|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-224 |
4.37e-109 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 313.90 E-value: 4.37e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSD 81
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IRKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITL 161
Cdd:COG1136 83 LRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 162 PSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQIFTE 224
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-221 |
1.04e-102 |
|
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: 297.09 E-value: 1.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDIR 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPS 163
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 164 IIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-225 |
5.85e-70 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 215.72 E-value: 5.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkals 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 dirkHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDtmlDRYEKVAEALNILDIS---DKYPSELSGGQRQRTSAARA 157
Cdd:COG1116 80 ----PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKA---ERRERARELLELVGLAgfeDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690417 158 FITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPV-AASYANRVVMLKD--GQIFTEL 225
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVFLADRVVVLSArpGRIVEEI 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-221 |
7.40e-69 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 211.45 E-value: 7.40e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKkmaQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDI 82
Cdd:COG2884 1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKHdIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRyekVAEALNILDISDK---YPSELSGGQRQRTSAARAFI 159
Cdd:COG2884 78 RRR-IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRR---VREVLDLVGLSDKakaLPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 160 TLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHDP-VAASYANRVVMLKDGQI 221
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLeLVDRMPKRVLELEDGRL 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-216 |
6.49e-67 |
|
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: 206.55 E-value: 6.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkalsdir 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 kHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDtmlDRYEKVAEALNILDIS---DKYPSELSGGQRQRTSAARAFIT 160
Cdd:cd03293 73 -PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKA---EARERAEELLELVGLSgfeNAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 161 LPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDpV--AASYANRVVML 216
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD-IdeAVFLADRVVVL 205
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-221 |
1.06e-66 |
|
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: 206.52 E-value: 1.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSD 81
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IRKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKlDKD------TMLDRYEkVAEALnildisDKYPSELSGGQRQRTSAA 155
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLELAG-RRDarararALLERVG-LGHRL------DHYPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616690417 156 RAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-221 |
1.17e-66 |
|
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: 206.28 E-value: 1.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDI 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKHdIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDtmlDRYEKVAEALNILDISDK---YPSELSGGQRQRTSAARAFI 159
Cdd:cd03258 81 RRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKA---EIEERVLELLELVGLEDKadaYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 160 TLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEmEVVKRICDRVAVMEKGEV 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-221 |
5.34e-66 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 208.01 E-value: 5.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDI 82
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKhDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDtmlDRYEKVAEALNILDISDK---YPSELSGGQRQRTSAARAFI 159
Cdd:COG1135 81 RR-KIGMIFQHFNLLSSRTVAENVALPLEIAGVPKA---EIRKRVAELLELVGLSDKadaYPSQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 160 TLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEmDVVRRICDRVAVLENGRI 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-221 |
1.33e-65 |
|
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: 202.75 E-value: 1.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNkkmaQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkalsdIR 83
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP------PE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPS 163
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 164 IIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPV-AASYANRVVMLKDGQI 221
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEeALALADRIAVMNEGRI 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-221 |
3.52e-65 |
|
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: 202.35 E-value: 3.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSdI 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRK-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKHDIGFIFQE-YNLLH-TLTVKENIMLPLTVQKLDKDTMLdRYEKVAEALNIL----DISDKYPSELSGGQRQRTSAAR 156
Cdd:cd03257 80 RRKEIQMVFQDpMSSLNpRMTIGEQIAEPLRIHGKLSKKEA-RKEAVLLLLVGVglpeEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616690417 157 AFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDlGVVAKIADRVAVMYAGKI 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-221 |
4.57e-65 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 206.10 E-value: 4.57e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGnkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkals 80
Cdd:COG3842 3 MPALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 dIRKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDtmlDRYEKVAEALNILDIS---DKYPSELSGGQRQRTSAARA 157
Cdd:COG3842 74 -PEKRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKA---EIRARVAELLELVGLEglaDRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 158 FITLPSIIFADEPTGALDSK---STQDLLKRLMKmneEIKTTIIMVTHDPV-AASYANRVVMLKDGQI 221
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKlreEMREELRRLQR---ELGITFIYVTHDQEeALALADRIAVMNDGRI 214
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-222 |
4.07e-64 |
|
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: 199.50 E-value: 4.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDI 82
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLP 162
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 163 SIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQIF 222
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLF 220
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-231 |
5.50e-64 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 199.90 E-value: 5.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNKKMAqevLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSD 81
Cdd:COG3638 1 PMLELRNLSKRYPGGTPA---LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IRkHDIGFIFQEYNLLHTLTVKENIM---------LPLTVQKLDKDtmlDRyEKVAEALNILDISDKY---PSELSGGQR 149
Cdd:COG3638 78 LR-RRIGMIFQQFNLVPRLSVLTNVLagrlgrtstWRSLLGLFPPE---DR-ERALEALERVGLADKAyqrADQLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 150 QRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDP-VAASYANRVVMLKDGQI------- 221
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVdLARRYADRIIGLRDGRVvfdgppa 232
|
250
....*....|....*.
gi 616690417 222 ------FTELYQGDDD 231
Cdd:COG3638 233 eltdavLREIYGGEAE 248
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-221 |
6.71e-64 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 203.00 E-value: 6.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhkleklsnKALS 80
Cdd:COG3839 1 MASLELENVSKSYGGV----EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG--------RDVT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DI--RKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDtmlDRYEKVAEALNILDIS---DKYPSELSGGQRQRTSAA 155
Cdd:COG3839 69 DLppKDRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKA---EIDRRVREAAELLGLEdllDRKPKQLSGGQRQRVALG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 156 RAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPV-AASYANRVVMLKDGQI 221
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVeAMTLADRIAVMNDGRI 212
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-216 |
4.76e-63 |
|
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: 196.30 E-value: 4.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 6 VKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDIRKH 85
Cdd:TIGR03608 1 LKNISKKFGDK----VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 86 DIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSII 165
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 616690417 166 FADEPTGALDSKSTQDLLKRLMKMNEEIKtTIIMVTHDPVAASYANRVVML 216
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDEGK-TIIIVTHDPEVAKQADRVIEL 206
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-222 |
4.49e-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: 194.08 E-value: 4.49e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDI 82
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKHdIGFIFQEYNLLHTLTVKENIMLPLTVQ-KLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITL 161
Cdd:TIGR02982 81 RRR-IGYIFQAHNLLGFLTARQNVQMALELQpNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690417 162 PSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQIF 222
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-221 |
2.14e-61 |
|
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: 192.89 E-value: 2.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDI 82
Cdd:COG1127 5 MIEVRNLTKSFGDRV----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKHdIGFIFQEYNLLHTLTVKENIMLPLTVQ-KLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITL 161
Cdd:COG1127 81 RRR-IGMLFQGGALFDSLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690417 162 PSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKI 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-221 |
7.92e-61 |
|
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: 199.36 E-value: 7.92e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNKKM-AQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALS 80
Cdd:COG1123 259 PLLEVRNLSKRYPVRGKgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIRKHdIGFIFQ--EYNLLHTLTVKENIMLPLTVQKLDKDTmlDRYEKVAEALNIL----DISDKYPSELSGGQRQRTSA 154
Cdd:COG1123 339 ELRRR-VQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRA--ERRERVAELLERVglppDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 155 ARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlAVVRYIADRVAVMYDGRI 483
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-222 |
1.21e-59 |
|
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: 188.55 E-value: 1.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDIR 83
Cdd:cd03256 1 IEVENLSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRY-----EKVAEALNILDISDKY---PSELSGGQRQRTSAA 155
Cdd:cd03256 78 RQ-IGMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLFpkeekQRALAALERVGLLDKAyqrADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 156 RAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDP-VAASYANRVVMLKDGQIF 222
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVdLAREYADRIVGLKDGRIV 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-221 |
2.99e-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: 187.70 E-value: 2.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKAlsdiR 83
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA----F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQE-YNLLH-TLTVKENIMLPLTVQKLDkdtmlDRYEKVAEALNILDIS----DKYPSELSGGQRQRTSAARA 157
Cdd:COG1124 78 RRRVQMVFQDpYASLHpRHTVDRILAEPLRIHGLP-----DREERIAELLEQVGLPpsflDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 158 FITLPSIIFADEPTGALDSkSTQ----DLLKRLmkmNEEIKTTIIMVTHDPVAASY-ANRVVMLKDGQI 221
Cdd:COG1124 153 LILEPELLLLDEPTSALDV-SVQaeilNLLKDL---REERGLTYLFVSHDLAVVAHlCDRVAVMQNGRI 217
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-221 |
2.07e-58 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 185.20 E-value: 2.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLL---NVLSSIDyisQGSITLKGHKLEkLSNKAL 79
Cdd:COG1126 1 MIEIENLHKSFGDL----EVLKGISLDVEKGEVVVIIGPSGSGKSTLLrciNLLEEPD---SGTITVDGEDLT-DSKKDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 80 SDIRKHdIGFIFQEYNLLHTLTVKENIML-PLTVQKLDKDtmldryEKVAEALNILD---ISDK---YPSELSGGQRQRT 152
Cdd:COG1126 73 NKLRRK-VGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKA------EAEERAMELLErvgLADKadaYPAQLSGGQQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 153 SAARAFITLPSIIFADEPTGALDSKSTQDLLKrLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPELVGEVLD-VMRDLAKEGMTMVVVTHEmGFAREVADRVVFMDGGRI 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-221 |
2.40e-58 |
|
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: 184.84 E-value: 2.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALSDIR 83
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDG---KDITKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQ--EYNLLHTlTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITL 161
Cdd:COG1122 75 RK-VGLVFQnpDDQLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690417 162 PSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHDP-VAASYANRVVMLKDGQI 221
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLdLVAELADRVIVLDDGRI 212
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-221 |
6.19e-58 |
|
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: 183.50 E-value: 6.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKlSNKALSDIR 83
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTLTVKENIML-PLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLP 162
Cdd:cd03262 76 QK-VGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 163 SIIFADEPTGALDSKSTQDLLKrLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLD-VMKDLAEEGMTMVVVTHEmGFAREVADRVIFMDDGRI 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-222 |
7.39e-56 |
|
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: 179.03 E-value: 7.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAqevLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDI 82
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQA---LKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKHdIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRY--EKVAEALNILD---ISDKY---PSELSGGQRQRTSA 154
Cdd:TIGR02315 78 RRR-IGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGRFseEDKERALSALErvgLADKAyqrADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 155 ARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQIF 222
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQvDLAKKYADRIVGLKAGEIV 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-221 |
1.52e-55 |
|
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: 177.06 E-value: 1.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKalsdir 83
Cdd:cd03301 1 VELENVTKRFGNVT----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPS 163
Cdd:cd03301 71 DRDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 164 IIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAA-SYANRVVMLKDGQI 221
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQI 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-221 |
2.27e-55 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 181.11 E-value: 2.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTIlEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLekLSNKals 80
Cdd:COG1118 1 MSI-EVRNISKRFGSFT----LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL--FTNL--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIRKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDtmlDRYEKVAEALNILDIS---DKYPSELSGGQRQRTSAARA 157
Cdd:COG1118 71 PPRERRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKA---EIRARVEELLELVQLEglaDRYPSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616690417 158 FITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPV-AASYANRVVMLKDGQI 221
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEeALELADRVVVMNQGRI 212
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-221 |
3.86e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 176.79 E-value: 3.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKAlsdir 83
Cdd:COG1131 1 IEVRGLTKRYGDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPS 163
Cdd:COG1131 72 RRRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 164 IIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYlEEAERLCDRVAIIDKGRI 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-224 |
4.66e-55 |
|
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: 177.16 E-value: 4.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSdi 82
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKhdIGFIFQEYNLLHTLTVKENIML---PLT--VQKLDKDtmlDRyEKVAEAL---NILDISDKYPSELSGGQRQRTSA 154
Cdd:COG1120 75 RR--IAYVPQEPPAPFGLTVRELVALgryPHLglFGRPSAE---DR-EAVEEALertGLEHLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690417 155 ARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDP-VAASYANRVVMLKDGQIFTE 224
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQ 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-221 |
5.06e-55 |
|
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: 176.54 E-value: 5.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDIR 83
Cdd:cd03261 1 IELRGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTLTVKENIMLPLTVQ-KLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLP 162
Cdd:cd03261 77 RR-MGMLFQSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 163 SIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKI 215
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-225 |
1.39e-54 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 175.39 E-value: 1.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDI 82
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLP 162
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 163 SIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQIFTEL 225
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAEL 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-215 |
1.52e-54 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 177.94 E-value: 1.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTL----LNVLSSiDYISQGSITLKGHKLEKLSNKA 78
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaraiLGLLPP-PGITSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 79 LSDIRKHDIGFIFQE-YNLLH-TLTVKENIMLPLTV-QKLDKDtmlDRYEKVAEALNILDIS------DKYPSELSGGQR 149
Cdd:COG0444 80 LRKIRGREIQMIFQDpMTSLNpVMTVGDQIAEPLRIhGGLSKA---EARERAIELLERVGLPdperrlDRYPHELSGGMR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616690417 150 QRTSAARAFITLPSIIFADEPTGALDSkSTQ----DLLKRLmkmNEEIKTTIIMVTHD-PVAASYANRV-VM 215
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDV-TIQaqilNLLKDL---QRELGLAILFITHDlGVVAEIADRVaVM 224
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-221 |
1.62e-54 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 175.37 E-value: 1.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLsnkalsDIR 83
Cdd:TIGR00968 1 IEIANISKRFGSF----QALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRV------HAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPS 163
Cdd:TIGR00968 71 DRKIGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 164 IIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPV-AASYANRVVMLKDGQI 221
Cdd:TIGR00968 151 VLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEeAMEVADRIVVMSNGKI 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-221 |
2.74e-54 |
|
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: 2.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLsnkalsDIR 83
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL------PPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDtmlDRYEKVAEALNILDISD---KYPSELSGGQRQRTSAARAFIT 160
Cdd:cd03300 71 KRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKA---EIKERVAEALDLVQLEGyanRKPSQLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616690417 161 LPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAA-SYANRVVMLKDGQI 221
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKI 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-220 |
3.96e-53 |
|
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: 169.68 E-value: 3.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLsNKALSDIR 83
Cdd:cd03229 1 LELKNVSKRYGQKT----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KhDIGFIFQEYNLLHTLTVKENIMLPLtvqkldkdtmldryekvaealnildisdkypselSGGQRQRTSAARAFITLPS 163
Cdd:cd03229 76 R-RIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 164 IIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDP-VAASYANRVVMLKDGQ 220
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLdEAARLADRVVVLRDGK 178
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-227 |
7.04e-53 |
|
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: 174.84 E-value: 7.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGnkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKalsdir 83
Cdd:TIGR03265 5 LSIDNIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDtmlDRYEKVAEALNILDISD---KYPSELSGGQRQRTSAARAFIT 160
Cdd:TIGR03265 75 KRDYGIVFQSYALFPNLTVADNIAYGLKNRGMGRA---EVAERVAELLDLVGLPGserKYPGQLSGGQQQRVALARALAT 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 161 LPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAA-SYANRVVMLKDGQIF-----TELYQ 227
Cdd:TIGR03265 152 SPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEAlSMADRIVVMNHGVIEqvgtpQEIYR 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-220 |
5.83e-52 |
|
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: 168.03 E-value: 5.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 5 EVKQLTKIYGNKkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkaLSDIRK 84
Cdd:cd03225 1 ELKNLSFSYPDG--ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 85 HdIGFIFQ--EYNLLhTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLP 162
Cdd:cd03225 76 K-VGLVFQnpDDQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 163 SIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHDP-VAASYANRVVMLKDGQ 220
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLdLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-221 |
6.38e-52 |
|
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: 176.25 E-value: 6.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MT-ILEVKQLTKIYGNKkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTL---LNVLSSIDYISQGSITLKGHKLEKLSN 76
Cdd:COG1123 1 MTpLLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLalaLMGLLPHGGRISGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 77 KalsdIRKHDIGFIFQEY-NLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAA 155
Cdd:COG1123 79 A----LRGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 156 RAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDP-VAASYANRVVMLKDGQI 221
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLgVVAEIADRVVVMDDGRI 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-224 |
1.52e-51 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 167.65 E-value: 1.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDI 82
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLP 162
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616690417 163 SIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQIFTE 224
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-221 |
1.53e-51 |
|
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: 167.90 E-value: 1.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTIlEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKals 80
Cdd:cd03296 1 MSI-EVRNVSKRFGDFV----ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDV--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIRKHDIGFIFQEYNLLHTLTVKENIMLPLTVQK----LDKDTMldrYEKVAEALNILDIS---DKYPSELSGGQRQRTS 153
Cdd:cd03296 70 PVQERNVGFVFQHYALFRHMTVFDNVAFGLRVKPrserPPEAEI---RAKVHELLKLVQLDwlaDRYPAQLSGGQRQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 154 AARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAA-SYANRVVMLKDGQI 221
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRI 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-221 |
1.53e-51 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 177.61 E-value: 1.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MT-ILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKAL 79
Cdd:PRK10535 1 MTaLLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 80 SDIRKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFI 159
Cdd:PRK10535 81 AQLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616690417 160 TLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIImVTHDPVAASYANRVVMLKDGQI 221
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII-VTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-221 |
4.37e-51 |
|
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: 167.82 E-value: 4.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNK-----------KMAQEVL---------RDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGS 63
Cdd:cd03294 1 IKIKGLYKIFGKNpqkafkllakgKSKEEILkktgqtvgvNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 64 ITLKGHKLEKLSNKALSDIRKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSE 143
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 144 LSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAA-SYANRVVMLKDGQI 221
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEAlRLGDRIAIMKDGRL 239
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-221 |
5.93e-51 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 169.60 E-value: 5.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 5 EVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDIRk 84
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 85 HDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDtmlDRYEKVAEALNILDISDK---YPSELSGGQRQRTSAARAFITL 161
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKA---EIKARVTELLELVGLSDKadrYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690417 162 PSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEmDVVKRICDRVAVIDAGRL 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-222 |
5.98e-51 |
|
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: 164.15 E-value: 5.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 5 EVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDIrk 84
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 85 hdIGFIFQeynllhtltvkenimlpltvqkldkdtmldryekVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSI 164
Cdd:cd03214 75 --IAYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 165 IFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDP-VAASYANRVVMLKDGQIF 222
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-221 |
1.54e-49 |
|
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: 161.81 E-value: 1.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKMAqevLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDIR 83
Cdd:cd03292 1 IEFINVTKTYPNGTAA---LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTLTVKENIMLPLTV-QKLDKDTMldryEKVAEALNILDISDK---YPSELSGGQRQRTSAARAFI 159
Cdd:cd03292 78 RK-IGVVFQDFRLLPDRNVYENVAFALEVtGVPPREIR----KRVPAALELVGLSHKhraLPAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 160 TLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHDP-VAASYANRVVMLKDGQI 221
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKeLVDTTRHRVIALERGKL 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-221 |
2.57e-49 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 165.64 E-value: 2.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTIlEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkals 80
Cdd:PRK10851 1 MSI-EIANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 dIRKHDIGFIFQEYNLLHTLTVKENIMLPLTVqkLDKDTMLDRYE---KVAEALNILDIS---DKYPSELSGGQRQRTSA 154
Cdd:PRK10851 71 -ARDRKVGFVFQHYALFRHMTVFDNIAFGLTV--LPRRERPNAAAikaKVTQLLEMVQLAhlaDRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 155 ARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDqEEAMEVADRVVVMSQGNI 215
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-221 |
3.85e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 155.74 E-value: 3.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALSDIR 83
Cdd:COG4619 1 LELEGLSFRVGGKP----ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDG---KPLSAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTlTVKENIMLPLTVQKLDKDTmlDRYEKVAEALNI-LDISDKYPSELSGGQRQRTSAARAFITLP 162
Cdd:COG4619 74 RQ-VAYVPQEPALWGG-TVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 163 SIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDP-VAASYANRVVMLKDGQI 221
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPeQIERVADRVLTLEAGRL 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
4.83e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.40 E-value: 4.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKlsnkals 80
Cdd:COG1121 4 MPAIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 diRKHDIGFIFQEYNLLHT--LTVKENIMLPLTVQK-----LDKDtmlDRyEKVAEAL---NILDISDKYPSELSGGQRQ 150
Cdd:COG1121 73 --ARRRIGYVPQRAEVDWDfpITVRDVVLMGRYGRRglfrrPSRA---DR-EAVDEALervGLEDLADRPIGELSGGQQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 151 RTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHDP-VAASYANRVVMLKDGQIF 222
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLgAVREYFDRVLLLNRGLVA 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-220 |
9.23e-47 |
|
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: 153.31 E-value: 9.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkaLSDIR 83
Cdd:cd03228 1 IEFKNVSFSYPGR--PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTlTVKENImlpltvqkldkdtmldryekvaealnildisdkypseLSGGQRQRTSAARAFITLPS 163
Cdd:cd03228 76 KN-IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 164 IIFADEPTGALDSKSTQDLLKRLMKMNEEikTTIIMVTHDPVAASYANRVVMLKDGQ 220
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKG--KTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-221 |
1.48e-46 |
|
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: 152.94 E-value: 1.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKAlsdir 83
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENImlpltvqkldkdtmldryekvaealnildisdkypsELSGGQRQRTSAARAFITLPS 163
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 164 IIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-221 |
2.74e-46 |
|
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: 154.42 E-value: 2.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqevLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKalsdir 83
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPS 163
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 164 IIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPV-AASYANRVVMLKDGQI 221
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEeAWALADKVAIMLNGKL 208
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-221 |
6.58e-46 |
|
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: 153.61 E-value: 6.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKMAqevLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALSDIR 83
Cdd:cd03295 1 IEFENVTKRYGGGKKA---VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDG---EDIREQDPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTmldRYEKVAEALNILDI-----SDKYPSELSGGQRQRTSAARAF 158
Cdd:cd03295 75 RK-IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEK---IRERADELLALVGLdpaefADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616690417 159 ITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDiDEAFRLADRIAIMKNGEI 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-221 |
2.75e-45 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 151.56 E-value: 2.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLS-SIDYISQ----GSITLKGHKLEKLSNKA 78
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrLNDLIPGapdeGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 79 LSDIRKhdIGFIFQEYNLLHtLTVKENIMLPLTVQKLDKDTMLDryEKVAEALNILDISDK-----YPSELSGGQRQRTS 153
Cdd:cd03260 77 LELRRR--VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELD--ERVEEALRKAALWDEvkdrlHALGLSGGQQQRLC 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 154 AARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIktTIIMVTHDPV-AASYANRVVMLKDGQI 221
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQqAARVADRTAFLLNGRL 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-240 |
2.92e-45 |
|
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: 151.93 E-value: 2.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKAlsdir 83
Cdd:COG4555 2 IEVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPS 163
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 164 IIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHDP-VAASYANRVVMLKDGQI--------FTELYQGDDDKHT 234
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMqEVEALCDRVVILHKGKVvaqgsldeLREEIGEENLEDA 231
|
....*.
