|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-202 |
3.03e-129 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 362.20 E-value: 3.03e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIG 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 81 HQPGIKAVLTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAI 160
Cdd:PRK13538 81 HQPGIKTELTALENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491074653 161 DKQGVAELISLFEQHAQRGGMVLLTTHQDLAGVSQTVGKIRL 202
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKLRL 202
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-190 |
6.87e-100 |
|
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: 287.84 E-value: 6.87e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIG 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 81 HQPGIKAVLTPFENLQFYQAVRG-AAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGlRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190
....*....|....*....|....*....|.
gi 491074653 160 IDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTHQPL 192
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-190 |
1.09e-90 |
|
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: 264.22 E-value: 1.09e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGH 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 82 QPGIKAVLTPFENLQFYQAVrGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAI-HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180
....*....|....*....|....*....
gi 491074653 162 KQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:TIGR01189 160 KAGVALLAGLLRAHLARGGIVLLTTHQDL 188
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-203 |
5.20e-87 |
|
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: 255.11 E-value: 5.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGH 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 82 QPGIKAVLTPFENLQFYQAVRGAAeqqAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDE---QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491074653 162 KQGVAELISLFEQHAQRGGMVLLTTHQDLAGVSQTVGKIRLA 203
Cdd:cd03231 158 KAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-190 |
8.34e-67 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 203.95 E-value: 8.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT----LRDRAAYqqdl 76
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIddpdVAEACHY---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 77 lfIGHQPGIKAVLTPFENLQFYQAVRGAAEQqAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:PRK13539 78 --LGHRNAMKPALTVAENLEFWAAFLGGEEL-DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|....
gi 491074653 157 LTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK13539 155 TAALDAAAVALFAELIRAHLAQGGIVIAATHIPL 188
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-191 |
2.68e-52 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 167.33 E-value: 2.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR-NTLRDRAAYqqdLLFI 79
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtATRGDRSRF---MAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 80 GHQPGIKAVLTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:PRK13543 88 GHLPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
170 180 190
....*....|....*....|....*....|..
gi 491074653 160 IDKQGVAELISLFEQHAQRGGMVLLTTHQDLA 191
Cdd:PRK13543 168 LDLEGITLVNRMISAHLRGGGAALVTTHGAYA 199
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-191 |
2.77e-51 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 164.35 E-value: 2.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIG 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 81 HQPGIKAVLTPFEN----LQFYQAVRGAAEQQAIWRaleqvgLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:PRK13540 81 HRSGINPYLTLRENclydIHFSPGAVGITELCRLFS------LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|....*
gi 491074653 157 LTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDLA 191
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLP 189
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-200 |
2.14e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.93 E-value: 2.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRA--AY--QQ-- 74
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRriGYvpQRae 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 75 ----------DLLFIGHQPGIKAVLTPfenlqfyqavrGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLW 144
Cdd:COG1121 86 vdwdfpitvrDVVLMGRYGRRGLFRRP-----------SRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491074653 145 LSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHqDLAGVSQTVGKI 200
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTH-DLGAVREYFDRV 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-187 |
4.70e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 146.75 E-value: 4.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGH 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 82 QPGIKAVLTPFENLQFYQAVRGAAEQQA---IWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEArerIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180
....*....|....*....|....*....
gi 491074653 159 AIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTH 189
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-188 |
6.51e-44 |
|
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: 146.93 E-value: 6.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIG 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 81 HQPGIKAVLTPFENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIeelIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190
....*....|....*....|....*....|.
gi 491074653 158 TAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHI 191
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-187 |
8.97e-37 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 127.65 E-value: 8.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 3 EAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAyqqdllfIGHQ 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-------IGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 83 PGIKAVLTPFeNLQFYQAVR-------------GAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAP 149
Cdd:cd03235 74 PQRRSIDRDF-PISVRDVVLmglyghkglfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 491074653 150 LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTH 190
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-200 |
3.60e-35 |
|
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: 123.10 E-value: 3.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQdllfIG---HQPGIKAVLTPFEN 94
Cdd:cd03268 17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR----IGaliEAPGFYPNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 95 LQFYQAVRGAAEQqAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQ 174
Cdd:cd03268 93 LRLLARLLGIRKK-RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILS 171
|
170 180
....*....|....*....|....*.
gi 491074653 175 HAQRGGMVLLTTHQdLAGVSQTVGKI 200
Cdd:cd03268 172 LRDQGITVLISSHL-LSEIQKVADRI 196
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-190 |
4.02e-35 |
|
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: 124.39 E-value: 4.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN----TLRDRA---AY- 72
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslSRRELArriAYv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 73 -QQ----------DLLFIGHQPGIKAVLTPfenlqfyqavrGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALA 141
Cdd:COG1120 81 pQEppapfgltvrELVALGRYPHLGLFGRP-----------SAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491074653 142 RLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGM-VLLTTHqDL 190
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRtVVMVLH-DL 198
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-158 |
1.12e-34 |
|
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: 120.06 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRDRAAYQQDLLFIGHQPGIKAVLTPFENLQFY 98
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDlTDDERKSLRKEIGYVFQDPQLFPRLTVRENLRLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491074653 99 ---QAVRGAAEQQAIWRALEQVGLVGYEDLPV----AQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:pfam00005 84 lllKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-187 |
9.69e-34 |
|
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: 118.65 E-value: 9.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGH 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 82 QPGIKAVLTPFENLqfyqavrgaaeqqaiwraleqvglvgyedlpvaQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:cd03230 81 EPSLYENLTVRENL---------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180
....*....|....*....|....*.
gi 491074653 162 KQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:cd03230 128 PESRREFWELLRELKKEGKTILLSSH 153
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-188 |
2.48e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 119.09 E-value: 2.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILfsELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAA-------YQ 73
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAerpvsmlFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 74 QDLLF----------IGHQPGIKavLTpfenlqfyqavrgAAEQQAIWRALEQVGLVGYED-LPvAQLSAGQQRRVALAR 142
Cdd:COG3840 79 ENNLFphltvaqnigLGLRPGLK--LT-------------AEQRAQVEQALERVGLAGLLDrLP-GQLSGGQRQRVALAR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491074653 143 LWLSAAPLWILDEPLTAID---KQGVAELISlfEQHAQRGGMVLLTTHQ 188
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDpalRQEMLDLVD--ELCRERGLTVLMVTHD 189
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-188 |
3.63e-33 |
|
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: 116.58 E-value: 3.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 3 EAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRaayqqdllfighq 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 83 pgikavltpfenlqfyqavrgaaeqqaIWRALEQVGLVGyedlpvaQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDK 162
Cdd:cd00267 68 ---------------------------LEELRRRIGYVP-------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180
....*....|....*....|....*.
gi 491074653 163 QGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:cd00267 114 ASRERLLELLRELAEEGRTVIIVTHD 139
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-189 |
7.26e-33 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 116.89 E-value: 7.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFsELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYqqdLLFIG 80
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY---CTYIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 81 HQPGIKAVLTPFENLQFYQAVRGAAEqqAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAI 160
Cdd:PRK13541 77 HNLGLKLEMTVFENLKFWSEIYNSAE--TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL 154
|
170 180
....*....|....*....|....*....
gi 491074653 161 DKQGVAELISLFEQHAQRGGMVLLTTHQD 189
Cdd:PRK13541 155 SKENRDLLNNLIVMKANSGGIVLLSSHLE 183
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-191 |
5.88e-32 |
|
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: 115.51 E-value: 5.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCV-RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRD--RAAYQQdllf 78
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnlRELRRK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 79 IG-------HQ---PgikavlTPFENLQF---YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLwL 145
Cdd:COG1122 77 VGlvfqnpdDQlfaP------TVEEDVAFgpeNLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV-L 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491074653 146 SAAP-LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ-DLA 191
Cdd:COG1122 150 AMEPeVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDlDLV 197
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-188 |
8.02e-31 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 112.18 E-value: 8.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT-------LRDRAAY--QQ-DLLFIG 80
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtklslkeLRRKVGLvfQNpDDQFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 81 HqpgikavlTPFENLQFYQAVRGAAE---QQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:cd03225 91 P--------TVEEEVAFGLENLGLPEeeiEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190
....*....|....*....|....*....|.
gi 491074653 158 TAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKAEGKTIIIVTHD 193
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-187 |
1.11e-30 |
|
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: 111.84 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN----TLRDRA---AYQQ 74
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvPPERRNigmVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 75 DLLFiGHqpgikavLTPFENLQF---YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLW 151
Cdd:cd03259 81 YALF-PH-------LTVAENIAFglkLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 491074653 152 ILDEPLTAIDKQGVAELISLFEQ-HAQRGGMVLLTTH 187
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKElQRELGITTIYVTH 189
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-187 |
2.11e-30 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 114.42 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRnTLRDRAAYQ------- 73
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR-DVTGLPPEKrnvgmvf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 74 QDL-LFiGHqpgikavLTPFENLQFYQAVRG--AAEQQA-IWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP 149
Cdd:COG3842 84 QDYaLF-PH-------LTVAENVAFGLRMRGvpKAEIRArVAELLELVGLEGLADRYPHQLSGGQQQRVALARA-LAPEP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491074653 150 -LWILDEPLTAIDKQGVAELIS-LFEQHAQRGGMVLLTTH 187
Cdd:COG3842 155 rVLLLDEPLSALDAKLREEMREeLRRLQRELGITFIYVTH 194
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
20-187 |
4.47e-30 |
|
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: 110.54 E-value: 4.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVLTPFENLQFYQ 99
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTGLYDRLTARENLEYFA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 100 AVRGAAEQQAIWRALEQVGLVGYEDL---PVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHA 176
Cdd:cd03266 104 GLYGLKGDELTARLEELADRLGMEELldrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLR 183
|
170
....*....|.
gi 491074653 177 QRGGMVLLTTH 187
Cdd:cd03266 184 ALGKCILFSTH 194
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
21-191 |
5.03e-30 |
|
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: 110.27 E-value: 5.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTL----RDRAAY-QQDLLFIGHQPGIKAVLTPFEN- 94
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklseKELAAFrRRHIGFVFQSFNLLPDLTALENv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 95 ---LQFYQAVRGAAEQQAIWrALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISL 171
Cdd:cd03255 104 elpLLLAGVPKKERRERAEE-LLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMEL 182
|
170 180
....*....|....*....|..
gi 491074653 172 F-EQHAQRGGMVLLTTH-QDLA 191
Cdd:cd03255 183 LrELNKEAGTTIVVVTHdPELA 204
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-187 |
2.09e-29 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 109.79 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCV----RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN---TLRDRA-AY 72
Cdd:COG1116 7 ALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvtgPGPDRGvVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 73 QQDLLFighqPGikavLTPFENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAP 149
Cdd:COG1116 87 QEPALL----PW----LTVLDNVALGLELRGVPKAERRERArelLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 491074653 150 LWILDEPLTAIDKQGVAELISLFEQHAQRGGM-VLLTTH 187
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKtVLFVTH 197
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
20-191 |
2.32e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 108.59 E-value: 2.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTL----RDRAAYQQDLL-FIGHQPGIKAVLTPFEN 94
Cdd:COG1136 27 VSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslseRELARLRRRHIgFVFQFFNLLPELTALEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 95 LQF---YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISL 171
Cdd:COG1136 107 VALpllLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLEL 186
|
170 180
....*....|....*....|..
gi 491074653 172 FEQHAQRGGM-VLLTTH-QDLA 191
Cdd:COG1136 187 LRELNRELGTtIVMVTHdPELA 208
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-187 |
4.82e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 107.83 E-value: 4.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRDRAAYQ---------QDLLFI 79
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsRLKRREIPYlrrrigvvfQDFRLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 80 GHqpgikavLTPFENLQFYQAVRGAAE---QQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:COG2884 92 PD-------RTVYENVALPLRVTGKSRkeiRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEP 164
|
170 180 190
....*....|....*....|....*....|.
gi 491074653 157 LTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:COG2884 165 TGNLDPETSWEIMELLEEINRRGTTVLIATH 195
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-187 |
8.57e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 106.80 E-value: 8.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDggeVCWRGRNTLRDRAA--------- 71
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPA---FSASGEVLLNGRRLtalpaeqrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 72 ----YQQDLLFiGHqpgikavLTPFENLQFY--QAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWL 145
Cdd:COG4136 78 igilFQDDLLF-PH-------LSVGENLAFAlpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491074653 146 SAAPLWILDEPLTAIDKQGVAELISL-FEQHAQRGGMVLLTTH 187
Cdd:COG4136 150 AEPRALLLDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTH 192
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-188 |
1.32e-28 |
|
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: 111.77 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLR--DRAAYQQDLLFIGHQPGIkavl 89
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD-LSdlDPASWRRQIAWVPQNPYL---- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 90 tpF-----ENLQFYqavRGAAEQQAIWRALEQVGL--------VGYeDLPV----AQLSAGQQRRVALARLWLSAAPLWI 152
Cdd:COG4988 423 --FagtirENLRLG---RPDASDEELEAALEAAGLdefvaalpDGL-DTPLgeggRGLSGGQAQRLALARALLRDAPLLL 496
|
170 180 190
....*....|....*....|....*....|....*.
