtsvESMKDKELAA 81
Cdd:COG4152 1 MLELKGLTKRFG----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIrIILGIL-APDSGEVLWDG---EPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 FrnktlGFvfqsfhlinslnvidnveLPL---LYRKM------------------AAKERtrlAKEVLERVGLSHRMRHM 140
Cdd:COG4152 73 I-----GY------------------LPEergLYPKMkvgeqlvylarlkglskaEAKRR---ADEWLERLGLGDRANKK 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 141 PTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSkMGAEVM-ELLHKLnKEDGRTIVMVTHNEEQA 207
Cdd:COG4152 127 VEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDP-VNVELLkDVIREL-AAKGTTVIFSSHQMELV 192
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-203 |
3.61e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 93.37 E-value: 3.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdaPSSGKIEINGTSVESMKDKELAAFR-----NKTLGFVFQSFHL 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLL--PGQGEILLNGRPLSDWSAAELARHRaylsqQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 97 InSLNvidnvelplLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIV-----GNPE--IILADE 169
Cdd:COG4138 90 L-ALH---------QPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDE 159
|
170 180 190
....*....|....*....|....*....|....
gi 495112432 170 PTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHN 203
Cdd:COG4138 160 PMNSLDVAQQAALDRLLREL-CQQGITVVMSSHD 192
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-221 |
3.99e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.56 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTL---LNIMGLLDAPS--SGKIEINGTSVESMKdKE 78
Cdd:PRK14258 8 IKVNNLSFYYDTQKI----LEGVSMEIYQSKVTAIIGPSGCGKSTFlkcLNRMNELESEVrvEGRVEFFNQNIYERR-VN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 79 LAAFRnKTLGFVFQSFHLInSLNVIDNVELPLLYRKMAAK-ERTRLAKEVLERVGL----SHRMRHMPTQLSGGQCQRVA 153
Cdd:PRK14258 83 LNRLR-RQVSMVHPKPNLF-PMSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 154 IARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQ 221
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-223 |
4.20e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.52 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRTneieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVesmkdkela 80
Cdd:PRK11288 2 SPYLSFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 AFRNKTLGF------VFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEV---LERVGL----SHRMRHmptqLSGG 147
Cdd:PRK11288 69 RFASTTAALaagvaiIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAreqLEHLGVdidpDTPLKY----LSIG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 148 QCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRFF-DGRQVQ 223
Cdd:PRK11288 145 QRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFkDGRYVA 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-206 |
4.66e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 94.53 E-value: 4.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEI----------NGTSVESMKDKELAAFRN--KT 86
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELITNPYSKKIKNFKElrRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 87 LGFVFQ--SFHLINslnviDNVELPLLYRKMA---AKERTR-LAKEVLERVGLSHR-MRHMPTQLSGGQCQRVAIARAIV 159
Cdd:PRK13631 118 VSMVFQfpEYQLFK-----DTIEKDIMFGPVAlgvKKSEAKkLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLhKLNKEDGRTIVMVTHNEEQ 206
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHTMEH 238
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-203 |
9.76e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 93.61 E-value: 9.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNE-----------------IETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKI 64
Cdd:COG4586 1 IIEVENLSKTYRVYEkepglkgalkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtGIL-VPTSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 65 EINGTsVESMKDKELAafrnKTLGFVF-QSFHLINSLNVIDNVELpllYRKM----AAKERTRLaKEVLERVGLSHRMrH 139
Cdd:COG4586 80 RVLGY-VPFKRRKEFA----RRIGVVFgQRSQLWWDLPAIDSFRL---LKAIyripDAEYKKRL-DELVELLDLGELL-D 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 140 MPT-QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:COG4586 150 TPVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHD 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
22-202 |
2.15e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.53 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTL-----GFVFQsfHL 96
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRRLlrtewGFVHQ--HP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 97 INSL--------NVIDnvelpllyRKMAAKER-----TRLAKEVLERVGL-SHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:PRK11701 99 RDGLrmqvsaggNIGE--------RLMAVGARhygdiRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARNLVTHP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:PRK11701 171 RLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTH 210
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-214 |
2.53e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 92.66 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 15 TNEIET-----LALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDAP---SSGKIEINGTSVESMKDKELAAFRNK 85
Cdd:COG4170 10 TIEIDTpqgrvKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKDNwhvTADRFRWNGIDLLKLSPRERRKIIGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 86 TLGFVFQsfHLINSLN-----------VIDNVEL--PLLYRKMAAKERtrlAKEVLERVGL-SHR--MRHMPTQLSGGQC 149
Cdd:COG4170 90 EIAMIFQ--EPSSCLDpsakigdqlieAIPSWTFkgKWWQRFKWRKKR---AIELLHRVGIkDHKdiMNSYPHELTEGEC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 150 QRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTI 214
Cdd:COG4170 165 QKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTI 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-223 |
2.72e-22 |
|
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: 94.40 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEIEtlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVEsmkDKELAAFR 83
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRP--ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA---DYTLASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 NKtLGFVFQSFHLINSlNVIDNVElpllYRKMAAKERTRL--------AKEVLERV--GLSHRMRHMPTQLSGGQCQRVA 153
Cdd:TIGR02203 406 RQ-VALVSQDVVLFND-TIANNIA----YGRTEQADRAEIeralaaayAQDFVDKLplGLDTPIGENGVLLSGGQRQRLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 154 IARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
38-203 |
3.36e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 92.63 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 38 IMGPSGCGKSTLLNIMGLLDAPSSGKIEING-TSVESMKDKELAAFRNKtLGFVFQSFHLINSLNVIDNvelpLLYrKMA 116
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrVLFDAEKGICLPPEKRR-IGYVFQDARLFPHYKVRGN----LRY-GMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 117 AKERTRLAKeVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRT 196
Cdd:PRK11144 103 KSMVAQFDK-IVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIP 181
|
....*..
gi 495112432 197 IVMVTHN 203
Cdd:PRK11144 182 ILYVSHS 188
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
23-202 |
3.90e-22 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 93.66 E-value: 3.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTSVESMKDKELAAFrnktLGFVFQSFHL----- 96
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVW-PPTAGSVRLDGADLSQWDREELGRH----IGYLPQDVELfdgti 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 97 ---------INSLNVIDnvelpllyrkmAAKertrlakevleRVGLsHRM-RHMP-----------TQLSGGQCQRVAIA 155
Cdd:COG4618 423 aeniarfgdADPEKVVA-----------AAK-----------LAGV-HEMiLRLPdgydtrigeggARLSGGQRQRIGLA 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495112432 156 RAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITH 525
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-203 |
7.09e-22 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 92.94 E-value: 7.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIETL-ALENVNLDVIKGEFVSIMGPSGCGKSTLLNI-MGLLDaPSSGKIEIN-GTSVESMKDK-- 77
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIiAGVLE-PTSGEVNVRvGDEWVDMTKPgp 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 78 ELAAFRNKTLGFVFQSFHLINSLNVIDN------VELPLLYRKMAAKERTRL-------AKEVLERvglshrmrhMPTQL 144
Cdd:TIGR03269 358 DGRGRAKRYIGILHQEYDLYPHRTVLDNlteaigLELPDELARMKAVITLKMvgfdeekAEEILDK---------YPDEL 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 145 SGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHD 487
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-206 |
1.71e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.07 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVES--MKDKELAAFRnKTLGFVFQ--SF 94
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEVKRLR-KEIGLVFQfpEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 95 HLINSlNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHR-MRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGN 173
Cdd:PRK13645 102 QLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190
....*....|....*....|....*....|...
gi 495112432 174 LDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQ 206
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQ 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-202 |
2.46e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.38 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMkDKELAAfrNKTLGFVFQSFHLINSLN 101
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL-DHKLAA--QLGIGIIYQELSVIDELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVEL-PLLYRKMAA------KERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:PRK09700 97 VLENLYIgRHLTKKVCGvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180
....*....|....*....|....*...
gi 495112432 175 DSKMGAEVMELLHKLNKEdGRTIVMVTH 202
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKE-GTAIVYISH 203
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-203 |
2.62e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.09 E-value: 2.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELa 80
Cdd:PRK13652 1 MHLIETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 afrNKTLGFVFQ-SFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIV 159
Cdd:PRK13652 77 ---RKFVGLVFQnPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQ 197
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-207 |
4.43e-21 |
|
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: 91.23 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESmkdkELAAFRnKTLGFVFQSFHLINSLN 101
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVR-QSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVelpLLYRKMAAK--ERTRLAKE-VLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKM 178
Cdd:TIGR01257 1020 VAEHI---LFYAQLKGRswEEAQLEMEaMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180
....*....|....*....|....*....
gi 495112432 179 GAEVMELLhkLNKEDGRTIVMVTHNEEQA 207
Cdd:TIGR01257 1097 RRSIWDLL--LKYRSGRTIIMSTHHMDEA 1123
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
19-207 |
5.09e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.90 E-value: 5.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAafrnKTLGFVFQSFHLIN 98
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS----RRVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 SLNVIDNVEL---PLLYRKMAAKERTRLA-KEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:PRK09536 91 EFDVRQVVEMgrtPHRSRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190
....*....|....*....|....*....|...
gi 495112432 175 DSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQA 207
Cdd:PRK09536 171 DINHQVRTLELVRRL-VDDGKTAVAAIHDLDLA 202
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-203 |
6.77e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.26 E-value: 6.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELA 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRV----VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 afrNKTLGFVFQSFHLINSLNVIDNVELPLLYRK-MAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIV 159
Cdd:PRK10895 77 ---RRGIGYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHN 203
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHN 196
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-220 |
7.14e-21 |
|
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: 86.82 E-value: 7.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNE------------------IETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIE 65
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 66 INGTSVESMkdkELAAFrnktlgfvfqsFHliNSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMrHMPT-QL 144
Cdd:cd03220 81 VRGRVSSLL---GLGGG-----------FN--PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFI-DLPVkTY 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 145 SGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQT-SRTIRFFDGR 220
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLcDRALVLEKGK 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-223 |
7.90e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.06 E-value: 7.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MA-MIKLTGINKIYRTNEI------------------ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSS 61
Cdd:COG1134 1 MSsMIEVENVSKSYRLYHEpsrslkelllrrrrtrreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 62 GKIEINGtSVESMkdkeLAafrnktLGFVFQsfhliNSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMrHMP 141
Cdd:COG1134 81 GRVEVNG-RVSAL----LE------LGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFI-DQP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 142 TQ-LSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQT-SRTIRFFDG 219
Cdd:COG1134 144 VKtYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLcDRAIWLEKG 222
|
....