gi 616690417 235 FFKEII 240
Cdd:COG4555 232 FVALIG 237
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-222 |
3.93e-45 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 152.61 E-value: 3.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYG-NKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDI 82
Cdd:TIGR04521 1 IKLKNVSYIYQpGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKHdIGFIFQ--EYNLLHTlTVKENIMLPLTVQKLDKDtmlDRYEKVAEALNILDISDKY----PSELSGGQRQRTSAAR 156
Cdd:TIGR04521 81 RKK-VGLVFQfpEHQLFEE-TVYKDIAFGPKNLGLSEE---EAEERVKEALELVGLDEEYlersPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 157 AFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQIF 222
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIV 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-229 |
7.16e-45 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 150.93 E-value: 7.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTIlEVKQLTKIYGNkkmaQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKL---EKLSNK 77
Cdd:COG4161 1 MSI-QLKNINCFYGS----HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 78 ALSDIRKhDIGFIFQEYNLLHTLTVKEN-IMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAAR 156
Cdd:COG4161 76 AIRLLRQ-KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616690417 157 AFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIImVTHD-PVAASYANRVVMLKDGQIfteLYQGD 229
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVI-VTHEvEFARKVASQVVYMEKGRI---IEQGD 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-231 |
9.78e-45 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 150.55 E-value: 9.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTIlEVKQLTKIYGnkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALS 80
Cdd:PRK11124 1 MSI-QLNGINCFYG----AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIR--KHDIGFIFQEYNLLHTLTVKEN-IMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARA 157
Cdd:PRK11124 76 AIRelRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616690417 158 FITLPSIIFADEPTGALDSKSTQDLLKrLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQIfteLYQGDDD 231
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVS-IIRELAETGITQVIVTHEvEVARKTASRVVYMENGHI---VEQGDAS 226
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-221 |
5.43e-44 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 150.24 E-value: 5.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 5 EVKQLTKIYGNKKMAqevLRDINMSVEEGEFIAIMGPSGSGKTTLL---NVLssIDyISQGSITLKGhkleklsnkalSD 81
Cdd:COG1125 3 EFENVTKRYPDGTVA---VDDLSLTIPAGEFTVLVGPSGCGKTTTLrmiNRL--IE-PTSGRILIDG-----------ED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IRKHD-------IGFIFQEYNLLHTLTVKENIMlplTVQKL---DKDTMLDRyekVAEALNILDIS-----DKYPSELSG 146
Cdd:COG1125 66 IRDLDpvelrrrIGYVIQQIGLFPHMTVAENIA---TVPRLlgwDKERIRAR---VDELLELVGLDpeeyrDRYPHELSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 147 GQRQRTSAARAFITLPSIIFADEPTGALDS---KSTQDLLKRLmkmNEEIKTTIIMVTHDpV--AASYANRVVMLKDGQI 221
Cdd:COG1125 140 GQQQRVGVARALAADPPILLMDEPFGALDPitrEQLQDELLRL---QRELGKTIVFVTHD-IdeALKLGDRIAVMREGRI 215
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
3-221 |
1.31e-43 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 150.61 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKmaqevLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKalsdi 82
Cdd:NF040840 1 MIRIENLSKDWKEFK-----LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPE----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 rKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLP 162
Cdd:NF040840 71 -KRGIAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 163 SIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:NF040840 150 KLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNfEEALSLADRVGIMLNGRL 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-217 |
6.42e-43 |
|
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: 144.98 E-value: 6.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 5 EVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKalsdirk 84
Cdd:cd03235 1 EVEDLTVSYGGH----PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 85 hdIGFIFQEYNLLHT--LTVKENIMLPLT-----VQKLDKDtmldRYEKVAEAL---NILDISDKYPSELSGGQRQRTSA 154
Cdd:cd03235 70 --IGYVPQRRSIDRDfpISVRDVVLMGLYghkglFRRLSKA----DKAKVDEALervGLSELADRQIGELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616690417 155 ARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHDPVAAS-YANRVVMLK 217
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLeYFDRVLLLN 206
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-232 |
7.79e-43 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 145.28 E-value: 7.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKMaqevlrDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkalsdIR 83
Cdd:COG3840 2 LRLDDLTYRYGDFPL------RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP------PA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENIMLPLTVQ-KLDKDtmlDRyEKVAEAL---NILDISDKYPSELSGGQRQRTSAARAFI 159
Cdd:COG3840 70 ERPVSMLFQENNLFPHLTVAQNIGLGLRPGlKLTAE---QR-AQVEQALervGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616690417 160 TLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPV-AASYANRVVMLKDGQIfteLYQGDDDK 232
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEdAARIADRVLLVADGRI---AADGPTAA 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-171 |
9.53e-43 |
|
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: 142.40 E-value: 9.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 23 LRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALsdiRKHdIGFIFQEYNLLHTLTV 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL---RKE-IGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 103 KENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISD----KYPSELSGGQRQRTSAARAFITLPSIIFADEPT 171
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-221 |
1.74e-42 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 144.94 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGnkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKG----------HKLEK 73
Cdd:COG4598 9 LEVRDLHKSFG----DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdrdGELVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 74 LSNKALSDIRKHdIGFIFQEYNLLHTLTVKENIML-PLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRT 152
Cdd:COG4598 85 ADRRQLQRIRTR-LGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 153 SAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKtTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEmGFARDVSSHVVFLHQGRI 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-203 |
2.49e-42 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 145.00 E-value: 2.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNkals 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 dirkhDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDtmlDRYEKVAEALNILDISD---KYPSELSGGQRQRTSAARA 157
Cdd:COG4525 77 -----DRGVVFQKDALLPWLNVLDNVAFGLRLRGVPKA---ERRARAEELLALVGLADfarRRIWQLSGGMRQRVGIARA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 616690417 158 FITLPSIIFADEPTGALDS---KSTQDLLKRLMKmneEIKTTIIMVTHD 203
Cdd:COG4525 149 LAADPRFLLMDEPFGALDAltrEQMQELLLDVWQ---RTGKGVFLITHS 194
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-221 |
2.65e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 144.51 E-value: 2.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKiygnKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLL---NVLSSID--YISQGSITLKGHKLEKLS 75
Cdd:PRK11264 1 MSAIEVKNLVK----KFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLrciNLLEQPEagTIRVGDITIDTARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 76 NKALSDIRKHdIGFIFQEYNLLHTLTVKENIML-PLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSA 154
Cdd:PRK11264 77 KGLIRQLRQH-VGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 155 ARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEmSFARDVADRAIFMDQGRI 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-220 |
3.71e-42 |
|
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: 141.23 E-value: 3.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 5 EVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALsdirK 84
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 85 HDIGFIFQeynllhtltvkenimlpltvqkldkdtmldryekvaealnildisdkypseLSGGQRQRTSAARAFITLPSI 164
Cdd:cd00267 73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 165 IFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHDP-VAASYANRVVMLKDGQ 220
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPeLAELAADRVIVLKDGK 157
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-221 |
8.91e-42 |
|
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: 151.14 E-value: 8.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkaLSDIR 83
Cdd:COG2274 474 IELENVSFRYPGD--SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTlTVKENIMLpltvqkLDKDTMLDRYEKVAEALNILDISDKYP-----------SELSGGQRQRT 152
Cdd:COG2274 549 RQ-IGVVLQDVFLFSG-TIRENITL------GDPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 153 SAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIktTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-221 |
3.13e-41 |
|
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: 140.51 E-value: 3.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 32 EGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDIRKHDIGFIFQEYNLLHTLTVKENIMLPLT 111
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 112 VQKLDKDTmlDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNE 191
Cdd:cd03297 102 RKRNREDR--ISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|.
gi 616690417 192 EIKTTIIMVTHDPVAASY-ANRVVMLKDGQI 221
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-219 |
3.21e-41 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 141.06 E-value: 3.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 23 LRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNkalsdirkhDIGFIFQEYNLLHTLTV 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---------DRMVVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 103 KENIMLPL-----TVQKLDKDTMLDRYekvAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSK 177
Cdd:TIGR01184 72 RENIALAVdrvlpDLSKSERRAIVEEH---IALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 616690417 178 STQDLLKRLMKMNEEIKTTIIMVTHDPVAASY-ANRVVMLKDG 219
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDVDEALLlSDRVVMLTNG 191
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-224 |
1.09e-40 |
|
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: 140.56 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGnkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkaLS 80
Cdd:COG0411 2 DPLLEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP---PH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIRKHDIGFIFQEYNLLHTLTVKENIMLPLTVQK----LDKDTMLDRY--------EKVAEALNILDISDK---YPSELS 145
Cdd:COG0411 75 RIARLGIARTFQNPRLFPELTVLENVLVAAHARLgrglLAALLRLPRArreerearERAEELLERVGLADRadePAGNLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 146 GGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQIFTE 224
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDmDLVMGLADRIVVLDFGRVIAE 234
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-221 |
1.44e-40 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 143.16 E-value: 1.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKals 80
Cdd:PRK09452 12 SPLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 dirKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRyekVAEALNIL---DISDKYPSELSGGQRQRTSAARA 157
Cdd:PRK09452 85 ---NRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPR---VMEALRMVqleEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 158 FITLPSIIFADEPTGALD---SKSTQDLLKRLMKmneEIKTTIIMVTHDPVAA-SYANRVVMLKDGQI 221
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDyklRKQMQNELKALQR---KLGITFVFVTHDQEEAlTMSDRIVVMRDGRI 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-229 |
1.46e-40 |
|
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: 146.44 E-value: 1.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkaLSDIR 83
Cdd:COG4988 337 IELEDVSFSYPG---GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLD---PASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTlTVKENIML--PltvqKLDKDTMldryEKVAEALNILDISDKYP-----------SELSGGQRQ 150
Cdd:COG4988 411 RQ-IAWVPQNPYLFAG-TIRENLRLgrP----DASDEEL----EAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQ 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 151 RTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEikTTIIMVTHDPVAASYANRVVMLKDGQI-----FTEL 225
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLAQADRILVLDDGRIveqgtHEEL 558
|
....
gi 616690417 226 YQGD 229
Cdd:COG4988 559 LAKN 562
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-224 |
2.95e-40 |
|
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: 138.72 E-value: 2.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNkalSDIR 83
Cdd:cd03219 1 LEVRGLTKRFGGLV----ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP---HEIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENIMLPLTVQK-------LDKDTMLDRYEKVAEALNILDISDKY---PSELSGGQRQRTS 153
Cdd:cd03219 74 RLGIGRTFQIPRLFPELTVLENVMVAAQARTgsglllaRARREEREARERAEELLERVGLADLAdrpAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616690417 154 AARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHD-PVAASYANRVVMLKDGQIFTE 224
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDmDVVMSLADRVTVLDQGRVIAE 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-221 |
1.61e-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: 143.29 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKT----TLLNVLSSIDYISQGSITLKGHKLEKLSN 76
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 77 KALSDIRKHDIGFIFQE----YNLLHTltVKENIMLPLTVQKldkdtMLDRYEKVAEALNILD---ISD------KYPSE 143
Cdd:COG4172 84 RELRRIRGNRIAMIFQEpmtsLNPLHT--IGKQIAEVLRLHR-----GLSGAAARARALELLErvgIPDperrldAYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 144 LSGGQRQRTSAARAFITLPSIIFADEPTGALDSkSTQ----DLLKRLMKmneEIKTTIIMVTHD-PVAASYANRVVMLKD 218
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVQaqilDLLKDLQR---ELGMALLLITHDlGVVRRFADRVAVMRQ 232
|
...
gi 616690417 219 GQI 221
Cdd:COG4172 233 GEI 235
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-252 |
2.98e-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: 138.78 E-value: 2.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 38 IMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKAlsdIRKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDK 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDG---EDVTNVP---PHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 118 DTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTI 197
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690417 198 IMVTHDPVAA-SYANRVVMLKDGQIFT-----ELYQgdDDKHTFFKEIIRVQSVLGGINYE 252
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKGKIAQigtpeEIYE--EPANLFVARFIGEINVFEATVIE 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-221 |
5.08e-39 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 135.61 E-value: 5.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGnkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLeKLSNKALSDI 82
Cdd:PRK09493 1 MIEFKNVSKHFG----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-NDPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKhDIGFIFQEYNLLHTLTVKENIML-PLTVQKLDKDTMldryEKVAEAL----NILDISDKYPSELSGGQRQRTSAARA 157
Cdd:PRK09493 76 RQ-EAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEA----EKQARELlakvGLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616690417 158 FITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEiGFAEKVASRLIFIDKGRI 214
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-227 |
2.25e-38 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 136.90 E-value: 2.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKkmaQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLsnkals 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIRKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFIT 160
Cdd:PRK11650 72 EPADRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 161 LPSIIFADEPTGALDSK-------STQDLLKRLmkmneeiKTTIIMVTHDPVAA-SYANRVVMLKDG---QIFT--ELYQ 227
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAKlrvqmrlEIQRLHRRL-------KTTSLYVTHDQVEAmTLADRVVVMNGGvaeQIGTpvEVYE 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-221 |
2.95e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 140.30 E-value: 2.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 20 QEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkaLSDIRKHdIGFIFQEYNLLHT 99
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRRQ-IGVVPQDTFLFSG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 100 lTVKENIMLPltvqklDKDTMLDRYEKVAEALNILDISDKYP-----------SELSGGQRQRTSAARAFITLPSIIFAD 168
Cdd:COG1132 429 -TIRENIRYG------RPDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 616690417 169 EPTGALDSKS---TQDLLKRLMKmneeiKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:COG1132 502 EATSALDTETealIQEALERLMK-----GRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-221 |
5.17e-38 |
|
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: 132.29 E-value: 5.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 27 NMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhkleklSNKALSDIRKHDIGFIFQEYNLLHTLTVKENI 106
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVND------QSHTGLAPYQRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 107 ML----PLTVQKLDKDTMldryEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDL 182
Cdd:TIGR01277 92 GLglhpGLKLNAEQQEKV----VDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 616690417 183 LKRLMKMNEEIKTTIIMVTHDPV-AASYANRVVMLKDGQI 221
Cdd:TIGR01277 168 LALVKQLCSERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-220 |
9.58e-38 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 135.73 E-value: 9.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGnkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLeklsnkALSDI 82
Cdd:PRK11607 19 LLEIRNLTKSFD----GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL------SHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLP 162
Cdd:PRK11607 89 YQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 163 SIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQ 220
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDqEEAMTMAGRIAIMNRGK 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
1.18e-37 |
|
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: 131.47 E-value: 1.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLeklsNKALSDIR 83
Cdd:cd03263 1 LQIRNLTKTYKKGT--KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPS 163
Cdd:cd03263 75 QS-LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 164 IIFADEPTGALDSKSTQDLLKRLMKMNEeiKTTIIMVTHDP-VAASYANRVVMLKDGQI 221
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMdEAEALCDRIAIMSDGKL 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-222 |
3.00e-37 |
|
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: 131.36 E-value: 3.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQG-SITLKGHKLEKLSnkaL 79
Cdd:COG1119 1 DPLLELRNVTVRRGGKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGED---V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 80 SDIRKHdIGFI---FQEYnLLHTLTVKE--------NIMLPLTVQkldkDTMLDRYEKVAEALNILDISDKYPSELSGGQ 148
Cdd:COG1119 74 WELRKR-IGLVspaLQLR-FPRDETVLDvvlsgffdSIGLYREPT----DEQRERARELLELLGLAHLADRPFGTLSQGE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616690417 149 RQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTH--DPVAASYaNRVVMLKDGQIF 222
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHhvEEIPPGI-THVLLLKDGRVV 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-221 |
4.45e-37 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 129.99 E-value: 4.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAqevLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDI 82
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQA---LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKHdIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLP 162
Cdd:PRK10908 78 RRQ-IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 163 SIIFADEPTGALDSKSTQDLLkRLMKMNEEIKTTIIMVTHDPVAASYAN-RVVMLKDGQI 221
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGIL-RLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-221 |
4.86e-37 |
|
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: 133.30 E-value: 4.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 25 DINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLekLSNKALSDIRKHD--IGFIFQEYNLLHTLTV 102
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGIFLPPHRrrIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 103 KENIMLplTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDL 182
Cdd:COG4148 95 RGNLLY--GRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 616690417 183 LKRLMKMNEEIKTTIIMVTHDPV-AASYANRVVMLKDGQI 221
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDeVARLADHVVLLEQGRV 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-221 |
7.48e-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: 129.48 E-value: 7.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGnkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALSDIR 83
Cdd:cd03224 1 LEVENLNAGYG----KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG---RDITGLPPHERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTmlDRYEKVAEALNIL-DISDKYPSELSGGQRQRTSAARAFITLP 162
Cdd:cd03224 74 RAGIGYVPEGRRIFPELTVEENLLLGAYARRRAKRK--ARLERVYELFPRLkERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 163 SIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNaRFALEIADRAYVLERGRV 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-232 |
1.21e-36 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 129.32 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEvkQLTKIYGNKKMAqevlrdINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhkleklSNKALS 80
Cdd:PRK10771 1 MLKLT--DITWLYHHLPMR------FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG------QDHTTT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIRKHDIGFIFQEYNLLHTLTVKENIMLPLTVQ-KLDKDTMlDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFI 159
Cdd:PRK10771 67 PPSRRPVSMLFQENNLFSHLTVAQNIGLGLNPGlKLNAAQR-EKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616690417 160 TLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTH---DpvAASYANRVVMLKDGQIFtelYQGDDDK 232
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHsleD--AARIAPRSLVVADGRIA---WDGPTDE 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-224 |
2.17e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 129.75 E-value: 2.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYgnKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALSD 81
Cdd:PRK13635 4 EIIRVEHISFRY--PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IRKHdIGFIFQEY-NLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFIT 160
Cdd:PRK13635 79 VRRQ-VGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616690417 161 LPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQIFTE 224
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-221 |
2.33e-36 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 126.56 E-value: 2.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLsnkALSDIR 83
Cdd:cd03246 1 LEVENVSFRYPGAE--PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW---DPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLhTLTVKENImlpltvqkldkdtmldryekvaealnildisdkypseLSGGQRQRTSAARAFITLPS 163
Cdd:cd03246 76 DH-VGYLPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 164 IIFADEPTGALDSKSTQdLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:cd03246 117 ILVLDEPNSHLDVEGER-ALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-221 |
2.90e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 129.03 E-value: 2.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSItLKGhkleklsNKALSD 81
Cdd:PRK11247 11 TPLLLNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG-------TAPLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IRKhDIGFIFQEYNLLHTLTVKENIMLPLtvqkldKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITL 161
Cdd:PRK11247 79 ARE-DTRLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616690417 162 PSIIFADEPTGALDSKS---TQDLLKRLMkmnEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:PRK11247 152 PGLLLLDEPLGALDALTrieMQDLIESLW---QQHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-221 |
3.18e-36 |
|
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: 134.51 E-value: 3.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLS-SIDYiSQGSITLKGHKLEKLSNKALsdi 82
Cdd:COG4987 334 LELEDVSFRYPGA--GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLrFLDP-QSGSITLGGVDLRDLDEDDL--- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKHdIGFIFQEYNLLHTlTVKENIML--PltvqKLDKDTMLDryekVAEALNILDISDKYP-----------SELSGGQR 149
Cdd:COG4987 408 RRR-IAVVPQRPHLFDT-TLRENLRLarP----DATDEELWA----ALERVGLGDWLAALPdgldtwlgeggRRLSGGER 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616690417 150 QRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEikTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG--RTVLLITHRLAGLERMDRILVLEDGRI 547
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-215 |
5.60e-36 |
|
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: 126.82 E-value: 5.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEklsnKALSDIR 83
Cdd:COG4133 3 LEAENLSCRRGERL----LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR----DAREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTLTVKENIMLpltVQKLDKDTM-LDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLP 162
Cdd:COG4133 75 RR-LAYLGHADGLKPELTVRENLRF---WAALYGLRAdREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 616690417 163 SIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHDPVAASYANRVVM 215
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLELAAARVLDL 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-228 |
7.53e-36 |
|
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: 126.13 E-value: 7.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 21 EVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSS--IDYISQGSITLKGHKLEKLSNKALsdirkhdIGFIFQEYNLLH 98
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKI-------IGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 99 TLTVKENIMlpltvqkldkdtmldryekVAEALnildisdkypSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKS 178
Cdd:cd03213 96 TLTVRETLM-------------------FAAKL----------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 616690417 179 TQDLLKRLMKMNEEIKtTIIMVTHDPVAASYA--NRVVMLKDGQIfteLYQG 228
Cdd:cd03213 147 ALQVMSLLRRLADTGR-TIICSIHQPSSEIFElfDKLLLLSQGRV---IYFG 194
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-224 |
1.33e-35 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 127.12 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 5 EVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSdiRK 84
Cdd:COG4604 3 EIKNVSKRYGGKV----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA--KR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 85 hdIGFIFQEYNLLHTLTVKENIML---P-----LTVQkldkdtmlDRyEKVAEA---LNILDISDKYPSELSGGQRQrts 153
Cdd:COG4604 77 --LAILRQENHINSRLTVRELVAFgrfPyskgrLTAE--------DR-EIIDEAiayLDLEDLADRYLDELSGGQRQ--- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 154 aaRAFI--TL---PSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQIFTE 224
Cdd:COG4604 143 --RAFIamVLaqdTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDiNFASCYADHIVAMKDGRVVAQ 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-221 |
1.65e-35 |
|
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: 125.78 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNkkMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkaLSDIR 83
Cdd:cd03245 3 IEFRNVSFSYPN--QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTlTVKENIMLPLTVQKlDKDTMldryeKVAEALNILDISDKYP-----------SELSGGQRQRT 152
Cdd:cd03245 78 RN-IGYVPQDVTLFYG-TLRDNITLGAPLAD-DERIL-----RAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 153 SAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEikTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
3.16e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 127.51 E-value: 3.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTIlEVKQLTKIYgNKKMAQE--VLRDINMSVEEGEFIAIMGPSGSGKTTL---LNVL-----SSIDYI----------- 59
Cdd:PRK13651 1 MQI-KVKNIVKIF-NKKLPTElkALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALllpdtGTIEWIfkdeknkkktk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 60 ----SQGSITLKGHKLEKLsnKALSDIRKHdIGFIFQ--EYNLLHTlTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNi 133
Cdd:PRK13651 79 ekekVLEKLVIQKTRFKKI--KKIKEIRRR-VGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVG- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 134 LDIS--DKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKtTIIMVTHD-PVAASYA 210
Cdd:PRK13651 154 LDESylQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDlDNVLEWT 232
|
250
....*....|.
gi 616690417 211 NRVVMLKDGQI 221
Cdd:PRK13651 233 KRTIFFKDGKI 243
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-224 |
3.17e-35 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 125.17 E-value: 3.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNkkmaQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkalSDIR 83
Cdd:cd03265 1 IEVENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP----REVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPS 163
Cdd:cd03265 73 RR-IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616690417 164 IIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQIFTE 224
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYmEEAEQLCDRVAIIDHGRIIAE 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-221 |
4.00e-35 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 128.61 E-value: 4.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKKMAqevlRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSItlkghkleKLSNKALS 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVIS----KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL--------FIGEKRMN 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DI--RKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAF 158
Cdd:PRK11000 69 DVppAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616690417 159 ITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAA-SYANRVVMLKDGQI 221
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAmTLADKIVVLDAGRV 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-243 |
6.45e-35 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 125.51 E-value: 6.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSI---DYISQGSITLKGHKLEKlSNKA 78
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQR-EGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 79 LSDIRKH--DIGFIFQEYNLLHTLTVKENIML------PL------TVQKLDKDTMLDRYEKVAEAlnilDISDKYPSEL 144
Cdd:PRK09984 78 ARDIRKSraNTGYIFQQFNLVNRLSVLENVLIgalgstPFwrtcfsWFTREQKQRALQALTRVGMV----HFAHQRVSTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 145 SGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQIFT 223
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQGHVFY 233
|
250 260
....*....|....*....|...