gi 491074653 153 LDEPLTAIDKQGVAELISLFEQHAqRGGMVLLTTHQ 188
Cdd:COG4988 497 LDEPTAHLDAETEAEILQALRRLA-KGRTVILITHR 531
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-191 |
2.03e-28 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 106.68 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCV-RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAA-------- 71
Cdd:COG3638 2 MLELRNLSKRyPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRalrrlrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 72 ----YQQDLLfIGHQPGIKAVLTP-FENLQFYQAVRG---AAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARL 143
Cdd:COG3638 82 igmiFQQFNL-VPRLSVLTNVLAGrLGRTSTWRSLLGlfpPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491074653 144 WLSAAPLWILDEPLTAID---KQGVAELisLFEQHAQRGGMVLLTTHQ-DLA 191
Cdd:COG3638 161 LVQEPKLILADEPVASLDpktARQVMDL--LRRIAREDGITVVVNLHQvDLA 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-187 |
2.35e-28 |
|
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: 106.05 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQ--------DLLFIGhqpgikavLTP 91
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQslgycpqfDALFDE--------LTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 92 FENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID---KQGV 165
Cdd:cd03263 93 REHLRFYARLKGLPKSEIKEEVellLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDpasRRAI 172
|
170 180
....*....|....*....|..
gi 491074653 166 AELIslfeQHAQRGGMVLLTTH 187
Cdd:cd03263 173 WDLI----LEVRKGRSIILTTH 190
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
20-187 |
8.19e-28 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 106.71 E-value: 8.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVLTPFENLQFYQ 99
Cdd:TIGR01188 12 VNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGRENLEMMG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 100 AVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHA 176
Cdd:TIGR01188 92 RLYGLPKDEAEERAeelLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRALK 171
|
170
....*....|.
gi 491074653 177 QRGGMVLLTTH 187
Cdd:TIGR01188 172 EEGVTILLTTH 182
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-191 |
1.06e-27 |
|
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: 104.96 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVR-DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRG--RNTLRDRAAYQ----- 73
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdINKLKGKALRQlrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 74 ----QDLLFIGHQPGIKAVLTP-FENLQFYQAVRG---AAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLwL 145
Cdd:cd03256 81 gmifQQFNLIERLSVLENVLSGrLGRRSTWRSLFGlfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA-L 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491074653 146 SAAPLWIL-DEPLTAIDKQGVAELISLFEQHAQRGGM-VLLTTHQ-DLA 191
Cdd:cd03256 160 MQQPKLILaDEPVASLDPASSRQVMDLLKRINREEGItVIVSLHQvDLA 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-190 |
2.00e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.43 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN----TLRDRAAyqqdl 76
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPlaawSPWELAR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 77 lfighqpgIKAVLTPFENLQF----YQAVR---------GAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALAR- 142
Cdd:COG4559 76 --------RRAVLPQHSSLAFpftvEEVVAlgraphgssAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARv 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491074653 143 ---LW--LSAAPLWI-LDEPLTAID---KQGVAELISlfeQHAQRGGMVLLTTHqDL 190
Cdd:COG4559 148 laqLWepVDGGPRWLfLDEPTSALDlahQHAVLRLAR---QLARRGGGVVAVLH-DL 200
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-188 |
3.78e-27 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 103.63 E-value: 3.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCW-----RGRNTLRD-R----- 69
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerRGGEDVWElRkrigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 70 --AAYQQDllFIGHQPGIKAVLTPFEN-LQFYQAVrGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLS 146
Cdd:COG1119 83 vsPALQLR--FPRDETVLDVVLSGFFDsIGLYREP-TDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491074653 147 AAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGM-VLLTTHQ 188
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPtLVLVTHH 202
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-195 |
1.05e-26 |
|
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: 106.39 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-------TLRDRAAY--QQDLLFIGhqp 83
Cdd:COG4987 347 GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDlrdldedDLRRRIAVvpQRPHLFDT--- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 84 gikavlTPFENLQFyqaVRGAAEQQAIWRALEQVGL--------VGYeDLPV----AQLSAGQQRRVALARLWLSAAPLW 151
Cdd:COG4987 424 ------TLRENLRL---ARPDATDEELWAALERVGLgdwlaalpDGL-DTWLgeggRRLSGGERRRLALARALLRDAPIL 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491074653 152 ILDEPLTAIDKQGVAELISLFEQHAQrGGMVLLTTHqDLAGVSQ 195
Cdd:COG4987 494 LLDEPTEGLDAATEQALLADLLEALA-GRTVLLITH-RLAGLER 535
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
19-187 |
1.24e-26 |
|
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: 101.68 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVLTPFENLQFY 98
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSVDDELTGWENLYIH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 99 ---QAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQH 175
Cdd:cd03265 98 arlYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKL 177
|
170
....*....|...
gi 491074653 176 AQRGGM-VLLTTH 187
Cdd:cd03265 178 KEEFGMtILLTTH 190
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
17-187 |
1.92e-26 |
|
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: 101.01 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 17 FSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRDRAAY--QQDLLFighqPGikavLTPF 92
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvTGPGPDRGYvfQQDALL----PW----LTVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 93 ENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAIDKQGVAEL 168
Cdd:cd03293 92 DNVALGLELQGVPKAEARERAeelLELVGLSGFENAYPHQLSGGMRQRVALARA-LAVDPdVLLLDEPFSALDALTREQL 170
|
170 180
....*....|....*....|
gi 491074653 169 ISLFEQHAQRGGM-VLLTTH 187
Cdd:cd03293 171 QEELLDIWRETGKtVLLVTH 190
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-187 |
2.87e-26 |
|
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: 100.35 E-value: 2.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGdIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGH 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 82 QPGIKAVLTPFENLQFYQAVRGAA---EQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPskeVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190
....*....|....*....|....*....|...
gi 491074653 159 AIDkqgVAELIS----LFEQHAQRggMVLLTTH 187
Cdd:cd03264 160 GLD---PEERIRfrnlLSELGEDR--IVILSTH 187
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-190 |
3.31e-26 |
|
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: 99.43 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 3 EAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN----TLRDRAayqqdllf 78
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaslSPKELA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 79 ighqpGIKAVLtpfenLQfyqavrgaaeqqaiwrALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:cd03214 73 -----RKIAYV-----PQ----------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190
....*....|....*....|....*....|...
gi 491074653 159 AIDKQGVAELISLFEQHAQRGGM-VLLTTHqDL 190
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKtVVMVLH-DL 158
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-189 |
1.22e-25 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 98.63 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT--LRDRA-AYQ--------QDLLFIGHqpgik 86
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdLRGRAiPYLrrkigvvfQDFRLLPD----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 87 avLTPFENLQFYQAVRGAAEQQAIWR---ALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQ 163
Cdd:cd03292 93 --RNVYENVAFALEVTGVPPREIRKRvpaALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180
....*....|....*....|....*.
gi 491074653 164 GVAELISLFEQHAQRGGMVLLTTHQD 189
Cdd:cd03292 171 TTWEIMNLLKKINKAGTTVVVATHAK 196
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-187 |
1.25e-25 |
|
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: 99.05 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLLFIG--HQ-PGIKAVLTPFENLQ 96
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGED-ITGLPPHEIARLGIGrtFQiPRLFPELTVLENVM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 97 ------------FYQAVRGAAE-QQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAIDK 162
Cdd:cd03219 98 vaaqartgsgllLARARREEREaRERAEELLERVGLADLADRPAGELSYGQQRRLEIARA-LATDPkLLLLDEPAAGLNP 176
|
170 180
....*....|....*....|....*
gi 491074653 163 QGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:cd03219 177 EETEELAELIRELRERGITVLLVEH 201
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
19-188 |
2.37e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 97.74 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTlrDRAAYQQdllfIGHQP---GIKAVLTPFENL 95
Cdd:cd03269 18 DISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL--DIAARNR----IGYLPeerGLYPKMKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 96 QFYQAVRGAAEQQA---IWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLF 172
Cdd:cd03269 92 VYLAQLKGLKKEEArrrIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVI 171
|
170
....*....|....*.
gi 491074653 173 EQHAQRGGMVLLTTHQ 188
Cdd:cd03269 172 RELARAGKTVILSTHQ 187
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
16-191 |
2.50e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 100.61 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 16 LFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAA--------YQQDLLFiGHqpgika 87
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPrerrvgfvFQHYALF-PH------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 88 vLTPFENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAIDKQ 163
Cdd:COG1118 90 -MTVAENIAFGLRVRPPSKAEIRARVeelLELVQLEGLADRYPSQLSGGQRQRVALARA-LAVEPeVLLLDEPFGALDAK 167
|
170 180 190
....*....|....*....|....*....|
gi 491074653 164 GVAEL-ISLFEQHAQRGGMVLLTTH-QDLA 191
Cdd:COG1118 168 VRKELrRWLRRLHDELGGTTVFVTHdQEEA 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-156 |
3.57e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 3.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcWRGRNTlrdRAAY--Qqdllf 78
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGETV---KIGYfdQ----- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 79 igHQPGIKAVLTPFENLQfyQAVRGAAEQQAiwRA-LEQVGLVGyEDL--PVAQLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:COG0488 386 --HQEELDPDKTVLDELR--DGAPGGTEQEV--RGyLGRFLFSG-DDAfkPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
.
gi 491074653 156 P 156
Cdd:COG0488 459 P 459
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
11-189 |
4.70e-25 |
|
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: 101.59 E-value: 4.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLR-DRAAYQQDLLFIGHQPGIKAVl 89
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWVPQHPFLFAG- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 90 TPFENLQFYqavRGAAEQQAIWRALEQVGLVGY-EDLPV----------AQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:TIGR02857 411 TIAENIRLA---RPDASDAEIREALERAGLDEFvAALPQgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
170 180 190
....*....|....*....|....*....|.
gi 491074653 159 AIDKQGVAELISLFEQHAQrGGMVLLTTHQD 189
Cdd:TIGR02857 488 HLDAETEAEVLEALRALAQ-GRTVLLVTHRL 517
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
21-191 |
5.49e-25 |
|
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: 101.52 E-value: 5.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTL----RDRAAYQQDLLFIGHQPG--------IKAV 88
Cdd:COG1123 285 SLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrRSLRELRRRVQMVFQDPYsslnprmtVGDI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 89 LTpfENLQFYQAVRGAAEQQAIWRALEQVGLV-GYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAIDKQGVA 166
Cdd:COG1123 365 IA--EPLRLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARA-LALEPkLLILDEPTSALDVSVQA 441
|
170 180
....*....|....*....|....*.