gi 495112432 220 RQVQ 223
Cdd:COG1134 223 RLVM 226
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
25-223 |
1.17e-20 |
|
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: 86.81 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 25 NVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEI---NGTSVE--SMKDKELAAFRNKTLGFVFQsfHLINS 99
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAELElyQLSEAERRRLMRTEWGFVHQ--NPRDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 100 LNVIDNVELPLLYRKMAAKER-----TRLAKEVLERVGLS-HRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGN 173
Cdd:TIGR02323 99 LRMRVSAGANIGERLMAIGARhygniRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495112432 174 LDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGRQVQ 223
Cdd:TIGR02323 179 LDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAqRLLVMQQGRVVE 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-223 |
1.42e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 89.25 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkeLAAFRnKTLGFVFQSFHLINSlN 101
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLR-RNIAVVFQDAGLFNR-S 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPllyRKMAAKERTRLAKEV------LER--VGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGN 173
Cdd:PRK13657 425 IEDNIRVG---RPDATDEEMRAAAERaqahdfIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495112432 174 LDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:PRK13657 502 LDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
23-214 |
3.94e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 85.91 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvESMKDKELAAFRNKtLGFVFQS-FHLINSLN 101
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNLRRK-IGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAE 181
Cdd:PRK13642 99 VEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190
....*....|....*....|....*....|...
gi 495112432 182 VMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTI 214
Cdd:PRK13642 179 IMRVIHEIKEKYQLTVLSITHDLDEAASSDRIL 211
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
23-202 |
5.49e-20 |
|
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: 87.79 E-value: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMkDKElaaFRNKTLGFVFQSFHLI----- 97
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQW-DRE---TFGKHIGYLPQDVELFpgtva 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 98 -NSLNVIDNVElpllYRKMAAKERTRLAKEVLERV--GLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:TIGR01842 410 eNIARFGENAD----PEKIIEAAKLAGVHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
|
170 180
....*....|....*....|....*...
gi 495112432 175 DSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:TIGR01842 486 DEEGEQALANAIKAL-KARGITVVVITH 512
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-201 |
1.30e-19 |
|
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: 82.48 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLlDAPSSGKIEINGtsvESMKDKELAAFRNKTLGFVFQSFH---LI 97
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEaLFGL-RPPASGEITLDG---KPVTRRSPRDAIRAGIAYVPEDRKregLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 98 NSLNVIDNVELPLLyrkmaakertrlakevlervglshrmrhmptqLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSK 177
Cdd:cd03215 91 LDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180
....*....|....*....|....
gi 495112432 178 MGAEVMELLHKLnKEDGRTIVMVT 201
Cdd:cd03215 139 AKAEIYRLIREL-ADAGKAVLLIS 161
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-210 |
2.55e-19 |
|
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: 82.02 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVEsmkdkELAAFRNKTLGFVFQSFHLIN 98
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 SLNVIDNVELpllYRKMAAKERtRLAKEVLERVGLSHRmRHMPT-QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDsK 177
Cdd:TIGR01189 87 ELSALENLHF---WAAIHGGAQ-RTIEDALAAVGLTGF-EDLPAaQLSAGQQRRLALARLWLSRRPLWILDEPTTALD-K 160
|
170 180 190
....*....|....*....|....*....|...
gi 495112432 178 MGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQT 210
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTHQDLGLVEA 193
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-202 |
3.08e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 83.06 E-value: 3.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdaPSSGKIEINGTSVESMKDKELAAFR-----NKTLGF---VFQ- 92
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMaGLL--PGSGSIQFAGQPLEAWSAAELARHRaylsqQQTPPFampVFQy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 93 -SFHLiNSLNVIDNVELPLlyrkmaakertrlaKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAI-----VGNPE--I 164
Cdd:PRK03695 90 lTLHQ-PDKTRTEAVASAL--------------NEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqL 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 495112432 165 ILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSH 191
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-202 |
3.56e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 85.46 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVesmKDKELAAFRNKtLGFVFQSFHLIN 98
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASLRNQ-VALVSQNVHLFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 slnviDNVELPLLYrkmAAKER-TRlaKEVLERVGLSHRM---RHMP-----------TQLSGGQCQRVAIARAIVGNPE 163
Cdd:PRK11176 431 -----DTIANNIAY---ARTEQySR--EQIEEAARMAYAMdfiNKMDngldtvigengVLLSGGQRQRIAIARALLRDSP 500
|
170 180 190
....*....|....*....|....*....|....*....
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEdgRTIVMVTH 202
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKN--RTSLVIAH 537
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-205 |
4.28e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.93 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 16 NEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMG-LLDAPSSGKIEIngtsvesmkdKELAAFRNKTLgfvfqs 93
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRlLAGaLKGTPVAGCVDV----------PDNQFGREASL------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 94 fhlinslnvIDNVelpllYRKMAAKErtrlAKEVLERVGLSHR--MRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:COG2401 103 ---------IDAI-----GRKGDFKD----AVELLNAVGLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|....
gi 495112432 172 GNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEE 205
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-204 |
4.69e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFrnktLGfvfqsfH--- 95
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY----LG------Hrna 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 96 LINSLNVIDNVElplLYRKMAAKERTRLAkEVLERVGLSHrMRHMPTQ-LSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:PRK13539 84 MKPALTVAENLE---FWAAFLGGEELDIA-AALEAVGLAP-LAHLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|...
gi 495112432 175 DS---KMGAEVMEllHKLNKedGRTIVMVTHNE 204
Cdd:PRK13539 159 DAaavALFAELIR--AHLAQ--GGIVIAATHIP 187
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-209 |
6.85e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.93 E-value: 6.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 2 AMIKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMkdkelAA 81
Cdd:PRK13537 6 APIDFRNVEKRYG----DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR-----AR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 FRNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGN 161
Cdd:PRK13537 77 HARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495112432 162 PEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQ 209
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAER 203
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-209 |
9.42e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.96 E-value: 9.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMkdkelAAFR 83
Cdd:PRK13536 42 IDLAGVSKSYGDKAV----VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR-----ARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 NKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQ 209
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAER 237
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-203 |
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 495112432 3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKS-TLLNIMGLLDApSSGKIEING----------TSV 71
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKmllrrrsrqvIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 72 ESMKDKELAAFRNKTLGFVFQsfHLINSLNVIDNV-----ELPLLYRKMAAKERTRLAKEVLERVGL--SHRM-RHMPTQ 143
Cdd:PRK10261 91 SEQSAAQMRHVRGADMAMIFQ--EPMTSLNPVFTVgeqiaESIRLHQGASREEAMVEAKRMLDQVRIpeAQTIlSRYPHQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 144 LSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHD 228
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-203 |
1.32e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.85 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDApSSGKIEINGTSVESmkdkelaAFRNKTLGFVFQSFHLINSL 100
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKaLMGFVRL-ASGKISILGQPTRQ-------ALQKNLVAYVPQSEEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NV-IDNVELPLLYRKMA----AKERTR-LAKEVLERVG-LSHRMRHMpTQLSGGQCQRVAIARAIVGNPEIILADEPTGN 173
Cdd:PRK15056 94 PVlVEDVVMMGRYGHMGwlrrAKKRDRqIVTAALARVDmVEFRHRQI-GELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190
....*....|....*....|....*....|
gi 495112432 174 LDSKMGAEVMELLHKLnKEDGRTIVMVTHN 203
Cdd:PRK15056 173 VDVKTEARIISLLREL-RDEGKTMLVSTHN 201
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-204 |
1.50e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 83.64 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDApSSGKIEINGTSVESmkdKELAAFRNktLGFVFQSFHLINSL 100
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLtGLLPA-SEGEAWLFGQPVDA---GDIATRRR--VGYMSQAFSLYGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVEL-PLLYRkMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSkmG 179
Cdd:NF033858 355 TVRQNLELhARLFH-LPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP--V 431
|
170 180
....*....|....*....|....*....
gi 495112432 180 AEVM--ELLHKLNKEDGRTIVMVTH--NE 204
Cdd:NF033858 432 ARDMfwRLLIELSREDGVTIFISTHfmNE 460
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
23-203 |
2.50e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.54 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEingtsvesmKDKELaafrnkTLGFVFQSFHLinslnv 102
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKL------RIGYVPQKLYL------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 103 idNVELPL-LYRKMAAKERTRLAK--EVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMG 179
Cdd:PRK09544 79 --DTTLPLtVNRFLRLRPGTKKEDilPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|....