gi 616690417 224 E--LYQGDDDKHT-FFKEIIRVQ 243
Cdd:PRK09984 234 DgsSQQFDNERFDhLYRSINRVE 256
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
8-221 |
7.76e-35 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 124.14 E-value: 7.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 8 QLTKI---YGNKKMaqevlrDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhkleklSNKALSDIRK 84
Cdd:cd03298 2 RLDKIrfsYGEQPM------HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING------VDVTAAPPAD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 85 HDIGFIFQEYNLLHTLTVKENIMLPLtVQKLdKDTMLDRyEKVAEALNILDISDK---YPSELSGGQRQRTSAARAFITL 161
Cdd:cd03298 70 RPVSMLFQENNLFAHLTVEQNVGLGL-SPGL-KLTAEDR-QAIEVALARVGLAGLekrLPGELSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690417 162 PSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPV-AASYANRVVMLKDGQI 221
Cdd:cd03298 147 KPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGRI 207
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-224 |
8.56e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 125.08 E-value: 8.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNkkmaQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLE---------KL 74
Cdd:PRK10619 6 LNVIDLHKRYGE----HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 75 SNKALSDIRKHDIGFIFQEYNLLHTLTVKENIM-LPLTVQKLDKDTMLDRYEKVAEALNILDIS-DKYPSELSGGQRQRT 152
Cdd:PRK10619 82 ADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 153 SAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIImVTHD-PVAASYANRVVMLKDGQIFTE 224
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEmGFARHVSSHVIFLHQGKIEEE 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-243 |
1.18e-34 |
|
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: 124.19 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 20 QEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLsnkALSDIRKHdIGFIFQEYNLLHT 99
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL---NLRWLRSQ-IGLVSQEPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 100 lTVKENIMLPltvqklDKDTMLDRYEKVAEALNILDISDKYP-----------SELSGGQRQRTSAARAFITLPSIIFAD 168
Cdd:cd03249 92 -TIAENIRYG------KPDATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 169 EPTGALDSKST---QDLLKRLMKmneeiKTTIIMVTHDPVAASYANRVVMLKDGQI-----FTELYQgdddKHTFFKEII 240
Cdd:cd03249 165 EATSALDAESEklvQEALDRAMK-----GRTTIVIAHRLSTIRNADLIAVLQNGQVveqgtHDELMA----QKGVYAKLV 235
|
...
gi 616690417 241 RVQ 243
Cdd:cd03249 236 KAQ 238
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-221 |
1.62e-34 |
|
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: 129.42 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNKK--MAQEV-----LRDINMSVEEGEFIAIMGPSGSGKTTL-LNVLSSIDyiSQGSITLKGHKLEK 73
Cdd:COG4172 274 PLLEARDLKVWFPIKRglFRRTVghvkaVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLIP--SEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 74 LSNKALSDIRKHdIGFIFQE-YNLLHT-LTVKENIMLPLTVQ--KLDKDtmlDRYEKVAEALNI--LD--ISDKYPSELS 145
Cdd:COG4172 352 LSRRALRPLRRR-MQVVFQDpFGSLSPrMTVGQIIAEGLRVHgpGLSAA---ERRARVAEALEEvgLDpaARHRYPHEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 146 GGQRQRTSAARAFITLPSIIFADEPTGALDsKSTQ----DLLKRLmkmNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQ 220
Cdd:COG4172 428 GGQRQRIAIARALILEPKLLVLDEPTSALD-VSVQaqilDLLRDL---QREHGLAYLFISHDlAVVRALAHRVMVMKDGK 503
|
.
gi 616690417 221 I 221
Cdd:COG4172 504 V 504
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-221 |
1.63e-34 |
|
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: 122.75 E-value: 1.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 5 EVKQLTKIYGNKkmaQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKAlsdiRK 84
Cdd:cd03226 1 RIENISFSYKKG---TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKE----RR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 85 HDIGFIFQE-YNLLHTLTVKENIMLPLTvqklDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPS 163
Cdd:cd03226 71 KSIGYVMQDvDYQLFTDSVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616690417 164 IIFADEPTGALDSKSTQ---DLLKRLMKMneeiKTTIIMVTHDP-VAASYANRVVMLKDGQI 221
Cdd:cd03226 147 LLIFDEPTSGLDYKNMErvgELIRELAAQ----GKAVIVITHDYeFLAKVCDRVLLLANGAI 204
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-221 |
1.68e-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: 126.77 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 25 DINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDIRKHDIGFIFQEYNLLHTLTVKE 104
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 105 NimLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLK 184
Cdd:TIGR02142 95 N--LRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 616690417 185 RLMKMNEEIKTTIIMVTHDPV-AASYANRVVMLKDGQI 221
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQeVLRLADRVVVLEDGRV 210
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-221 |
1.00e-33 |
|
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: 121.57 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKMAqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkaLSDIR 83
Cdd:cd03251 1 VEFKNVTFRYPGDGPP--VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTlTVKENIMLPltvqklDKDTMLDRYEKVAEALNILDISDKYP-----------SELSGGQRQRT 152
Cdd:cd03251 76 RQ-IGLVSQDVFLFND-TVAENIAYG------RPGATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616690417 153 SAARAFITLPSIIFADEPTGALDSKS---TQDLLKRLMKMneeiKTTIImVTHDPVAASYANRVVMLKDGQI 221
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESerlVQAALERLMKN----RTTFV-IAHRLSTIENADRIVVLEDGKI 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-221 |
4.40e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 121.31 E-value: 4.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTIlEVKQLTKIYgNKKM--AQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKa 78
Cdd:PRK13637 1 MSI-KIENLTHIY-MEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 79 LSDIRKHdIGFIFQ--EYNLLHTlTVKENIMLPLTVQKLDKDTMLDRyekVAEALNIL-----DISDKYPSELSGGQRQR 151
Cdd:PRK13637 78 LSDIRKK-VGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENR---VKRAMNIVgldyeDYKDKSPFELSGGQKRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616690417 152 TSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTH--DPVaASYANRVVMLKDGQI 221
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHsmEDV-AKLADRIIVMNKGKC 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-221 |
5.87e-33 |
|
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: 119.39 E-value: 5.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhkLEKLSNKALSDI 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RkhdIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLP 162
Cdd:cd03266 79 R---LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 163 SIIFADEPTGALDSKSTQDLLKRLMKMNEEIKtTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHImQEVERLCDRVVVLHRGRV 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-202 |
1.02e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 119.76 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSI-DYISQ----GSITLKGHKLekLSN 76
Cdd:COG1117 10 PKIEVRNLNVYYGDKQ----ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIPGarveGEILLDGEDI--YDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 77 KA-LSDIRKHdIGFIFQEYNLLhTLTVKENIMLPLTVQKLDKDTMLDryEKVAEAL----------NILdisDKYPSELS 145
Cdd:COG1117 84 DVdVVELRRR-VGMVFQKPNPF-PKSIYDNVAYGLRLHGIKSKSELD--EIVEESLrkaalwdevkDRL---KKSALGLS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 146 GGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQ---DLLKRLMKmneeiKTTIIMVTH 202
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAkieELILELKK-----DYTIVIVTH 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-242 |
1.35e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.71 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 5 EVKQLTKIYGNkkMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALSDIRK 84
Cdd:PRK13632 9 KVENVSFSYPN--SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG---ITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 85 HdIGFIFQEY-NLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPS 163
Cdd:PRK13632 84 K-IGIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 164 IIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQIfteLYQGDDDKHTFFKEIIRV 242
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL---IAQGKPKEILNNKEILEK 238
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
25-221 |
1.69e-32 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 118.63 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 25 DINMSVEEGEFIAIMGPSGSGKTT----LLNVLSSIDYISQGSITLKGHKLEKLSnkalsdIRKHDIGFIFQE----YNL 96
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNprtaFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 97 LHTLT--VKENIMLPLTVQKLDKDTMLDRYEKV--AEALNILDisdKYPSELSGGQRQRTSAARAFITLPSIIFADEPTG 172
Cdd:TIGR02770 78 LFTMGnhAIETLRSLGKLSKQARALILEALEAVglPDPEEVLK---KYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 616690417 173 ALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDlGVVARIADEVAVMDDGRI 204
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-227 |
2.35e-32 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 120.98 E-value: 2.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkalsdIR 83
Cdd:PRK11432 7 VVLKNITKRFGSNT----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS------IQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDtmlDRYEKVAEALNILDIS---DKYPSELSGGQRQRTSAARAFIT 160
Cdd:PRK11432 77 QRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKE---ERKQRVKEALELVDLAgfeDRYVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 161 LPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAA-SYANRVVMLKDGQIF-----TELYQ 227
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDTVIVMNKGKIMqigspQELYR 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-221 |
3.10e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 119.07 E-value: 3.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYgNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALS 80
Cdd:PRK13650 2 SNIIEVKNLTFKY-KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIRkHDIGFIFQEY-NLLHTLTVKENIMLPLTVQKLDKDTMLDRyekVAEALNILDISD---KYPSELSGGQRQRTSAAR 156
Cdd:PRK13650 78 DIR-HKIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKER---VNEALELVGMQDfkeREPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616690417 157 AFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-224 |
3.21e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.03 E-value: 3.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLeKLSNKALSDI 82
Cdd:PRK13639 1 ILETRDLKYSYPD---GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKhDIGFIFQEY-NLLHTLTVKENIML-PLTVqKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFIT 160
Cdd:PRK13639 77 RK-TVGIVFQNPdDQLFAPTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616690417 161 LPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHD-PVAASYANRVVMLKDGQIFTE 224
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDvDLVPVYADKVYVMSDGKIIKE 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-220 |
4.19e-32 |
|
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: 117.15 E-value: 4.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIY-----GNKKMaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLssidY----ISQGSITLK--GHK 70
Cdd:COG4778 3 TLLEVENLSKTFtlhlqGGKRL--PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCI----YgnylPDSGSILVRhdGGW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 71 LE--KLSNKALSDIRKHDIGFIFQeynLLHTL---TVKENIMLPLTVQKLDKDTMLDRyekVAEALNILDISDK----YP 141
Cdd:COG4778 77 VDlaQASPREILALRRRTIGYVSQ---FLRVIprvSALDVVAEPLLERGVDREEARAR---ARELLARLNLPERlwdlPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 142 SELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQ---DLLkrlmkmnEEIK---TTIIMVTHDP-VAASYANRVV 214
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAvvvELI-------EEAKargTAIIGIFHDEeVREAVADRVV 223
|
....*.
gi 616690417 215 MLKDGQ 220
Cdd:COG4778 224 DVTPFS 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-182 |
4.91e-32 |
|
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: 117.26 E-value: 4.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkalSDIR 83
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP----MHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHD-IGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLP 162
Cdd:cd03218 73 ARLgIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180
....*....|....*....|
gi 616690417 163 SIIFADEPTGALDSKSTQDL 182
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDI 172
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-221 |
6.88e-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: 6.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGnkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKalsDI 82
Cdd:COG1129 4 LLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPR---DA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKHDIGFIFQEYNLLHTLTVKENIML---PLTVQKLDKDTMLDRYEKVAEALNiLDIS-DKYPSELSGGQRQRTSAARAF 158
Cdd:COG1129 77 QAAGIAIIHQELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLG-LDIDpDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616690417 159 ITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTH--DPVAAsYANRVVMLKDGQI 221
Cdd:COG1129 156 SRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHrlDEVFE-IADRVTVLRDGRL 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-221 |
9.61e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.18 E-value: 9.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSsiDYI--SQGSITLKGHKLEKLSNKAL 79
Cdd:PRK13548 1 AMLEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS--GELspDSGEVRLNGRPLADWSPAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 80 SDIR-----KHDIGFIFqeynllhtlTVKENI-M--LPLTvQKLDKDTMLdryekVAEALNILDISD----KYPsELSGG 147
Cdd:PRK13548 75 ARRRavlpqHSSLSFPF---------TVEEVVaMgrAPHG-LSRAEDDAL-----VAAALAQVDLAHlagrDYP-QLSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 148 QRQRTSAARAFITL------PSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQ 220
Cdd:PRK13548 139 EQQRVQLARVLAQLwepdgpPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDlNLAARYADRIVLLHQGR 218
|
.
gi 616690417 221 I 221
Cdd:PRK13548 219 L 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-231 |
1.27e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 117.10 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGN-----KKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLS 75
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 76 NKALSDIRKhDIGFIFQE----YNLLHtlTVKENIMLPLT-VQKLDKDtmlDRYEKVAEALNILD----ISDKYPSELSG 146
Cdd:PRK10419 81 RAQRKAFRR-DIQMVFQDsisaVNPRK--TVREIIREPLRhLLSLDKA---ERLARASEMLRAVDlddsVLDKRPPQLSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 147 GQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQIFTEL 225
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDlRLVERFCQRVMVMDNGQIVETQ 234
|
....*.
gi 616690417 226 YQGDDD 231
Cdd:PRK10419 235 PVGDKL 240
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-219 |
1.31e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 116.72 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNkalsdi 82
Cdd:PRK11248 1 MLQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 rkhDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDtmlDRYEKVAEALNILDIS---DKYPSELSGGQRQRTSAARAFI 159
Cdd:PRK11248 71 ---ERGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKM---QRLEIAHQMLKKVGLEgaeKRYIWQLSGGQRQRVGIARALA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690417 160 TLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASY-ANRVVMLKDG 219
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFmATELVLLSPG 205
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-228 |
2.67e-31 |
|
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: 115.51 E-value: 2.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIY-------GNKKMAQ----------EVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITL 66
Cdd:cd03267 1 IEVSNLSKSYrvyskepGLIGSLKslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 67 KGHKLEKLSNKALsdirkHDIGFIF-QEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELS 145
Cdd:cd03267 81 AGLVPWKRRKKFL-----RRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 146 GGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD--PVAAsYANRVVMLKDGQIft 223
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYmkDIEA-LARRVLVIDKGRL-- 232
|
....*
gi 616690417 224 eLYQG 228
Cdd:cd03267 233 -LYDG 236
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-221 |
4.92e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 115.57 E-value: 4.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYgNKKMAQE--VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkalS 80
Cdd:COG1101 1 MLELKNLSKTF-NPGTVNEkrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP----E 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIRKHDIGFIFQEyNLLHT---LTVKENIMLPLTVQK-------LDKdtmlDRYEKVAEALNILD------ISDKYPSeL 144
Cdd:COG1101 76 YKRAKYIGRVFQD-PMMGTapsMTIEENLALAYRRGKrrglrrgLTK----KRRELFRELLATLGlglenrLDTKVGL-L 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 145 SGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAA-SYANRVVMLKDGQI 221
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQAlDYGNRLIMMHEGRI 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-216 |
6.41e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 113.73 E-value: 6.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNkkmaQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLS---SIDYISQGSITLKGHKLEKLSnkals 80
Cdd:COG4136 2 LSLENLTITLGG----RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgtlSPAFSASGEVLLNGRRLTALP----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 dIRKHDIGFIFQEyNLL--HtLTVKENIM--LPLTVQKldkdtmLDRYEKVAEAL---NILDISDKYPSELSGGQRQRTS 153
Cdd:COG4136 73 -AEQRRIGILFQD-DLLfpH-LSVGENLAfaLPPTIGR------AQRRARVEQALeeaGLAGFADRDPATLSGGQRARVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 154 AARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVML 216
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-229 |
7.84e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 115.22 E-value: 7.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYgnkKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKalsDI 82
Cdd:PRK13647 4 IIEVEDLHFRY---KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK---WV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKHdIGFIFQEYN-LLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITL 161
Cdd:PRK13647 78 RSK-VGLVFQDPDdQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 162 PSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHD-PVAASYANRVVMLKDGQIfteLYQGD 229
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDvDLAAEWADQVIVLKEGRV---LAEGD 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-221 |
1.32e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 114.24 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYIS-----QGSITLKGHKLEKLS 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQV----EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 76 nkaLSDIRKHdIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMlDRYEKVAEALN-------ILDISDKYPSELSGGQ 148
Cdd:PRK14247 77 ---VIELRRR-VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKK-ELQERVRWALEkaqlwdeVKDRLDAPAGKLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616690417 149 RQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIktTIIMVTHDPV-AASYANRVVMLKDGQI 221
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQqAARISDYVAFLYKGQI 223
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-221 |
1.45e-30 |
|
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: 119.05 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkaLSDIR 83
Cdd:TIGR02203 331 VEFRNVTFRYPGR--DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTlTVKENIMLPLTVQKLDKdtmldRYEKVAEALNILDISDKYP-----------SELSGGQRQRT 152
Cdd:TIGR02203 406 RQ-VALVSQDVVLFND-TIANNIAYGRTEQADRA-----EIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616690417 153 SAARAFITLPSIIFADEPTGALDSKS---TQDLLKRLMKMneeiKTTIImVTHDPVAASYANRVVMLKDGQI 221
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESerlVQAALERLMQG----RTTLV-IAHRLSTIEKADRIVVMDDGRI 545
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-216 |
1.51e-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: 118.54 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALsdiR 83
Cdd:TIGR02857 322 LEFSGVSVAYPG---RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---R 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTlTVKENIML------PLTVQKLDKDTMLDRYEKVAEALNILDISDKyPSELSGGQRQRTSAARA 157
Cdd:TIGR02857 396 DQ-IAWVPQHPFLFAG-TIAENIRLarpdasDAEIREALERAGLDEFVAALPQGLDTPIGEG-GAGLSGGQAQRLALARA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 158 FITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEeiKTTIIMVTHDPVAASYANRVVML 216
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-224 |
1.64e-30 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.96 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSd 81
Cdd:PRK11231 1 MTLRTENLTVGYGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 irKHdIGFIFQEynllhtLTVKENImlplTVQKL----------------DKDTMLdrYEKVAEALNILDISDKYPSELS 145
Cdd:PRK11231 76 --RR-LALLPQH------HLTPEGI----TVRELvaygrspwlslwgrlsAEDNAR--VNQAMEQTRINHLADRRLTDLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 146 GGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKtTIIMVTHDPVAAS-YANRVVMLKDGQIFTE 224
Cdd:PRK11231 141 GGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASrYCDHLVVLANGHVMAQ 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-221 |
1.78e-30 |
|
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: 113.15 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGnkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALS 80
Cdd:COG0410 1 MPMLEVENLHAGYG----GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG---EDITGLPPH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIRKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKlDKDTMLDRYEKVAEALNIL-DISDKYPSELSGGQRQRTSAARAFI 159
Cdd:COG0410 74 RIARLGIGYVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYELFPRLkERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 160 TLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNaRFALEIADRAYVLERGRI 214
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-221 |
2.99e-30 |
|
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: 118.43 E-value: 2.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKMAqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNkalSDIR 83
Cdd:TIGR03375 464 IEFRNVSFAYPGQETP--ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDP---ADLR 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 kHDIGFIFQEYNLLHTlTVKENIMLplTVQKLDKDTMLdryeKVAEALNILDISDKYPS-----------ELSGGQRQRT 152
Cdd:TIGR03375 539 -RNIGYVPQDPRLFYG-TLRDNIAL--GAPYADDEEIL----RAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAV 610
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 153 SAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEikTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:TIGR03375 611 ALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAG--KTLVLVTHRTSLLDLVDRIIVMDNGRI 677
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-203 |
4.47e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 114.44 E-value: 4.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKK----MAQEVLR---DINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLS 75
Cdd:COG4608 7 LLEVRDLKKHFPVRGglfgRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 76 NKALSDIRKhDIGFIFQE-YNLLHT-LTVKENIMLPLTVQKLDKDTmlDRYEKVAEALNILDIS----DKYPSELSGGQR 149
Cdd:COG4608 87 GRELRPLRR-RMQMVFQDpYASLNPrMTVGDIIAEPLRIHGLASKA--ERRERVAELLELVGLRpehaDRYPHEFSGGQR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 150 QRTSAARAFITLPSIIFADEPTGALDsKSTQ----DLLKRLmkmNEEIKTTIIMVTHD 203
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALD-VSIQaqvlNLLEDL---QDELGLTYLFISHD 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-228 |
6.62e-30 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 111.13 E-value: 6.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGeFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKalsdIR 83
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPS 163
Cdd:cd03264 72 RR-IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 164 IIFADEPTGALDSKST---QDLLKRLMKmneeiKTTIIMVTH--DPVAASyANRVVMLKDGQIfteLYQG 228
Cdd:cd03264 151 ILIVDEPTAGLDPEERirfRNLLSELGE-----DRIVILSTHivEDVESL-CNQVAVLNKGKL---VFEG 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-221 |
7.39e-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: 111.55 E-value: 7.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 13 YGNKKmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALsdiRKHdIGFIFQ 92
Cdd:cd03254 12 YDEKK---PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---RSM-IGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 93 EYNLLHTlTVKENIMLPltvqklDKDTMLDRYEKVAEALNILDISDKYP-----------SELSGGQRQRTSAARAFITL 161
Cdd:cd03254 85 DTFLFSG-TIMENIRLG------RPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 162 PSIIFADEPTGALDSKS---TQDLLKRLMKmneeiKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:cd03254 158 PKILILDEATSNIDTETeklIQEALEKLMK-----GRTSIIIAHRLSTIKNADKILVLDDGKI 215
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
4-228 |
1.57e-29 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 116.30 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVL---SSIDYISQGSITLKGHKLEKLSNKALS 80
Cdd:TIGR00955 22 QLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrSPKGVKGSGSVLLNGMPIDAKEMRAIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 dirkhdiGFIFQEYNLLHTLTVKENIMLPLTVQ---KLDKDTMLDRYEKVAEALNILDISD------KYPSELSGGQRQR 151
Cdd:TIGR00955 102 -------AYVQQDDLFIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 152 TSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKtTIIMVTHDPVAASYA--NRVVMLKDGQIfteLYQG 228
Cdd:TIGR00955 175 LAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGK-TIICTIHQPSSELFElfDKIILMAEGRV---AYLG 249
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-241 |
1.68e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.86 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEkLSNKALSD 81
Cdd:PRK13636 4 YILKVEELNYNYSD---GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IRKhDIGFIFQEY-NLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFIT 160
Cdd:PRK13636 80 LRE-SVGMVFQDPdNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 161 LPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQIfteLYQGDDDKHTFFKEI 239
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGRV---ILQGNPKEVFAEKEM 235
|
..
gi 616690417 240 IR 241
Cdd:PRK13636 236 LR 237
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-221 |
2.62e-29 |
|
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: 115.23 E-value: 2.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKMAqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSdir 83
Cdd:COG4618 331 LSVENLTVVPPGSKRP--ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTlTVKENI-MLPltvqklDKDTmldryEKVAEALN-------ILDISDKYPSE-------LSGGQ 148
Cdd:COG4618 406 RH-IGYLPQDVELFDG-TIAENIaRFG------DADP-----EKVVAAAKlagvhemILRLPDGYDTRigeggarLSGGQ 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 149 RQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:COG4618 473 RQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-170 |
2.84e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 110.12 E-value: 2.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLS--NKA 78
Cdd:COG1137 1 MMTLEAENLVKSYGKRT----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 79 lsdirKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAF 158
Cdd:COG1137 77 -----RLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170
....*....|..