gi 491074653 167 ELISLFEQHAQRGGM-VLLTTHqDLA 191
Cdd:COG1123 442 QILNLLRDLQRELGLtYLFISH-DLA 466
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-163 |
9.47e-25 |
|
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: 96.92 E-value: 9.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAA-------YQQDLLFiGHqpgikavLTPF 92
Cdd:cd03300 19 VSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHkrpvntvFQNYALF-PH-------LTVF 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491074653 93 ENLQF---YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQ 163
Cdd:cd03300 91 ENIAFglrLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-197 |
1.88e-24 |
|
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: 94.56 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN---TLRDRAAYQQDLLF 78
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 79 IGHQPGIKAVLTPFENLQFyqavrgaaeqqaiwraleqvglvgyedlpvaQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL-------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491074653 159 AIDKQGVAELISLFEQ-HAQRGGMVLLTTHQ--DLAGVSQTV 197
Cdd:cd03229 130 ALDPITRREVRALLKSlQAQLGITVVLVTHDldEAARLADRV 171
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-191 |
2.71e-24 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 95.82 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRDRAAY------ 72
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitGLSEKELYelrrri 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 73 ----QQDLLFIGhqpgikavLTPFENLQFY---------QAVRGAAEQqaiwrALEQVGLVGYEDLPVAQLSAGQQRRVA 139
Cdd:COG1127 85 gmlfQGGALFDS--------LTVFENVAFPlrehtdlseAEIRELVLE-----KLELVGLPGAADKMPSELSGGMRKRVA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491074653 140 LARLWLSAAPLWILDEPLTAIDKQGVAELISLF-EQHAQRGGMVLLTTHqDLA 191
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIrELRDELGLTSVVVTH-DLD 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-187 |
3.63e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.98 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 4 AKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcWRGRNTlrdRAAY-QQDLLFIGHQ 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-SIPKGL---RIGYlPQEPPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 83 PGIKAVLTPFENLQFYQAVRGAAEQQ------------AIWRALEQVGlvGYE-------------------DLPVAQLS 131
Cdd:COG0488 77 TVLDTVLDGDAELRALEAELEELEAKlaepdedlerlaELQEEFEALG--GWEaearaeeilsglgfpeedlDRPVSELS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 132 AGQQRRVALARLWLSAAPLWILDEP---LtaiDkqgvAELISLFEQH-AQRGGMVLLTTH 187
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPtnhL---D----LESIEWLEEFlKNYPGTVLVVSH 207
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-188 |
7.20e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.95 E-value: 7.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtlRDRAAYQQdllfIG 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP--LDPEDRRR----IG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 81 HQP---GIKAVLTPFENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALArlwlsAA----P- 149
Cdd:COG4152 75 YLPeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRAdewLERLGLGDRANKKVEELSKGNQQKVQLI-----AAllhdPe 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 491074653 150 LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQ 188
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-188 |
1.02e-23 |
|
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: 93.00 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARP--DGGEVCWRGRN----TLRDRAAY-QQDLLFIGHqp 83
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPldkrSFRKIIGYvPQDDILHPT-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 84 gikavLTPFENLQFYQAVRGaaeqqaiwraleqvglvgyedlpvaqLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQ 163
Cdd:cd03213 97 -----LTVRETLMFAAKLRG--------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180
....*....|....*....|....*
gi 491074653 164 GVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:cd03213 146 SALQVMSLLRRLADTGRTIICSIHQ 170
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
20-188 |
1.40e-23 |
|
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: 93.36 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR---------NTLRDRAA--YQQDLLFighqpgikAV 88
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltddkkniNELRQKVGmvFQQFNLF--------PH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 89 LTPFENLQFYQ-AVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAPLWIL-DEPLTAIDKQ 163
Cdd:cd03262 91 LTVLENITLAPiKVKGMSKAEAEERAlelLEKVGLADKADAYPAQLSGGQQQRVAIARA-LAMNPKVMLfDEPTSALDPE 169
|
170 180
....*....|....*....|....*
gi 491074653 164 GVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:cd03262 170 LVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-169 |
1.55e-23 |
|
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: 94.34 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLR----DRAA------YQQDLLF----------I 79
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlpphRIARlgiartFQNPRLFpeltvlenvlV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 80 GHQPGIKA-VLTPFENLQFYQAVRGAAEQQAiWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEP- 156
Cdd:COG0411 103 AAHARLGRgLLAALLRLPRARREEREARERA-EELLERVGLADRADEPAGNLSYGQQRRLEIARA-LATEPkLLLLDEPa 180
|
170
....*....|....*
gi 491074653 157 --LTAIDKQGVAELI 169
Cdd:COG0411 181 agLNPEETEELAELI 195
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
20-200 |
1.64e-23 |
|
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: 93.34 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTL----RDRAAYQQDLLFIGHQPGikAVLTP---- 91
Cdd:cd03257 24 VSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLklsrRLRKIRRKEIQMVFQDPM--SSLNPrmti 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 92 ----FENLQFYQAVRGAAEQQ-AIWRALEQVGLV-GYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAIDKQG 164
Cdd:cd03257 102 geqiAEPLRIHGKLSKKEARKeAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARA-LALNPkLLIADEPTSALDVSV 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 491074653 165 VAELISLFEQHAQRGGM-VLLTTHqDLAGVSQTVGKI 200
Cdd:cd03257 181 QAQILDLLKKLQEELGLtLLFITH-DLGVVAKIADRV 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
20-187 |
2.05e-23 |
|
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: 92.71 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT---LRDRAAY--QQDLlfiGHQPGIKAVltpFEN 94
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakERRKSIGyvMQDV---DYQLFTDSV---REE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 95 LqFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQ 174
Cdd:cd03226 93 L-LLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRE 171
|
170
....*....|...
gi 491074653 175 HAQRGGMVLLTTH 187
Cdd:cd03226 172 LAAQGKAVIVITH 184
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-187 |
2.45e-23 |
|
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: 90.59 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWrgrntlrdraayqqdllfigh 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 82 QPGIKavltpfenlqfyqavrgaaeqqaiwraleqvglVGYedlpVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:cd03221 60 GSTVK---------------------------------IGY----FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180
....*....|....*....|....*.
gi 491074653 162 KQGVAELISLFEQHAqrgGMVLLTTH 187
Cdd:cd03221 103 LESIEALEEALKEYP---GTVILVSH 125
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
11-188 |
7.86e-23 |
|
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: 91.79 E-value: 7.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDL------LFighQPG 84
Cdd:cd03261 10 FGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrmgmLF---QSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 85 ikAV---LTPFENLQFYQAVRGAAEQQAIWR----ALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:cd03261 87 --ALfdsLTVFENVAFPLREHTRLSEEEIREivleKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190
....*....|....*....|....*....|....*
gi 491074653 158 TAID---KQGVAELI-SLfeqHAQRGGMVLLTTHQ 188
Cdd:cd03261 165 AGLDpiaSGVIDDLIrSL---KKELGLTSIMVTHD 196
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-191 |
1.09e-22 |
|
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: 91.59 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCV--RDERILfSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR----------NTLRD 68
Cdd:TIGR02315 1 MLEVENLSKVypNGKQAL-KNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTditklrgkklRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 69 RAAYQ-QDLLFIGHQPGIKAVLTPFenLQFYQAVRG------AAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALA 141
Cdd:TIGR02315 80 RIGMIfQHYNLIERLTVLENVLHGR--LGYKPTWRSllgrfsEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491074653 142 RLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGM-VLLTTHQ-DLA 191
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGItVIINLHQvDLA 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-187 |
1.41e-22 |
|
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: 94.90 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRG-------RNTLRDRAAY--QQDLLFIGhq 82
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidPASLRRQIGVvlQDVFLFSG-- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 83 pgikavlTPFENLQFYqavRGAAEQQAIWRALEQVGLV--------GYeDLPV----AQLSAGQQRRVALARLWLSAAPL 150
Cdd:COG2274 564 -------TIRENITLG---DPDATDEEIIEAARLAGLHdfiealpmGY-DTVVgeggSNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190
....*....|....*....|....*....|....*..
gi 491074653 151 WILDEPLTAIDKQGVAELISLFEQHAQrGGMVLLTTH 187
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLK-GRTVIIIAH 668
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
21-161 |
1.57e-22 |
|
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: 93.18 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT------LRDRA-AYQQDLLFighqPGikavLTPFE 93
Cdd:TIGR03265 24 SLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDItrlppqKRDYGiVFQSYALF----PN----LTVAD 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491074653 94 NLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:TIGR03265 96 NIAYGLKNRGMGRAEVAERVaelLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALD 166
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-188 |
4.63e-22 |
|
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: 89.95 E-value: 4.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCV----RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRDRA--AY 72
Cdd:cd03258 1 MIELKNVSKVfgdtGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltLLSGKElrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 73 QQDLLFIGHQPGIKAVLTPFENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP 149
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVlelLELVGLEDKADAYPAQLSGGQKQRVGIARA-LANNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491074653 150 LWIL-DEPLTAIDKQGVAELISLFEQ-HAQRGGMVLLTTHQ 188
Cdd:cd03258 160 KVLLcDEATSALDPETTQSILALLRDiNRELGLTIVLITHE 200
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
20-187 |
6.44e-22 |
|
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: 89.71 E-value: 6.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN----TLRDRA---AYQQDLLFiGHqpgikavLTPF 92
Cdd:cd03296 21 VSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDatdvPVQERNvgfVFQHYALF-RH-------MTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 93 ENLQFYQAVRGAAE-------QQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAIDKQG 164
Cdd:cd03296 93 DNVAFGLRVKPRSErppeaeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARA-LAVEPkVLLLDEPFGALDAKV 171
|
170 180
....*....|....*....|....
gi 491074653 165 VAELIS-LFEQHAQRGGMVLLTTH 187
Cdd:cd03296 172 RKELRRwLRRLHDELHVTTVFVTH 195
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-200 |
8.76e-22 |
|
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: 92.27 E-value: 8.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCV--RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDG---GEVCWRGRNTLR-DRAAYQQ 74
Cdd:COG1123 4 LLEVRDLSVRypGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLElSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 75 DLLFIGHQPGikAVLTPF-------ENLQFYQAVRGAAEQQAIWrALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSA 147
Cdd:COG1123 84 RIGMVFQDPM--TQLNPVtvgdqiaEALENLGLSRAEARARVLE-LLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491074653 148 APLWILDEPLTAIDKQGVAELISLFEQHAQRGGM-VLLTTHqDLAGVSQTVGKI 200
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTtVLLITH-DLGVVAEIADRV 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-161 |
3.61e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 87.90 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLlfig 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP-LADWSPAELAR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 81 hqpgIKAVLTPFENLQFYQAVR-------------GAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALAR----L 143
Cdd:PRK13548 77 ----RRAVLPQHSSLSFPFTVEevvamgraphglsRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARvlaqL 152
|
170 180
....*....|....*....|
gi 491074653 144 WL-SAAPLW-ILDEPLTAID 161
Cdd:PRK13548 153 WEpDGPPRWlLLDEPTSALD 172
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-187 |
4.12e-21 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 85.90 E-value: 4.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-------TLRDRAAY--QQDLLFIGhq 82
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlrdldleSLRKNIAYvpQDPFLFSG-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 83 pgikavlTPFENLqfyqavrgaaeqqaiwraleqvglvgyedlpvaqLSAGQQRRVALARLWLSAAPLWILDEPLTAIDK 162
Cdd:cd03228 91 -------TIRENI----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180
....*....|....*....|....*
gi 491074653 163 QGVAELISLFEQHAQrGGMVLLTTH 187
Cdd:cd03228 130 ETEALILEALRALAK-GKTVIVIAH 153
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
15-191 |
4.15e-21 |
|
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: 87.10 E-value: 4.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 15 ILfSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTL--RDRAAY--------QQDLLFIGHQ 82
Cdd:COG4181 27 IL-KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlFALdeDARARLrarhvgfvFQSFQLLPTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 83 PGIKAVLTPFEnlqfyqaVRGA--AEQQAIwRALEQVGLVGYED-LPvAQLSAGQQRRVALARLWLSAAPLWILDEP--- 156
Cdd:COG4181 106 TALENVMLPLE-------LAGRrdARARAR-ALLERVGLGHRLDhYP-AQLSGGEQQRVALARAFATEPAILFADEPtgn 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 491074653 157 LTAIDKQGVAELisLFEQHAQRGGMVLLTTH-QDLA 191
Cdd:COG4181 177 LDAATGEQIIDL--LFELNRERGTTLVLVTHdPALA 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-188 |
8.04e-21 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 86.01 E-value: 8.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRDRAAYQQDLLFigHQPGIKAVLTPFENLQFY 98
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDvTAAPPADRPVSMLF--QENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 99 QAVR---GAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLF-EQ 174
Cdd:cd03298 95 LSPGlklTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVlDL 174
|
170
....*....|....
gi 491074653 175 HAQRGGMVLLTTHQ 188
Cdd:cd03298 175 HAETKMTVLMVTHQ 188
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-187 |
9.91e-21 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 85.81 E-value: 9.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 19 ELSFSVqPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEV-----CW-RGRNTL----RDRA---AYQQDLLFiGHqpgi 85
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtVLfDSRKKInlppQQRKiglVFQQYALF-PH---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 86 kavLTPFENLQFyqAVRGAAEQQAIWRALEQVGLVGYEDL---PVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDK 162
Cdd:cd03297 90 ---LNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLlnrYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180
....*....|....*....|....*.
gi 491074653 163 QGVAELISLFEQ-HAQRGGMVLLTTH 187
Cdd:cd03297 165 ALRLQLLPELKQiKKNLNIPVIFVTH 190
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
20-187 |
1.50e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.82 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTL----RDRA-AYQQDLLFighqPGikavLTPF 92
Cdd:COG3839 22 IDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvTDLppkdRNIAmVFQSYALY----PH----MTVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 93 ENLQFYQAVRG--AAE-QQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARlwlsA----APLWILDEPLTAID---- 161
Cdd:COG3839 94 ENIAFPLKLRKvpKAEiDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGR----AlvrePKVFLLDEPLSNLDaklr 169
|
170 180
....*....|....*....|....*.