gi 495112432 180 AEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK09544 157 VALYDLIDQLRRELDCAVLMVSHD 180
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
22-223 |
2.74e-18 |
|
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: 82.87 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNktlgFVFQSfHLINSLN 101
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFIN----YLPQE-PYIFSGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNvelpLLyrkMAAKERTRLAK--EVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILAD 168
Cdd:TIGR01193 564 ILEN----LL---LGAKENVSQDEiwAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILD 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 169 EPTGNLDSKMGAEVMELLHKLNKedgRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNNLLNLQD---KTIIFVAHRLSVAKQSDKIIVLDHGKIIE 688
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-202 |
3.46e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEInGTSVEsmkdkelaa 81
Cdd:COG0488 315 VLELEGLSKSYGDKTL----LDDLSLRIDRGDRIGLIGPNGAGKSTLLKlLAGEL-EPDSGTVKL-GETVK--------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 frnktLGFVFQSFHLIN-SLNVIDNVelpllyRKMAAKERTRLAKEVLERVGLSHRMRHMPT-QLSGGQCQRVAIARAIV 159
Cdd:COG0488 380 -----IGYFDQHQEELDpDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFSGDDAFKPVgVLSGGEKARLALAKLLL 448
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495112432 160 GNPEIILADEPTGNLD--SKmgaEVMELLhkLNKEDGrTIVMVTH 202
Cdd:COG0488 449 SPPNVLLLDEPTNHLDieTL---EALEEA--LDDFPG-TVLLVSH 487
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-211 |
3.90e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.22 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkelAAFRNKTLGFVFQSFHliNSLN 101
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD----YSYRSQRIRMIFQDPS--TSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 ----VIDNVELPL-LYRKMAAKERTRLAKEVLERVGL-SHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLD 175
Cdd:PRK15112 102 prqrISQILDFPLrLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 495112432 176 SKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS 211
Cdd:PRK15112 182 MSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHIS 217
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-203 |
6.32e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 79.74 E-value: 6.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 17 EIETLALE-------NVNLDVIKGEFVSIMGPSGCGKS-TLLNIMGLLDA---PSSGKIEINGTSVEsmkdkeLAAFRNK 85
Cdd:PRK10418 6 ELRNIALQaaqplvhGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGRVLLDGKPVA------PCALRGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 86 TLGFVFQ----SFhliNSL-NVIDNVELPLLYRKMAAKERTRLAkeVLERVGLSHRMRHM---PTQLSGGQCQRVAIARA 157
Cdd:PRK10418 80 KIATIMQnprsAF---NPLhTMHTHARETCLALGKPADDATLTA--ALEAVGLENAARVLklyPFEMSGGMLQRMMIALA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495112432 158 IVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHD 200
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-202 |
8.86e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 81.31 E-value: 8.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELaafrNKTLGFVFQSFHLINSlNV 102
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQEPVLFSG-SV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 103 IDNVELPLLYRKMAakERTRLAKEVlervGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:TIGR00958 572 RENIAYGLTDTPDE--EIMAAAKAA----NAHDFIMEFPngydtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190
....*....|....*....|....*....|.
gi 495112432 172 GNLDskmgAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:TIGR00958 646 SALD----AECEQLLQESRSRASRTVLLIAH 672
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-203 |
2.49e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.13 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLdAPSSGKIEINGTSVESMKdKELAAFRNKtLGFVFQS-FHLINSL 100
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLL-RPQKGAVLWQGKPLDYSK-RGLLALRQQ-VATVFQDpEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHrMRHMPTQ-LSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMG 179
Cdd:PRK13638 94 DIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQH-FRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180
....*....|....*....|....
gi 495112432 180 AEVMELLHKLNKEdGRTIVMVTHN 203
Cdd:PRK13638 173 TQMIAIIRRIVAQ-GNHVIISSHD 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-201 |
2.56e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.68 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLlDAPSSGKIEINGTSVE--SMKDkelaAFRN---------KTLGf 89
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARaLFGA-DPADSGEIRLDGKPVRirSPRD----AIRAgiayvpedrKGEG- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 90 vfqsfhLINSLNVIDNVELPLLyRKMA-------AKERtRLAKEVLERVGLSHRMRHMPTQ-LSGGQCQRVAIARAIVGN 161
Cdd:COG1129 341 ------LVLDLSIRENITLASL-DRLSrgglldrRRER-ALAEEYIKRLRIKTPSPEQPVGnLSGGNQQKVVLAKWLATD 412
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495112432 162 PEIILADEPTGNLD--SKmgAEVMELLHKLNKEdGRTIVMVT 201
Cdd:COG1129 413 PKVLILDEPTRGIDvgAK--AEIYRLIRELAAE-GKAVIVIS 451
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-218 |
3.80e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.54 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 33 GEFVSIMGPSGCGKSTLLN-IMGLLDAPS-SGKIEINgtsvesmkDKELAAFRNKTLGFVFQSFHLINSLNVIDN---VE 107
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNaLAGRIQGNNfTGTILAN--------NRKPTKQILKRTGFVTQDDILYPHLTVRETlvfCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 108 LPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQ-----LSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEV 182
Cdd:PLN03211 166 LLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180 190
....*....|....*....|....*....|....*.
gi 495112432 183 MELLHKLNKEdGRTIVMVTHneeqaKQTSRTIRFFD 218
Cdd:PLN03211 246 VLTLGSLAQK-GKTIVTSMH-----QPSSRVYQMFD 275
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
33-203 |
4.45e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.52 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 33 GEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAafrnKTLGFVFQSFHLINSLNVidnVELPLLY 112
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGMTV---RELVAIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 113 R--------KMAAKERTRLaKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVME 184
Cdd:PRK10575 110 RypwhgalgRFGAADREKV-EEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLA 188
|
170
....*....|....*....
gi 495112432 185 LLHKLNKEDGRTIVMVTHN 203
Cdd:PRK10575 189 LVHRLSQERGLTVIAVLHD 207
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-215 |
7.71e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.70 E-value: 7.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDApSSGKIEINgtsvesmKDKELAafrnktlgFVFQSFHLIN-SL 100
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRaIAGLWPY-GSGRIARP-------AGARVL--------FLPQRPYLPLgTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 nvIDNVELPLLYRKMAAKErtrlAKEVLERVGLSHRMRHMPTQ------LSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:COG4178 443 --REALLYPATAEAFSDAE----LREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495112432 175 DSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIR 215
Cdd:COG4178 517 DEENEAALYQLLREELP--GTTVISVGHRSTLAAFHDRVLE 555
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-204 |
9.38e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 76.26 E-value: 9.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLD-APSSGKIEINGTSVESMKDKELAafrNKTLGFVFQ-------- 92
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKvLMGHPKyEVTSGSILLDGEDILELSPDERA---RAGIFLAFQypveipgv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 93 --SFHLINSLNVIDNVELPllyrkmaAKERTRLAKEVLERVGLSHRM--RHMPTQLSGGQCQRVAIARAIVGNPEIILAD 168
Cdd:COG0396 93 svSNFLRTALNARRGEELS-------AREFLKLLKEKMKELGLDEDFldRYVNEGFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495112432 169 EPtgnlDS-------KMGAEVMELLHklnkEDGRTIVMVTHNE 204
Cdd:COG0396 166 ET----DSgldidalRIVAEGVNKLR----SPDRGILIITHYQ 200
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-215 |
1.01e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.23 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 24 ENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDaPSSGKIEINGTSVESMKDkelaAFRNKTL--GfvfqsfHL--IN 98
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILaGLAR-PDAGEVLWQGEPIRRQRD----EYHQDLLylG------HQpgIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 S-LNVIDNVelpLLYRKMAAKERTRLAKEVLERVGLSHRMrHMPT-QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDs 176
Cdd:PRK13538 87 TeLTALENL---RFYQRLHGPGDDEALWEALAQVGLAGFE-DVPVrQLSAGQQRRVALARLWLTRAPLWILDEPFTAID- 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495112432 177 KMGAEVMELLHKLNKEDGRTIVMVTHNE-EQAKQTSRTIR 215
Cdd:PRK13538 162 KQGVARLEALLAQHAEQGGMVILTTHQDlPVASDKVRKLR 201
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-219 |
2.47e-16 |
|
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: 74.67 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLLDApSSGKIEINGTSVESMKDKELAAFRNKTLGFVFQSFHLINSln 101
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 vidNVELPLLYRKMAAKERTrlaKEVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:cd03290 94 ---TVEENITFGSPFNKQRY---KAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495112432 171 TGNLDSKMGAEVM-ELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:cd03290 168 FSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
120-203 |
2.57e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 75.99 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 120 RTRLAKEVLERVGL-SHR--MRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRT 196
Cdd:PRK15093 132 RKRRAIELLHRVGIkDHKdaMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTT 211
|
....*..
gi 495112432 197 IVMVTHN 203
Cdd:PRK15093 212 ILLISHD 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-202 |
2.87e-16 |
|
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: 76.90 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 8 GINKIYRTN-EIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGkieingtsvesmkdkELAAFRNKT 86
Cdd:TIGR03719 9 RVSKVVPPKkEI----LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG---------------EARPQPGIK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 87 LGFVFQSFHLINSLNVIDNVELPL------------LYRKMA---------AKERTRLaKEVLERVG---LSHRM----- 137
Cdd:TIGR03719 70 VGYLPQEPQLDPTKTVRENVEEGVaeikdaldrfneISAKYAepdadfdklAAEQAEL-QEIIDAADawdLDSQLeiamd 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495112432 138 --RHMP-----TQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDskmgAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:TIGR03719 149 alRCPPwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTH 216
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-221 |
5.60e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 71.71 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMglldapsSGKIEINGTSVESMKDKELAAFr 83
Cdd:cd03221 1 IELENLSKTYGGKLL----LKDISLTINPGDRIGLVGRNGAGKSTLLKLI-------AGELEPDEGIVTWGSTVKIGYF- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 nktlgfvfqsfhlinslnvidnvelpllyrkmaakertrlakevlervglshrmrhmpTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03221 69 ----------------------------------------------------------EQLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNkedgRTIVMVTHNEEQAKQTSRTIRFFDGRQ 221
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEYP----GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-202 |
5.98e-16 |
|
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: 73.66 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 13 YRTNEiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELaafrNKTLGFVFQ 92
Cdd:cd03248 21 YPTRP-DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL----HSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 93 SFHLInSLNVIDNVELPL----LYRKMAAKER-------TRLAKEVLERVGlshrmrHMPTQLSGGQCQRVAIARAIVGN 161
Cdd:cd03248 96 EPVLF-ARSLQDNIAYGLqscsFECVKEAAQKahahsfiSELASGYDTEVG------EKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495112432 162 PEIILADEPTGNLDSKMGAEVMELLHKLNKEdgRTIVMVTH 202
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAH 207
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
13-202 |
2.28e-15 |
|
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: 72.14 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 13 YRTNEieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELaafRNKtLGFVF 91
Cdd:cd03244 12 YRPNL--PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLaLFRLVE-LSSGSILIDGVDISKIGLHDL---RSR-ISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 92 QSFHL--------INSLNVIDNVELpllyrkMAAKERTRLAKEVLE-RVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:cd03244 85 QDPVLfsgtirsnLDPFGEYSDEEL------WQALERVGLKEFVESlPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495112432 163 EIILADEPTGNLDSkmgaEVMELLHKLNKE--DGRTIVMVTH 202
Cdd:cd03244 159 KILVLDEATASVDP----ETDALIQKTIREafKDCTVLTIAH 196
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-202 |
2.36e-15 |
|
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: 74.09 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDaPSSGKIEINGTSVesmKDKELAAFRnKTLGFVFQSFHLINsln 101
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfRFYD-VTSGRILIDGQDI---RDVTQASLR-AAIGIVPQDTVLFN--- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 viDNVELPLLYRKMAAKER-----TRLAK--------------EVLERvGLshrmrhmptQLSGGQCQRVAIARAIVGNP 162
Cdd:COG5265 446 --DTIAYNIAYGRPDASEEeveaaARAAQihdfieslpdgydtRVGER-GL---------KLSGGEKQRVAIARTLLKNP 513
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTH 202
Cdd:COG5265 514 PILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAH 551
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-202 |
2.68e-15 |
|
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: 71.37 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDkELAafrnKTLGFVFQSFHLINSLNV 102
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIA----RGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 103 IDNVelpllyRKMAAKERTRLAKEVLERVGLSHrMRHMPT-QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAE 181
Cdd:cd03231 91 LENL------RFWHADHSDEQVEEALARVGLNG-FEDRPVaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|.