gi 616690417 159 ITLPSIIFADEP 170
Cdd:COG1137 152 ATNPKFILLDEP 163
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-224 |
3.77e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 110.46 E-value: 3.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKMAQevlrDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSdiR 83
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAE----NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KhdIGFIFQEYNLLHTLTVKENIM------LPLTVQKLDKDTmlDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARA 157
Cdd:PRK10253 82 R--IGLLAQNATTPGDITVQELVArgryphQPLFTRWRKEDE--EAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 158 FITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQIFTE 224
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALREGKIVAQ 225
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
20-221 |
4.92e-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: 109.63 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 20 QEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkaLSDIRKHdIGFIFQEYNLLHT 99
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLRRA-IGVVPQDTVLFND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 100 lTVKENImlpltvqkldkdtmldRY----------EKVAEALNILDI----SDKYPSE-------LSGGQRQRTSAARAF 158
Cdd:cd03253 90 -TIGYNI----------------RYgrpdatdeevIEAAKAAQIHDKimrfPDGYDTIvgerglkLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 159 ITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTiIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSKG-RTT-IVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-224 |
8.69e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.84 E-value: 8.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 23 LRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLeklSNKALSDIRKHdIGFIFQE-YNLLHTLT 101
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKLRKH-IGIVFQNpDNQFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 102 VKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQD 181
Cdd:PRK13648 101 VKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 616690417 182 LLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQIFTE 224
Cdd:PRK13648 181 LLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKE 223
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-221 |
9.62e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 112.05 E-value: 9.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGN----------KKMAQEVL----------RDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGS 63
Cdd:PRK10070 5 LEIKNLYKIFGEhpqrafkyieQGLSKEQIlektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 64 ITLKGHKLEKLSNKALSDIRKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDtmlDRYEKVAEALNILDISD---KY 140
Cdd:PRK10070 85 VLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAE---ERREKALDALRQVGLENyahSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 141 PSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDG 219
Cdd:PRK10070 162 PDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNG 241
|
..
gi 616690417 220 QI 221
Cdd:PRK10070 242 EV 243
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-246 |
1.07e-28 |
|
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: 109.15 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAqevlRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKG-----HKLEKLSNK 77
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGC----RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaeLELYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 78 ALSDIRKHDIGFIFQEY--NLLHTLTVKENI---MLPLTVQKLDK--DTMLDRYEKVAEALNILDisDKyPSELSGGQRQ 150
Cdd:TIGR02323 79 ERRRLMRTEWGFVHQNPrdGLRMRVSAGANIgerLMAIGARHYGNirATAQDWLEEVEIDPTRID--DL-PRAFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 151 RTSAARAFITLPSIIFADEPTGALDSkSTQ----DLLKRLMKmneEIKTTIIMVTHD-PVAASYANRVVMLKDGQI---- 221
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDV-SVQarllDLLRGLVR---DLGLAVIIVTHDlGVARLLAQRLLVMQQGRVvesg 231
|
250 260
....*....|....*....|....*
gi 616690417 222 FTElyQGDDDKHTFFKEIIrVQSVL 246
Cdd:TIGR02323 232 LTD--QVLDDPQHPYTQLL-VSSIL 253
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-221 |
1.27e-28 |
|
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: 107.01 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkalsDIR 83
Cdd:cd03247 1 LSINNVSFSYPEQE--QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-----KAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTlTVKENIMLPLtvqkldkdtmldryekvaealnildisdkypselSGGQRQRTSAARAFITLPS 163
Cdd:cd03247 74 SSLISVLNQRPYLFDT-TLRNNLGRRF----------------------------------SGGERQRLALARILLQDAP 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 164 IIFADEPTGALDSKSTQDLLKRLMKMNEEikTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-221 |
2.12e-28 |
|
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: 112.83 E-value: 2.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 19 AQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSdirKHdIGFIFQEYNLLH 98
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG---KH-IGYLPQDVELFP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 99 TlTVKENImlpltvQKLDKDtmLDRyEKVAEALN-------ILDISDKYPSE-------LSGGQRQRTSAARAFITLPSI 164
Cdd:TIGR01842 406 G-TVAENI------ARFGEN--ADP-EKIIEAAKlagvhelILRLPDGYDTVigpggatLSGGQRQRIALARALYGDPKL 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 165 IFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:TIGR01842 476 VVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-215 |
2.32e-28 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 109.81 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKT----TLLNVLSSIDYISqGSITLKGHKLEKLSN 76
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIG-GSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 77 KALSDIRKHDIGFIFQE--YNLLHTLTVKENIMLPLTVQK-LDKDT-------MLDRYeKVAEALNILDIsdkYPSELSG 146
Cdd:PRK09473 89 KELNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKgMSKAEafeesvrMLDAV-KMPEARKRMKM---YPHEFSG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690417 147 GQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRV-VM 215
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVlVM 235
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-221 |
1.40e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 106.16 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSD- 81
Cdd:PRK11701 6 LLSVRGLTKLYGPRK----GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IRKH----DIGFIFQ--EYNLLHTLTVKENIMLPLTVQ------KLdKDTMLDRYEKVAEALNILDisDKyPSELSGGQR 149
Cdd:PRK11701 82 ERRRllrtEWGFVHQhpRDGLRMQVSAGGNIGERLMAVgarhygDI-RATAGDWLERVEIDAARID--DL-PTTFSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 150 QRTSAARAFITLPSIIFADEPTGALDSkSTQ----DLLKRLMKmneEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDV-SVQarllDLLRGLVR---ELGLAVVIVTHDlAVARLLAHRLLVMKQGRV 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-221 |
2.12e-27 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 107.65 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 37 AIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDIRKHDIGFIFQEYNLLHTLTVKENI---Mlpltvq 113
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLrygM------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 114 kldKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEI 193
Cdd:PRK11144 102 ---AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREI 178
|
170 180 190
....*....|....*....|....*....|
gi 616690417 194 KTTIIMVTH--DPVaASYANRVVMLKDGQI 221
Cdd:PRK11144 179 NIPILYVSHslDEI-LRLADRVVVLEQGKV 207
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-221 |
2.42e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.04 E-value: 2.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAqeVLRDINMSVEEGEFIAIMGPSGSGKTT---LLNVLSSIDYISQGSITLKGhklEKLSNKAL 79
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG---ITLTAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 80 SDIRKHdIGFIFQEY-NLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAF 158
Cdd:PRK13640 80 WDIREK-VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 159 ITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
19-216 |
2.52e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 103.85 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 19 AQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKleklsnkalsdirkhDIGFIFQEYNLLH 98
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA---------------RVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 99 TLtvkenimlPLTVQKLDkdTM-----------LDRYEKVA-----EALNILDISDKYPSELSGGQRQRTSAARAFITLP 162
Cdd:NF040873 69 SL--------PLTVRDLV--AMgrwarrglwrrLTRDDRAAvddalERVGLADLAGRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 616690417 163 SIIFADEPTGALDSKSTQDLLkRLMKMNEEIKTTIIMVTHDPVAASYANRVVML 216
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERII-ALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-220 |
2.78e-27 |
|
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: 104.09 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 22 VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHkleklsnkalsdirkhdIGFIFQEYNLLHTlT 101
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------------IAYVSQEPWIQNG-T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 102 VKENImlpLTVQKLDKdtmlDRYEKVAEA------LNILDISDKypSE-------LSGGQRQRTSAARAFITLPSIIFAD 168
Cdd:cd03250 82 IRENI---LFGKPFDE----ERYEKVIKAcalepdLEILPDGDL--TEigekginLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 616690417 169 EPTGALDSKSTQDLLKR-LMKMNEEIKtTIIMVTHDPVAASYANRVVMLKDGQ 220
Cdd:cd03250 153 DPLSAVDAHVGRHIFENcILGLLLNNK-TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-204 |
3.06e-27 |
|
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: 104.66 E-value: 3.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 22 VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLS---SIDYISQGSITLKGHKLEKlsnkalsDIRKHDIGFIFQEYNLLH 98
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKP-------DQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 99 TLTVKENI----MLPLTVQKLDKdtmldRYEKVAE-----ALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADE 169
Cdd:cd03234 95 GLTVRETLtytaILRLPRKSSDA-----IRKKRVEdvllrDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 616690417 170 PTGALDSKSTQDL---LKRLMKMNEeiktTIIMVTHDP 204
Cdd:cd03234 170 PTSGLDSFTALNLvstLSQLARRNR----IVILTIHQP 203
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-221 |
3.13e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 106.75 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKT-TLLNVLSSIDY---ISQGSITLKGHKLEKLSN 76
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYpgrVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 77 KALSDIRKHDIGFIFQE--YNLLHTLTVKENIMLPLTV-QKLDKDTmldRYEKVAEALNILDISDK------YPSELSGG 147
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKT---RRQRAIDLLNQVGIPDPasrldvYPHQLSGG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616690417 148 QRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlALVAEAAHKIIVMYAGQV 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-204 |
5.62e-27 |
|
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: 108.60 E-value: 5.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 19 AQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDIrkhdIGFIFQEYNLLH 98
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR----VSVCAQDAHLFD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 99 TlTVKENIMlpLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSE-------LSGGQRQRTSAARAFITLPSIIFADEPT 171
Cdd:TIGR02868 423 T-TVRENLR--LARPDATDEELWAALERVGLADWLRALPDGLDTVlgeggarLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|...
gi 616690417 172 GALDSKSTQDLLKRLMKMNEEikTTIIMVTHDP 204
Cdd:TIGR02868 500 EHLDAETADELLEDLLAALSG--RTVVLITHHL 530
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-235 |
1.28e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 103.70 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSI-DYISQ----GSITLKGHKLEKLSN 76
Cdd:PRK14239 4 PILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMnDLNPEvtitGSIVYNGHNIYSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 77 KALsDIRKhDIGFIFQEYNLLhTLTVKENIMLPLTVQKL-DKDTMLDRYEKVAEALNILD-ISDKYPSE---LSGGQRQR 151
Cdd:PRK14239 80 DTV-DLRK-EIGMVFQQPNPF-PMSIYENVVYGLRLKGIkDKQVLDEAVEKSLKGASIWDeVKDRLHDSalgLSGGQQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 152 TSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEeiKTTIIMVTHDPVAAS-YANRVVMLKDGqiftELYQGDD 230
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASrISDRTGFFLDG----DLIEYND 230
|
....*
gi 616690417 231 DKHTF 235
Cdd:PRK14239 231 TKQMF 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-222 |
1.62e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 104.33 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 19 AQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLE-KLSNKALSDIRKHdIGFIFQ--EYN 95
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKPLRKK-VGIVFQfpEHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 96 LLHTlTVKENIML-PLTVQKLDKDTMldryEKVAEALNIL----DISDKYPSELSGGQRQRTSAARAFITLPSIIFADEP 170
Cdd:PRK13634 98 LFEE-TVEKDICFgPMNFGVSEEDAK----QKAREMIELVglpeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 616690417 171 TGALDSKSTQDLLKRLMKMNEEIKTTIIMVTH---DpvAASYANRVVMLKDGQIF 222
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHsmeD--AARYADQIVVMHKGTVF 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-221 |
1.80e-26 |
|
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: 102.60 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGnkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSdir 83
Cdd:TIGR03410 1 LEVSNLNVYYG----QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENIMLPLTVQKldkdtmlDRYEKVAEalnilDISDKYP----------SELSGGQRQRTS 153
Cdd:TIGR03410 74 RAGIAYVPQGREIFPRLTVEENLLTGLAALP-------RRSRKIPD-----EIYELFPvlkemlgrrgGDLSGGQQQQLA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 154 AARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMV-THDPVAASYANRVVMLKDGQI 221
Cdd:TIGR03410 142 IARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVeQYLDFARELADRYYVMERGRV 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-221 |
2.11e-26 |
|
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: 100.58 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGnkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALSDIR 83
Cdd:cd03216 1 LELRGITKRFG----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---KEVSFASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQeynllhtltvkenimlpltvqkldkdtmldryekvaealnildisdkypseLSGGQRQRTSAARAFITLPS 163
Cdd:cd03216 74 RAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 164 IIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTH--DPVAAsYANRVVMLKDGQI 221
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHrlDEVFE-IADRVTVLRDGRV 160
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-224 |
2.31e-26 |
|
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: 101.91 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKalsdiR 83
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA-----L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTLTVKENIMLpltvqkldKDTMLD-RYEKVAEALNIL---DISDKYPSELSGGQRQRTSAARAFI 159
Cdd:cd03268 72 RR-IGALIEAPGFYPNLTARENLRL--------LARLLGiRKKRIDEVLDVVglkDSAKKKVKGFSLGMKQRLGIALALL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 160 TLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIImvthdpvaASY--------ANRVVMLKDGQIFTE 224
Cdd:cd03268 143 GNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLI--------SSHllseiqkvADRIGIINKGKLIEE 207
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-224 |
2.35e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 103.63 E-value: 2.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYgNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALSDI 82
Cdd:PRK13642 4 ILEVENLVFKY-EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKhDIGFIFQEY-NLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITL 161
Cdd:PRK13642 80 RR-KIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 162 PSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQIFTE 224
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKE 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-220 |
2.96e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.26 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKKmAqevLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLeKLSNKAls 80
Cdd:COG3845 3 PPALELRGITKRFGGVV-A---NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIRKHDIGFIFQEYNLLHTLTVKENIML---PLTVQKLDKDTMLDRYEKVAEALNiLDIS-DKYPSELSGGQRQRTSAAR 156
Cdd:COG3845 76 DAIALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYG-LDVDpDAKVEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616690417 157 AFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKtTIIMVTH--DPVAAsYANRVVMLKDGQ 220
Cdd:COG3845 155 ALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGK-SIIFITHklREVMA-IADRVTVLRRGK 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-229 |
3.30e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.33 E-value: 3.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNKK-------MAQEVLRDINMSVEEGEFIAIMGPSGSGKTT----LLNVLSSidyisQGSITLKGHK 70
Cdd:PRK15134 274 PLLDVEQLQVAFPIRKgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 71 LEKLSNKALSDIRkHDIGFIFQEYN--LLHTLTVKENIMLPLTVQKLDKdTMLDRYEKVAEALNIL----DISDKYPSEL 144
Cdd:PRK15134 349 LHNLNRRQLLPVR-HRIQVVFQDPNssLNPRLNVLQIIEEGLRVHQPTL-SAAQREQQVIAVMEEVgldpETRHRYPAEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 145 SGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQIft 223
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDlHVVRALCHQVIVLRQGEV-- 504
|
....*.
gi 616690417 224 eLYQGD 229
Cdd:PRK15134 505 -VEQGD 509
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-221 |
3.56e-26 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 102.18 E-value: 3.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 19 AQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALsdirKHDIGFIFQEyNLLH 98
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL----RRQVGVVLQE-NVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 99 TLTVKENIMLpltvqkldKDTMLDRyEKVAEALNILDISD---KYP-----------SELSGGQRQRTSAARAFITLPSI 164
Cdd:cd03252 89 NRSIRDNIAL--------ADPGMSM-ERVIEAAKLAGAHDfisELPegydtivgeqgAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 165 IFADEPTGALDSKSTQDLLKRLMKMNEeiKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRI 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-221 |
1.10e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 101.07 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNkkmaQEVLRDINMSVEEGEFIAIMGPSGSGKTTLL---NVLSSIDYIS--QGSITLKGHKLEKLSNKA 78
Cdd:PRK14267 5 IETVNLRVYYGS----NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfNRLLELNEEArvEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 79 LsDIRKhDIGFIFQEYNLLHTLTVKENIMLPLTVQKL--DKDTMLDRYE----KVAEALNILDISDKYPSELSGGQRQRT 152
Cdd:PRK14267 81 I-EVRR-EVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEwalkKAALWDEVKDRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 153 SAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIktTIIMVTHDPV-AASYANRVVMLKDGQI 221
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAqAARVSDYVAFLYLGKL 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-220 |
1.98e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.02 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKT-TLLNVL-----SSIDYiSQGSITLKGHKLEKL 74
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpsPPVVY-PSGDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 75 SNKALSDIRKHDIGFIFQE----YNLLHTLTVKENIMLPL---TVQKLDKDTMLDRYEKV-----AEALNildisdKYPS 142
Cdd:PRK15134 82 SEQTLRGVRGNKIAMIFQEpmvsLNPLHTLEKQLYEVLSLhrgMRREAARGEILNCLDRVgirqaAKRLT------DYPH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 143 ELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQ 220
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNlSIVRKLADRVAVMQNGR 234
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-221 |
3.94e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 99.74 E-value: 3.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 20 QEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKL---EKLSNKALSDIRKhDIGFIFQEYNL 96
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLRK-EVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 97 LHTLTVKENIMLPLTVQKLD-----KDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPT 171
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKekreiKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 616690417 172 GALDSKSTQDLLKRLMKMNEEIktTIIMVTHDP-VAASYANRVVMLKDGQI 221
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEI--AIVIVSHNPqQVARVADYVAFLYNGEL 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-215 |
6.17e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 100.55 E-value: 6.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLtKIYGN----------KKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLE 72
Cdd:PRK15079 8 LLEVADL-KVHFDikdgkqwfwqPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 73 KLSNKALSDIRKhDIGFIFQE--YNLLHTLTVKENIMLPLTV--QKLDKDTMLDRYEKVAEALNIL-DISDKYPSELSGG 147
Cdd:PRK15079 87 GMKDDEWRAVRS-DIQMIFQDplASLNPRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLpNLINRYPHEFSGG 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 148 QRQRTSAARAFITLPSIIFADEPTGALD-SKSTQ--DLLKRLMKmneEIKTTIIMVTHD-PVAASYANRV-VM 215
Cdd:PRK15079 166 QCQRIGIARALILEPKLIICDEPVSALDvSIQAQvvNLLQQLQR---EMGLSLIFIAHDlAVVKHISDRVlVM 235
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-224 |
9.16e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 99.07 E-value: 9.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALS 80
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRC----IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIRKHdIGFIFQEYNLLHTLTVKENIMLPLT-----VQKLDKDTMLDRYEkvaeALNILDISDKYPSELSGGQRQRTSAA 155
Cdd:PRK11831 81 TVRKR-MSMLFQSGALFTDMNVFDNVAYPLRehtqlPAPLLHSTVMMKLE----AVGLRGAAKLMPSELSGGMARRAALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 156 RAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQIFTE 224
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDvPEVLSIADHAYIVADKKIVAH 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-227 |
1.19e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 102.23 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 26 INMSVEEGEFIAIMGPSGSGKTTLLNVLSS-IDYisQGSITLKGHKLEKLSnkaLSDIRKHdIGFIFQEYNLLHTlTVKE 104
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGfLPY--QGSLKINGIELRELD---PESWRKH-LSWVGQNPQLPHG-TLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 105 NIML---PLTVQKLdkDTMLDRyEKVAEALNIL------DISDKyPSELSGGQRQRTSAARAFITLPSIIFADEPTGALD 175
Cdd:PRK11174 442 NVLLgnpDASDEQL--QQALEN-AWVSEFLPLLpqgldtPIGDQ-AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 176 SKSTQDLLKRLMKMNEeiKTTIIMVTH--DPVAAsyANRVVMLKDGQI-----FTELYQ 227
Cdd:PRK11174 518 AHSEQLVMQALNAASR--RQTTLMVTHqlEDLAQ--WDQIWVMQDGQIvqqgdYAELSQ 572
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-221 |
1.47e-24 |
|
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: 96.97 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKleklsnkaLSDIR 83
Cdd:cd03269 1 LEVENVTKRFGRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP--------LDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPS 163
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 164 IIFADEPTGALDSKStQDLLKRLMKMNEEIKTTIIMVTH--DPVAAsYANRVVMLKDGQI 221
Cdd:cd03269 149 LLILDEPFSGLDPVN-VELLKDVIRELARAGKTVILSTHqmELVEE-LCDRVLLLNKGRA 206
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-220 |
1.90e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 101.86 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKT-TLLNVLSSIDY----ISQGSITLKGH-----KLE 72
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQagglVQCDKMLLRRRsrqviELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 73 KLSNKALSDIRKHDIGFIFQE--YNLLHTLTVKENIMLPLTVQKldkdtMLDRYEKVAEALNILD---------ISDKYP 141
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQ-----GASREEAMVEAKRMLDqvripeaqtILSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 142 SELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQ 220
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDmGVVAEIADRVLVMYQGE 246
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-221 |
3.15e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.98 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTIlEVKQLTKIYG-NKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKG-HKLEKLSNKA 78
Cdd:PRK13641 1 MSI-KFENVDYIYSpGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyHITPETGNKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 79 LSDIRKhDIGFIFQ--EYNLLHTlTVKENIML-PLTV---QKLDKDTMLDRYEKVAEALnilDISDKYPSELSGGQRQRT 152
Cdd:PRK13641 80 LKKLRK-KVSLVFQfpEAQLFEN-TVLKDVEFgPKNFgfsEDEAKEKALKWLKKVGLSE---DLISKSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690417 153 SAARAFITLPSIIFADEPTGALDSKSTQDLLKrLMKMNEEIKTTIIMVTH--DPVaASYANRVVMLKDGQI 221
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ-LFKDYQKAGHTVILVTHnmDDV-AEYADDVLVLEHGKL 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-220 |
4.27e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.65 E-value: 4.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 20 QEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKleklsnkalsdirkhDIGFIFQE-YNLLH 98
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA---------------RVLFLPQRpYLPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 99 TLtvKENIMLPLTVQKLDKDTMLDRYEKV--AEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDS 176
Cdd:COG4178 441 TL--REALLYPATAEAFSDAELREALEAVglGHLAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 616690417 177 KSTQDLLKRLMKMNEEikTTIIMVTHDPVAASYANRVVMLKDGQ 220
Cdd:COG4178 519 ENEAALYQLLREELPG--TTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-224 |
4.59e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.47 E-value: 4.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAQE--VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNkaLS 80
Cdd:PRK13633 4 MIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--LW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIRKHdIGFIFQEY-NLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFI 159
Cdd:PRK13633 82 DIRNK-AGMVFQNPdNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616690417 160 TLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQIFTE 224
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-203 |
5.28e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 98.11 E-value: 5.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKK--MAQE----VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKL 74
Cdd:PRK11308 3 QPLLQAIDLKKHYPVKRglFKPErlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 75 SNKALSDIRKhDIGFIFQeyNLLHTLTVKENIMLPLTvQKLDKDTMLDRYEKVAEALNIL-------DISDKYPSELSGG 147
Cdd:PRK11308 83 DPEAQKLLRQ-KIQIVFQ--NPYGSLNPRKKVGQILE-EPLLINTSLSAAERREKALAMMakvglrpEHYDRYPHMFSGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 616690417 148 QRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD 203
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
22-243 |
1.01e-23 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 99.65 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 22 VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALsdiRKHdIGFIFQEYNLLhTLT 101
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAV---RRQ-LGVVLQNGRLM-SGS 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 102 VKENIM--LPLTVqkldkdtmldryEKVAEALNIL----DISD------KYPSE----LSGGQRQRTSAARAFITLPSII 165
Cdd:TIGR03797 543 IFENIAggAPLTL------------DEAWEAARMAglaeDIRAmpmgmhTVISEgggtLSGGQRQRLLIARALVRKPRIL 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 166 FADEPTGALDSKsTQDL----LKRLmkmneeiKTTIIMVTHDPVAASYANRVVMLKDGQI-----FTELYQgdddKHTFF 236
Cdd:TIGR03797 611 LFDEATSALDNR-TQAIvsesLERL-------KVTRIVIAHRLSTIRNADRIYVLDAGRVvqqgtYDELMA----REGLF 678
|
....*..