gi 491074653 162 KQGVAELISLfeqHAQRGGMVLLTTH 187
Cdd:COG3839 170 VEMRAEIKRL---HRRLGTTTIYVTH 192
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-161 |
3.74e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.20 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRDRAAYQQdllf 78
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvEALSARAASRR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 79 IGHQPGIKAVLTPFENLQFYQAVR----------GAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAA 148
Cdd:PRK09536 79 VASVPQDTSLSFEFDVRQVVEMGRtphrsrfdtwTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170
....*....|...
gi 491074653 149 PLWILDEPLTAID 161
Cdd:PRK09536 159 PVLLLDEPTASLD 171
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-187 |
7.70e-20 |
|
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: 83.46 E-value: 7.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcWRGRNTLRDRAAYQQDLLFIGH 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI-YIGGRDVTDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 82 QPGIKAVLTPFENLQFYQAVRGAAEQ---QAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDeidERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190
....*....|....*....|....*....|...
gi 491074653 159 AIDK----QGVAELISLfeqHAQRGGMVLLTTH 187
Cdd:cd03301 160 NLDAklrvQMRAELKRL---QQRLGTTTIYVTH 189
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-187 |
8.54e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 85.24 E-value: 8.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT-LRDRAAYQQdllfIGHQPGIKAV-- 88
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQR----VGVVPQFDNLdp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 89 -LTPFENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQG 164
Cdd:PRK13537 94 dFTVRENLLVFGRYFGLSAAAARALVpplLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQA 173
|
170 180
....*....|....*....|...
gi 491074653 165 VAELISLFEQHAQRGGMVLLTTH 187
Cdd:PRK13537 174 RHLMWERLRSLLARGKTILLTTH 196
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-190 |
2.42e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.14 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRDRAaYQQDLLF 78
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpiSMLSSRQ-LARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 79 IGHQPgikavLTPfENLQFYQAVR-------------GAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWL 145
Cdd:PRK11231 81 LPQHH-----LTP-EGITVRELVAygrspwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491074653 146 SAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHqDL 190
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH-DL 198
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
19-205 |
3.32e-19 |
|
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: 84.00 E-value: 3.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRnTLRDRAA--------------YQQDLLFiGHqpg 84
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE-VLQDSARgiflpphrrrigyvFQEARLF-PH--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 85 ikavLTPFENLQFYQAVRGAAEQQAiwrALEQ-VGLVGYEDL---PVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAI 160
Cdd:COG4148 92 ----LSVRGNLLYGRKRAPRAERRI---SFDEvVELLGIGHLldrRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491074653 161 DKQGVAELISLFEQHAQRGGM-VLLTTHqDLAGVSqtvgkiRLAEH 205
Cdd:COG4148 165 DLARKAEILPYLERLRDELDIpILYVSH-SLDEVA------RLADH 203
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
11-188 |
4.98e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 84.71 E-value: 4.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPD---GGEVCWRGR----NTLRDRAAY-QQDLLFIGHq 82
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMpidaKEMRAISAYvQQDDLFIPT- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 83 pgikavLTPFENLQFYQAVRGAAE------QQAIWRALEQVGL-------VGYEDLpVAQLSAGQQRRVALARLWLSAAP 149
Cdd:TIGR00955 114 ------LTVREHLMFQAHLRMPRRvtkkekRERVDEVLQALGLrkcantrIGVPGR-VKGLSGGERKRLAFASELLTDPP 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 491074653 150 LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQ 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-200 |
7.03e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 83.23 E-value: 7.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLLFIGHQPGIKAVLTPFENLQF-- 97
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED-VTHRSIQQRDICMVFQSYALFPHMSLGENVGYgl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 98 -YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID---KQGVAELISLFE 173
Cdd:PRK11432 104 kMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDanlRRSMREKIRELQ 183
|
170 180 190
....*....|....*....|....*....|....
gi 491074653 174 QhaQRGGMVLLTTH-QDLA-GVSQTV-----GKI 200
Cdd:PRK11432 184 Q--QFNITSLYVTHdQSEAfAVSDTVivmnkGKI 215
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-174 |
7.16e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.12 E-value: 7.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRDRAAYQ----Q 74
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipAMSRSRLYTvrkrM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 75 DLLFighQPG-IKAVLTPFENLQF----YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAP 149
Cdd:PRK11831 87 SMLF---QSGaLFTDMNVFDNVAYplreHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180
....*....|....*....|....*
gi 491074653 150 LWILDEPLTAIDKQGVAELISLFEQ 174
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISE 188
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
15-176 |
1.38e-18 |
|
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: 80.17 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 15 ILFsELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLLFIGHQP---GIKAVLTP 91
Cdd:cd03224 15 ILF-GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRD-ITGLPPHERARAGIGYVPegrRIFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 92 FENLQFYQAVRGAAEQQAIwraLEQVglvgYEDLPV---------AQLSAGQQRRVALARLWLSAAPLWILDEP------ 156
Cdd:cd03224 93 EENLLLGAYARRRAKRKAR---LERV----YELFPRlkerrkqlaGTLSGGEQQMLAIARALMSRPKLLLLDEPseglap 165
|
170 180
....*....|....*....|....*....
gi 491074653 157 ---------LTAIDKQGVAelISLFEQHA 176
Cdd:cd03224 166 kiveeifeaIRELRDEGVT--ILLVEQNA 192
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-161 |
1.76e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 82.91 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-------TLRDRAAY--QQDLLFIGhq 82
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDirdltleSLRRQIGVvpQDTFLFSG-- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 83 pgikavlTPFENLQFYqavRGAAEQQAIWRALEQVGLV--------GYeDLPVAQ----LSAGQQRRVALARLWLSAAPL 150
Cdd:COG1132 429 -------TIRENIRYG---RPDATDEEVEEAAKAAQAHefiealpdGY-DTVVGErgvnLSGGQRQRIAIARALLKDPPI 497
|
170
....*....|.
gi 491074653 151 WILDEPLTAID 161
Cdd:COG1132 498 LILDEATSALD 508
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-193 |
1.82e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.89 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLS-CVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRaayqQDLLFI 79
Cdd:PRK13639 1 ILETRDLKySYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDK----KSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 80 GHQPGI------KAVLTPF--ENLQFYQAVRGAAEQQAIWR---ALEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAA 148
Cdd:PRK13639 77 RKTVGIvfqnpdDQLFAPTveEDVAFGPLNLGLSKEEVEKRvkeALKAVGMEGFENKPPHHLSGGQKKRVAIAGI-LAMK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491074653 149 P-LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ-DLAGV 193
Cdd:PRK13639 156 PeIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDvDLVPV 202
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-187 |
1.83e-18 |
|
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: 79.94 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-------TLRDRAAY-QQDL-LFIGhqpgikavlT 90
Cdd:cd03245 23 VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDirqldpaDLRRNIGYvPQDVtLFYG---------T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 91 PFENLQFYqavRGAAEQQAIWRALEQVGLV--------GYeDLPV----AQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:cd03245 94 LRDNITLG---APLADDERILRAAELAGVTdfvnkhpnGL-DLQIgergRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180
....*....|....*....|....*....
gi 491074653 159 AIDKQGVAELISLFEQHAqRGGMVLLTTH 187
Cdd:cd03245 170 AMDMNSEERLKERLRQLL-GDKTLIIITH 197
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-187 |
2.04e-18 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 80.40 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLLFIGH 81
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQD-ITHLPMHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 82 ---QPGIKAVLTPFENLQFYQAVRG---AAEQQAIWRAL-EQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAPLWI-L 153
Cdd:TIGR04406 81 lpqEASIFRKLTVEENIMAVLEIRKdldRAEREERLEALlEEFQISHLRDNKAMSLSGGERRRVEIARA-LATNPKFIlL 159
|
170 180 190
....*....|....*....|....*....|....
gi 491074653 154 DEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDH 193
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-187 |
3.48e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.44 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFS-ELSFSVQPgdIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN---TLRDRAAYQQDLLFIGHQPGIK 86
Cdd:PRK13638 12 QDEPVLKGlNLDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldySKRGLLALRQQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 87 AVLTPFE-NLQFYQAVRGAAEQQAIWRALEQVGLV---GYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDK 162
Cdd:PRK13638 90 IFYTDIDsDIAFSLRNLGVPEAEITRRVDEALTLVdaqHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180
....*....|....*....|....*
gi 491074653 163 QGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGNHVIISSH 194
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
18-181 |
3.50e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 81.28 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRG----RNTLRDRA---AYQQDLLFiGHqpgikavLT 90
Cdd:PRK10851 19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsRLHARDRKvgfVFQHYALF-RH-------MT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 91 PFENLQFYQAV-------RGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAIDK 162
Cdd:PRK10851 91 VFDNIAFGLTVlprrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARA-LAVEPqILLLDEPFGALDA 169
|
170 180 190
....*....|....*....|....*....|..
gi 491074653 163 QGVAEL-------------ISLFEQHAQRGGM 181
Cdd:PRK10851 170 QVRKELrrwlrqlheelkfTSVFVTHDQEEAM 201
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
21-185 |
3.65e-18 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 79.65 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN---TLRDRAAYQQDL--------LFiGHqpgikavL 89
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDltdSKKDINKLRRKVgmvfqqfnLF-PH-------L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 90 TPFENLQFYQ-AVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAPLWIL-DEPLTAIDKQG 164
Cdd:COG1126 93 TVLENVTLAPiKVKKMSKAEAEERAmelLERVGLADKADAYPAQLSGGQQQRVAIARA-LAMEPKVMLfDEPTSALDPEL 171
|
170 180
....*....|....*....|..
gi 491074653 165 VAELISLFEQHAQRG-GMVLLT 185
Cdd:COG1126 172 VGEVLDVMRDLAKEGmTMVVVT 193
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-197 |
5.25e-18 |
|
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: 78.91 E-value: 5.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFI-GHQPGIKAVLTPFENLQFY 98
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfGQKTQLWWDLPVIDSFYLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 99 QAVRGAAEQQAIWRALEQVGLVGYEDL---PVAQLSAGQQRRVALARLWLSAAPLWILDEP---LTAIDKQGVAELISlf 172
Cdd:cd03267 120 AAIYDLPPARFKKRLDELSELLDLEELldtPVRQLSLGQRMRAEIAAALLHEPEILFLDEPtigLDVVAQENIRNFLK-- 197
|
170 180
....*....|....*....|....*..
gi 491074653 173 EQHAQRGGMVLLTTH--QDLAGVSQTV 197
Cdd:cd03267 198 EYNRERGTTVLLTSHymKDIEALARRV 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-187 |
6.92e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.26 E-value: 6.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 14 RILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT-LRDRAAYQQdllfIGHQPGIKAVLTPF 92
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLARAR----IGVVPQFDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 93 ---ENLQFYQAVRGAAEQQ---AIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVA 166
Cdd:PRK13536 130 tvrENLLVFGRYFGMSTREieaVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARH 209
|
170 180
....*....|....*....|.
gi 491074653 167 ELISLFEQHAQRGGMVLLTTH 187
Cdd:PRK13536 210 LIWERLRSLLARGKTILLTTH 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-184 |
1.22e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.09 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAA-------YQQDLLF----------IGHQP 83
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSrrpvsmlFQENNLFshltvaqnigLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 84 GIKavLTpfenlqfyqavrgAAEQQAIWRALEQVGLVGY-EDLPvAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDK 162
Cdd:PRK10771 99 GLK--LN-------------AAQREKLHAIARQMGIEDLlARLP-GQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180
....*....|....*....|..
gi 491074653 163 QGVAELISLFEQHAQRGGMVLL 184
Cdd:PRK10771 163 ALRQEMLTLVSQVCQERQLTLL 184
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-187 |
1.36e-17 |
|
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: 77.61 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGL-----ARPDGGEVCWRGRN---------TLR 67
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDiydldvdvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 68 DRAA--YQQDLLFIGhqpgikavlTPFENLQFYQAVRGAAEQQAIWR----ALEQVGLVGYED--LPVAQLSAGQQRRVA 139
Cdd:cd03260 81 RRVGmvFQKPNPFPG---------SIYDNVAYGLRLHGIKLKEELDErveeALRKAALWDEVKdrLHALGLSGGQQQRLC 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491074653 140 LARLWLSAAPLWILDEPLTAID---KQGVAELIslFEQHAQRggMVLLTTH 187
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDpisTAKIEELI--AELKKEY--TIVIVTH 198
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-190 |
1.63e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.96 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLArPDGGEVCWRGRN-------TLRDRAAY---QQDLLFIghqpgikavL 89
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPlsdwsaaELARHRAYlsqQQSPPFA---------M 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 90 TPFENLQFYQAvrGAAEQQAIWRALEQV-GLVGYEDL---PVAQLSAGQQRRVALAR----LWLSAAP---LWILDEPLT 158
Cdd:COG4138 85 PVFQYLALHQP--AGASSEAVEQLLAQLaEALGLEDKlsrPLTQLSGGEWQRVRLAAvllqVWPTINPegqLLLLDEPMN 162
|
170 180 190
....*....|....*....|....*....|..