gi 495112432 182 VMELLHKlNKEDGRTIVMVTH 202
Cdd:cd03231 164 FAEAMAG-HCARGGMVVLTTH 183
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-202 |
7.14e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 7.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 2 AMIKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSV--ESMKDKEL 79
Cdd:PRK10762 3 ALLQLKGIDKAFPGVK----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfNGPKSSQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 80 AAfrnktLGFVFQSFHLINSLNVIDNVEL---------PLLYRKMAAKertrlAKEVLERVGLSHRMRHMPTQLSGGQCQ 150
Cdd:PRK10762 79 AG-----IGIIHQELNLIPQLTIAENIFLgrefvnrfgRIDWKKMYAE-----ADKLLARLNLRFSSDKLVGELSIGEQQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495112432 151 RVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISH 199
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-202 |
1.41e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.37 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 24 ENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTsvESMKDKELAAFRNKtLGFVFQ----------- 92
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS--HNLKDINLKWWRSK-IGVVSQdpllfsnsikn 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 93 ----SFHLINSLNVIDN------------------------VELPLLYRKMAAKERTRLAKE-----------VLERVGL 133
Cdd:PTZ00265 479 nikySLYSLKDLEALSNyynedgndsqenknkrnscrakcaGDLNDMSNTTDSNELIEMRKNyqtikdsevvdVSKKVLI 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 134 SHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:PTZ00265 559 HDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-216 |
1.78e-14 |
|
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: 68.33 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEIngtsvesmkdkelaAFRNKTLgFVFQsfhlinslnv 102
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--------------PEGEDLL-FLPQ---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 103 idnveLPLLYRkmaakerTRLaKEVL----ERVglshrmrhmptqLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKM 178
Cdd:cd03223 72 -----RPYLPL-------GTL-REQLiypwDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180 190
....*....|....*....|....*....|....*...
gi 495112432 179 GAEVMELLhklnKEDGRTIVMVTHNEEQAKQTSRTIRF 216
Cdd:cd03223 127 EDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDL 160
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-214 |
2.12e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.30 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKElaAFRNKtLGFVFQSFHLINSLN 101
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALENG-ISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVEL---PLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKM 178
Cdd:PRK10982 90 VMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 495112432 179 GAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTI 214
Cdd:PRK10982 170 VNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEI 204
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-218 |
2.27e-14 |
|
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: 71.37 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 26 VNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVEsmkDKELAAFRNKtlgF--VFQSFHLINSLNVI 103
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAYRQL---FsaVFSDFHLFDRLLGL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 104 DNVELPllyrkmaakertRLAKEVLERVGLSHRMRHM-----PTQLSGGQCQRVAIARAIVGNPEIILADE------P-- 170
Cdd:COG4615 425 DGEADP------------ARARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLALLVALLEDRPILVFDEwaadqdPef 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495112432 171 -----TgnldskmgaevmELLHKLnKEDGRTIVMVTHNEeqakqtsrtiRFFD 218
Cdd:COG4615 493 rrvfyT------------ELLPEL-KARGKTVIAISHDD----------RYFD 522
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-205 |
2.86e-14 |
|
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: 68.71 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLD-APSSGKIEINGTSVESMKDKELAafrNKTLGFVFQSfhlinsl 100
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKtIMGHPKyEVTEGEILFKGEDITDLPPEERA---RLGIFLAFQY------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 nvidNVELPllyrkmaakertrlakevleRVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGA 180
Cdd:cd03217 86 ----PPEIP--------------------GVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180
....*....|....*....|....*
gi 495112432 181 EVMELLHKLnKEDGRTIVMVTHNEE 205
Cdd:cd03217 142 LVAEVINKL-REEGKSVLIITHYQR 165
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
23-218 |
3.94e-14 |
|
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: 68.04 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNI------MGLLdapsSGKIEINGtsveSMKDKELAafrnKTLGFVFQSFHL 96
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVlagrktAGVI----TGEILING----RPLDKNFQ----RSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 97 INSLNVIDNVELPLLYRkmaakertrlakevlervGLSHRMRhmptqlsggqcQRVAIARAIVGNPEIILADEPTGNLDS 176
Cdd:cd03232 91 SPNLTVREALRFSALLR------------------GLSVEQR-----------KRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495112432 177 KMGAEVMELLHKLnKEDGRTIVMVTHneeqakQTSRTI-RFFD 218
Cdd:cd03232 142 QAAYNIVRFLKKL-ADSGQAILCTIH------QPSASIfEKFD 177
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-207 |
4.38e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.75 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 1 MAMIKLTGINKIYrtNEIEtlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVesmKDKELA 80
Cdd:PRK11614 3 KVMLSFDKVSAHY--GKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI---TDWQTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 AFRNKTLGFVFQSFHLINSLNVIDNVELPLLY-RKMAAKERTRLAKEVLERvgLSHRMRHMPTQLSGGQCQRVAIARAIV 159
Cdd:PRK11614 76 KIMREAVAIVPEGRRVFSRMTVEENLAMGGFFaERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQA 207
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQA 200
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
13-202 |
1.63e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.98 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 13 YRTNEietLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKEL------------ 79
Cdd:PRK10790 350 YRDDN---LVLQNINLSVPSRGFVALVGHTGSGKSTLASlLMGYY-PLTEGEIRLDGRPLSSLSHSVLrqgvamvqqdpv 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 80 ----AAFRNKTLGFVFQSFHLinsLNVIDNVELPLLYRKMAAKERTRLAKEvlervglshrmrhmPTQLSGGQCQRVAIA 155
Cdd:PRK10790 426 vladTFLANVTLGRDISEEQV---WQALETVQLAELARSLPDGLYTPLGEQ--------------GNNLSVGQKQLLALA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495112432 156 RAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDgrTIVMVTH 202
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAH 533
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
23-205 |
2.42e-13 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 66.90 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDAP-SSGKIEINGTSVESMKDKELAAfrnKTLGFVFQSFHLINSL 100
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKtIAGHPSYEvTSGTILFKGQDLLELEPDERAR---AGLFLAFQYPEEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVELPLLYRKMAAKERT-------RLAKEVLERVGLSHRM--RHMPTQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:TIGR01978 93 SNLEFLRSALNARRSARGEEPldlldfeKLLKEKLALLDMDEEFlnRSVNEGFSGGEKKRNEILQMALLEPKLAILDEID 172
|
170 180 190
....*....|....*....|....*....|....
gi 495112432 172 GNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEE 205
Cdd:TIGR01978 173 SGLDIDALKIVAEGINRL-REPDRSFLIITHYQR 205
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-175 |
3.10e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.73 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGllDAPSS--------GKIEINGTSVESMKdkelaafrnKTLGFVFQS 93
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSlITG--DHPQGysndltlfGRRRGSGETIWDIK---------KHIGYVSSS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 94 FHL-----INSLNVI-----DNVELpllYRKMAAKERtRLAKEVLERVGLSHRMRHMPTQ-LSGGQcQRVA-IARAIVGN 161
Cdd:PRK10938 345 LHLdyrvsTSVRNVIlsgffDSIGI---YQAVSDRQQ-KLAQQWLDILGIDKRTADAPFHsLSWGQ-QRLAlIVRALVKH 419
|
170
....*....|....
gi 495112432 162 PEIILADEPTGNLD 175
Cdd:PRK10938 420 PTLLILDEPLQGLD 433
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-222 |
3.18e-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: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDAPS-SGKIEINGTSVE--SMKDKElaafrNKTLGFVFQSFHLI 97
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILsGVYPHGTwDGEIYWSGSPLKasNIRDTE-----RAGIVIIHQELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 98 NSLNVIDNV----ELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPT-QLSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:TIGR02633 91 PELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVgDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495112432 173 NLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRFF-DGRQV 222
Cdd:TIGR02633 171 SLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIrDGQHV 220
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
19-204 |
3.31e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.07 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVEsmkDKELAAFRnKTLGFVFQSFHLIN 98
Cdd:PRK10522 335 NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYR-KLFSAVFTDFHLFD 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 SLnvidnvelpLLYRKMAAKErtRLAKEVLERVGLSHRMRH-----MPTQLSGGQCQRVAIARAIVGNPEIILADEPTGN 173
Cdd:PRK10522 411 QL---------LGPEGKPANP--ALVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAAD 479
|
170 180 190
....*....|....*....|....*....|.
gi 495112432 174 LDSKMGAEVMELLHKLNKEDGRTIVMVTHNE 204
Cdd:PRK10522 480 QDPHFRREFYQVLLPLLQEMGKTIFAISHDD 510
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-202 |
3.31e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.84 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTginKIYRTN-EIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGkieingtsvesmkdkELAA 81
Cdd:PRK11819 9 MNRVS---KVVPPKkQI----LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG---------------EARP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 82 FRNKTLGFVFQSFHLINSLNVIDNVELPL------------LYRKMA---------AKERTRLaKEVLERVG---LSHRM 137
Cdd:PRK11819 67 APGIKVGYLPQEPQLDPEKTVRENVEEGVaevkaaldrfneIYAAYAepdadfdalAAEQGEL-QEIIDAADawdLDSQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 138 -RHM-----P------TQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDskmgAE-VMELLHKLNKEDGrTIVMVTH 202
Cdd:PRK11819 146 eIAMdalrcPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AEsVAWLEQFLHDYPG-TVVAVTH 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-222 |
3.40e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.65 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLlniMGLLDA--PS---SGKIEINGTSVE--SMKDKELAAfrnktLGFVFQSF 94
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTL---MKVLSGvyPHgtyEGEIIFEGEELQasNIRDTERAG-----IAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 95 HLINSLNVIDNVEL---PLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:PRK13549 92 ALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495112432 172 GNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRFF-DGRQV 222
Cdd:PRK13549 172 ASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIrDGRHI 222
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-208 |
4.55e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 67.61 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSvesmkdkelaafrnktlGFVFQSFHLINSLN 101
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-----------------ALIAISSGLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAE 181
Cdd:PRK13545 102 GIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180
....*....|....*....|....*..