gi 616690417 237 KEIIRVQ 243
Cdd:TIGR03797 679 AQLARRQ 685
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-221 |
1.16e-23 |
|
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: 94.04 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTkiygnkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNkalSD 81
Cdd:cd03215 3 PVLEVRGLS--------VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSP---RD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IRKHDIGFI---FQEYNLLHTLTVKENIMLpltvqkldkdtmldryekvaealnildisdkyPSELSGGQRQRTSAARAF 158
Cdd:cd03215 72 AIRAGIAYVpedRKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616690417 159 ITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
1.43e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.03 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYgnkKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALS 80
Cdd:PRK13652 1 MHLIETRDLCYSY---SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG---EPITKENIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIRKHdIGFIFQEYN-LLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFI 159
Cdd:PRK13652 75 EVRKF-VGLVFQNPDdQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 160 TLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQlDLVPEMADYIYVMDKGRI 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-224 |
1.60e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.00 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 21 EVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKL-EKLSNKALSDIRKhDIGFIFQ--EYNLL 97
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRPVRK-RIGMVFQfpESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 98 HTLTVKENIMLPLTVqKLDKDTMLDRYEKVAEALNI-LDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDS 176
Cdd:PRK13646 100 EDTVEREIIFGPKNF-KMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 616690417 177 KSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQIFTE 224
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIVSQ 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
33-221 |
2.57e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.39 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 33 GEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDIRKhDIGFIFQE--YNLLHTLTVKENIMLPL 110
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRR-DIQFIFQDpyASLDPRQTVGDSIMEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 111 TVQKL-DKDTMLDRYEKVAEALNIL-DISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMK 188
Cdd:PRK10261 429 RVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLD 508
|
170 180 190
....*....|....*....|....*....|....
gi 616690417 189 MNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:PRK10261 509 LQRDFGIAYLFISHDmAVVERISHRVAVMYLGQI 542
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
21-221 |
2.96e-23 |
|
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: 98.28 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 21 EVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALsdirKHDIGFIFQEyNLLHTL 100
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWL----RRQMGVVLQE-NVLFSR 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 101 TVKENImlpltvqKLDKDTMLDRY----EKVAEALN-ILDISDKYPSE-------LSGGQRQRTSAARAFITLPSIIFAD 168
Cdd:TIGR01846 546 SIRDNI-------ALCNPGAPFEHvihaAKLAGAHDfISELPQGYNTEvgekganLSGGQRQRIAIARALVGNPRILIFD 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 616690417 169 EPTGALDSKSTQDLLKRLMKMNEeiKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:TIGR01846 619 EATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRACDRIIVLEKGQI 669
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-227 |
4.83e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 97.34 E-value: 4.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 13 YGNKKMAqevLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALsdirKHDIGFIFQ 92
Cdd:PRK13657 344 YDNSRQG---VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 93 EYNLLHTlTVKENImlplTVQKLD-KDTMLDRYEKVAEALN-ILDISDKYP-------SELSGGQRQRTSAARAFITLPS 163
Cdd:PRK13657 417 DAGLFNR-SIEDNI----RVGRPDaTDEEMRAAAERAQAHDfIERKPDGYDtvvgergRQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616690417 164 IIFADEPTGALDSKS---TQDLLKRLMKMneeiKTTIImVTHDPVAASYANRVVMLKDGQI-----FTELYQ 227
Cdd:PRK13657 492 ILILDEATSALDVETeakVKAALDELMKG----RTTFI-IAHRLSTVRNADRILVFDNGRVvesgsFDELVA 558
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
19-216 |
5.96e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.24 E-value: 5.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 19 AQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALsdirKHDIGFIFQEYNLLH 98
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY----RQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 99 TlTVKENIMLPLTV--QKLDKDTMLDRYEKVAEALNILDisdKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDS 176
Cdd:PRK10247 95 D-TVYDNLIFPWQIrnQQPDPAIFLDDLERFALPDTILT---KNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 616690417 177 KSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVML 216
Cdd:PRK10247 171 SNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-221 |
6.31e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.06 E-value: 6.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNkkmaQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALS 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGD----TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 dirkHDIGFIFQEYNLLHTLTVKENIMLPLT--VQKLDKDTMLDRyEKVAEALNILDIS---DKYPSELSGGQRQRTSAA 155
Cdd:PRK09536 77 ----RRVASVPQDTSLSFEFDVRQVVEMGRTphRSRFDTWTETDR-AAVERAMERTGVAqfaDRPVTSLSGGERQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 156 RAFITLPSIIFADEPTGALD---SKSTQDLLKRLMkmnEEIKTTIIMVtHD-PVAASYANRVVMLKDGQI 221
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDinhQVRTLELVRRLV---DDGKTAVAAI-HDlDLAARYCDELVLLADGRV 217
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
28-216 |
7.34e-23 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 92.99 E-value: 7.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 28 MSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhkleklsnkALSDIRKHDIGFIFQ--EYNLLHTLTVKEN 105
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG---------ASPGKGWRHIGYVPQrhEFAWDFPISVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 106 IMLPLT-VQKLDKDTMLDRYEKVAEAL---NILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQD 181
Cdd:TIGR03771 72 VMSGRTgHIGWLRRPCVADFAAVRDALrrvGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQEL 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 616690417 182 LLKRLMKMNEEiKTTIIMVTHD-PVAASYANRVVML 216
Cdd:TIGR03771 152 LTELFIELAGA-GTAILMTTHDlAQAMATCDRVVLL 186
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-184 |
8.98e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 93.03 E-value: 8.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALS 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD---EDISLLPLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIRKHDIGFIFQEYNLLHTLTVKENIMLPLTVQK-LDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFI 159
Cdd:PRK10895 74 ARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180
....*....|....*....|....*
gi 616690417 160 TLPSIIFADEPTGALDSKSTQDLLK 184
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKR 178
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-221 |
9.98e-23 |
|
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: 96.41 E-value: 9.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGN-KKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLK-GHKLEKLSNKALs 80
Cdd:TIGR03269 279 IIKVRNVSKRYISvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGP- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIR---KHDIGFIFQEYNLLHTLTVKEN------IMLPLTVQKLDKDTMLdryeKVA-----EALNILDisdKYPSELSG 146
Cdd:TIGR03269 358 DGRgraKRYIGILHQEYDLYPHRTVLDNlteaigLELPDELARMKAVITL----KMVgfdeeKAEEILD---KYPDELSE 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616690417 147 GQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKI 506
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-243 |
1.42e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 94.00 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYgnkKMAQ--------------------EVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQG 62
Cdd:COG4586 1 IIEVENLSKTY---RVYEkepglkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 63 SITLKGH---KLEKlsnkalsDIRKHdIGFIF-QEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISD 138
Cdd:COG4586 78 EVRVLGYvpfKRRK-------EFARR-IGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 139 KYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDP--VAAsYANRVVML 216
Cdd:COG4586 150 TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMddIEA-LCDRVIVI 228
|
250 260 270
....*....|....*....|....*....|
gi 616690417 217 KDGQIfteLYQGDDD--KHTFFKE-IIRVQ 243
Cdd:COG4586 229 DHGRI---IYDGSLEelKERFGPYkTIVLE 255
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-230 |
1.57e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 96.33 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 20 QEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALsdiRKHdIGFIFQEyNLLHT 99
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL---HRQ-VALVGQE-PVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 100 LTVKENIMLPLTvqkldkDTMLDRYEKVAEALNILDISDKYP-----------SELSGGQRQRTSAARAFITLPSIIFAD 168
Cdd:TIGR00958 569 GSVRENIAYGLT------DTPDEEIMAAAKAANAHDFIMEFPngydtevgekgSQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 169 EPTGALDSKSTQdLLKRLMKMNEEiktTIIMVTHDPVAASYANRVVMLKDGQI-----FTELYQGDD 230
Cdd:TIGR00958 643 EATSALDAECEQ-LLQESRSRASR---TVLLIAHRLSTVERADQILVLKKGSVvemgtHKQLMEDQG 705
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
1.68e-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: 95.64 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSID--------------------YISQ-- 61
Cdd:TIGR03269 1 IEVKNLTKKFDGK----EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyeptsgriiyhvalcekcgYVERps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 62 ----------GSITLKGHKLEKLSNKALSDIRKHdIGFIFQE-YNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEA 130
Cdd:TIGR03269 77 kvgepcpvcgGTLEPEEVDFWNLSDKLRRRIRKR-IAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 131 LNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDP-VAASY 209
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPeVIEDL 235
|
250
....*....|....*
gi 616690417 210 ANRVVMLKDGQIFTE 224
Cdd:TIGR03269 236 SDKAIWLENGEIKEE 250
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-221 |
2.43e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.89 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 23 LRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLS-NKALSDIRKHdIGFIFQ--EYNLLHT 99
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSkNKDIKQIRKK-VGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 100 LTVKENIMLP--LTVQKLDKdtmldryEKVA-EALNILDIS----DKYPSELSGGQRQRTSAARAFITLPSIIFADEPTG 172
Cdd:PRK13649 102 TVLKDVAFGPqnFGVSQEEA-------EALArEKLALVGISeslfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 616690417 173 ALDSKSTQDLLkRLMKMNEEIKTTIIMVTH--DPVaASYANRVVMLKDGQI 221
Cdd:PRK13649 175 GLDPKGRKELM-TLFKKLHQSGMTIVLVTHlmDDV-ANYADFVYVLEKGKL 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-229 |
4.14e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 6 VKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhkleklsnkalsDIRkh 85
Cdd:COG0488 1 LENLSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------------GLR-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 86 dIGFIFQEYNLLHTLTVKENIMLPLT-----VQKLDK--------DTMLDRYE----------------KVAEALNILDI 136
Cdd:COG0488 63 -IGYLPQEPPLDDDLTVLDTVLDGDAelralEAELEEleaklaepDEDLERLAelqeefealggweaeaRAEEILSGLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 137 SDKYP----SELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQ---DLLKRLmkmneeiKTTIIMVTHD-----P 204
Cdd:COG0488 142 PEEDLdrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEwleEFLKNY-------PGTVLVVSHDryfldR 214
|
250 260
....*....|....*....|....*
gi 616690417 205 VaasyANRVVMLKDGQIFTelYQGD 229
Cdd:COG0488 215 V----ATRILELDRGKLTL--YPGN 233
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-203 |
5.73e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 91.20 E-value: 5.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNKKMAQEVlrdiNMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKAlsd 81
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNV----NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IRKHDIGFIFQEYNLLHTLTVKENImlpLTVQKLDKDT------------------MLDRYEKVAEALNILDISDKYPSE 143
Cdd:PRK11300 77 IARMGVVRTFQHVRLFREMTVIENL---LVAQHQQLKTglfsgllktpafrraeseALDRAATWLERVGLLEHANRQAGN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 144 LSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD 203
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
22-221 |
1.33e-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: 89.51 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 22 VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhkleKLSnkalSDIrkhDIGFIFQEynllhTLT 101
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----RVS----SLL---GLGGGFNP-----ELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 102 VKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQD 181
Cdd:cd03220 101 GRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 616690417 182 LLKRLMKMNEEIKtTIIMVTHDPVA-ASYANRVVMLKDGQI 221
Cdd:cd03220 181 CQRRLRELLKQGK-TVILVSHDPSSiKRLCDRALVLEKGKI 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
22-221 |
1.83e-21 |
|
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: 89.09 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 22 VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkaLSDIRKHdIGFIFQEyNLLHTLT 101
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSR-ISIIPQD-PVLFSGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 102 VKENIMlPLTV-------QKLDKDTMLDRYEKVAEALNiLDISDKyPSELSGGQRQRTSAARAFITLPSIIFADEPTGAL 174
Cdd:cd03244 94 IRSNLD-PFGEysdeelwQALERVGLKEFVESLPGGLD-TVVEEG-GENLSVGQRQLLCLARALLRKSKILVLDEATASV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 616690417 175 DSkSTQDLLKRLMKmnEEIK-TTIIMVTH--DPVAASyaNRVVMLKDGQI 221
Cdd:cd03244 171 DP-ETDALIQKTIR--EAFKdCTVLTIAHrlDTIIDS--DRILVLDKGRV 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-203 |
2.32e-21 |
|
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: 92.69 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITL-KGHKleklsnkalsd 81
Cdd:TIGR03719 4 IYTMNRVSKVVPPKK---EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIK----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 irkhdIGFIFQEYNLLHTLTVKENIMLPLTvqklDKDTMLDRYEKVAEAL------------------NILDISDKY--- 140
Cdd:TIGR03719 70 -----VGYLPQEPQLDPTKTVRENVEEGVA----EIKDALDRFNEISAKYaepdadfdklaaeqaelqEIIDAADAWdld 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 141 ------------P------SELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLmkmnEEIKTTIIMVTH 202
Cdd:TIGR03719 141 sqleiamdalrcPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTH 216
|
.
gi 616690417 203 D 203
Cdd:TIGR03719 217 D 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-222 |
3.60e-21 |
|
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: 87.70 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 21 EVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSI--DYIS-QGSITLKGHKLEKLSNKAlsdirKHDIGFIFQEYNLL 97
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRteGNVSvEGDIHYNGIPYKEFAEKY-----PGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 98 HTLTVKENImlpltvqkldkdtmldryEKVAEALNildisDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSK 177
Cdd:cd03233 96 PTLTVRETL------------------DFALRCKG-----NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 616690417 178 STQDLLKRLMKMNEEIKTTIIMVTHDPVAASYA--NRVVMLKDG-QIF 222
Cdd:cd03233 153 TALEILKCIRTMADVLKTTTFVSLYQASDEIYDlfDKVLVLYEGrQIY 200
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-218 |
4.39e-21 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 86.82 E-value: 4.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 22 VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHkleklsnkalsdirkHDIGFIFQE-YNLLHTL 100
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG---------------EDLLFLPQRpYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 101 tvkenimlpltvqkldkdtmldryekvAEALNildisdkYP--SELSGGQRQRTSAARAFITLPSIIFADEPTGALDsks 178
Cdd:cd03223 81 ---------------------------REQLI-------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD--- 123
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 616690417 179 tQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKD 218
Cdd:cd03223 124 -EESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-221 |
7.87e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.91 E-value: 7.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 23 LRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHK----LEKLsnKALSDIRKhDIGFIFQ--EYNL 96
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAipanLKKI--KEVKRLRK-EIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 97 LHTLTVKENIMLPLTVQKlDKDtmlDRYEKVAEALNILDISDKY----PSELSGGQRQRTSAARAFITLPSIIFADEPTG 172
Cdd:PRK13645 104 FQETIEKDIAFGPVNLGE-NKQ---EAYKKVPELLKLVQLPEDYvkrsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 616690417 173 ALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKV 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-202 |
1.02e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.71 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKAlsdi 82
Cdd:PRK13537 7 PIDFRNVEKRYGDKL----VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 rKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLP 162
Cdd:PRK13537 79 -RQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 616690417 163 SIIFADEPTGALDSKSTQDLLKRLMKMNEEIKtTIIMVTH 202
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTH 196
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-223 |
1.45e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 88.25 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 15 NKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLS-NKALSDIRKhDIGFIFQ- 92
Cdd:PRK13643 14 NSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkQKEIKPVRK-KVGVVFQf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 93 -EYNLLHTLTVKENIMLP--LTVQKLDKDTMldryekVAEALNILDIS----DKYPSELSGGQRQRTSAARAFITLPSII 165
Cdd:PRK13643 93 pESQLFEETVLKDVAFGPqnFGIPKEKAEKI------AAEKLEMVGLAdefwEKSPFELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 166 FADEPTGALDSKSTQDLLKrLMKMNEEIKTTIIMVTH--DPVaASYANRVVMLKDGQIFT 223
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHlmDDV-ADYADYVYLLEKGHIIS 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-220 |
1.90e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.59 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 23 LRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDirkHDIGFIFQEYNLLHTLTV 102
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA---AGVAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 103 KENIMLPLTVQKLDkdtMLDRYEKVAEALNIL-----DISDKYP-SELSGGQRQRTSAARAFITLPSIIFADEPTGALDS 176
Cdd:PRK11288 97 AENLYLGQLPHKGG---IVNRRLLNYEAREQLehlgvDIDPDTPlKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 616690417 177 KSTQdllkRLMKMNEEIK---TTIIMVTH--DPVAAsYANRVVMLKDGQ 220
Cdd:PRK11288 174 REIE----QLFRVIRELRaegRVILYVSHrmEEIFA-LCDAITVFKDGR 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-221 |
2.71e-20 |
|
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: 85.99 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAQeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSDI 82
Cdd:cd03248 11 IVKFQNVTFAYPTRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 rkhdIGFIFQEyNLLHTLTVKENIMLPLTVQKLDKDTMLDryEKVAEALNILDISDKYPSE-------LSGGQRQRTSAA 155
Cdd:cd03248 90 ----VSLVGQE-PVLFARSLQDNIAYGLQSCSFECVKEAA--QKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616690417 156 RAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEeiKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-221 |
4.33e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.73 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALsdir 83
Cdd:PRK11160 339 LTLNNVSFTYPDQ--PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTlTVKENImlpltvqKLDKDTMLDryEKVAEALNILDISDKYPSE-------------LSGGQRQ 150
Cdd:PRK11160 413 RQAISVVSQRVHLFSA-TLRDNL-------LLAAPNASD--EALIEVLQQVGLEKLLEDDkglnawlgeggrqLSGGEQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690417 151 RTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEikTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN--KTVLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-245 |
5.66e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.45 E-value: 5.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSI----DYisQGSITLKGhklEKLSN 76
Cdd:PRK13549 3 EYLLEMKNITKTFGGVK----ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgTY--EGEIIFEG---EELQA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 77 KALSDIRKHDIGFIFQEYNLLHTLTVKENIML---PLTVQKLDKDTMLDRYEKVAEALNiLDISDKYP-SELSGGQRQRT 152
Cdd:PRK13549 74 SNIRDTERAGIAIIHQELALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLK-LDINPATPvGNLGLGQQQLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 153 SAARAFITLPSIIFADEPTGALDSKSTQ---DLLKRLM-----------KMNE--EIKTTIIM------VTHDPVAASYA 210
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASLTESETAvllDIIRDLKahgiaciyishKLNEvkAISDTICVirdgrhIGTRPAAGMTE 232
|
250 260 270
....*....|....*....|....*....|....*
gi 616690417 211 NRVVMLKDGQIFTELYQGddDKHTFFKEIIRVQSV 245
Cdd:PRK13549 233 DDIITMMVGRELTALYPR--EPHTIGEVILEVRNL 265
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
4-202 |
7.59e-20 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 88.46 E-value: 7.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTkiYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSdir 83
Cdd:TIGR03796 478 VELRNIT--FGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLA--- 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 kHDIGFIFQEYNLLHTlTVKENIMLpltvqkLDkDTMLDryEKVAEALN-------ILDISDKYPSEL-------SGGQR 149
Cdd:TIGR03796 553 -NSVAMVDQDIFLFEG-TVRDNLTL------WD-PTIPD--ADLVRACKdaaihdvITSRPGGYDAELaegganlSGGQR 621
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 616690417 150 QRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNeeikTTIIMVTH 202
Cdd:TIGR03796 622 QRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRRG----CTCIIVAH 670
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-221 |
1.16e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.77 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkaLSDIR 83
Cdd:PRK11176 342 IEFRNVTFTYPGKE--VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT---LASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTlTVKENIMLPLTvqkldkdtmlDRY-----EKVAEALNILDISDKYPS-----------ELSGG 147
Cdd:PRK11176 417 NQ-VALVSQNVHLFND-TIANNIAYART----------EQYsreqiEEAARMAYAMDFINKMDNgldtvigengvLLSGG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616690417 148 QRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLmkmnEEIKT--TIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAAL----DELQKnrTSLVIAHRLSTIEKADEILVVEDGEI 556
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-250 |
1.26e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.06 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAQ-EVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLK----GHKLEKLSNK 77
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENElVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 78 ALSDIRK--------HDIGFIFQ--EYNLLHTlTVKENIMLPLTVQKLDKDtmlDRYEKVAEALNILDISDKY----PSE 143
Cdd:PRK13631 101 TNPYSKKiknfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKS---EAKKLAKFYLNKMGLDDSYlersPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 144 LSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLkRLMKMNEEIKTTIIMVTH--DPVaASYANRVVMLKDGQI 221
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMM-QLILDAKANNKTVFVITHtmEHV-LEVADEVIVMDKGKI 254
|
250 260 270
....*....|....*....|....*....|.
gi 616690417 222 FT--ELYQGDDDKHTFFKEIIRVQSVLGGIN 250
Cdd:PRK13631 255 LKtgTPYEIFTDQHIINSTSIQVPRVIQVIN 285
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-221 |
2.56e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.96 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSI-DY-ISQGSITLKGHKLEKLSnkalSD 81
Cdd:COG0396 1 LEIKNLHVSVEGK----EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpKYeVTSGSILLDGEDILELS----PD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IR-KHDIGFIFQE---------YNLLHTLtvkenimlpLTVQKLDKDTMLDRYEKVAEALNILDISDKYPS-----ELSG 146
Cdd:COG0396 73 ERaRAGIFLAFQYpveipgvsvSNFLRTA---------LNARRGEELSAREFLKLLKEKMKELGLDEDFLDryvneGFSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 147 GQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHDPVAASY--ANRVVMLKDGQI 221
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHYQRILDYikPDFVHVLVDGRI 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-221 |
6.18e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.82 E-value: 6.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MT-ILEVKQLTKIY----------------GNKKMAQE--VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQ 61
Cdd:COG1134 1 MSsMIEVENVSKSYrlyhepsrslkelllrRRRTRREEfwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 62 GSITLKGhkleKLSnkALsdIrkhDIGFIFQeynllHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAE-AlnilDISDK- 139
Cdd:COG1134 81 GRVEVNG----RVS--AL--L---ELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEfA----ELGDFi 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 140 ------YPSelsgGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKtTIIMVTHDP-VAASYANR 212
Cdd:COG1134 141 dqpvktYSS----GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMgAVRRLCDR 215
|
....*....