gi 491074653 159 AIDKQGVAELISLFEQHAQRGGMVLLTTHqDL 190
Cdd:COG4138 163 SLDVAQQAALDRLLRELCQQGITVVMSSH-DL 193
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-187 |
1.78e-17 |
|
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: 75.93 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTlrdraayqqdllfighqpgikAVLTPFEnlqfyqa 100
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV---------------------SFASPRD------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 101 vrgaAEQQAIWRaleqvglvgyedlpVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGG 180
Cdd:cd03216 72 ----ARRAGIAM--------------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGV 133
|
....*..
gi 491074653 181 MVLLTTH 187
Cdd:cd03216 134 AVIFISH 140
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-190 |
1.84e-17 |
|
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: 78.07 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRD---RAAYQQDLLFIGHQPGIKAVLTPFENL 95
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiAAMSRkelRELRRKKISMVFQSFALLPHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 96 QFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID----KQGVAEL 168
Cdd:cd03294 124 AFGLEVQGVPRAEREERAaeaLELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDEL 203
|
170 180
....*....|....*....|..
gi 491074653 169 ISLfeqHAQRGGMVLLTTHqDL 190
Cdd:cd03294 204 LRL---QAELQKTIVFITH-DL 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-188 |
3.22e-17 |
|
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: 76.93 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDG---GEVCWRG----RNTLRDRAAY-QQDLLFIGHq 82
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGqprkPDQFQKCVAYvRQDDILLPG- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 83 pgikavLTPFENLQFYQAVRGAAEQ-QAIWRAL-EQVGLVGYEDLPVA-----QLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:cd03234 96 ------LTVRETLTYTAILRLPRKSsDAIRKKRvEDVLLRDLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|...
gi 491074653 156 PLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQ 202
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
20-208 |
3.63e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 77.06 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRnTLRDRAA------------YQQDLLFighqPGika 87
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGL-KVNDPKVderlirqeagmvFQQFYLF----PH--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 88 vLTPFENLQF-YQAVRGAAEQQAIWRALEQVGLVGYED----LPvAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAID 161
Cdd:PRK09493 92 -LTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAErahhYP-SELSGGQQQRVAIARA-LAVKPkLMLFDEPTSALD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491074653 162 KQGVAELISLFEQHAQRGGMVLLTTHQdlAGVSQTVGKiRLAEHDAG 208
Cdd:PRK09493 169 PELRHEVLKVMQDLAEEGMTMVIVTHE--IGFAEKVAS-RLIFIDKG 212
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-190 |
3.89e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.08 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcwrgrntlrdraaYQQDLLFIG 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 81 HQPGiKAVLTPFENLQF--YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:PRK09544 71 YVPQ-KLYLDTTLPLTVnrFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190
....*....|....*....|....*....|..
gi 491074653 159 AIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-187 |
4.01e-17 |
|
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: 77.92 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 34 GPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLLFIGHQPGIKAVLTPFENLQFYQAVRG--AAEQQA-I 110
Cdd:TIGR01187 3 GPSGCGKTTLLRLLAGFEQPDSGSIMLDGED-VTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKvpRAEIKPrV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 111 WRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDK----QGVAELISLfeqHAQRGGMVLLTT 186
Cdd:TIGR01187 82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKklrdQMQLELKTI---QEQLGITFVFVT 158
|
.
gi 491074653 187 H 187
Cdd:TIGR01187 159 H 159
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
20-187 |
4.41e-17 |
|
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: 76.43 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcWRGRNTLRDRAAYQQDLLFIGH---QPGIKAVLTPFENLQ 96
Cdd:cd03218 19 VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKI-LLDGQDITKLPMHKRARLGIGYlpqEASIFRKLTVEENIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 97 FYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAPLWI-LDEPLTAIDKQGVAELISLF 172
Cdd:cd03218 98 AVLEIRGLSKKEREEKLeelLEEFHITHLRKSKASSLSGGERRRVEIARA-LATNPKFLlLDEPFAGVDPIAVQDIQKII 176
|
170
....*....|....*
gi 491074653 173 EQHAQRGGMVLLTTH 187
Cdd:cd03218 177 KILKDRGIGVLITDH 191
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-187 |
4.50e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 76.29 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVR------DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRDRaAY 72
Cdd:PRK10247 1 MQENSPLLQLQnvgylaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDisTLKPE-IY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 73 QQDLLFIGHQPgikaVL---TPFENLQF-YQAVRGAAEQQAIWRALEQVGLVGYE-DLPVAQLSAGQQRRVALARLWLSA 147
Cdd:PRK10247 80 RQQVSYCAQTP----TLfgdTVYDNLIFpWQIRNQQPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491074653 148 APLWILDEPLTAID---KQGVAELISLFEQhaQRGGMVLLTTH 187
Cdd:PRK10247 156 PKVLLLDEITSALDesnKHNVNEIIHRYVR--EQNIAVLWVTH 196
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
15-188 |
4.70e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.59 E-value: 4.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 15 ILFsELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcwrgrntlrDRAAYQQDLlfiGHQPGIKAV------ 88
Cdd:PRK11124 17 ALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL---------NIAGNHFDF---SKTPSDKAIrelrrn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 89 -------------LTPFENLqfYQA---VRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAP 149
Cdd:PRK11124 84 vgmvfqqynlwphLTVQQNL--IEApcrVLGLSKDQALARAeklLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 491074653 150 LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-178 |
5.84e-17 |
|
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: 76.17 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDE-RILFsELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLLFI 79
Cdd:COG0410 3 MLEVENLHAGYGGiHVLH-GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED-ITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 80 GHQP---GIKAVLTPFENLQFYQAVRGAAEQQAiwRALEQVglvgYEDLPV---------AQLSAGQQRRVALARLWLSA 147
Cdd:COG0410 81 GYVPegrRIFPSLTVEENLLLGAYARRDRAEVR--ADLERV----YELFPRlkerrrqraGTLSGGEQQMLAIGRALMSR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491074653 148 APLWILDEP---------------LTAIDKQGVAelISLFEQHAQR 178
Cdd:COG0410 155 PKLLLLDEPslglapliveeifeiIRRLNREGVT--ILLVEQNARF 198
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-188 |
7.48e-17 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 78.17 E-value: 7.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRntlrDRAAYQQDLL-----FIGHQPGIK 86
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV----PVSSLDQDEVrrrvsVCAQDAHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 87 AVlTPFENLQFyqaVRGAAEQQAIWRALEQVGLVGY-EDLP----------VAQLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:TIGR02868 422 DT-TVRENLRL---ARPDATDEELWAALERVGLADWlRALPdgldtvlgegGARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|...
gi 491074653 156 PLTAIDKQGVAELISLFEQhAQRGGMVLLTTHQ 188
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLA-ALSGRTVVLITHH 529
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-188 |
8.92e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.94 E-value: 8.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIG 80
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 81 HQPGIKAVLTPF---------EN-LQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSA 147
Cdd:PRK11264 83 LRQHVGFVFQNFnlfphrtvlENiIEGPVIVKGEPKEEATARArelLAKVGLAGKETSYPRRLSGGQQQRVAIARA-LAM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491074653 148 APLWIL-DEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:PRK11264 162 RPEVILfDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE 203
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-187 |
1.03e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.62 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRDRAAYQ---QDLLFIGHQPGIKAVLTPFE 93
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmSKLSSAAKAElrnQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 94 NLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLP---VAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELIS 170
Cdd:PRK11629 107 NVAMPLLIGKKKPAEINSRALEMLAAVGLEHRAnhrPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ 186
|
170
....*....|....*...
gi 491074653 171 LF-EQHAQRGGMVLLTTH 187
Cdd:PRK11629 187 LLgELNRLQGTAFLVVTH 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
11-187 |
1.60e-16 |
|
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: 75.03 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT-------LRDRAAY--QQDLLFiGH 81
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIreqdpveLRRKIGYviQQIGLF-PH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 82 qpgikavLTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVA-----QLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:cd03295 90 -------MTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFAdryphELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190
....*....|....*....|....*....|..
gi 491074653 157 LTAIDKQGVAELISLFEQ-HAQRGGMVLLTTH 187
Cdd:cd03295 163 FGALDPITRDQLQEEFKRlQQELGKTIVFVTH 194
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-187 |
2.10e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 74.68 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLLFIG 80
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED-ITHLPMHKRARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 81 H---QPGIKAVLTPFENLqfyQAV-----RGAAEQQAIWRAL-EQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAPLW 151
Cdd:COG1137 82 YlpqEASIFRKLTVEDNI---LAVlelrkLSKKEREERLEELlEEFGITHLRKSKAYSLSGGERRRVEIARA-LATNPKF 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 491074653 152 I-LDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:COG1137 158 IlLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH 194
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-187 |
2.47e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.03 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTlrdraayqQDLlfIGHQPGIKAV------------ 88
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI--------EGL--PGHQIARMGVvrtfqhvrlfre 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 89 LTPFENL--------------------QFYQAVRGAAEQQAIWraLEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAA 148
Cdd:PRK11300 95 MTVIENLlvaqhqqlktglfsgllktpAFRRAESEALDRAATW--LERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491074653 149 PLWILDEPLTAIDKQGVAELISLFEQ-HAQRGGMVLLTTH 187
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAElRNEHNVTVLLIEH 212
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
24-187 |
2.57e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.43 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 24 VQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLR----DRAAYQ-QDLLFIGHQPGIKAVLTPFENLQFY 98
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARAKLRaKHVGFVFQSFMLIPTLNALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 99 QAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQG---VAELisLF 172
Cdd:PRK10584 113 ALLRGESSRQSRNGAkalLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkIADL--LF 190
|
170
....*....|....*
gi 491074653 173 EQHAQRGGMVLLTTH 187
Cdd:PRK10584 191 SLNREHGTTLILVTH 205
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-161 |
2.95e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.14 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR------------NTLrdr 69
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvpaenrhvNTV--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 70 aaYQQDLLFiGHqpgikavLTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLP---VAQLSAGQQRRVALARLWLS 146
Cdd:PRK09452 92 --FQSYALF-PH-------MTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAqrkPHQLSGGQQQRVAIARAVVN 161
|
170
....*....|....*
gi 491074653 147 AAPLWILDEPLTAID 161
Cdd:PRK09452 162 KPKVLLLDESLSALD 176
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-195 |
3.03e-16 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 73.12 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVlTPFENLQfyq 99
Cdd:cd03247 21 LSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT-TLRNNLG--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 100 avrgaaeqqaiwraleqvglvgyedlpvAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAqRG 179
Cdd:cd03247 97 ----------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVL-KD 147
|
170
....*....|....*.
gi 491074653 180 GMVLLTTHQdLAGVSQ 195
Cdd:cd03247 148 KTLIWITHH-LTGIEH 162
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-187 |
3.49e-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: 76.59 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVLTPFENLQFYQ 99
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 100 AVRGAA----EQQAIWrALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQH 175
Cdd:TIGR01257 2038 RLRGVPaeeiEKVANW-SIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
|
170
....*....|..
gi 491074653 176 AQRGGMVLLTTH 187
Cdd:TIGR01257 2117 IREGRAVVLTSH 2128
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-161 |
5.01e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 75.74 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCW----------RGRNTLRD-RA 70
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklayvdQSRDALDPnKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 71 AYQ-----QDLLFIG-HQPGIKAVLTPFenlqfyqAVRGAAEQQaiwraleqvglvgyedlPVAQLSAGQQRRVALARLW 144
Cdd:TIGR03719 403 VWEeisggLDIIKLGkREIPSRAYVGRF-------NFKGSDQQK-----------------KVGQLSGGERNRVHLAKTL 458
|
170
....*....|....*..