gi 495112432 182 VMELLHKLnKEDGRTIVMVTHNEEQAK 208
Cdd:PRK13545 182 CLDKMNEF-KEQGKTIFFISHSLSQVK 207
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-203 |
4.69e-13 |
|
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: 66.24 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 33 GEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEING---TSVESMKDKEL----AAFRNKTLGFVF--QSFHLINslNVI 103
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdEILDEFRGSELqnyfTKLLEGDVKVIVkpQYVDLIP--KAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 104 DNVELPLLYRKmaaKERTRLaKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVM 183
Cdd:cd03236 104 KGKVGELLKKK---DERGKL-DELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170 180
....*....|....*....|
gi 495112432 184 ELLHKLNkEDGRTIVMVTHN 203
Cdd:cd03236 180 RLIRELA-EDDNYVLVVEHD 198
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-189 |
8.09e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.59 E-value: 8.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 15 TNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKdkeLAAFRNKTLGFVFQS 93
Cdd:COG3845 266 RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEaLAGLR-PPASGSIRLDGEDITGLS---PRERRRLGVAYIPED 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 94 FH---LINSLNVIDNVELPLLYRK-------MAAKERTRLAKEVLER-----VGLSHRMRhmptQLSGGQCQRVAIARAI 158
Cdd:COG3845 342 RLgrgLVPDMSVAENLILGRYRRPpfsrggfLDRKAIRAFAEELIEEfdvrtPGPDTPAR----SLSGGNQQKVILAREL 417
|
170 180 190
....*....|....*....|....*....|.
gi 495112432 159 VGNPEIILADEPTGNLDskMGAevMELLHKL 189
Cdd:COG3845 418 SRDPKLLIAAQPTRGLD--VGA--IEFIHQR 444
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-220 |
1.02e-12 |
|
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: 66.89 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDApSSGKIEINGTsvesmkdkelaafrnktLGFVFQSFHLINsln 101
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKGS-----------------VAYVPQQAWIQN--- 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 viDNVELPLLYRKMAAKERTRlakEVLERVGLSHRMRHMPT-----------QLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:TIGR00957 713 --DSLRENILFGKALNEKYYQ---QVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495112432 171 TGNLDSKMGAEVMEllHKLNKE---DGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:TIGR00957 788 LSAVDAHVGKHIFE--HVIGPEgvlKNKTRILVTHGISYLPQVDVIIVMSGGK 838
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-219 |
2.01e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.91 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDAPSSGKIEINGTsvesmkdkelaafrnktLGFVFQSFHLINSlN 101
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMlGELPPRSDASVVIRGT-----------------VAYVPQVSWIFNA-T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPLLYrkmaakERTRLAKeVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:PLN03130 695 VRDNILFGSPF------DPERYER-AIDVTALQHDLDLLPggdlteigergVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495112432 171 TGNLDSKMGAEVMEllhKLNKED--GRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:PLN03130 768 LSALDAHVGRQVFD---KCIKDElrGKTRVLVTNQLHFLSQVDRIILVHEG 815
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
22-202 |
2.30e-12 |
|
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: 63.59 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLDaPSSGKIEINGTSVESMKdkeLAAFRNKtLGFVFQ-----SFH 95
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLiLALFRFLE-AEEGKIEIDGIDISTIP---LEDLRSS-LTIIPQdptlfSGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 96 LINSLNVIDNVELPLLYRKMAAKERtrlakevlervGLShrmrhmptqLSGGQCQRVAIARAIVGNPEIILADEPTGNLD 175
Cdd:cd03369 98 IRSNLDPFDEYSDEEIYGALRVSEG-----------GLN---------LSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
170 180
....*....|....*....|....*..
gi 495112432 176 SKMGAEVMELLHKLNKedGRTIVMVTH 202
Cdd:cd03369 158 YATDALIQKTIREEFT--NSTILTIAH 182
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-219 |
7.24e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 62.91 E-value: 7.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEingtsvesmkdkelaafRNKTLGFVFQSFHLINSLN 101
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------------RNGEVSVIAISAGLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAE 181
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 495112432 182 VMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:PRK13546 182 CLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEG 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
11-216 |
1.06e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.89 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 11 KIYRTNEIETLALENVNldvikgEFVSIMGPSGCGKSTLLNimglldapSSGKIEINGTSVesmKDKELAAFRNkTLGFV 90
Cdd:PTZ00265 1240 QDYQGDEEQNVGMKNVN------EFSLTKEGGSGEDSTVFK--------NSGKILLDGVDI---CDYNLKDLRN-LFSIV 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 91 FQSFHLINsLNVIDNVELPllyRKMAAKERTrlaKEVLERVGLSHRMRHMPTQ-----------LSGGQCQRVAIARAIV 159
Cdd:PTZ00265 1302 SQEPMLFN-MSIYENIKFG---KEDATREDV---KRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALL 1374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRF 216
Cdd:PTZ00265 1375 REPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVF 1431
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-202 |
1.66e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.88 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 32 KGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTsvesmKDKELAAFRNKTLGFVFQSfhLIN-SLNV---IDNV 106
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILsGEL-KPNLGDYDEEPS-----WDEVLKRFRGTELQDYFKK--LANgEIKVahkPQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 107 EL-P---------LLyrkMAAKERTRLaKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDS 176
Cdd:COG1245 170 DLiPkvfkgtvreLL---EKVDERGKL-DELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180
....*....|....*....|....*.
gi 495112432 177 KMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:COG1245 246 YQRLNVARLIREL-AEEGKYVLVVEH 270
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-214 |
1.91e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVesmkdKELAAF 82
Cdd:PRK15439 11 LLCARSISKQYSGVEV----LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC-----ARLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 83 RNKTLG--FVFQSFHLINSLNVIDNVeLPLLYRKMAAKERTrlaKEVLERVGlSHRMRHMPT-QLSGGQCQRVAIARAIV 159
Cdd:PRK15439 82 KAHQLGiyLVPQEPLLFPNLSVKENI-LFGLPKRQASMQKM---KQLLAALG-CQLDLDSSAgSLEVADRQIVEILRGLM 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 160 GNPEIILADEPTGNLDSkmgAEVMELLHKLNK--EDGRTIVMVTHNEEQAKQTSRTI 214
Cdd:PRK15439 157 RDSRILILDEPTASLTP---AETERLFSRIREllAQGVGIVFISHKLPEIRQLADRI 210
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-219 |
4.55e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.50 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 29 DVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVeSMKDKELAAfrnKTLGFVFQsfhlinslnvidnvel 108
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKA---DYEGTVRD---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 109 pLLYRKMAAK-ERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLH 187
Cdd:cd03237 81 -LLSSITKDFyTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
170 180 190
....*....|....*....|....*....|..
gi 495112432 188 KLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:cd03237 160 RFAENNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
23-205 |
4.59e-11 |
|
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: 60.35 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLL---------------------NIMGLLDAPSSGKIEinGTSVE-SMKDKELA 80
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSIE--GLSPAiAIDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 AFRNKTLGFVFQsfhlINSLnvidnveLPLLYRKMAAKERTRLakevLERVGLSH-RM-RHMPTqLSGGQCQRVAIARAI 158
Cdd:cd03270 89 RNPRSTVGTVTE----IYDY-------LRLLFARVGIRERLGF----LVDVGLGYlTLsRSAPT-LSGGEAQRIRLATQI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495112432 159 ----VGnpEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEE 205
Cdd:cd03270 153 gsglTG--VLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDED 200
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-202 |
4.86e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.79 E-value: 4.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 33 GEFVSIMGPSGCGKSTLLNIM------GLLDapssGKIEINGTSvesmKDKELAAfrnKTLGFVFQSFhlINSLNVidNV 106
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLagrktgGYIE----GDIRISGFP----KKQETFA---RISGYCEQND--IHSPQV--TV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 107 ELPLLY-------RKMAAKERTRLAKEVLERV---GLSHRMRHMP--TQLSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:PLN03140 971 RESLIYsaflrlpKEVSKEEKMMFVDEVMELVeldNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180
....*....|....*....|....*....