gi 616690417 213 VVMLKDGQI 221
Cdd:COG1134 216 AIWLEKGRL 224
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-203 |
8.04e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 85.17 E-value: 8.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITL-KGHKleklsnkalsd 81
Cdd:PRK11819 6 IYTMNRVSKVVPPKK---QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIK----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 irkhdIGFIFQEYNLLHTLTVKENIMLPLTvqklDKDTMLDRYEKVAEAL------------------NILDISDKY--- 140
Cdd:PRK11819 72 -----VGYLPQEPQLDPEKTVRENVEEGVA----EVKAALDRFNEIYAAYaepdadfdalaaeqgelqEIIDAADAWdld 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 141 ------------P------SELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLmkmnEEIKTTIIMVTH 202
Cdd:PRK11819 143 sqleiamdalrcPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYPGTVVAVTH 218
|
.
gi 616690417 203 D 203
Cdd:PRK11819 219 D 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-229 |
1.98e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.96 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLkGHKLEklsnkalsd 81
Cdd:COG0488 314 KVLELEGLSKSYGDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK--------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 irkhdIGFIFQEYNLLH-TLTVKENImlpltvqkldKDTMLDRYEKvaEALNIL-------DISDKYPSELSGGQRQRTS 153
Cdd:COG0488 380 -----IGYFDQHQEELDpDKTVLDEL----------RDGAPGGTEQ--EVRGYLgrflfsgDDAFKPVGVLSGGEKARLA 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 154 AARAFITLPSIIFADEPTGALDSKSTQDLLKRLmkmnEEIKTTIIMVTHDPvaasY-----ANRVVMLKDGQIftELYQG 228
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLDIETLEALEEAL----DDFPGTVLLVSHDR----YfldrvATRILEFEDGGV--REYPG 512
|
.
gi 616690417 229 D 229
Cdd:COG0488 513 G 513
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-224 |
1.98e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.96 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 23 LRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNkaLSDIRKHdIGFIFQ--EYNLLHTl 100
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGIRKL-VGIVFQnpETQFVGR- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 101 TVKENIML--------PLTVQKL-DK---DTMLDRYEKvaealnildisdKYPSELSGGQRQRTSAARAFITLPSIIFAD 168
Cdd:PRK13644 94 TVEEDLAFgpenlclpPIEIRKRvDRalaEIGLEKYRH------------RSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 616690417 169 EPTGALDSKSTQDLLKRLMKMNEEIKtTIIMVTHDPVAASYANRVVMLKDGQIFTE 224
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-220 |
2.11e-18 |
|
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: 83.72 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSI----DYisQGSITLKGhklEKLSNKA 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK----ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgTW--DGEIYWSG---SPLKASN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 79 LSDIRKHDIGFIFQEYNLLHTLTVKENIML----PLTVQKLDKDTMLDRYEKVAEALNILDISDKYP-SELSGGQRQRTS 153
Cdd:TIGR02633 72 IRDTERAGIVIIHQELTLVPELSVAENIFLgneiTLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 154 AARAFITLPSIIFADEPTGALDSKSTQDLLKrLMKMNEEIKTTIIMVTH--DPVAAsYANRVVMLKDGQ 220
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLD-IIRDLKAHGVACVYISHklNEVKA-VCDTICVIRDGQ 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-224 |
5.54e-18 |
|
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: 79.11 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSI-DY-ISQGSITLKGHKLEKLSnkaLSD 81
Cdd:cd03217 1 LEIKDLHVSVGGK----EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpKYeVTEGEILFKGEDITDLP---PEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IRKHDIGFIFQEynllhtltvkenimlPLTVQKLdkdtmldryeKVAEALNILDISdkypseLSGGQRQRTSAARAFITL 161
Cdd:cd03217 74 RARLGIFLAFQY---------------PPEIPGV----------KNADFLRYVNEG------FSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616690417 162 PSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHDPVAASY--ANRVVMLKDGQIFTE 224
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYikPDRVHVLYDGRIVKS 186
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-219 |
5.88e-18 |
|
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: 79.68 E-value: 5.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 23 LRDINMSVEEGEFIAIMGPSGSGKTTLL-NVLSSIDYISqGSITLKGHKLEKLSNKALSDIRKHDIGFIFQEYNLLHTlT 101
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLE-GKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA-T 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 102 VKENIMLPLTVQKldkdtmlDRYEKVAEALNILDISDKYPS-----------ELSGGQRQRTSAARAFITLPSIIFADEP 170
Cdd:cd03290 95 VEENITFGSPFNK-------QRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 616690417 171 TGALDSKSTQDLLKR-LMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDG 219
Cdd:cd03290 168 FSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-208 |
6.85e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 80.21 E-value: 6.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNKkMAqevLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSI-DYI----SQGSITLKGHKLEKlSN 76
Cdd:PRK14243 9 TVLRTENLNVYYGSF-LA---VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLnDLIpgfrVEGKVTFHGKNLYA-PD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 77 KALSDIRKHdIGFIFQEYNLLHTlTVKENIMLPLTVQ--KLDKDTMLDRYEKVAEALNilDISDKYP---SELSGGQRQR 151
Cdd:PRK14243 84 VDPVEVRRR-IGMVFQKPNPFPK-SIYDNIAYGARINgyKGDMDELVERSLRQAALWD--EVKDKLKqsgLSLSGGQQQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 152 TSAARAFITLPSIIFADEPTGALDSKST---QDLLKRLMKmneeiKTTIIMVTHDPVAAS 208
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTlriEELMHELKE-----QYTIIIVTHNMQQAA 214
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-221 |
6.97e-18 |
|
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: 82.56 E-value: 6.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 21 EVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALsdiRKHdIGFIFQEYNLLHTl 100
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---RAA-IGIVPQDTVLFND- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 101 TVKENImlpltvqkldkdtmldRY----------EKVAEALNILD-IS---DKYPSE-------LSGGQRQRTSAARAFI 159
Cdd:COG5265 447 TIAYNI----------------AYgrpdaseeevEAAARAAQIHDfIEslpDGYDTRvgerglkLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 160 TLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIM------VTHdpvaasyANRVVMLKDGQI 221
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVARG-RTTLVIahrlstIVD-------ADEILVLEAGRI 570
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-221 |
7.20e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.13 E-value: 7.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 19 AQEVLRDINMSVEEGEFIAIMGPSGSGKT----TLLNVLSSIDYISQGSITLKGHKLeklsnkALSDIRKHDIGFIFQE- 93
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPV------APCALRGRKIATIMQNp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 94 ---YNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKV--AEALNILDIsdkYPSELSGGQRQRTSAARAFITLPSIIFAD 168
Cdd:PRK10418 89 rsaFNPLHTMHTHARETCLALGKPADDATLTAALEAVglENAARVLKL---YPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 616690417 169 EPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDmGVVARLADDVAVMSHGRI 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-204 |
9.33e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.76 E-value: 9.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSdir 83
Cdd:PRK13539 3 LEGEDLACVRGGR----VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAC--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 kHDIGfifqeynllH------TLTVKENIMLpltVQKLDKDTMLDryekVAEALNILDISD------KYpseLSGGQRQR 151
Cdd:PRK13539 76 -HYLG---------HrnamkpALTVAENLEF---WAAFLGGEELD----IAAALEAVGLAPlahlpfGY---LSAGQKRR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 616690417 152 TSAARAFITLPSIIFADEPTGALDSkSTQDLLKRLMKMNEEIKTTIIMVTHDP 204
Cdd:PRK13539 136 VALARLLVSNRPIWILDEPTAALDA-AAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-219 |
1.14e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.75 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGnkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKalsDIR 83
Cdd:PRK09700 6 ISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK---LAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENIML-PLTVQKLDKDTMLDRYE---KVAEALNILDIS---DKYPSELSGGQRQRTSAAR 156
Cdd:PRK09700 79 QLGIGIIYQELSVIDELTVLENLYIgRHLTKKVCGVNIIDWREmrvRAAMMLLRVGLKvdlDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616690417 157 AFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKtTIIMVTHD-PVAASYANRVVMLKDG 219
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-221 |
1.32e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 81.69 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKMaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALsdiR 83
Cdd:PRK10790 341 IDIDNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---R 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTlTVKENIMLPltvQKLDKDTMLDRYEKVAEALNILDISDKYPSE-------LSGGQRQRTSAAR 156
Cdd:PRK10790 415 QG-VAMVQQDPVVLAD-TFLANVTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPlgeqgnnLSVGQKQLLALAR 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616690417 157 AFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEeiKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVEADTILVLHRGQA 552
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-225 |
1.65e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.22 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTkiygnkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALSD 81
Cdd:COG1129 255 VVLEVEGLS--------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPVRIRSPRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IRKHDIGFI---FQEYNLLHTLTVKENIMLPlTVQK------LDKDTMLDRYEKVAEALNIldisdKYPS------ELSG 146
Cdd:COG1129 324 AIRAGIAYVpedRKGEGLVLDLSIRENITLA-SLDRlsrgglLDRRRERALAEEYIKRLRI-----KTPSpeqpvgNLSG 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 147 GQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHD-PVAASYANRVVMLKDGQIFTEL 225
Cdd:COG1129 398 GNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSElPELLGLSDRILVMREGRIVGEL 476
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
10-240 |
1.82e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.46 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 10 TKIYGNKKMAQE--VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYIS--QGSITLKGHKLEKLSNKAlsdirkh 85
Cdd:PLN03211 69 PKISDETRQIQErtILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKR------- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 86 dIGFIFQEYNLLHTLTVKENIM------LPLTVQKLDKDTMLdryEKVAEALNILD-----ISDKYPSELSGGQRQRTSA 154
Cdd:PLN03211 142 -TGFVTQDDILYPHLTVRETLVfcsllrLPKSLTKQEKILVA---ESVISELGLTKcentiIGNSFIRGISGGERKRVSI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 155 ARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKtTIIMVTHDPVAASYA--NRVVMLKDGQIfteLYQGDDDK 232
Cdd:PLN03211 218 AHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGK-TIVTSMHQPSSRVYQmfDSVLVLSEGRC---LFFGKGSD 293
|
....*...
gi 616690417 233 HTFFKEII 240
Cdd:PLN03211 294 AMAYFESV 301
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-220 |
3.48e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.18 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLT-KIYGNKKMAQEVLRdINMSVEEGEFIAIMGPSGSGKT----TLLNVLSSIDYISQGSITLKGHKLEKLS 75
Cdd:COG4170 1 MPLLDIRNLTiEIDTPQGRVKAVDR-VSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 76 NKALSDIRKHDIGFIFQEYN--LLHTLTVKENIMlpltvQKLDKDTMLDRY-----EKVAEALNIL---------DISDK 139
Cdd:COG4170 80 PRERRKIIGREIAMIFQEPSscLDPSAKIGDQLI-----EAIPSWTFKGKWwqrfkWRKKRAIELLhrvgikdhkDIMNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 140 YPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSkSTQDLLKRLM-KMNEEIKTTIIMVTHDPVA-ASYANRVVMLK 217
Cdd:COG4170 155 YPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMES-TTQAQIFRLLaRLNQLQGTSILLISHDLESiSQWADTITVLY 233
|
...
gi 616690417 218 DGQ 220
Cdd:COG4170 234 CGQ 236
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-229 |
5.64e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.91 E-value: 5.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 22 VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKALSdiRKhdIGFIFQEYNLLHTLT 101
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA--RK--VAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 102 VKENImlplTVQKLDKDTMLDRY-----EKVAEALNILDI---SDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGA 173
Cdd:PRK10575 102 VRELV----AIGRYPWHGALGRFgaadrEKVEEAISLVGLkplAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616690417 174 LDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQIFT-----ELYQGD 229
Cdd:PRK10575 178 LDIAHQVDVLALVHRLSQERGLTVIAVLHDiNMAARYCDYLVALRGGEMIAqgtpaELMRGE 239
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-219 |
6.06e-17 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 76.13 E-value: 6.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 16 KKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSS--IDYISQGSITLKGHKLEKLSNKAlsdirkhdIGFIFQE 93
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQRS--------TGYVEQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 94 YNLLHTLTVKENIMLpltvqkldkdtmldryekvaEALNildisdkypSELSGGQRQRTSAARAFITLPSIIFADEPTGA 173
Cdd:cd03232 88 DVHSPNLTVREALRF--------------------SALL---------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 616690417 174 LDSKSTQDLLKRLMKMNEEiKTTIIMVTHDPVAA--SYANRVVMLKDG 219
Cdd:cd03232 139 LDSQAAYNIVRFLKKLADS-GQAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-219 |
6.44e-17 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 79.77 E-value: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLS---SIDYISQGSITLKGHKLEKlsnkal 79
Cdd:TIGR00956 759 IFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervTTGVITGGDRLVNGRPLDS------ 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 80 SDIRKhdIGFIFQEYNLLHTLTVKENIM------LPLTVQKLDKdtmlDRY-EKVAEALNILDISDKY---PSE-LSGGQ 148
Cdd:TIGR00956 833 SFQRS--IGYVQQQDLHLPTSTVRESLRfsaylrQPKSVSKSEK----MEYvEEVIKLLEMESYADAVvgvPGEgLNVEQ 906
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 149 RQRTSAARAFITLP-SIIFADEPTGALDSK---STQDLLKRLMKMNEEIKTTIimvtHDPVAASYA--NRVVMLKDG 219
Cdd:TIGR00956 907 RKRLTIGVELVAKPkLLLFLDEPTSGLDSQtawSICKLMRKLADHGQAILCTI----HQPSAILFEefDRLLLLQKG 979
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-224 |
8.04e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.83 E-value: 8.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 19 AQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSID-----YISQGSITLKGHKLekLSNKALSDIRKHdIGFIFQE 93
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGRSI--FNYRDVLEFRRR-VGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 94 YNLLhTLTVKENIMLPLTVQKLdkdTMLDRYEKVAEA----LNILD-----ISDKyPSELSGGQRQRTSAARAFITLPSI 164
Cdd:PRK14271 110 PNPF-PMSIMDNVLAGVRAHKL---VPRKEFRGVAQArlteVGLWDavkdrLSDS-PFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690417 165 IFADEPTGALDSKSTQDLLKRLMKMNEEIktTIIMVTHD-PVAASYANRVVMLKDGQIFTE 224
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNlAQAARISDRAALFFDGRLVEE 243
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-204 |
8.69e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.54 E-value: 8.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 20 QEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLssidyisqgsitlkghkLEKLSNKALSDIRKHDIGFIFQEYNLLht 99
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL-----------------AGALKGTPVAGCVDVPDNQFGREASLI-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 100 ltvkENImlpltvqkLDKDTMLDryekVAEALNILDISDKY-----PSELSGGQRQRTSAARAFITLPSIIFADEPTGAL 174
Cdd:COG2401 104 ----DAI--------GRKGDFKD----AVELLNAVGLSDAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190
....*....|....*....|....*....|
gi 616690417 175 DSKSTQDLLKRLMKMNEEIKTTIIMVTHDP 204
Cdd:COG2401 168 DRQTAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-221 |
1.22e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.14 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNK-----KMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEklsn 76
Cdd:PRK15112 3 TLLEVRNLSKTFRYRtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 77 kaLSD--IRKHDIGFIFQEYNllHTLTVKENIM----LPLtvqKLDKD-TMLDRYEKVAEALNIL----DISDKYPSELS 145
Cdd:PRK15112 79 --FGDysYRSQRIRMIFQDPS--TSLNPRQRISqildFPL---RLNTDlEPEQREKQIIETLRQVgllpDHASYYPHMLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 146 GGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVT-HDPVAASYANRVVMLKDGQI 221
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHLGMMKHISDQVLVMHQGEV 228
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
22-221 |
1.87e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 78.22 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 22 VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLsnkALSDIRKH-----DIGFIFQEynl 96
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRlavvsQTPFLFSD--- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 97 lhtlTVKENIML--PLTVQkldkdtmlDRYEKVAEALN----ILDISDKYPSE-------LSGGQRQRTSAARAFITLPS 163
Cdd:PRK10789 404 ----TVANNIALgrPDATQ--------QEIEHVARLASvhddILRLPQGYDTEvgergvmLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 164 IIFADEPTGALDSKSTQDLLKRLMKMNEeiKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-202 |
2.03e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.18 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALS 80
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG---VPVPARARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIRKhdIGFIFQEYNLLHTLTVKENIML-----PLTVQKLDK--DTMLD--RYEKVAealnildisDKYPSELSGGQRQR 151
Cdd:PRK13536 112 ARAR--IGVVPQFDNLDLEFTVRENLLVfgryfGMSTREIEAviPSLLEfaRLESKA---------DARVSDLSGGMKRR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 616690417 152 TSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKtTIIMVTH 202
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTH 230
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-237 |
2.23e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 78.23 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 22 VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQ----GSITLKGHKLEklsnkalsDIRKH---DIGFIFQEY 94
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHigveGVITYDGITPE--------EIKKHyrgDVVYNAETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 95 NLLHTLTVKENIMLPL---TVQK----LDKDTMLDRYEKVAEALNILDIS------DKYPSELSGGQRQRTSAARAFITL 161
Cdd:TIGR00956 148 VHFPHLTVGETLDFAArckTPQNrpdgVSREEYAKHIADVYMATYGLSHTrntkvgNDFVRGVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 162 PSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYA--NRVVMLKDGQIfteLYQGDDDK-HTFFK 237
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYElfDKVIVLYEGYQ---IYFGPADKaKQYFE 303
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-222 |
2.86e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 78.13 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 6 VKQLTKIYgnKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKlsnkALSDIRKh 85
Cdd:TIGR01257 931 VKNLVKIF--EPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQ- 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 86 DIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSII 165
Cdd:TIGR01257 1004 SLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 166 FADEPTGALDSKSTQDLLKRLMKMNEeiKTTIIMVTHDPVAAS-YANRVVMLKDGQIF 222
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADlLGDRIAIISQGRLY 1139
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-221 |
2.98e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.40 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGnkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLS-NKAlsd 81
Cdd:PRK15439 11 LLCARSISKQYS----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKA--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 irkHDIG--FIFQEYNLLHTLTVKENIMLPLTVQKldkdtmlDRYEKVAEALNILDIS---DKYPSELSGGQRQRTSAAR 156
Cdd:PRK15439 84 ---HQLGiyLVPQEPLLFPNLSVKENILFGLPKRQ-------ASMQKMKQLLAALGCQldlDSSAGSLEVADRQIVEILR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616690417 157 AFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:PRK15439 154 GLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKlPEIRQLADRISVMRDGTI 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-230 |
3.47e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.52 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKiYGNKKmaqevLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALSD 81
Cdd:PRK09700 264 TVFEVRNVTS-RDRKK-----VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNG---KDISPRSPLD 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IRKHDIGFIFQ---EYNLLHTLTVKENIMLPLTVQK--------LDKDTMLDRY-EKVAEALNILDIS-DKYPSELSGGQ 148
Cdd:PRK09700 335 AVKKGMAYITEsrrDNGFFPNFSIAQNMAISRSLKDggykgamgLFHEVDEQRTaENQRELLALKCHSvNQNITELSGGN 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 149 RQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKtTIIMVTHD-PVAASYANRVVMLKDGQIFTELYQ 227
Cdd:PRK09700 415 QQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSElPEIITVCDRIAVFCEGRLTQILTN 493
|
...
gi 616690417 228 GDD 230
Cdd:PRK09700 494 RDD 496
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-224 |
4.42e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.92 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALS 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKI----QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG---KDITDWQTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIRKHDIGFIFQEYNLLHTLTVKENimLPLTVQKLDKDTMLDRYEKVAEAL-NILDISDKYPSELSGGQRQRTSAARAFI 159
Cdd:PRK11614 76 KIMREAVAIVPEGRRVFSRMTVEEN--LAMGGFFAERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616690417 160 TLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQIFTE 224
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-232 |
7.77e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.69 E-value: 7.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 20 QEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYIsQGSITLKGhKLEkLSNKALSDIR------KHDIGFIFQE 93
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEG-RVE-FFNQNIYERRvnlnrlRRQVSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 94 YNLLhTLTVKENIMLPLTV----QKLDKDTMLDRYEKVAEALN-ILDISDKYPSELSGGQRQRTSAARAFITLPSIIFAD 168
Cdd:PRK14258 97 PNLF-PMSVYDNVAYGVKIvgwrPKLEIDDIVESALKDADLWDeIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616690417 169 EPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDpvaasyANRVVMLKDgqiFTELYQGDDDK 232
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN------LHQVSRLSD---FTAFFKGNENR 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-203 |
8.57e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.38 E-value: 8.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSItLKGHKLEklsnkals 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRR----VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-KRNGKLR-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 dirkhdIGFIFQEYNLLHT--LTVKENIMLPLTVQKLDKDTMLDRyekvAEALNILDisdkYP-SELSGGQRQRTSAARA 157
Cdd:PRK09544 69 ------IGYVPQKLYLDTTlpLTVNRFLRLRPGTKKEDILPALKR----VQAGHLID----APmQKLSGGETQRVLLARA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 616690417 158 FITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD 203
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-184 |
1.38e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALSD 81
Cdd:PRK10762 3 ALLQLKGIDKAFPGVK----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IRKHDIGFIFQEYNLLHTLTVKENIML----PLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARA 157
Cdd:PRK10762 76 SQEAGIGIIHQELNLIPQLTIAENIFLgrefVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180
....*....|....*....|....*..