gi 491074653 145 LSAAPLWILDEPLTAID 161
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLD 475
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-187 |
5.61e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 75.74 E-value: 5.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 14 RILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEvcwrgrntlrdraAYQQDLLFIGH---QPGIKAVLT 90
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE-------------ARPQPGIKVGYlpqEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 91 PFEN-----------LQFYQAVRG------------AAEQQAIWRALEQVGLVGYE---------------DLPVAQLSA 132
Cdd:TIGR03719 85 VRENveegvaeikdaLDRFNEISAkyaepdadfdklAAEQAELQEIIDAADAWDLDsqleiamdalrcppwDADVTKLSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491074653 133 GQQRRVALARLWLSAAPLWILDEPLTAIDkqgvAELISLFEQHAQR-GGMVLLTTH 187
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEyPGTVVAVTH 216
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
12-175 |
6.21e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 75.61 E-value: 6.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGL--------ARPDGGEVCW--------RGrnTLRDraayqqd 75
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwpygsgriARPAGARVLFlpqrpylpLG--TLRE------- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 76 llfighqpgikAVLTPFENLQFyqavrgaaEQQAIWRALEQVGLVGY-EDLPVAQ-----LSAGQQRRVALARLWLSAAP 149
Cdd:COG4178 445 -----------ALLYPATAEAF--------SDAELREALEAVGLGHLaERLDEEAdwdqvLSLGEQQRLAFARLLLHKPD 505
|
170 180
....*....|....*....|....*.
gi 491074653 150 LWILDEPLTAIDKQGVAELISLFEQH 175
Cdd:COG4178 506 WLFLDEATSALDEENEAALYQLLREE 531
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
10-187 |
6.59e-16 |
|
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: 73.52 E-value: 6.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 10 VRDERILFSE-----LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTL------RDRAAYQQDLLF 78
Cdd:cd03299 3 VENLSKDWKEfklknVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITnlppekRDISYVPQNYAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 79 IGHqpgikavLTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDL---PVAQLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:cd03299 83 FPH-------MTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLlnrKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190
....*....|....*....|....*....|...
gi 491074653 156 PLTAIDKQGVAELISLFEQ-HAQRGGMVLLTTH 187
Cdd:cd03299 156 PFSALDVRTKEKLREELKKiRKEFGVTVLHVTH 188
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-187 |
8.85e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 73.57 E-value: 8.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 6 SLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLR----DRAAYQQDLLFIgH 81
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraQRKAFRRDIQMV-F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 82 QPGIKAVltpfeNLQfyQAVR-------------GAAEQQAiwRALEQVGLVGYED-----LPvAQLSAGQQRRVALARL 143
Cdd:PRK10419 96 QDSISAV-----NPR--KTVReiireplrhllslDKAERLA--RASEMLRAVDLDDsvldkRP-PQLSGGQLQRVCLARA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491074653 144 wLSAAP-LWILDEPLTAIDKQGVAELISLFEQHAQRGGMV-LLTTH 187
Cdd:PRK10419 166 -LAVEPkLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITH 210
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-187 |
1.09e-15 |
|
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: 72.57 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLrdraayqqdLLFIGHqpGIKAVLTPFENLQFYQ 99
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS---------LLGLGG--GFNPELTGRENIYLNG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 100 AVRG--AAEQQAIWRALEQV-GLVGYEDLPVAQLSAGQQRRVALArlwLSAA---PLWILDEPLTAIDKQGVAELISLFE 173
Cdd:cd03220 110 RLLGlsRKEIDEKIDEIIEFsELGDFIDLPVKTYSSGMKARLAFA---IATAlepDILLIDEVLAVGDAAFQEKCQRRLR 186
|
170
....*....|....
gi 491074653 174 QHAQRGGMVLLTTH 187
Cdd:cd03220 187 ELLKQGKTVILVSH 200
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-191 |
1.29e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.58 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDllfIGhqpgikAV----------L 89
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARR---IG------VVfgqrsqlwwdL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 90 TPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDL---PVAQLSAGQQRRVALArlwlsAAPLW-----ILDEP---LT 158
Cdd:COG4586 112 PAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELldtPVRQLSLGQRMRCELA-----AALLHrpkilFLDEPtigLD 186
|
170 180 190
....*....|....*....|....*....|...
gi 491074653 159 AIDKQGVAELISlfEQHAQRGGMVLLTTHqDLA 191
Cdd:COG4586 187 VVSKEAIREFLK--EYNRERGTTILLTSH-DMD 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-197 |
1.80e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.40 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCwRGRNTLrdrAAYQQD--LLFighQpgiKAVLT 90
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-AGTAPL---AEAREDtrLMF---Q---DARLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 91 PF----ENLQFyqAVRGAAEQQAIwRALEQVGLVGY-EDLPVAqLSAGQQRRVALARLWLSAAPLWILDEPLTAIDK--- 162
Cdd:PRK11247 94 PWkkviDNVGL--GLKGQWRDAAL-QALAAVGLADRaNEWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLGALDAltr 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 491074653 163 ---QGVAEliSLFEQHaqrGGMVLLTTHQdlagVSQTV 197
Cdd:PRK11247 170 iemQDLIE--SLWQQH---GFTVLLVTHD----VSEAV 198
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
12-187 |
1.91e-15 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 70.71 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEV--------CWrGRNTLRDRAAY--QQDLLFIGh 81
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisQW-DPNELGDHVGYlpQDDELFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 82 qpgikavlTPFENLqfyqavrgaaeqqaiwraleqvglvgyedlpvaqLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:cd03246 91 --------SIAENI----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180
....*....|....*....|....*.
gi 491074653 162 KQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:cd03246 129 VEGERALNQAIAALKAAGATRIVIAH 154
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-187 |
2.20e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.42 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRA----AYQQDL 76
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAergvVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 77 LFighqPGIKAVltpfENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWIL 153
Cdd:PRK11248 81 LL----PWRNVQ----DNVAFGLQLAGVEKMQRLEIAhqmLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*
gi 491074653 154 DEPLTAIDKQGVAELISLFEQHAQRGG-MVLLTTH 187
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGkQVLLITH 187
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-190 |
2.55e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLArPDGGEVCWRGRN-------TLRDRAAY---QQDLLFIghqpgikavL 89
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPleawsaaELARHRAYlsqQQTPPFA---------M 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 90 TPFENLQFYQA--VRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALA----RLWLSAAP---LWILDEPLTAI 160
Cdd:PRK03695 85 PVFQYLTLHQPdkTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlQVWPDINPagqLLLLDEPMNSL 164
|
170 180 190
....*....|....*....|....*....|
gi 491074653 161 DKQGVAELISLFEQHAQRGGMVLLTTHqDL 190
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGIAVVMSSH-DL 193
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
21-195 |
3.16e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.22 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTlrdRAAYQQDLlfIGHQPGIKAVLTPFENLQFYQA 100
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT---RQALQKNL--VAYVPQSEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 101 VRG------------AAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAEL 168
Cdd:PRK15056 102 MMGryghmgwlrrakKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
170 180
....*....|....*....|....*..
gi 491074653 169 ISLFEQHAQRGGMVLLTTHqDLAGVSQ 195
Cdd:PRK15056 182 ISLLRELRDEGKTMLVSTH-NLGSVTE 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-187 |
3.48e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.14 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRD-RAAYQqdlLFIG--HQ-----PgikaVLTP 91
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvRIRSpRDAIA---LGIGmvHQhfmlvP----NLTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 92 FENLQ------FYQAVRGAAEQQAIWRALEQVGL-VgyeDL--PVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDK 162
Cdd:COG3845 98 AENIVlgleptKGGRLDRKAARARIRELSERYGLdV---DPdaKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTP 174
|
170 180
....*....|....*....|....*
gi 491074653 163 QGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:COG3845 175 QEADELFEILRRLAAEGKSIIFITH 199
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-187 |
3.75e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 71.06 E-value: 3.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAA------YQQDLLFIGHQpgIKAVLTPFE 93
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpflrRQIGMIFQDHH--LLMDRTVYD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 94 NLQFYQAVRGAAEQQAIWR---ALEQVGLVG-YEDLPVaQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELI 169
Cdd:PRK10908 99 NVAIPLIIAGASGDDIRRRvsaALDKVGLLDkAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIL 177
|
170
....*....|....*...
gi 491074653 170 SLFEQHAQRGGMVLLTTH 187
Cdd:PRK10908 178 RLFEEFNRVGVTVLMATH 195
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-188 |
1.13e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.11 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRntlrdRAAyqqdLLFIGHqpGIKAVLTPFENLQFYQ 99
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-----VSA----LLELGA--GFHPELTGRENIYLNG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 100 AVRGAAEQQaIWRALEQV----GLVGYEDLPVAQLSAGQQRRVALArlwLSAA---PLWILDEPLTAIDKQGVAELISLF 172
Cdd:COG1134 114 RLLGLSRKE-IDEKFDEIvefaELGDFIDQPVKTYSSGMRARLAFA---VATAvdpDILLVDEVLAVGDAAFQKKCLARI 189
|
170
....*....|....*.
gi 491074653 173 EQHAQRGGMVLLTTHQ 188
Cdd:COG1134 190 RELRESGRTVIFVSHS 205
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-163 |
1.43e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.02 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLLFIG 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 81 HQPGIKAVLTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVA---QLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRkphQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
....*.
gi 491074653 158 TAIDKQ 163
Cdd:PRK11607 178 GALDKK 183
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
11-190 |
1.85e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRgrntlrdraayQQDLLFIGHQPGIKAVLt 90
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----------VPDNQFGREASLIDAIG- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 91 pfENLQFYQAVrgaaeqqaiwRALEQVGLVgyeDL-----PVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGV 165
Cdd:COG2401 108 --RKGDFKDAV----------ELLNAVGLS---DAvlwlrRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180
....*....|....*....|....*..
gi 491074653 166 AELISLFEQHAQRGG--MVLLTTHQDL 190
Cdd:COG2401 173 KRVARNLQKLARRAGitLVVATHHYDV 199
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-162 |
1.87e-14 |
|
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: 69.18 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-------TLRDRAAY--QQDLLFIGhqp 83
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDirdisrkSLRSMIGVvlQDTFLFSG--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 84 gikavlTPFENLQFYqavRGAAEQQAIWRALEQVGLV--------GYEDLPVAQ---LSAGQQRRVALARLWLSAAPLWI 152
Cdd:cd03254 92 ------TIMENIRLG---RPNATDEEVIEAAKEAGAHdfimklpnGYDTVLGENggnLSQGERQLLAIARAMLRDPKILI 162
|
170
....*....|
gi 491074653 153 LDEPLTAIDK 162
Cdd:cd03254 163 LDEATSNIDT 172
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-193 |
2.53e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.11 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLL---FIGHQPGIK----------- 86
Cdd:PRK13651 27 SVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVlekLVIQKTRFKkikkikeirrr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 87 -AVLTPFENLQFYQAV-----------RGAAEQQAIWRALEQVGLVGyedLPVA-------QLSAGQQRRVALARLwLSA 147
Cdd:PRK13651 107 vGVVFQFAEYQLFEQTiekdiifgpvsMGVSKEEAKKRAAKYIELVG---LDESylqrspfELSGGQKRRVALAGI-LAM 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491074653 148 AP-LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHqDLAGV 193
Cdd:PRK13651 183 EPdFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH-DLDNV 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-187 |
2.98e-14 |
|
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: 68.65 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLR---DR-AAYQQDLLFighqpgikAVLTPFENL 95
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpDRmVVFQNYSLL--------PWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 96 qfYQAVRGA------AEQQAIWRA-LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAID---KQG 164
Cdd:TIGR01184 76 --ALAVDRVlpdlskSERRAIVEEhIALVGLTEAADKRPGQLSGGMKQRVAIARA-LSIRPkVLLLDEPFGALDaltRGN 152
|
170 180
....*....|....*....|....