gi 495112432 175 DSKMGAEVMELLHklNKED-GRTIVMVTH 202
Cdd:PLN03140 1051 DARAAAIVMRTVR--NTVDtGRTVVCTIH 1077
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-208 |
4.89e-11 |
|
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: 61.95 E-value: 4.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 6 LTGINK--IYRTNEIETL-------ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSV-ESMK 75
Cdd:TIGR01257 1929 ISGGNKtdILRLNELTKVysgtsspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNIS 2008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 76 DKelaafrNKTLGFVFQsFHLINSLnvIDNVELPLLY---RKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRV 152
Cdd:TIGR01257 2009 DV------HQNMGYCPQ-FDAIDDL--LTGREHLYLYarlRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKL 2079
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495112432 153 AIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAK 208
Cdd:TIGR01257 2080 STAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECE 2134
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-201 |
5.53e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.34 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 25 NVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESmkDKELAAFRnKTLGFV---------FQSFH 95
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP--RSPLDAVK-KGMAYItesrrdngfFPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 96 LINSLNVIDNVELPLLYRKMA---AKERTRLAKEVLERVGLS-HRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:PRK09700 358 IAQNMAISRSLKDGGYKGAMGlfhEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190
....*....|....*....|....*....|
gi 495112432 172 GNLDSKMGAEVMELLHKLnKEDGRTIVMVT 201
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQL-ADDGKVILMVS 466
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-202 |
5.90e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.72 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNimGLLdapssGKIEINGTSVesmkdkeLAAfrnKTLGFVFQSFHLINSlNV 102
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQ--SLL-----SQFEISEGRV-------WAE---RSIAYVPQQAWIMNA-TV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 103 IDNVelpLLYrkmaAKERT-RLAKEVleRV------------GLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADE 169
Cdd:PTZ00243 738 RGNI---LFF----DEEDAaRLADAV--RVsqleadlaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190
....*....|....*....|....*....|....*
gi 495112432 170 PTGNLDSKMGAEVME--LLHKLNkedGRTIVMVTH 202
Cdd:PTZ00243 809 PLSALDAHVGERVVEecFLGALA---GKTRVLATH 840
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
22-202 |
6.28e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.27 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkeLAAFRNKtLGFVFQSFHLInSLN 101
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ---LDSWRSR-LAVVSQTPFLF-SDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPllyRKMAAKER----TRLAK--------------EVLERvglshrmrhmPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:PRK10789 405 VANNIALG---RPDATQQEiehvARLASvhddilrlpqgydtEVGER----------GVMLSGGQKQRISIARALLLNAE 471
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495112432 164 IILADEPTGNLDskmGAEVMELLHKLNK-EDGRTIVMVTH 202
Cdd:PRK10789 472 ILILDDALSAVD---GRTEHQILHNLRQwGEGRTVIISAH 508
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
33-175 |
7.52e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.48 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 33 GEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLGF-----VFQSFHLINSLNvidnve 107
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLkadlsTLENLHFLCGLH------ 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 108 lpllyrkmaAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLD 175
Cdd:PRK13543 111 ---------GRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-202 |
8.60e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 8.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMG---LLDapsSGKIEINGTSVESM------KDKELAAFRN-----KTLG 88
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLD---DGRIIYEQDLIVARlqqdppRNVEGTVYDFvaegiEEQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 89 FVFQSFHLINSLNVIDNVElPLLYRKMAAKER----------TRLaKEVLERVGLShrmRHMP-TQLSGGQCQRVAIARA 157
Cdd:PRK11147 96 EYLKRYHDISHLVETDPSE-KNLNELAKLQEQldhhnlwqleNRI-NEVLAQLGLD---PDAAlSSLSGGWLRKAALGRA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495112432 158 IVGNPEIILADEPTGNLDskmgAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISH 211
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-204 |
9.65e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.57 E-value: 9.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDAPS-SGKIEINGtsvesmkdkELAAFRN----KTLGFVF--QS 93
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLsGVYPHGSyEGEILFDG---------EVCRFKDirdsEALGIVIihQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 94 FHLINSLNVIDNVEL---PLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:NF040905 87 LALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 495112432 171 TGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH--NE 204
Cdd:NF040905 167 TAALNEEDSAALLDLLLEL-KAQGITSIIISHklNE 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-202 |
1.23e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 30 VIKGEFVSIMGPSGCGKSTLLNIMglldapsSGKIEIN--GTSVESMKDKELAAFRNKTLGFVF--------------QS 93
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIL-------SGELIPNlgDYEEEPSWDEVLKRFRGTELQNYFkklyngeikvvhkpQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 94 FHLINSL---NVIDnvelpLLYRkmaAKERTRLaKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:PRK13409 169 VDLIPKVfkgKVRE-----LLKK---VDERGKL-DEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|..
gi 495112432 171 TGNLDSKMGAEVMELLHKLNKedGRTIVMVTH 202
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAE--GKYVLVVEH 269
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-219 |
1.92e-10 |
|
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: 59.92 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 20 TLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVES----------MKDkelaafrNKTLG 88
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELE-PSEGKIKHSGRISFSpqtswimpgtIKD-------NIIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 89 FVFQSFHLInslNVIDNVELPLLYRKMAAKERTrlakeVLERVGLShrmrhmptqLSGGQCQRVAIARAIVGNPEIILAD 168
Cdd:TIGR01271 511 LSYDEYRYT---SVIKACQLEEDIALFPEKDKT-----VLGEGGIT---------LSGGQRARISLARAVYKDADLYLLD 573
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495112432 169 EPTGNLDSKMGAEVME-LLHKLNKEdgRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFEsCLCKLMSN--KTRILVTSKLEHLKKADKILLLHEG 623
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-222 |
1.98e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.07 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDAPS-------SGKIEINGTSVESMKDKELAAFR-----NKTLGF 89
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRavlpqAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 90 VFqSFHLINSLNvidnvELPLLYRKMAAKERTR-LAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAI---------V 159
Cdd:PRK13547 97 AF-SAREIVLLG-----RYPHARRAGALTHRDGeIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFF-DGRQV 222
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLaDGAIV 234
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-202 |
2.74e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.50 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNImgLLDAPS----SGKIEINGTSVESMKDKELAafrnkTLGfVFQSF 94
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKV--IAGHPAykilEGDILFKGESILDLEPEERA-----HLG-IFLAF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 95 HLINSLNVIDNVE-LPLLY---RKMAAK------ERTRLAKEVLERVGLSHRM--RHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:CHL00131 91 QYPIEIPGVSNADfLRLAYnskRKFQGLpeldplEFLEIINEKLKLVGMDPSFlsRNVNEGFSGGEKKRNEILQMALLDS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:CHL00131 171 ELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITH 209
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-219 |
2.85e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 58.71 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLLDaPSSGKIEINGTSVESMKDKEL---AAFRNKTLGFVFQSFHLin 98
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLmLILGELE-PSEGKIKHSGRISFSSQFSWImpgTIKENIIFGVSYDEYRY-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 sLNVIDNVELPLLYRKMAAKERTrlakeVLERVGLShrmrhmptqLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKM 178
Cdd:cd03291 130 -KSVVKACQLEEDITKFPEKDNT-----VLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495112432 179 GAEVME-LLHKLNKEdgRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:cd03291 195 EKEIFEsCVCKLMAN--KTRILVTSKMEHLKKADKILILHEG 234
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
115-222 |
1.04e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.44 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 115 MAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKeDG 194
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DG 194
|
90 100
....*....|....*....|....*....
gi 495112432 195 RTIVMVTHNEEQAKQTSRTIRFFD-GRQV 222
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAHELTVIDrGRVI 223
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
23-175 |
1.89e-09 |
|
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: 56.02 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDapSSGKIEINGTSVESMKdkeLAAFRnKTLGFVFQSFhLINSLN 101
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLN--TEGDIQIDGVSWNSVP---LQKWR-KAFGVIPQKV-FIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVElPllYRKMAAKERTRLAKEVlervGLSHRMRHMPTQL-----------SGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:cd03289 93 FRKNLD-P--YGKWSDEEIWKVAEEV----GLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEP 165
|
....*
gi 495112432 171 TGNLD 175
Cdd:cd03289 166 SAHLD 170
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-175 |
1.94e-09 |
|
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: 57.23 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLdAPSSGKIEINGTSVESMKdkeLAAFRnKTLGFVFQSFhLINSLNV 102
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVT---LQTWR-KAFGVIPQKV-FIFSGTF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 103 IDNVElPllYRKMAAKERTRLAKEVlervGLSHRMRHMPTQL-----------SGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:TIGR01271 1309 RKNLD-P--YEQWSDEEIWKVAEEV----GLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
....
gi 495112432 172 GNLD 175
Cdd:TIGR01271 1382 AHLD 1385
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-219 |
2.06e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.91 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDAPSSGKIEINGTsvesmkdkelaafrnktLGFVFQSFHLINSlN 101
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMlGELSHAETSSVVIRGS-----------------VAYVPQVSWIFNA-T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVelplLYRKMAAKERTRLAKEVlerVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:PLN03232 695 VRENI----LFGSDFESERYWRAIDV---TALQHDLDLLPgrdlteigergVNISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495112432 171 TGNLDSKMGAEVMELLHKlNKEDGRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:PLN03232 768 LSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLMDRIILVSEG 815
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-204 |
2.34e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.96 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVesmkDKELAAFRnKTLGFVFQSFHLIN 98
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQ-KQLCFVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 SLNVIDNVELPLLYRK--MAAKERTRLAKevlervgLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDS 176
Cdd:PRK13540 88 YLTLRENCLYDIHFSPgaVGITELCRLFS-------LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*...
gi 495112432 177 KMGAEVMELLHKLNKEDGrTIVMVTHNE 204
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGG-AVLLTSHQD 187
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-204 |
3.14e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.41 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 21 LALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIeingtsvesmkdkelaaFRNKTLGFVFQSFHLINSL 100
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-----------------FRSAKVRMAVFSQHHVDGL 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNvelPLLY--RKMAAKERTRLaKEVLERVGLSHRMRHMPT-QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSK 177
Cdd:PLN03073 586 DLSSN---PLLYmmRCFPGVPEQKL-RAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD 661
|
170 180
....*....|....*....|....*..
gi 495112432 178 mgaEVMELLHKLNKEDGrTIVMVTHNE 204
Cdd:PLN03073 662 ---AVEALIQGLVLFQG-GVLMVSHDE 684
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
3-202 |
4.19e-09 |
|
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: 55.91 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIetlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMG--------LLDAPSSGKI--------EI 66
Cdd:TIGR00954 451 GIKFENIPLVTPNGDV---LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLfyvpqrpyMT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 67 NGT---------SVESMKDKelaAFRNKTLgfvfqsfhlinsLNVIDNVELpllyrkmaakertrlaKEVLERVGLSHRM 137
Cdd:TIGR00954 528 LGTlrdqiiypdSSEDMKRR---GLSDKDL------------EQILDNVQL----------------THILEREGGWSAV 576
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 138 RHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTgnldSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:TIGR00954 577 QDWMDVLSGGEKQRIAMARLFYHKPQFAILDECT----SAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-175 |
5.30e-09 |
|
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: 55.33 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 21 LALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGT----SVESMKDKeLAAfrNKTlgfVFQSFHL 96
Cdd:TIGR03719 336 LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvklaYVDQSRDA-LDP--NKT---VWEEISG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 97 INSLNVIDNVELPllyrkmaakERTRLAK------EVLERVGlshrmrhmptQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:TIGR03719 410 GLDIIKLGKREIP---------SRAYVGRfnfkgsDQQKKVG----------QLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
....*
gi 495112432 171 TGNLD 175
Cdd:TIGR03719 471 TNDLD 475
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-202 |
7.24e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 7.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNI------MGLLdapSSGKIEINGTSVESmkdkelaAFRNKTlGFVFQSFHL 96
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVlaervtTGVI---TGGDRLVNGRPLDS-------SFQRSI-GYVQQQDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 97 INSLNVIDNVELPLLYR---KMAAKERTRLAKEVLERVGlshrMRHMPTQLSG--------GQCQRVAIARAIVGNPEII 165
Cdd:TIGR00956 848 LPTSTVRESLRFSAYLRqpkSVSKSEKMEYVEEVIKLLE----MESYADAVVGvpgeglnvEQRKRLTIGVELVAKPKLL 923
|
170 180 190
....*....|....*....|....*....|....*...