gi 616690417 158 FITLPSIIFADEPTGALDSKSTQDLLK 184
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTETESLFR 182
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-205 |
1.74e-15 |
|
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: 72.39 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGnkkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkalsDIR 83
Cdd:TIGR01189 1 LAARNLACSRG----ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-----DEP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENimlpLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPS 163
Cdd:TIGR01189 72 HENILYLGHLPGLKPELSALEN----LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 616690417 164 IIFADEPTGALDsKSTQDLLKRLMKMNEEIKTTIIMVTHDPV 205
Cdd:TIGR01189 148 LWILDEPTTALD-KAGVALLAGLLRAHLARGGIVLLTTHQDL 188
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-221 |
1.75e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 73.71 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 22 VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSiDYIS---------QGSITLKGHKLEKLSNKALSDIRkhdiGFIFQ 92
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGggaprgarvTGDVTLNGEPLAAIDAPRLARLR----AVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 93 EYNLLHTLTVKENIMLPL--------TVQKLDKDTMLDRYEKV-AEALNILDISdkypsELSGGQRQRTSAARAFITL-- 161
Cdd:PRK13547 91 AAQPAFAFSAREIVLLGRypharragALTHRDGEIAWQALALAgATALVGRDVT-----TLSGGELARVQFARVLAQLwp 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 162 -------PSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDP-VAASYANRVVMLKDGQI 221
Cdd:PRK13547 166 phdaaqpPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPnLAARHADRIAMLADGAI 233
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-220 |
2.60e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 74.07 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 1 MTILEVKQLTKIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSID----YISQGSITLKGHKLEKLSN 76
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 77 KALSDIRKHDIGFIFQEYNllHTLTVKENIMLPLtVQKLDKDTMLDRY--------EKVAEALNILDISD------KYPS 142
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQ--SCLDPSERVGRQL-MQNIPGWTYKGRWwqrfgwrkRRAIELLHRVGIKDhkdamrSFPY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 143 ELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQ 220
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDlQMLSQWADKINVLYCGQ 236
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-203 |
3.46e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 70.17 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLkghkleklsnkalsdIR 83
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW---------------GS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQeynllhtltvkenimlpltvqkldkdtmldryekvaealnildisdkypseLSGGQRQRTSAARAFITLPS 163
Cdd:cd03221 62 TVKIGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 616690417 164 IIFADEPTGALDSKStQDLLKRLMKmneEIKTTIIMVTHD 203
Cdd:cd03221 91 LLLLDEPTNHLDLES-IEALEEALK---EYPGTVILVSHD 126
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-204 |
9.82e-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: 70.60 E-value: 9.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKlsnkaLSDIR 83
Cdd:cd03231 1 LEADELTCERDGRA----LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF-----QRDSI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDIGFIFQEYNLLHTLTVKENimlpLTVQKLDKDTmldryEKVAEALNILDIS---DKYPSELSGGQRQRTSAARAFIT 160
Cdd:cd03231 72 ARGLLYLGHAPGIKTTLSVLEN----LRFWHADHSD-----EQVEEALARVGLNgfeDRPVAQLSAGQQRRVALARLLLS 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 616690417 161 LPSIIFADEPTGALDsKSTQDLLKRLMKMNEEIKTTIIMVTHDP 204
Cdd:cd03231 143 GRPLWILDEPTTALD-KAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-189 |
1.10e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.75 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTkIYGNKKmaQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKAlsd 81
Cdd:COG3845 256 VVLEVENLS-VRDDRG--VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE--- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IRKHDIGFIFQE---YNLLHTLTVKENIMLPLTVQK-------LDKDTMLDRYEKVAEALNIldisdKYPSE------LS 145
Cdd:COG3845 330 RRRLGVAYIPEDrlgRGLVPDMSVAENLILGRYRRPpfsrggfLDRKAIRAFAEELIEEFDV-----RTPGPdtparsLS 404
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 616690417 146 GGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKM 189
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL 448
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
21-228 |
2.22e-14 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 72.57 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 21 EVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLS---SIDYIsQGSITLKGHKLEKLSNKALSDirkhdigfiFQEYNLL 97
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrkTGGYI-EGDIRISGFPKKQETFARISG---------YCEQNDI 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 98 HT--LTVKENIM------LPLTVQKLDKDTMLDRYEKVAEALNILDISDKYP--SELSGGQRQRTSAARAFITLPSIIFA 167
Cdd:PLN03140 964 HSpqVTVRESLIysaflrLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616690417 168 DEPTGALDSKSTQdLLKRLMKMNEEIKTTIIMVTHDP---VAASYANRVVMLKDGQIfteLYQG 228
Cdd:PLN03140 1044 DEPTSGLDARAAA-IVMRTVRNTVDTGRTVVCTIHQPsidIFEAFDELLLMKRGGQV---IYSG 1103
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-241 |
3.20e-14 |
|
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: 71.90 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 23 LRDINMSVEEGEFIAIMGPSGSGKTTLLN-VLSSIDYIsQGSITLKGhkleklsnkalsdirkhDIGFIFQEyNLLHTLT 101
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVHMKG-----------------SVAYVPQQ-AWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 102 VKENIMLPLTVQKldkdtmlDRYEKVAEALNILDISDKYPS-----------ELSGGQRQRTSAARAFITLPSIIFADEP 170
Cdd:TIGR00957 715 LRENILFGKALNE-------KYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616690417 171 TGALDSKSTQDLLKRLMKMNEEIKT-TIIMVTHDPVAASYANRVVMLKDGQIfTEL--YQGDDDKHTFFKEIIR 241
Cdd:TIGR00957 788 LSAVDAHVGKHIFEHVIGPEGVLKNkTRILVTHGISYLPQVDVIIVMSGGKI-SEMgsYQELLQRDGAFAEFLR 860
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-221 |
3.39e-14 |
|
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: 69.36 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkaLSDIR 83
Cdd:cd03369 7 IEVENLSVRYAPD--LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTlTVKENimlpltvqkldkdtmLDRY-----EKVAEALNILDISdkypSELSGGQRQRTSAARAF 158
Cdd:cd03369 82 SS-LTIIPQDPTLFSG-TIRSN---------------LDPFdeysdEEIYGALRVSEGG----LNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 159 ITLPSIIFADEPTGALDSkSTQDLLKRLMKmNEEIKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:cd03369 141 LKRPRVLVLDEATASIDY-ATDALIQKTIR-EEFTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
6-217 |
3.84e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.30 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 6 VKQLTKIYGNKKMAqevLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLkghkLEKLSNKALsdiRKH 85
Cdd:PRK15056 9 VNDVTVTWRNGHTA---LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI----LGQPTRQAL---QKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 86 DIGFIFQ--EYNLLHTLTVKENIMLPLT--VQKLDKDTMLDRyEKVAEALNILDISD---KYPSELSGGQRQRTSAARAF 158
Cdd:PRK15056 79 LVAYVPQseEVDWSFPVLVEDVVMMGRYghMGWLRRAKKRDR-QIVTAALARVDMVEfrhRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 159 ITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLK 217
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-202 |
9.69e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.14 E-value: 9.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 23 LRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLE-KLSNKALsdirKHDIGFIFQEYNLLHTLT 101
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEAL----ENGISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 102 VKENIML---PLTVQKLDKDTMLDRYEKVAEALNI-LDISDKYpSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSK 177
Cdd:PRK10982 90 VMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIdIDPRAKV-ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180
....*....|....*....|....*
gi 616690417 178 STQDLLKRLMKMNEEiKTTIIMVTH 202
Cdd:PRK10982 169 EVNHLFTIIRKLKER-GCGIVYISH 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-218 |
2.60e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.29 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 21 EVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLK-GHKLEKLSNK---------------------- 77
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKwwrskigvvsqdpllfsnsikn 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 78 -------------ALSDIRKHDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMLD---RYEKVAEAlNILDIS---- 137
Cdd:PTZ00265 479 nikyslyslkdleALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEmrkNYQTIKDS-EVVDVSkkvl 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 138 ---------DKY-------PSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRL--MKMNEEiKTTIIm 199
Cdd:PTZ00265 558 ihdfvsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNEN-RITII- 635
|
250
....*....|....*....
gi 616690417 200 VTHDPVAASYANRVVMLKD 218
Cdd:PTZ00265 636 IAHRLSTIRYANTIFVLSN 654
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-240 |
4.56e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.46 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 17 KMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLN-VLSSIDYISQGSITLKGhkleklsnkalSDIRKHDIGFIFQEyn 95
Cdd:PLN03232 627 KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-----------SVAYVPQVSWIFNA-- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 96 llhtlTVKENIMLpltvqklDKDTMLDRYEKVAEALNILDISDKYPSE-----------LSGGQRQRTSAARAFITLPSI 164
Cdd:PLN03232 694 -----TVRENILF-------GSDFESERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDI 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 165 IFADEPTGALDSKSTQDLLKRLMKmnEEIK-TTIIMVTHDPVAASYANRVVMLKDGQI-----FTELYQGDddkhTFFKE 238
Cdd:PLN03232 762 YIFDDPLSALDAHVAHQVFDSCMK--DELKgKTRVLVTNQLHFLPLMDRIILVSEGMIkeegtFAELSKSG----SLFKK 835
|
..
gi 616690417 239 II 240
Cdd:PLN03232 836 LM 837
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-207 |
5.01e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.98 E-value: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhkleklsnkalSDIR 83
Cdd:PRK13538 2 LEARNLACERDERI----LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG-----------EPIR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHDigfifQEY--NLL---HT------LTVKEN--IMLPLTvQKLDKDTMLDRYEKVaealNILDISDKYPSELSGGQRQ 150
Cdd:PRK13538 67 RQR-----DEYhqDLLylgHQpgikteLTALENlrFYQRLH-GPGDDEALWEALAQV----GLAGFEDVPVRQLSAGQQR 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 151 RTSAARAFITLPSIIFADEPTGALDSKSTqDLLKRLMKMNEEIKTTIIMVTHDPVAA 207
Cdd:PRK13538 137 RVALARLWLTRAPLWILDEPFTAIDKQGV-ARLEALLAQHAEQGGMVILTTHQDLPV 192
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-221 |
7.46e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.84 E-value: 7.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 17 KMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLN-VLSSIDYISQGSITLKGhkleklsnkalSDIRKHDIGFIFQEyn 95
Cdd:PLN03130 627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-----------TVAYVPQVSWIFNA-- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 96 llhtlTVKENIMLPLTVQKldkdtmlDRYEKVAEA------LNILDISD-----KYPSELSGGQRQRTSAARAFITLPSI 164
Cdd:PLN03130 694 -----TVRDNILFGSPFDP-------ERYERAIDVtalqhdLDLLPGGDlteigERGVNISGGQKQRVSMARAVYSNSDV 761
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 165 IFADEPTGALDSKSTQDLLKRLMKmNEEIKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:PLN03130 762 YIFDDPLSALDAHVGRQVFDKCIK-DELRGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-222 |
1.81e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.92 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 22 VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLsnkALSDIRKhdIGFIFQEYNLLHTLT 101
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF---GLTDLRR--VLSIIPQSPVLFSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 102 VKENImlpltvQKLDKDTMLDRYEKVAEAlNILDISDKYP-----------SELSGGQRQRTSAARAFITLPSIIFADEP 170
Cdd:PLN03232 1326 VRFNI------DPFSEHNDADLWEALERA-HIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 616690417 171 TGALDSKsTQDLLKRLMKmnEEIKT-TIIMVTHDPVAASYANRVVMLKDGQIF 222
Cdd:PLN03232 1399 TASVDVR-TDSLIQRTIR--EEFKScTMLVIAHRLNTIIDCDKILVLSSGQVL 1448
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-202 |
4.25e-12 |
|
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: 65.81 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKkmAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLekLSNkaLSDI 82
Cdd:TIGR01257 1937 ILRLNELTKVYSGT--SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTN--ISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 RKhDIGFIFQEYNLLHTLTVKENIMLPLTVQKLDKDTMldryEKVA----EALNILDISDKYPSELSGGQRQRTSAARAF 158
Cdd:TIGR01257 2011 HQ-NMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEI----EKVAnwsiQSLGLSLYADRLAGTYSGGNKRKLSTAIAL 2085
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 616690417 159 ITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKtTIIMVTH 202
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSH 2128
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-220 |
4.32e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.20 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSI----DYisQGSITLKGhklEKLSNKA 78
Cdd:NF040905 1 ILEMRGITKTFPGVK----ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgSY--EGEILFDG---EVCRFKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 79 LSDIRKHDIGFIFQEYNLLHTLTVKENIMLPLTVQK---LDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAA 155
Cdd:NF040905 72 IRDSEALGIVIIHQELALIPYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 156 RAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIImVTH--DPVAAsYANRVVMLKDGQ 220
Cdd:NF040905 152 KALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSII-ISHklNEIRR-VADSITVLRDGR 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-225 |
1.32e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.16 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 22 VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHkleklsnkalsdirkhdIGFIFQeYNLLHTLT 101
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------------ISFSPQ-TSWIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 102 VKENIMLPLTVQKLdkdtmldRYEKVAEALNILDISDKYPSE-----------LSGGQRQRTSAARAFITLPSIIFADEP 170
Cdd:TIGR01271 503 IKDNIIFGLSYDEY-------RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690417 171 TGALDSKSTQDLLKR-LMKMneEIKTTIIMVTHDPVAASYANRVVMLKDGQ-----IFTEL 225
Cdd:TIGR01271 576 FTHLDVVTEKEIFEScLCKL--MSNKTRILVTSKLEHLKKADKILLLHEGVcyfygTFSEL 634
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-221 |
1.48e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.76 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSItlkghkleKLSNKAlsdir 83
Cdd:PRK15064 320 LEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSENA----- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 khDIGFIFQ--EYNLLHTLTVKEnIMLPLTVQKlDKDTMldryekVAEALNIL----DISDKYPSELSGGQRQRTSAARA 157
Cdd:PRK15064 383 --NIGYYAQdhAYDFENDLTLFD-WMSQWRQEG-DDEQA------VRGTLGRLlfsqDDIKKSVKVLSGGEKGRMLFGKL 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616690417 158 FITLPSIIFADEPTGALDSKSTQDLLKRLmkmnEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDMESIESLNMAL----EKYEGTLIFVSHDrEFVSSLATRIIEITPDGV 513
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-220 |
2.56e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.87 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 29 SVEEGEFIAIMGPSGSGKTTLLNVLSSIdYISQGSITLKGHKLEKLSNKALSDIRkhdiGFIFQEYNLLHTLTVKENIML 108
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFAMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 109 PLTvQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITL-PSI------IFADEPTGALDSkSTQD 181
Cdd:PRK03695 93 HQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVwPDInpagqlLLLDEPMNSLDV-AQQA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 616690417 182 LLKRLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQ 220
Cdd:PRK03695 171 ALDRLLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGK 210
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-222 |
3.54e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 61.80 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 22 VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHkleklsnkalsdirkhdIGFIFQeYNLLHTLT 101
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------------ISFSSQ-FSWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 102 VKENIMLPLTVQKLdkdtmldRYEKVAEALNILDISDKYPSE-----------LSGGQRQRTSAARAFITLPSIIFADEP 170
Cdd:cd03291 114 IKENIIFGVSYDEY-------RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 616690417 171 TGALDSKSTQDLLK----RLMKmneeiKTTIIMVTHDPVAASYANRVVMLKDGQIF 222
Cdd:cd03291 187 FGYLDVFTEKEIFEscvcKLMA-----NKTRILVTSKMEHLKKADKILILHEGSSY 237
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-221 |
1.39e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGNKkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSS-IDY-ISQGSITLKGHKLEKLSnkal 79
Cdd:CHL00131 6 PILEIKNLHASVNEN----EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhPAYkILEGDILFKGESILDLE---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 80 SDIRKH-DIGFIFQEYNLLHTLTVKENIMLPL-TVQKLDKDTMLDR---YEKVAEALNILDISDKYPSE-----LSGGQR 149
Cdd:CHL00131 78 PEERAHlGIFLAFQYPIEIPGVSNADFLRLAYnSKRKFQGLPELDPlefLEIINEKLKLVGMDPSFLSRnvnegFSGGEK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 150 QRTSAARAFITLPSIIFADEPTGALDS---KSTQDLLKRLMKMNeeikTTIIMVTHDPVAASY--ANRVVMLKDGQI 221
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIdalKIIAEGINKLMTSE----NSIILITHYQRLLDYikPDYVHVMQNGKI 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-224 |
2.61e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKiygnkkmaqEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKL------EKLSNK 77
Cdd:PRK10762 258 LKVDNLSG---------PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtrspqDGLANG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 78 A--LSDIRKHDigfifqeyNLLHTLTVKENIMLpltvqkldkdTMLDRYEKVAEALN----ILDISD-------KYPS-- 142
Cdd:PRK10762 329 IvyISEDRKRD--------GLVLGMSVKENMSL----------TALRYFSRAGGSLKhadeQQAVSDfirlfniKTPSme 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 143 ----ELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHD-PVAASYANRVVMLK 217
Cdd:PRK10762 391 qaigLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEmPEVLGMSDRILVMH 469
|
....*..
gi 616690417 218 DGQIFTE 224
Cdd:PRK10762 470 EGRISGE 476
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-220 |
2.91e-10 |
|
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: 58.57 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 25 DINMSVEEGEF-----IAIMGPSGSGKTTLLNVLSSIDYISQGSItlkGHKLEKLSNKAlsdirkhdigfifQEYNLLHT 99
Cdd:cd03237 12 EFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYKP-------------QYIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 100 LTVKENIMlpltvqKLDKDTMLDRYEK--VAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSK 177
Cdd:cd03237 76 GTVRDLLS------SITKDFYTHPYFKteIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 616690417 178 STQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQ 220
Cdd:cd03237 150 QRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEGE 192
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-240 |
8.59e-10 |
|
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: 57.56 E-value: 8.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKMAqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYIsQGSITLKGHKLEKLSnkaLSDIR 83
Cdd:cd03289 3 MTVKDLTAKYTEGGNA--VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVP---LQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYnLLHTLTVKENimlpltvqkldkdtmLDRYE--------KVAEALNILDISDKYPSE-----------L 144
Cdd:cd03289 77 KA-FGVIPQKV-FIFSGTFRKN---------------LDPYGkwsdeeiwKVAEEVGLKSVIEQFPGQldfvlvdggcvL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 145 SGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQdLLKRLMKmNEEIKTTIIMVTHDPVAASYANRVVMLKDGQIFT- 223
Cdd:cd03289 140 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQ-VIRKTLK-QAFADCTVILSEHRIEAMLECQRFLVIEENKVRQy 217
|
250
....*....|....*..
gi 616690417 224 ELYQGDDDKHTFFKEII 240
Cdd:cd03289 218 DSIQKLLNEKSHFKQAI 234
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-231 |
1.68e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.93 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 16 KKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLS-----SIDYisQGSITLKGHKLEKLSNKALSdirkhdiGFI 90
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAgkldpSLKV--SGEITYNGYRLNEFVPRKTS-------AYI 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 91 FQeyNLLHT--LTVKENIMLPLTVQ----KLDKDTMLDRYEKVA----EA-----------------------LNIL--D 135
Cdd:PLN03140 245 SQ--NDVHVgvMTVKETLDFSARCQgvgtRYDLLSELARREKDAgifpEAevdlfmkatamegvksslitdytLKILglD 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 136 I------SDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASY 209
Cdd:PLN03140 323 IckdtivGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETF 402
|
250 260
....*....|....*....|....
gi 616690417 210 A--NRVVMLKDGQIfteLYQGDDD 231
Cdd:PLN03140 403 DlfDDIILLSEGQI---VYQGPRD 423
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-203 |
2.17e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.10 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 29 SVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKghklEKLSNKAlsdirkhdiGFIFQEYNllhtLTVKENIMl 108
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED----LKISYKP---------QYISPDYD----GTVEEFLR- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 109 pltvqKLDKDTMLDRYEK--VAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSK---STQDLL 183
Cdd:COG1245 424 -----SANTDDFGSSYYKteIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAI 498
|
170 180
....*....|....*....|
gi 616690417 184 KRLMkmnEEIKTTIIMVTHD 203
Cdd:COG1245 499 RRFA---ENRGKTAMVVDHD 515
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-225 |
3.31e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKMAqevLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALSDIR 83
Cdd:PRK10522 323 LELRNVTFAYQDNGFS---VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG---KPVTAEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 84 KHdIGFIFQEYNLLHTLtvkenimlpLTVQKLDKDTmldryEKVAEALNILDISDKYPSE--------LSGGQRQRTSAA 155
Cdd:PRK10522 397 KL-FSAVFTDFHLFDQL---------LGPEGKPANP-----ALVEKWLERLKMAHKLELEdgrisnlkLSKGQKKRLALL 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616690417 156 RAFITLPSIIFADEptGALDSKST------QDLLKRLMKMNEeiktTIIMVTHDPVAASYANRVVMLKDGQIfTEL 225
Cdd:PRK10522 462 LALAEERDILLLDE--WAADQDPHfrrefyQVLLPLLQEMGK----TIFAISHDDHYFIHADRLLEMRNGQL-SEL 530
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-218 |
4.19e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 22 VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSI-DYISQGSITLKGHKLEKLSN-KALSDIRKHDIGF---------- 89
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFyDLKNDHHIVFKNEHTNDMTNeQDYQGDEEQNVGMknvnefsltk 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 90 ---------IFQ-------------EYNL-----LHTLTVKENIMLPLTVQKLDK----DTMLDRYEKVAEALNILDISD 138
Cdd:PTZ00265 1263 eggsgedstVFKnsgkilldgvdicDYNLkdlrnLFSIVSQEPMLFNMSIYENIKfgkeDATREDVKRACKFAAIDEFIE 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 139 KYPSE-----------LSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAA 207
Cdd:PTZ00265 1343 SLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1422
|
250
....*....|.
gi 616690417 208 SYANRVVMLKD 218
Cdd:PTZ00265 1423 KRSDKIVVFNN 1433
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-186 |
4.86e-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: 56.46 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 4 LEVKQLTKIYGNKKMAqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVL---------SSIDYISQGSITLKGHKlekl 74
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRA--VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALlrllstegeIQIDGVSWNSVTLQTWR---- 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 75 snKALSDIRKHDigFIFqeynllhTLTVKENimlpltvqkldkdtmLDRYE--------KVAEALNILDISDKYPSEL-- 144
Cdd:TIGR01271 1292 --KAFGVIPQKV--FIF-------SGTFRKN---------------LDPYEqwsdeeiwKVAEEVGLKSVIEQFPDKLdf 1345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 616690417 145 ---------SGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRL 186
Cdd:TIGR01271 1346 vlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTL 1396
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-221 |
6.26e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.11 E-value: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 22 VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLsnkALSDIRkHDIGFIFQEyNLLHTLT 101
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI---GLHDLR-FKITIIPQD-PVLFSGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 102 VKENimlpltvqkLDKdtmLDRY--EKVAEALNILDISDKYPSE--------------LSGGQRQRTSAARAFITLPSII 165
Cdd:TIGR00957 1376 LRMN---------LDP---FSQYsdEEVWWALELAHLKTFVSALpdkldhecaeggenLSVGQRQLVCLARALLRKTKIL 1443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 616690417 166 FADEPTGALDSKsTQDLLKRLMKMNEEiKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:TIGR00957 1444 VLDEATAAVDLE-TDNLIQSTIRTQFE-DCTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-225 |
7.86e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 21 EVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSNKAlsdirKHDIGFIF-----QEYN 95
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpedrQSSG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 96 L---------LHTLTVKEnimLPLTVQKLDKDTMLDRYEKvaeALNI-LDISDKYPSELSGGQRQRTSAARAFITLPSII 165
Cdd:PRK15439 352 LyldaplawnVCALTHNR---RGFWIKPARENAVLERYRR---ALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616690417 166 FADEPTGALDSKSTQD---LLKRLMKMNeeikTTIIMVTHD-PVAASYANRVVMLKDGQIFTEL 225
Cdd:PRK15439 426 IVDEPTRGVDVSARNDiyqLIRSIAAQN----VAVLFISSDlEEIEQMADRVLVMHQGEISGAL 485
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-243 |
1.45e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 30 VEEGEFIAIMGPSGSGKTTLLNVLSS--------------------------------IDYISQGSitlkGHKLEKLsnK 77
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGevllddgriiyeqdlivarlqqdpprnvegtvYDFVAEGI----EEQAEYL--K 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 78 ALSDIrKHDIGFIFQEYNLLHTLTVKEnimlpltvqKLDKDTMLDRYEKVAEALNILDIS-DKYPSELSGGQRQRTSAAR 156
Cdd:PRK11147 100 RYHDI-SHLVETDPSEKNLNELAKLQE---------QLDHHNLWQLENRINEVLAQLGLDpDAALSSLSGGWLRKAALGR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 157 AFITLPSIIFADEPTGALDSkSTQDLLKRLMKmneEIKTTIIMVTHD-PVAASYANRVVMLKDGQIFTelYQGDDDKHTF 235
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDI-ETIEWLEGFLK---TFQGSIIFISHDrSFIRNMATRIVDLDRGKLVS--YPGNYDQYLL 243
|
....*....