gi 491074653 165 VAE-LISLFEQHaqrGGMVLLTTH 187
Cdd:TIGR01184 153 LQEeLMQIWEEH---RVTVLMVTH 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-187 |
3.54e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 70.24 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-------TLRDRAAY--QQDLLFIGhqpgikavlT 90
Cdd:PRK11160 359 LSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiadyseaALRQAISVvsQRVHLFSA---------T 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 91 PFENLQFyqAVRGAAEQQAIwRALEQVGLvgyEDLPVA-------------QLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:PRK11160 430 LRDNLLL--AAPNASDEALI-EVLQQVGL---EKLLEDdkglnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
170 180 190
....*....|....*....|....*....|
gi 491074653 158 TAIDKQGVAELISLFEQHAQrGGMVLLTTH 187
Cdd:PRK11160 504 EGLDAETERQILELLAEHAQ-NKTVLMITH 532
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
30-188 |
3.93e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 69.06 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 30 IQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVLTPF--ENLQFYQAVRGAAEQ 107
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIFSPTveQDIAFGPINLGLDEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 108 QAIWRALEQVGLVGYEDLPVA---QLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGM-VL 183
Cdd:PRK13652 113 TVAHRVSSALHMLGLEELRDRvphHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMtVI 192
|
....*
gi 491074653 184 LTTHQ 188
Cdd:PRK13652 193 FSTHQ 197
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
20-187 |
4.26e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.15 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSvqPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEvcwrgrntlrdraAYQQDLLFIGHQP---------------- 83
Cdd:PRK11819 28 LSFF--PGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-------------ARPAPGIKVGYLPqepqldpektvrenve 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 84 ----GIKAVLTPFE--NLQF------YQAVrgAAEQ---QAI------W---RALEQV--------GlvgyeDLPVAQLS 131
Cdd:PRK11819 93 egvaEVKAALDRFNeiYAAYaepdadFDAL--AAEQgelQEIidaadaWdldSQLEIAmdalrcppW-----DAKVTKLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491074653 132 AGQQRRVALARLWLSAAPLWILDEPLTAIDkqgvAELISLFEQHAQR-GGMVLLTTH 187
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLEQFLHDyPGTVVAVTH 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-188 |
4.60e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 68.50 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRG-----RNTLRDRAAYQ--Q 74
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfSQKPSEKAIRLlrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 75 DLLFIGHQPGIKAVLTPFENLqfYQA---VRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAA 148
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENL--IEApckVLGLSKEQAREKAmklLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491074653 149 PLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-187 |
6.05e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.66 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRD-RAAYQ-------QDL-----------LFIG 80
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPvRFRSpRDAQAagiaiihQELnlvpnlsvaenIFLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 81 HQPGIKAVLTpfenlqfYQAVRGAAEQqaiwrALEQVGLvgyeDL----PVAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:COG1129 104 REPRRGGLID-------WRAMRRRARE-----LLARLGL----DIdpdtPVGDLSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190
....*....|....*....|....*....|.
gi 491074653 157 LTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:COG1129 168 TASLTEREVERLFRIIRRLKAQGVAIIYISH 198
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-195 |
6.70e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.49 E-value: 6.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVR-DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLArPDGGEVCWRGRNtLR--DRAAYQQDLLF 78
Cdd:PRK11174 350 IEAEDLEILSpDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIE-LRelDPESWRKHLSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 79 IGHQPGIKAVlTPFENLQFYQAvrgAAEQQAIWRALEQV-----------GLvgyeDLPV----AQLSAGQQRRVALARL 143
Cdd:PRK11174 428 VGQNPQLPHG-TLRDNVLLGNP---DASDEQLQQALENAwvseflpllpqGL----DTPIgdqaAGLSVGQAQRLALARA 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491074653 144 WLSAAPLWILDEPLTAIDKQGvAELISLFEQHAQRGGMVLLTTHQ--DLAGVSQ 195
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHS-EQLVMQALNAASRRQTTLMVTHQleDLAQWDQ 552
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
20-188 |
6.94e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.50 E-value: 6.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDG---------GEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVLT 90
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDIRKSRANTGYIFQQFNLVNRLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 91 PFENL--------QFYQAVR---GAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:PRK09984 103 VLENVligalgstPFWRTCFswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
|
170 180 190
....*....|....*....|....*....|
gi 491074653 160 IDKQGVAELISLFEQHAQRGGM-VLLTTHQ 188
Cdd:PRK09984 183 LDPESARIVMDTLRDINQNDGItVVVTLHQ 212
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-187 |
7.14e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.00 E-value: 7.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT----LRDRAayQQDLL 77
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllpLHARA--RRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 78 FIGHQPGIKAVLTPFENLQFYQAVRG--AAEQQAIwRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAPLWI 152
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIRDdlSAEQRED-RAnelMEEFHIEHLRDSMGQSLSGGERRRVEIARA-LAANPKFI 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 491074653 153 -LDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:PRK10895 160 lLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
12-175 |
7.39e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 66.41 E-value: 7.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLarpdggevcW---RGRNTLRDRAayqqDLLFIGHQPgikav 88
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL---------WpwgSGRIGMPEGE----DLLFLPQRP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 89 LTPFENLqfyqavrgaaeQQAIWRALEQVglvgyedlpvaqLSAGQQRRVALARLWLsAAPLW-ILDEPLTAIDKQGVAE 167
Cdd:cd03223 74 YLPLGTL-----------REQLIYPWDDV------------LSGGEQQRLAFARLLL-HKPKFvFLDEATSALDEESEDR 129
|
....*...
gi 491074653 168 LISLFEQH 175
Cdd:cd03223 130 LYQLLKEL 137
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-187 |
8.96e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 69.37 E-value: 8.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRDRAAYQ---QDLLFIGHQPGIKAVLTPFEN 94
Cdd:PRK10535 27 ISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvaTLDADALAQlrrEHFGFIFQRYHLLSHLTAAQN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 95 LQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISL 171
Cdd:PRK10535 107 VEVPAVYAGLERKQRLLRAqelLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAI 186
|
170
....*....|....*.
gi 491074653 172 FEQHAQRGGMVLLTTH 187
Cdd:PRK10535 187 LHQLRDRGHTVIIVTH 202
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-190 |
9.89e-14 |
|
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: 67.17 E-value: 9.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRdRAAYQQDLLFIGHQP---GIKAVLTPFENLQ 96
Cdd:TIGR03410 19 VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITK-LPPHERARAGIAYVPqgrEIFPRLTVEENLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 97 FYQAVRGAAEQQAIWRAleqvglvgYEDLPVAQ---------LSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAE 167
Cdd:TIGR03410 98 TGLAALPRRSRKIPDEI--------YELFPVLKemlgrrggdLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKD 169
|
170 180
....*....|....*....|...
gi 491074653 168 LISLFEQHAQRGGMVLLTTHQDL 190
Cdd:TIGR03410 170 IGRVIRRLRAEGGMAILLVEQYL 192
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
14-187 |
9.99e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.22 E-value: 9.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 14 RILFsELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcwRGRNTLRDRAAYQQDLLFIGHQPGIKAVL---- 89
Cdd:PRK13643 20 RALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV--TVGDIVVSSTSKQKEIKPVRKKVGVVFQFpesq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 90 ----TPFENLQFYQAVRGAAEQQAIWRALEQVGLVG-----YEDLPVaQLSAGQQRRVALARLWLSAAPLWILDEPLTAI 160
Cdd:PRK13643 97 lfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGladefWEKSPF-ELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180
....*....|....*....|....*..
gi 491074653 161 DKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
20-188 |
1.98e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.92 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT--LRDRAA------------YQQDLLFIGHQPGI 85
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlVRDKDGqlkvadknqlrlLRTRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 86 KAVLTPFEN-LQFYQAVRGAAEQQAIWRALEQVGLVGYED-----LPVaQLSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:PRK10619 104 WSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDEraqgkYPV-HLSGGQQQRVSIARALAMEPEVLLFDEPTSA 182
|
170 180
....*....|....*....|....*....
gi 491074653 160 IDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:PRK10619 183 LDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-58 |
2.76e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.84 E-value: 2.76e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEV 58
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-182 |
3.14e-13 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 66.28 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 19 ELSFSVQPGD-----IIQVEGPNGAGKTSLLRILAGLARPDGGEVCWrgrntLRDRAAYQQDLLFIGHQPGIKAVLtpfe 93
Cdd:cd03237 12 EFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-----ELDTVSYKPQYIKADYEGTVRDLL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 94 nlqfYQAVRGAAEqQAIWRA--LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQG---VAEL 168
Cdd:cd03237 83 ----SSITKDFYT-HPYFKTeiAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlmASKV 157
|
170
....*....|....
gi 491074653 169 ISLFEQHAQRGGMV 182
Cdd:cd03237 158 IRRFAENNEKTAFV 171
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-187 |
4.65e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.19 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRnTLRDRAAYQqdllfIGHQPGIKavltpFENL--QF 97
Cdd:PRK13635 26 VSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM-VLSEETVWD-----VRRQVGMV-----FQNPdnQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 98 YQA-----VRGAAEQQAIWR---------ALEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAIDK 162
Cdd:PRK13635 95 VGAtvqddVAFGLENIGVPReemvervdqALRQVGMEDFLNREPHRLSGGQKQRVAIAGV-LALQPdIIILDEATSMLDP 173
|
170 180
....*....|....*....|....*.
gi 491074653 163 QGVAELISLFEQHAQRGGM-VLLTTH 187
Cdd:PRK13635 174 RGRREVLETVRQLKEQKGItVLSITH 199
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
13-188 |
5.60e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 66.20 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcwrgrnTLRDR----AAYQQDLLFIGHQPGIkaV 88
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV------TIGERvitaGKKNKKLKPLRKKVGI--V 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 89 LTPFENLQFYQAVR----------GAAEQQAIWRALEQVGLVGY-EDL----PVaQLSAGQQRRVALARLwLSAAP-LWI 152
Cdd:PRK13634 91 FQFPEHQLFEETVEkdicfgpmnfGVSEEDAKQKAREMIELVGLpEELlarsPF-ELSGGQMRRVAIAGV-LAMEPeVLV 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 491074653 153 LDEPLTAIDKQGVAELISLFEQ-HAQRGGMVLLTTHQ 188
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKlHKEKGLTTVLVTHS 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-184 |
7.01e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.58 E-value: 7.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRderiLFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR----NTLRD--RA--AY 72
Cdd:COG1129 256 VLEVEGLSVGG----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvriRSPRDaiRAgiAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 73 -----QQDLLFIGHqpGIK--AVLTPFENLQFYQAVRGAAEQQAIWRALEQVGL-VGYEDLPVAQLSAGQQRRVALARlW 144
Cdd:COG1129 332 vpedrKGEGLVLDL--SIRenITLASLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAK-W 408
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491074653 145 LSAAP-LWILDEPlTaidkQGV-----AELISLFEQHAQRGGMVLL 184
Cdd:COG1129 409 LATDPkVLILDEP-T----RGIdvgakAEIYRLIRELAAEGKAVIV 449
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-191 |
7.13e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.53 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLS-CVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT-------LRDRAA-- 71
Cdd:PRK13647 5 IEVEDLHfRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnaenekwVRSKVGlv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 72 YQ--QDLLFIGhqpgikavlTPFENLQF---YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLS 146
Cdd:PRK13647 85 FQdpDDQVFSS---------TVWDDVAFgpvNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491074653 147 AAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ-DLA 191
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDvDLA 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-197 |
7.35e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.39 E-value: 7.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSC---VRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGlARPDG--GEVCWRGR--NTLRDRAAYQ 73
Cdd:TIGR02633 257 ILEARNLTCwdvINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKfeGNVFINGKpvDIRNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 74 QDLLFI-------GHQP----GIKAVLTPFENLQFYQAVRGAAEQQAIWRALEQVGL-VGYEDLPVAQLSAGQQRRVALA 141
Cdd:TIGR02633 336 AGIAMVpedrkrhGIVPilgvGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLA 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491074653 142 RLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ--DLAGVSQTV 197
Cdd:TIGR02633 416 KMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSElaEVLGLSDRV 473
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
34-191 |
7.42e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.96 E-value: 7.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 34 GPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVLTPFENLQFYQAVRGAAEQQA---I 110
Cdd:TIGR01257 963 GHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAqleM 1042
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 111 WRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:TIGR01257 1043 EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDE 1122
|
.