gi 495112432 166 L-ADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTH 202
Cdd:TIGR00956 924 LfLDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIH 960
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-222 |
1.41e-08 |
|
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: 51.99 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 32 KGEFVSIMGPSGCGKSTLLN-IMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLGfvfqsfhlinslnvidnvelpl 110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKK---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 111 lyrkmaakertrlakevlervglshrmrhmpTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMEL----L 186
Cdd:smart00382 59 -------------------------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrL 107
|
170 180 190
....*....|....*....|....*....|....*.
gi 495112432 187 HKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-216 |
2.15e-08 |
|
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: 51.94 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNimglldapssgkiEINGTSVESMKDKELAAF-RNKTLgfvfqsfhLINSL 100
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-------------EGLYASGKARLISFLPKFsRNKLI--------FIDQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVELPLLyrkmaakertrlakevleRVGlshrmRHMPTqLSGGQCQRVAIARAIVGNPE--IILADEPTGNLDSKM 178
Cdd:cd03238 69 QFLIDVGLGYL------------------TLG-----QKLST-LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190
....*....|....*....|....*....|....*...
gi 495112432 179 GAEVMELLHKLNKEdGRTIVMVTHNEEQAKQTSRTIRF 216
Cdd:cd03238 125 INQLLEVIKGLIDL-GNTVILIEHNLDVLSSADWIIDF 161
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-201 |
2.19e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.47 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTSVESMKDKE-LAAfrnktlGFVFQSFH----- 95
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLyGAL-PRTSGYVTLDGHEVVTRSPQDgLAN------GIVYISEDrkrdg 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 96 LINSLNVIDNVELPLLYRKMAAKERTRLAKEVLErVGLSHRMRHMPT--------QLSGGQCQRVAIARAIVGNPEIILA 167
Cdd:PRK10762 341 LVLGMSVKENMSLTALRYFSRAGGSLKHADEQQA-VSDFIRLFNIKTpsmeqaigLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190
....*....|....*....|....*....|....
gi 495112432 168 DEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVT 201
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQF-KAEGLSIILVS 452
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-219 |
7.01e-08 |
|
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: 50.65 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 29 DVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVeSMKDKELaafrnktlgfvfqsfhlinslnvidnvel 108
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-VYKPQYI----------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 109 pllyrkmaakertrlakevlervglshrmrhmptQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHK 188
Cdd:cd03222 71 ----------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180 190
....*....|....*....|....*....|.
gi 495112432 189 LNKEDGRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:cd03222 117 LSEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-202 |
1.02e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEInGTSVE-SMKDKELAAFR-NKTlgfvfqsfhlins 99
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMlGQL-QADSGRIHC-GTKLEvAYFDQHRAELDpEKT------------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 100 lnVIDNVelpllyrkmaAKERtrlaKEVL----ERVGLS-------HRMRHM-PTQ-LSGGQCQRVAIARAIVGNPEIIL 166
Cdd:PRK11147 400 --VMDNL----------AEGK----QEVMvngrPRHVLGylqdflfHPKRAMtPVKaLSGGERNRLLLARLFLKPSNLLI 463
|
170 180 190
....*....|....*....|....*....|....*.
gi 495112432 167 ADEPTGNLDskmgAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:PRK11147 464 LDEPTNDLD----VETLELLEELLDSYQGTVLLVSH 495
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-202 |
1.41e-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: 51.32 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 32 KGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEingTSVE-SMKDKELAAFRNKTlgfvfqsfhlinslnVIDnvelpL 110
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---EDLKiSYKPQYISPDYDGT---------------VEE-----F 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 111 LYRKMAAKERTRLAK-EVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKL 189
Cdd:COG1245 422 LRSANTDDFGSSYYKtEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF 501
|
170
....*....|...
gi 495112432 190 NKEDGRTIVMVTH 202
Cdd:COG1245 502 AENRGKTAMVVDH 514
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-203 |
1.44e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 32 KGEFVSIMGPSGCGKSTLLNIM-GLLDaPSSGKIEingTSVE-SMKDKELAAFRNKTlgfvfqsfhlinslnvidnVELP 109
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLaGVLK-PDEGEVD---PELKiSYKPQYIKPDYDGT-------------------VEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 110 LlyRKMAAKERTRLAK-EVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHK 188
Cdd:PRK13409 421 L--RSITDDLGSSYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 498
|
170
....*....|....*
gi 495112432 189 LNKEDGRTIVMVTHN 203
Cdd:PRK13409 499 IAEEREATALVVDHD 513
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
140-205 |
4.18e-07 |
|
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: 48.76 E-value: 4.18e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495112432 140 MPTQLSGGQ------CQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVM-ELLHKLNKEDGRTIVMVTHNEE 205
Cdd:cd03240 112 MRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEENIEESLaEIIEERKSQKNFQLIVITHDEE 184
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-199 |
2.82e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkeLAAFRnKTLGFVFQS--------- 93
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLR-KVLGIIPQApvlfsgtvr 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 94 FHL--INSLNVIDNVElpllyrkmaAKERTRLaKEVLER--VGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADE 169
Cdd:PLN03130 1331 FNLdpFNEHNDADLWE---------SLERAHL-KDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190
....*....|....*....|....*....|
gi 495112432 170 PTGNLDSKMGAevmeLLHKLNKEDGRTIVM 199
Cdd:PLN03130 1401 ATAAVDVRTDA----LIQKTIREEFKSCTM 1426
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
3-222 |
3.54e-06 |
|
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: 46.10 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRT--NEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLdapSSGKIEINGT-SVESMKDKEL 79
Cdd:cd03233 1 ASTLSWRNISFTTgkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDiHYNGIPYKEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 80 AAFRNKTLGFVFQSFHLINSLNVidnvelpllyrkmaakertrlaKEVLERVgLSHRMRHMPTQLSGGQCQRVAIARAIV 159
Cdd:cd03233 78 AEKYPGEIIYVSEEDVHFPTLTV----------------------RETLDFA-LRCKGNEFVRGISGGERKRVSIAEALV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTH--NEEQAKQTSRTIRFFDGRQV 222
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYqaSDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-211 |
4.28e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.58 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 25 NVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAfrnktLGFVF-----QSFHLINS 99
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLA-----RGLVYlpedrQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 100 LNVIDNVeLPLLYRKMAAKERTRLAKEVLER------VGLSHRMRHMPTqLSGGQCQRVAIARAIVGNPEIILADEPTGN 173
Cdd:PRK15439 356 APLAWNV-CALTHNRRGFWIKPARENAVLERyrralnIKFNHAEQAART-LSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190
....*....|....*....|....*....|....*...
gi 495112432 174 LDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTS 211
Cdd:PRK15439 434 VDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMA 470
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-201 |
4.62e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 46.74 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLGFVFQSFHLINSLN 101
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPLLyRKMAAKERTRLAKEV------LERVGLSHRMRHMP-TQLSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:TIGR02633 356 VGKNITLSVL-KSFCFKMRIDAAAELqiigsaIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180
....*....|....*....|....*..
gi 495112432 175 DSKMGAEVMELLHKLNKEdGRTIVMVT 201
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQE-GVAIIVVS 460
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-200 |
7.10e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.06 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 24 ENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEING--TSVESMKDkelaAFR---------NKTLGFVfq 92
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRD----AIRagimlcpedRKAEGII-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 93 sfhLINSlnVIDNVELP----------LLYRKmaaKERtRLAKEVLERVGLSHRMRHMPT-QLSGGQCQRVAIARAIVGN 161
Cdd:PRK11288 344 ---PVHS--VADNINISarrhhlragcLINNR---WEA-ENADRFIRSLNIKTPSREQLImNLSGGNQQKAILGRWLSED 414
|
170 180 190
....*....|....*....|....*....|....*....
gi 495112432 162 PEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMV 200
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFV 452
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-202 |
1.30e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.78 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 3 MIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLDAP-SSGKIEINGTSVESMKDKELA 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAI----LRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREDYEvTGGTVEFKGKDLLELSPEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 ------AFRNKT-LGFVFQSFHLINSLNVIDNvelpllYRKMAAKERTRLAKEVLERVglshRMRHMPTQL--------- 144
Cdd:PRK09580 77 gegifmAFQYPVeIPGVSNQFFLQTALNAVRS------YRGQEPLDRFDFQDLMEEKI----ALLKMPEDLltrsvnvgf 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 145 SGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTH 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-171 |
1.90e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 4 IKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvESMKDkelAAFR 83
Cdd:NF033858 2 ARLEGVSHRYG----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG---GDMAD---ARHR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 84 NKT----------LGfvfqsFHLINSLNVIDNVELpllyrkMA------AKERTRLAKEVLERVGLsHRMRHMPT-QLSG 146
Cdd:NF033858 72 RAVcpriaympqgLG-----KNLYPTLSVFENLDF------FGrlfgqdAAERRRRIDELLRATGL-APFADRPAgKLSG 139
|
170 180
....*....|....*....|....*
gi 495112432 147 GQCQRVAIARAIVGNPEIILADEPT 171
Cdd:NF033858 140 GMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-200 |
2.06e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.53 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 25 NVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDAPSSGKIEINGTSVESMKDKElaAFRN---------KTLGFVFQsf 94
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKIRNPQQ--AIAQgiamvpedrKRDGIVPV-- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 95 hlinsLNVIDNVELPLLYRKM------AAKERTRLAKEVLE-RVGLSHRMRHMpTQLSGGQCQRVAIARAIVGNPEIILA 167
Cdd:PRK13549 356 -----MGVGKNITLAALDRFTggsridDAAELKTILESIQRlKVKTASPELAI-ARLSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190
....*....|....*....|....*....|...