gi 616690417 236 FK-EIIRVQ 243
Cdd:PRK11147 244 EKeEALRVE 252
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
25-171 |
2.03e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 25 DINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKlsnkalSDI--RKHdIGFIFQEYNLLHTLTV 102
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA------GDIatRRR-VGYMSQAFSLYGELTV 356
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690417 103 KENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPT 171
Cdd:NF033858 357 RQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-223 |
2.31e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.47 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 20 QEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEkLSNKALSDIRKHdIGFIFQ--EYNLL 97
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQQ-VATVFQdpEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 98 HTlTVKENIMLPLTVQKLDKDTMLDRyekVAEALNILDISD--KYPSE-LSGGQRQRTSAARAFITLPSIIFADEPTGAL 174
Cdd:PRK13638 92 YT-DIDSDIAFSLRNLGVPEAEITRR---VDEALTLVDAQHfrHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 616690417 175 DSKSTQDL---LKRLMKMNEEikttIIMVTHD-PVAASYANRVVMLKDGQIFT 223
Cdd:PRK13638 168 DPAGRTQMiaiIRRIVAQGNH----VIISSHDiDLIYEISDAVYVLRQGQILT 216
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-221 |
2.71e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 20 QEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSItlkghkleklsnkalsdIRKHDIGFIFQEYNLLHT 99
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----------------WAERSIAYVPQQAWIMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 100 lTVKENIMLpltvqkLDKdtmlDRYEKVAEALNI---------------LDISDKyPSELSGGQRQRTSAARAFITLPSI 164
Cdd:PTZ00243 736 -TVRGNILF------FDE----EDAARLADAVRVsqleadlaqlgggleTEIGEK-GVNLSGGQKARVSLARAVYANRDV 803
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 616690417 165 IFADEPTGALDSKSTQDLLKRLMKMNEEIKTTiIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:PTZ00243 804 YLLDDPLSALDAHVGERVVEECFLGALAGKTR-VLATHQVHVVPRADYVVALGDGRV 859
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-221 |
5.00e-08 |
|
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: 53.29 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMAQEVlRDINMSVEEGEFIAIMGPSGSGKTTLLNVL-SSIDYISQGSITLKGHKLEKlsnKALSD 81
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRV-DDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDI---RNPAQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IRKHDIGFIFQE---YNLLHTLTVKENImlplTVQKLDKDTMLDRYEKVAE------ALNILDISDKYP----SELSGGQ 148
Cdd:TIGR02633 333 AIRAGIAMVPEDrkrHGIVPILGVGKNI----TLSVLKSFCFKMRIDAAAElqiigsAIQRLKVKTASPflpiGRLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616690417 149 RQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKrLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYK-LINQLAQEGVAIIVVSSElAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2-221 |
1.20e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKiygnkkMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhklEKLSNKALSD 81
Cdd:PRK10982 249 VILEVRNLTS------LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG---KKINNHNANE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 IRKHDIGFIFQE-------------YN-LLHTLTVKENIMLPLTVQKLDKDTmldryEKVAEALNILDISDKYP-SELSG 146
Cdd:PRK10982 320 AINHGFALVTEErrstgiyayldigFNsLISNIRNYKNKVGLLDNSRMKSDT-----QWVIDSMRVKTPGHRTQiGSLSG 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616690417 147 GQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:PRK10982 395 GNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-203 |
1.27e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTKIYGnkkmaqevlrDINMSVE-----EGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKghklEKLSN 76
Cdd:PRK13409 339 TLVEYPDLTKKLG----------DFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----LKISY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 77 KAlsdirkhdiGFIFQEYNllhtLTVKEniMLPLTVQKLDkDTMLdrYEKVAEALNILDISDKYPSELSGGQRQRTSAAR 156
Cdd:PRK13409 405 KP---------QYIKPDYD----GTVED--LLRSITDDLG-SSYY--KSEIIKPLQLERLLDKNVKDLSGGELQRVAIAA 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 616690417 157 AFITLPSIIFADEPTGALDSK---STQDLLKRLMkmnEEIKTTIIMVTHD 203
Cdd:PRK13409 467 CLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRIA---EEREATALVVDHD 513
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-203 |
1.32e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.21 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 29 SVEEGEFIAIMGPSGSGKTTLLNVLSS------------------IDYIsQGSiTLKGHkLEKLSNKALSDIRKhdigfi 90
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdwdeiLDEF-RGS-ELQNY-FTKLLEGDVKVIVK------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 91 fQEYNLLHTLTVKENIMLPLTvqKLDKDTMLDRYEKVAEALNILDisdKYPSELSGGQRQRTSAARAFITLPSIIFADEP 170
Cdd:cd03236 93 -PQYVDLIPKAVKGKVGELLK--KKDERGKLDELVDQLELRHVLD---RNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190
....*....|....*....|....*....|...
gi 616690417 171 TGALDSKSTQDLLKRLMKMNEEIKtTIIMVTHD 203
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAEDDN-YVLVVEHD 198
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-221 |
1.53e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 51.06 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 18 MAQEVLRDINMSVEEGEFIAIMGPSGSGKTTL-LNVLSSIDyISQGSITLKGHKLEKLSNKALsdirKHDIGFIFQEyNL 96
Cdd:cd03288 32 NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVD-IFDGKIVIDGIDISKLPLHTL----RSRLSIILQD-PI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 97 LHTLTVKENimlpLTVQKLDKDTMLDRYEKVAEALNI-------LD-ISDKYPSELSGGQRQRTSAARAFITLPSIIFAD 168
Cdd:cd03288 106 LFSGSIRFN----LDPECKCTDDRLWEALEIAQLKNMvkslpggLDaVVTEGGENFSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 616690417 169 EPTGALDsKSTQDLLKRLMkMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:cd03288 182 EATASID-MATENILQKVV-MTAFADRTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-204 |
1.66e-07 |
|
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: 49.29 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 33 GEFIAIMGPSGSGKTTLLNVLSSIdyisqgsitlkghkleklsnkalsdIRKHDIGFIFqeynllhtltvkenimlpltv 112
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARE-------------------------LGPPGGGVIY--------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 113 qkldkdTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLK-----RLM 187
Cdd:smart00382 36 ------IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrLLL 109
|
170
....*....|....*..
gi 616690417 188 KMNEEIKTTIIMVTHDP 204
Cdd:smart00382 110 LLKSEKNLTVILTTNDE 126
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-221 |
1.83e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLTkIYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVL-SSIDYISQGSITLKGHKLeKLSNKAls 80
Cdd:PRK13549 258 VILEVRNLT-AWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPV-KIRNPQ-- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 81 DIRKHDIGFIFQE---YNLLHTLTVKENIMLPlTVQKLDKDTMLDRYEKVAEALNILD-ISDKYPS------ELSGGQRQ 150
Cdd:PRK13549 334 QAIAQGIAMVPEDrkrDGIVPVMGVGKNITLA-ALDRFTGGSRIDDAAELKTILESIQrLKVKTASpelaiaRLSGGNQQ 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616690417 151 RTSAARAFITLPSIIFADEPTGALDSKSTQDLLKrLMKMNEEIKTTIIMVTHD-PVAASYANRVVMLKDGQI 221
Cdd:PRK13549 413 KAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYK-LINQLVQQGVAIIVISSElPEVLGLSDRVLVMHEGKL 483
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
19-207 |
2.31e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.85 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 19 AQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLSnkalsdiRKHDIGFIFQEYNLLH 98
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 99 TLTVKENIMLPLTVQKLDKDTMldryekVAEALNIL---DISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALD 175
Cdd:PRK13543 96 DLSTLENLHFLCGLHGRRAKQM------PGSALAIVglaGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180 190
....*....|....*....|....*....|..
gi 616690417 176 SKSTqDLLKRLMKMNEEIKTTIIMVTHDPVAA 207
Cdd:PRK13543 170 LEGI-TLVNRMISAHLRGGGAALVTTHGAYAA 200
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
20-75 |
4.22e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.40 E-value: 4.22e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 20 QEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLS-SIDY-ISQGSITLKGHKLEKLS 75
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgREDYeVTGGTVEFKGKDLLELS 71
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-221 |
5.25e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 22 VLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEKLsnkALSDIRKhDIGFIFQEyNLLHTLT 101
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDLRK-VLGIIPQA-PVLFSGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 102 VKENImlpltvQKLDKDTMLDRYEKVAEAlNILDISDKYPSEL-----------SGGQRQRTSAARAFITLPSIIFADEP 170
Cdd:PLN03130 1329 VRFNL------DPFNEHNDADLWESLERA-HLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEA 1401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 616690417 171 TGALDSKsTQDLLKRLMKmnEEIKT-TIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:PLN03130 1402 TAAVDVR-TDALIQKTIR--EEFKScTMLIIAHRLNTIIDCDRILVLDAGRV 1450
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-202 |
5.86e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 13 YGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSiDYiSQG---SITLKGHKleKLSNKALSDIRKHdIGF 89
Cdd:PRK10938 270 YNDRP----ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DH-PQGysnDLTLFGRR--RGSGETIWDIKKH-IGY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 90 IfqeYNLLHtltvkenimLPLTVQKLDKDTML--------------DRYEKVA-EALNILDISD---KYP-SELSGGQRQ 150
Cdd:PRK10938 341 V---SSSLH---------LDYRVSTSVRNVILsgffdsigiyqavsDRQQKLAqQWLDILGIDKrtaDAPfHSLSWGQQR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 616690417 151 RTSAARAFITLPSIIFADEPTGALDSKSTQdLLKRLMK-MNEEIKTTIIMVTH 202
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRQ-LVRRFVDvLISEGETQLLFVSH 460
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-175 |
7.44e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.55 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLkGHKLeklsnkalsdi 82
Cdd:TIGR03719 322 VIEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 83 rkhDIGFIFQEYNllhTLTVKENImlpltvqkldkdtmldrYEKVAEALNILDISD--------------------KYPS 142
Cdd:TIGR03719 386 ---KLAYVDQSRD---ALDPNKTV-----------------WEEISGGLDIIKLGKreipsrayvgrfnfkgsdqqKKVG 442
|
170 180 190
....*....|....*....|....*....|...
gi 616690417 143 ELSGGQRQRTSAARAFITLPSIIFADEPTGALD 175
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-221 |
8.45e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 49.41 E-value: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 26 INMSVEEGEFIAIMGPSGSGKTTLLNVLSSIdYI-SQGSITLKGHKLEKlsnKALSDIRKHdigF--IFQEYNLLHTLtv 102
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGL-YRpESGEILLDGQPVTA---DNREAYRQL---FsaVFSDFHLFDRL-- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 103 kenimlpltvqkLDKDTMLDRyEKVAEALNILDISDKYPSE--------LSGGQRQRTsaarAFITL-----PSIIFaDE 169
Cdd:COG4615 422 ------------LGLDGEADP-ARARELLERLELDHKVSVEdgrfsttdLSQGQRKRL----ALLVAlledrPILVF-DE 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616690417 170 ptGALDskstQD----------LLKRLMKMNeeiKtTIIMVTHDPVAASYANRVVMLKDGQI 221
Cdd:COG4615 484 --WAAD----QDpefrrvfyteLLPELKARG---K-TVIAISHDDRYFDLADRVLKMDYGKL 535
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
143-220 |
1.16e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.57 E-value: 1.16e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 143 ELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQ 220
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
99-224 |
1.70e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.19 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 99 TLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKS 178
Cdd:NF000106 100 SFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 616690417 179 TQDLLKRLMKMNEEIKTTIIMVTHDPVAASYANRVVMLKDGQIFTE 224
Cdd:NF000106 180 RNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-202 |
6.03e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.81 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 23 LRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhkleklsNKALSDIRKhdigfifqeyNLLHTLTV 102
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-------SAALIAISS----------GLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 103 KENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDL 182
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180
....*....|....*....|..
gi 616690417 183 LKrlmKMNE--EIKTTIIMVTH 202
Cdd:PRK13545 183 LD---KMNEfkEQGKTIFFISH 201
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-186 |
1.28e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.94 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 20 QEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGHKLEklsnKALSDIRKHdIGFIFQEYNLLHT 99
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTYQKQ-LCFVGHRSGINPY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 100 LTVKENIMLPLTVQKLDKDtmLDRYEKVAEALNILDisdkYPSE-LSGGQRQRTSAARAFITLPSIIFADEPTGALDSKS 178
Cdd:PRK13540 89 LTLRENCLYDIHFSPGAVG--ITELCRLFSLEHLID----YPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
....*...
gi 616690417 179 TQDLLKRL 186
Cdd:PRK13540 163 LLTIITKI 170
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-231 |
2.02e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 20 QEVLRDINMSVEEGEFIAIMGPSGSGKTTLLN--VLSSIDYISQGSITLK------GHKLEKLSNKALSDIRKHDI---- 87
Cdd:PLN03073 190 RDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymAMHAIDGIPKNCQILHveqevvGDDTTALQCVLNTDIERTQLleee 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 88 GFIFQEYNLLHTLTVKENIMLPlTVQKLDKDTMLDRYEKV-------------AEALNIL-------DISDKYPSELSGG 147
Cdd:PLN03073 270 AQLVAQQRELEFETETGKGKGA-NKDGVDKDAVSQRLEEIykrlelidaytaeARAASILaglsftpEMQVKATKTFSGG 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 148 QRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEeiktTIIMVTHdpvAASYANRVV---MLKDGQIFTE 224
Cdd:PLN03073 349 WRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSH---AREFLNTVVtdiLHLHGQKLVT 421
|
....*..
gi 616690417 225 lYQGDDD 231
Cdd:PLN03073 422 -YKGDYD 427
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-204 |
3.52e-05 |
|
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: 44.74 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 20 QEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSsidyisqgsitlkghKLEKLSNKALSDIRKHDIGFIFQE-YNLLH 98
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILG---------------ELWPVYGGRLTKPAKGKLFYVPQRpYMTLG 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 99 TLtvKENIMLPLTVQKLDK----DTMLDRYEKVAEALNIL------DISDKYPSELSGGQRQRTSAARAFITLPSIIFAD 168
Cdd:TIGR00954 530 TL--RDQIIYPDSSEDMKRrglsDKDLEQILDNVQLTHILereggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|....*.
gi 616690417 169 EPTGALdSKSTQDLLKRLMKmneEIKTTIIMVTHDP 204
Cdd:TIGR00954 608 ECTSAV-SVDVEGYMYRLCR---EFGITLFSVSHRK 639
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2-175 |
9.78e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 2 TILEVKQLT---KIYGNKKmaqeVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVL---SSIDYISqGSITLKGHKLEkLS 75
Cdd:NF040905 256 VVFEVKNWTvyhPLHPERK----VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrSYGRNIS-GTVFKDGKEVD-VS 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 76 NkaLSDIRKHDIGFIFQ---EYNLLHTLTVKENIMLPlTVQKLDKDTMLDRYE--KVAE----ALNIldisdKYPS---- 142
Cdd:NF040905 330 T--VSDAIDAGLAYVTEdrkGYGLNLIDDIKRNITLA-NLGKVSRRGVIDENEeiKVAEeyrkKMNI-----KTPSvfqk 401
|
170 180 190
....*....|....*....|....*....|....*
gi 616690417 143 --ELSGGQRQRTSAARAFITLPSIIFADEPTGALD 175
Cdd:NF040905 402 vgNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
23-214 |
1.11e-04 |
|
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: 42.24 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 23 LRDINMSVEEGEFIAIMGPSGSGKTTL-------------LNVLSS-------------IDYISQGSITLKghklekLSN 76
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSAyarqflgqmdkpdVDSIEGLSPAIA------IDQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 77 KALSDIRKHDIGFIFQEYNLLHTLTVKENImlpltVQKLDkdtMLdryekVAEALNILDISDKYPSeLSGGQRQRTSAAR 156
Cdd:cd03270 85 KTTSRNPRSTVGTVTEIYDYLRLLFARVGI-----RERLG---FL-----VDVGLGYLTLSRSAPT-LSGGEAQRIRLAT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 157 AFIT-LPSIIFA-DEPTGALDSKSTQDLLKRLMKMnEEIKTTIIMVTHDPVAASYANRVV 214
Cdd:cd03270 151 QIGSgLTGVLYVlDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRAADHVI 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-203 |
1.60e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.63 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 3 ILEVKQLTKIYGNKKMaqevLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLssIDYISQGSITLK-GHKLEklsnkalsd 81
Cdd:PRK11147 319 VFEMENVNYQIDGKQL----VKDFSAQVQRGDKIALIGPNGCGKTTLLKLM--LGQLQADSGRIHcGTKLE--------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 82 irkhdIGFiFQEY--NLLHTLTVKENimlpltVQKLDKDTML---DRYekvaeALNILD---ISDK---YP-SELSGGQR 149
Cdd:PRK11147 384 -----VAY-FDQHraELDPEKTVMDN------LAEGKQEVMVngrPRH-----VLGYLQdflFHPKramTPvKALSGGER 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 616690417 150 QRTSAARAFITLPSIIFADEPTGALDSKsTQDLLKRLMkmnEEIKTTIIMVTHD 203
Cdd:PRK11147 447 NRLLLARLFLKPSNLLILDEPTNDLDVE-TLELLEELL---DSYQGTVLLVSHD 496
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-220 |
1.80e-04 |
|
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: 41.15 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 23 LRDINMSVEEGEFIAIMGPSGSGKTTLLNvlsSIDYISqgsitlkghkLEKLSNKALSDIRKHDIGFIFQeynlLHTLtv 102
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN---EGLYAS----------GKARLISFLPKFSRNKLIFIDQ----LQFL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 103 kenIMLPLTVQKLDKDTmldryekvaealnildisdkypSELSGGQRQRTS-AARAFITLPSIIFA-DEPTGALDSKSTQ 180
Cdd:cd03238 72 ---IDVGLGYLTLGQKL----------------------STLSGGELQRVKlASELFSEPPGTLFIlDEPSTGLHQQDIN 126
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 616690417 181 DLLKRLMKMNEEiKTTIIMVTHDPVAASYANRVVMLKDGQ 220
Cdd:cd03238 127 QLLEVIKGLIDL-GNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
23-51 |
3.85e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 3.85e-04
10 20
....*....|....*....|....*....
gi 616690417 23 LRDINMSVEEGEFIAIMGPSGSGKTTLLN 51
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
144-214 |
1.16e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 1.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690417 144 LSGGQRQRTSAARAF-ITLPSIIFA-DEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHDPVAASYANRVV 214
Cdd:PRK00635 477 LSGGEQERTALAKHLgAELIGITYIlDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDEQMISLADRII 548
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
28-51 |
1.35e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 38.64 E-value: 1.35e-03
10 20
....*....|....*....|....
gi 616690417 28 MSvEEGEFIAIMGPSGSGKTTLLN 51
Cdd:COG3709 1 MS-GPGRLIYVVGPSGAGKDSLLA 23
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
144-204 |
1.47e-03 |
|
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: 38.74 E-value: 1.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616690417 144 LSGGQRQ------RTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMNEEIKT-TIIMVTHDP 204
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSQKNfQLIVITHDE 183
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
23-51 |
1.53e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.13 E-value: 1.53e-03
10 20
....*....|....*....|....*....
gi 616690417 23 LRDINMSVEEGEFIAIMGPSGSGKTTLLN 51
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN 39
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
144-203 |
1.64e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 1.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 144 LSGGQRQRTSAARAFITLPSIIFADEPTGALDSKSTQDLLKRLMKMneeiKTTIIMVTHD 203
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLF----QGGVLMVSHD 683
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
23-51 |
1.79e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.29 E-value: 1.79e-03
10 20
....*....|....*....|....*....
gi 616690417 23 LRDINMSVEEGEFIAIMGPSGSGKTTLLN 51
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
144-204 |
1.83e-03 |
|
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: 38.11 E-value: 1.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616690417 144 LSGGQRQRTSAA-----RAFITLPSIIFaDEPTGALDSKSTQDLLKRLMKMNEEiKTTIIMVTHDP 204
Cdd:cd03227 78 LSGGEKELSALAlilalASLKPRPLYIL-DEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLP 141
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
12-203 |
1.86e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.64 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 12 IYGNKKMAQEVLRDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITLKGhkleklsnkalsdirkhDIGFIF 91
Cdd:PRK13546 29 IPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------------EVSVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690417 92 QEYNLLHTLTVKENIMLPLTVQKLDKDTMLDRYEKVAEALNILDISDKYPSELSGGQRQRTSAARAFITLPSIIFADEPT 171
Cdd:PRK13546 92 ISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAL 171
|
170 180 190
....*....|....*....|....*....|..
gi 616690417 172 GALDSKSTQDLLKRLMKMNEEIKtTIIMVTHD 203
Cdd:PRK13546 172 SVGDQTFAQKCLDKIYEFKEQNK-TIFFVSHN 202
|
|
| Twinkle_C |
cd01122 |
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid ... |
33-80 |
2.74e-03 |
|
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid localization, also known as C10orf2, PEO1, SCA8, ATXN8, IOSCA, PEOA3 or SANDO) is a homohexameric DNA helicases which unwinds short stretches of double-stranded DNA in the 5' to 3' direction and, along with mitochondrial single-stranded DNA binding protein and mtDNA polymerase gamma, is thought to play a key role in mtDNA replication. Mutations in the human gene cause infantile onset spinocerebellar ataxia (IOSCA) and progressive external ophthalmoplegia (PEO) and are also associated with several mitochondrial depletion syndromes. This group also contains viral GP4-like and related bacterial helicases.
Pssm-ID: 410867 Cd Length: 266 Bit Score: 38.37 E-value: 2.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 616690417 33 GEFIAIMGPSGSGKTTLLNVLsSIDYISQGSITLKGH---KLEKLSNKALS 80
Cdd:cd01122 43 GELTIFTGPTGSGKTTFLSEY-SLDLCMQGVNTLWGSfeiKNVRLAKTMLT 92
|
|
| VirB11 |
COG0630 |
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ... |
28-55 |
3.15e-03 |
|
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440395 [Multi-domain] Cd Length: 462 Bit Score: 38.52 E-value: 3.15e-03
10 20
....*....|....*....|....*...
gi 616690417 28 MSVEEGEFIAIMGPSGSGKTTLLNVLSS 55
Cdd:COG0630 285 LLLENGKSVLVAGGTASGKTTLLNALLS 312
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-66 |
3.24e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.56 E-value: 3.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616690417 2 TILEVKQLTKIYGNKkmaqeVL-RDINMSVEEGEFIAIMGPSGSGKTTLLNVLSSIDYISQGSITL 66
Cdd:PRK11819 323 KVIEAENLSKSFGDR-----LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
20-53 |
5.38e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.46 E-value: 5.38e-03
10 20 30
....*....|....*....|....*....|....*
gi 616690417 20 QEVLRDINMSVEEGE-FIAIMGPSGSGKTTLLNVL 53
Cdd:COG3267 29 REALARLEYALAQGGgFVVLTGEVGTGKTTLLRRL 63
|
|
| CpaF |
COG4962 |
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ... |
36-55 |
6.43e-03 |
|
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443988 [Multi-domain] Cd Length: 386 Bit Score: 37.45 E-value: 6.43e-03
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
35-81 |
7.01e-03 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 36.32 E-value: 7.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616690417 35 FIAIMGPSGSGKTTLLNVLS---SIDYISQGSI-----TLKGHKLEKLSNKALSD 81
Cdd:PRK04182 2 IITISGPPGSGKTTVARLLAeklGLKHVSAGEIfrelaKERGMSLEEFNKYAEED 56
|
|
| |