gi 495112432 168 DEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMV 200
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVI 461
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-175 |
2.18e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.72 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 21 LALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGlLDAPSSGKIEInGTSVEsmkdkelaafrnktLGFVFQSF-HLIN 98
Cdd:PRK11819 338 LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKmITG-QEQPDSGTIKI-GETVK--------------LAYVDQSRdALDP 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 99 SLNVIDNVELPLLYRKMAAKE---RTRLAK------EVLERVGlshrmrhmptQLSGGQCQRVAIARAIV--GNpeIILA 167
Cdd:PRK11819 402 NKTVWEEISGGLDIIKVGNREipsRAYVGRfnfkggDQQKKVG----------VLSGGERNRLHLAKTLKqgGN--VLLL 469
|
....*...
gi 495112432 168 DEPTGNLD 175
Cdd:PRK11819 470 DEPTNDLD 477
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-175 |
2.61e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLGFVF----------Q 92
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIdgdreyrqleA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 93 SFHLINSLNviDNVELPLLYRKMAAKE----RTRlAKEVLERVGLSHRMRHMP-TQLSGGQCQRVAIARAIVGNPEIILA 167
Cdd:PRK10636 97 QLHDANERN--DGHAIATIHGKLDAIDawtiRSR-AASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLL 173
|
....*...
gi 495112432 168 DEPTGNLD 175
Cdd:PRK10636 174 DEPTNHLD 181
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
23-203 |
4.10e-05 |
|
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: 43.37 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNimGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLgFVFQS--------- 93
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN--DTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVI-VIDQSpigrtprsn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 94 -------FHLINSL----------------------NVIDNVELP----LLYRKMAAKERTRLakEVLERVGLSH-RMRH 139
Cdd:cd03271 88 patytgvFDEIRELfcevckgkrynretlevrykgkSIADVLDMTveeaLEFFENIPKIARKL--QTLCDVGLGYiKLGQ 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 140 MPTQLSGGQCQRVAIARAIV----GNPEIILaDEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHN 203
Cdd:cd03271 166 PATTLSGGEAQRIKLAKELSkrstGKTLYIL-DEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIEHN 231
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
144-201 |
4.11e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 4.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 144 LSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDgRTIVMVT 201
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKD-KGIIIIS 448
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-200 |
5.44e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELaafrNKTLGFVFQSFHLInSLNV 102
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL----RRVLSIIPQSPVLF-SGTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 103 IDNVElPLLYRKMA----AKERTRLaKEVLER--VGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDS 176
Cdd:PLN03232 1327 RFNID-PFSEHNDAdlweALERAHI-KDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
|
170 180
....*....|....*....|....
gi 495112432 177 KMGAevmeLLHKLNKEDGRTIVMV 200
Cdd:PLN03232 1405 RTDS----LIQRTIREEFKSCTML 1424
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
24-175 |
9.06e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 24 ENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIeingtsvesMKDKelaafrNKTLG------FVFQSFhli 97
Cdd:PRK15064 18 ENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV---------SLDP------NERLGklrqdqFAFEEF--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 98 nslNVIDNVELPllYRKM--AAKERTRL--------------------------------AKEVLERVGLSHRMRHMP-T 142
Cdd:PRK15064 80 ---TVLDTVIMG--HTELweVKQERDRIyalpemseedgmkvadlevkfaemdgytaearAGELLLGVGIPEEQHYGLmS 154
|
170 180 190
....*....|....*....|....*....|...
gi 495112432 143 QLSGGQCQRVAIARAIVGNPEIILADEPTGNLD 175
Cdd:PRK15064 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
124-175 |
2.12e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 2.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 495112432 124 AKEVLERVGLSHRMRHMPT-QLSGGQCQRVAIARAIVGNPEIILADEPTGNLD 175
Cdd:PLN03073 324 AASILAGLSFTPEMQVKATkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
11-205 |
2.12e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 11 KIYRTN-EIETLA--------LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIeingtsvesmKDKEla 80
Cdd:PRK15064 314 KLHRNAlEVENLTkgfdngplFKNLNLLLEAGERLAIIGENGVGKTTLLRtLVGEL-EPDSGTV----------KWSE-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 81 afrNKTLGFVFQ--SFHLINSLNVIDNVElplLYRKmaAKERTRLAKEVLERVGLSH-RMRHMPTQLSGGQCQRVAIARA 157
Cdd:PRK15064 381 ---NANIGYYAQdhAYDFENDLTLFDWMS---QWRQ--EGDDEQAVRGTLGRLLFSQdDIKKSVKVLSGGEKGRMLFGKL 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495112432 158 IVGNPEIILADEPTGNLDskmgaevMELLHKLN----KEDGrTIVMVTHNEE 205
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMD-------MESIESLNmaleKYEG-TLIFVSHDRE 496
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
11-216 |
2.20e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.42 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 11 KIYRTNEIETLALENVNLdvikgefvsIMGPSGCGKSTLLNIMGLLdapssgkieingtsvesmkdkelaafrnktlgfV 90
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTI---------ITGPNGSGKSTILDAIGLA---------------------------------L 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 91 FQSFHLinslnvidnvelplLYRKMAAKERTRLAKEVLERVGLSHrmrhmptQLSGGQCQRVAIA-----RAIVGNPEII 165
Cdd:cd03227 46 GGAQSA--------------TRRRSGVKAGCIVAAVSAELIFTRL-------QLSGGEKELSALAlilalASLKPRPLYI 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495112432 166 LaDEPTGNLDSKMGAEVMELLHKLNKEDGRTIVmVTHNEEQAKQTSRTIRF 216
Cdd:cd03227 105 L-DEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPELAELADKLIHI 153
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
132-200 |
2.84e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 2.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 132 GLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMV 200
Cdd:PRK10938 124 GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-200 |
3.25e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLlnimglldAPS----------SGKIEINGTSVE--SMKDkelaAFRN------ 84
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTEL--------AMSvfgrsygrniSGTVFKDGKEVDvsTVSD----AIDAglayvt 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 85 ---KTLGFVFQ----------SFHLINSLNVIDNVElpllYRKMAAKERTRL---AKEVLERVGlshrmrhmptQLSGGQ 148
Cdd:NF040905 344 edrKGYGLNLIddikrnitlaNLGKVSRRGVIDENE----EIKVAEEYRKKMnikTPSVFQKVG----------NLSGGN 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495112432 149 CQRVAIARAIVGNPEIILADEPTGNLDskMGA--EVMELLHKLNKEdGRTIVMV 200
Cdd:NF040905 410 QQKVVLSKWLFTDPDVLILDEPTRGID--VGAkyEIYTIINELAAE-GKGVIVI 460
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
126-203 |
4.87e-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: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 126 EVLERVGLSH-RMRHMPTQLSGGQCQRVAIARAI---VGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVT 201
Cdd:TIGR00630 811 QTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIE 889
|
..
gi 495112432 202 HN 203
Cdd:TIGR00630 890 HN 891
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
23-51 |
1.01e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 1.01e-03
10 20
....*....|....*....|....*....
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN 51
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
18-208 |
1.49e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.31 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 18 IETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkelaafrNKTLGFVFQSFHLI 97
Cdd:PRK13541 11 IEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--------KPYCTYIGHNLGLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 98 NSLNVIDNVelpllyrKMAAK--ERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLd 175
Cdd:PRK13541 83 LEMTVFENL-------KFWSEiyNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL- 154
|
170 180 190
....*....|....*....|....*....|...
gi 495112432 176 SKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAK 208
Cdd:PRK13541 155 SKENRDLLNNLIVMKANSGGIVLLSSHLESSIK 187
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
18-51 |
1.52e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 38.65 E-value: 1.52e-03
10 20 30
....*....|....*....|....*....|....*...
gi 495112432 18 IETLALENVNLDVIKGEF---VSI-MGPSGCGKSTLLN 51
Cdd:PRK00098 145 LELSAKEGEGLDELKPLLagkVTVlAGQSGVGKSTLLN 182
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
23-51 |
2.80e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.52 E-value: 2.80e-03
10 20
....*....|....*....|....*....
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN 51
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
23-49 |
3.35e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 3.35e-03
10 20
....*....|....*....|....*..
gi 495112432 23 LENVNLDVIKGEFVSIMGPSGCGKSTL 49
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
109-203 |
4.76e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 109 PLLYRKMaakertrlakEVLERVGLSHrMR---HMPTqLSGGQCQRVAIARAIV----GNPEIILaDEPTGNL---DSKM 178
Cdd:COG0178 801 PKIARKL----------QTLQDVGLGY-IKlgqPATT-LSGGEAQRVKLASELSkrstGKTLYIL-DEPTTGLhfhDIRK 867
|
90 100
....*....|....*....|....*
gi 495112432 179 gaeVMELLHKLnKEDGRTIVMVTHN 203
Cdd:COG0178 868 ---LLEVLHRL-VDKGNTVVVIEHN 888
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
12-51 |
7.42e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 35.94 E-value: 7.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 495112432 12 IYRTNEIETL--ALENVNLDviKGEFVSIMGPSGCGKSTLLN 51
Cdd:pfam13191 3 VGREEELEQLldALDRVRSG--RPPSVLLTGEAGTGKTTLLR 42
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
11-51 |
7.68e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 35.98 E-value: 7.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 495112432 11 KIYRTNEIETLALENVN-------LDVIKGEFVSIMGPSGCGKSTLLN 51
Cdd:pfam03193 77 KIYRAIGYPVLFVSAKTgegiealKELLKGKTTVLAGQSGVGKSTLLN 124
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
109-203 |
9.83e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 36.59 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 109 PLLYRKMaakertrlakEVLERVGLSH-RMRHMPTQLSGGQCQRVAIA-----RAiVGNPEIILaDEPTGNLDSKMGAEV 182
Cdd:PRK00349 805 PKIARKL----------QTLVDVGLGYiKLGQPATTLSGGEAQRVKLAkelskRS-TGKTLYIL-DEPTTGLHFEDIRKL 872
|
90 100
....*....|....*....|.
gi 495112432 183 MELLHKLnKEDGRTIVMVTHN 203
Cdd:PRK00349 873 LEVLHRL-VDKGNTVVVIEHN 892
|
|
|