gi 491074653 191 A 191
Cdd:TIGR01257 1123 A 1123
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-188 |
8.83e-13 |
|
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: 64.41 E-value: 8.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 16 LFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR------------NTLRDraayqqDLLFiGHqp 83
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiayvsqepwiqnGTIRE------NILF-GK-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 84 gikavltPFENlQFYQAVRGAAeqqaiwrALEQvglvgyeDLPV-------------AQLSAGQQRRVALARLWLSAAPL 150
Cdd:cd03250 91 -------PFDE-ERYEKVIKAC-------ALEP-------DLEIlpdgdlteigekgINLSGGQKQRISLARAVYSDADI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491074653 151 WILDEPLTAIDKQgVAELIslFEQ----HAQRGGMVLLTTHQ 188
Cdd:cd03250 149 YLLDDPLSAVDAH-VGRHI--FENcilgLLLNNKTRILVTHQ 187
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
13-205 |
1.04e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 65.24 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcwrgrntlrDRAAYQqdllfIGHQPGIKAVL--- 89
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI---------TIAGYH-----ITPETGNKNLKklr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 90 -----------------TPFENLQFYQAVRGAAEQQAIWRALEQVGLVGY-EDL----PVaQLSAGQQRRVALARLWLSA 147
Cdd:PRK13641 85 kkvslvfqfpeaqlfenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLisksPF-ELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491074653 148 APLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHqDLAGVSQTVGKIRLAEH 205
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH-NMDDVAEYADDVLVLEH 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-197 |
1.23e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.15 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 14 RILFsELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcwRGRNTLRDRAAYQQDLLFIGHQPGIkaVLTPFE 93
Cdd:PRK13649 21 RALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSV--RVDDTLITSTSKNKDIKQIRKKVGL--VFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 94 NLQFYQAVR----------GAAEQQAIWRALEQVGLVGY-EDL----PVaQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:PRK13649 96 SQLFEETVLkdvafgpqnfGVSQEEAEALAREKLALVGIsESLfeknPF-ELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491074653 159 AIDKQGVAELISLFEQHAQRGGMVLLTTH--QDLAGVSQTV 197
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLHQSGMTIVLVTHlmDDVANYADFV 215
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-190 |
1.85e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 64.48 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIG-------HQPGIKAVltpF 92
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVGmvfqdpdNQLFSASV---Y 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 93 ENLQFYQAVRGAAE---QQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELI 169
Cdd:PRK13636 102 QDVSFGAVNLKLPEdevRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIM 181
|
170 180
....*....|....*....|.
gi 491074653 170 SLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK13636 182 KLLVEMQKELGLTIIIATHDI 202
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-156 |
2.78e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.91 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWrgrntlRDRAA---YQQDllf 78
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW------SENANigyYAQD--- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 79 igHQPGIKAVLTPFENLQFY-------QAVRGAaeqqaiwraleqVG--LVGYEDL--PVAQLSAGQQRRVALARLWLSA 147
Cdd:PRK15064 391 --HAYDFENDLTLFDWMSQWrqegddeQAVRGT------------LGrlLFSQDDIkkSVKVLSGGEKGRMLFGKLMMQK 456
|
....*....
gi 491074653 148 APLWILDEP 156
Cdd:PRK15064 457 PNVLVMDEP 465
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-161 |
7.23e-12 |
|
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: 62.25 E-value: 7.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR-------NTLRDRAAY--QQDLLFIGhq 82
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlASLRRQIGLvsQDVFLFND-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 83 pgikavlTPFENLQFyqAVRGAAEQQAIwRALEQVGLV--------GYeDLPVAQ----LSAGQQRRVALARLWLSAAPL 150
Cdd:cd03251 91 -------TVAENIAY--GRPGATREEVE-EAARAANAHefimelpeGY-DTVIGErgvkLSGGQRQRIAIARALLKDPPI 159
|
170
....*....|.
gi 491074653 151 WILDEPLTAID 161
Cdd:cd03251 160 LILDEATSALD 170
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-170 |
8.93e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 62.37 E-value: 8.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLAR------PDGGEVCWRGRNTLR-DRAAYQQDLLFIGHQPG 84
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQiDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 85 IKAVLTPFENLQFYQAVRGAAEQQAIWRALEQ----VGLVG--YEDL--PVAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIKEKREIKKIVEEclrkVGLWKevYDRLnsPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170
....*....|....*..
gi 491074653 157 LTAID---KQGVAELIS 170
Cdd:PRK14246 181 TSMIDivnSQAIEKLIT 197
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
11-188 |
9.12e-12 |
|
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: 61.49 E-value: 9.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGlaRPDG----GEVCWRGR---NTLRDRAAY--QQDLlfigH 81
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAgvitGEILINGRpldKNFQRSTGYveQQDV----H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 82 QPGikavLTPFENLQFYQAVRGaaeqqaiwraleqvglvgyedlpvaqLSAGQQRRVALArLWLSAAPLWI-LDEPLTAI 160
Cdd:cd03232 91 SPN----LTVREALRFSALLRG--------------------------LSVEQRKRLTIG-VELAAKPSILfLDEPTSGL 139
|
170 180
....*....|....*....|....*...
gi 491074653 161 DKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:cd03232 140 DSQAAYNIVRFLKKLADSGQAILCTIHQ 167
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-184 |
1.07e-11 |
|
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: 60.91 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCvrdeRILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRDRAAYQQDLLF 78
Cdd:cd03215 4 VLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 79 IG---HQPGIKAVLTPFENLqfyqavrgaaeqqaiwrALEQvglvgyedlpvaQLSAGQQRRVALARlWLSAAP-LWILD 154
Cdd:cd03215 80 VPedrKREGLVLDLSVAENI-----------------ALSS------------LLSGGNQQKVVLAR-WLARDPrVLILD 129
|
170 180 190
....*....|....*....|....*....|
gi 491074653 155 EPLTAIDKQGVAELISLFEQHAQRGGMVLL 184
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRELADAGKAVLL 159
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-205 |
1.64e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLaRPDG---GEVCWRGR----NTLRDR-----AAYQQDL-----------L 77
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEelqaSNIRDTeragiAIIHQELalvkelsvlenI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 78 FIGHQPgikavlTPFENLQFYQAVRGAAEqqaiwrALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:PRK13549 104 FLGNEI------TPGGIMDYDAMYLRAQK------LLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491074653 158 TAIDKQGVAELISLFEQHAQRGGMVLLTTHQ--DLAGVSQTVGKIRLAEH 205
Cdd:PRK13549 172 ASLTESETAVLLDIIRDLKAHGIACIYISHKlnEVKAISDTICVIRDGRH 221
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-195 |
1.72e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.59 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDG--GEVCWRGRN----TLRDRAAYQQDLLFIGHqpgik 86
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKptkqILKRTGFVTQDDILYPH----- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 87 avLTPFENLQFYQAVR--GAAEQQAIWRALEQV----GLVGYEDLPVAQ-----LSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:PLN03211 155 --LTVRETLVFCSLLRlpKSLTKQEKILVAESViselGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491074653 156 PLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDLAGVSQ 195
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQ 272
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-210 |
2.21e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.38 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAG----LARPDG----GEVCWRGRNTLR---DR 69
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRGarvtGDVTLNGEPLAAidaPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 70 AAYQQDLLFIGHQPGIKAVLTPFENLQFYQAVRGAAE-----QQAIWRALEQVGLVGYEDLPVAQLSAGQQRRV----AL 140
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGAlthrdGEIAWQALALAGATALVGRDVTTLSGGELARVqfarVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 141 ARLW-----LSAAPLWILDEPLTAIDkqgvaelisLFEQHAqrggmvLLTTHQDLA-----GVSQTVGKIRLAEHDAGSL 210
Cdd:PRK13547 161 AQLWpphdaAQPPRYLLLDEPTAALD---------LAHQHR------LLDTVRRLArdwnlGVLAIVHDPNLAARHADRI 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-185 |
4.12e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.31 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 10 VRDERILFSE------LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLAR--PDG---GEVCWRGRNTLR-DRAAYQQDLL 77
Cdd:PRK14247 6 IRDLKVSFGQvevldgVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKmDVIELRRRVQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 78 FIGHQPGIKAVLTPFEN----LQFYQAVRGAAE-QQAIWRALEQVGLvgYE------DLPVAQLSAGQQRRVALARLWLS 146
Cdd:PRK14247 86 MVFQIPNPIPNLSIFENvalgLKLNRLVKSKKElQERVRWALEKAQL--WDevkdrlDAPAGKLSGGQQQRLCIARALAF 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 491074653 147 AAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLT 185
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVT 202
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
12-190 |
6.82e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.15 E-value: 6.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWrgrntlRDRAAYQQDLLFIGHQPGIkaVLTP 91
Cdd:PRK13648 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY------NNQAITDDNFEKLRKHIGI--VFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 92 FENlQFY--------------QAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:PRK13648 92 PDN-QFVgsivkydvafglenHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190
....*....|....*....|....*....|...
gi 491074653 158 TAIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDL 203
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
13-190 |
7.14e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.20 E-value: 7.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPD--------------GGEVCWrgrnTLRDRAA--YQQ-D 75
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpnskitvdgitlTAKTVW----DIREKVGivFQNpD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 76 LLFIGHQPGiKAVLTPFENlqfyQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:PRK13640 95 NQFVGATVG-DDVAFGLEN----RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190
....*....|....*....|....*....|....*
gi 491074653 156 PLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKNNLTVISITHDI 204
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-163 |
8.11e-11 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 59.04 E-value: 8.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEV-------CWRGRNTLRDRAAY--QQDLLFIGhqpGIKAVLT 90
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIlidgvdiSKIGLHDLRSRISIipQDPVLFSG---TIRSNLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 91 PFenlqfyqavrGAAEQQAIWRALEQVGL-------VGYEDLPVA----QLSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:cd03244 100 PF----------GEYSDEELWQALERVGLkefveslPGGLDTVVEeggeNLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
....
gi 491074653 160 IDKQ 163
Cdd:cd03244 170 VDPE 173
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
12-194 |
8.33e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 59.75 E-value: 8.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDraayqqDLLFIGHQPGIKavltp 91
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEE------NVWDIRHKIGMV----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 92 FENL--QFYQAV-----------RGAAEQQAIWR---ALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:PRK13650 87 FQNPdnQFVGATveddvafglenKGIPHEEMKERvneALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDE 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 491074653 156 PLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDLAGVS 194
Cdd:PRK13650 167 ATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA 205
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-187 |
8.80e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.31 E-value: 8.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR-----NTlrdRAAYQQDLLFIGHQPGIKAVLTPF 92
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfaST---TAALAAGVAIIYQELHLVPEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 93 ENL---QFYQAVRGAAEQQAIWRALEQVGLVGYE---DLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVA 166
Cdd:PRK11288 98 ENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDidpDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIE 177
|
170 180
....*....|....*....|.
gi 491074653 167 ELISLFEQHAQRGGMVLLTTH 187
Cdd:PRK11288 178 QLFRVIRELRAEGRVILYVSH 198
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
21-188 |
9.23e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 60.09 E-value: 9.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRD---RAA-------YQQDLLFighqpgikAV 88
Cdd:COG1135 25 SLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltALSErelRAArrkigmiFQHFNLL--------SS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 89 LTPFENLQF--YQAVRGAAEQQAiwRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAPLwIL--DEPLTAID 161
Cdd:COG1135 97 RTVAENVALplEIAGVPKAEIRK--RVaelLELVGLSDKADAYPSQLSGGQKQRVGIARA-LANNPK-VLlcDEATSALD 172
|
170 180
....*....|....*....|....*...
gi 491074653 162 KQGVAELISLFEQ-HAQRGGMVLLTTHQ 188
Cdd:COG1135 173 PETTRSILDLLKDiNRELGLTIVLITHE 200
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-189 |
1.13e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.26 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 15 ILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCwrgRNTLRDRAAYQQDllfigHQPGIKAVLTPFen 94
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---RSAKVRMAVFSQH-----HVDGLDLSSNPL-- 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 95 LQFYQAVRGAAEQQAiwRA-LEQVGLVGYEDL-PVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELIS-- 170
Cdd:PLN03073 593 LYMMRCFPGVPEQKL--RAhLGSFGVTGNLALqPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQgl 670
|
170 180
....*....|....*....|
gi 491074653 171 -LFEqhaqrgGMVLLTTHQD 189
Cdd:PLN03073 671 vLFQ------GGVLMVSHDE 684
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
11-161 |
1.20e-10 |
|
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: 58.64 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRDRAAYQQDLLFIGHQP------ 83
Cdd:cd03248 24 RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPiSQYEHKYLHSKVSLVGQEPvlfars 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 84 -------GIKAVltPFENLQFYQAVRGAAE-----QQAIWRALEQVGlvgyedlpvAQLSAGQQRRVALARLWLSAAPLW 151
Cdd:cd03248 104 lqdniayGLQSC--SFECVKEAAQKAHAHSfiselASGYDTEVGEKG---------SQLSGGQKQRVAIARALIRNPQVL 172
|
170
....*....|
gi 491074653 152 ILDEPLTAID 161
Cdd:cd03248 173 ILDEATSALD 182
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-188 |
1.57e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 4 AKSLSCVRderiLFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRDRAAYQ-------Q 74
Cdd:PRK09700 12 GKSFGPVH----ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInyNKLDHKLAAQlgigiiyQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 75 DL-----------LFIGHQPgIKAVLTPfeNLQFYQAVRGAAEQqaiwrALEQVGLVGYEDLPVAQLSAGQQRRVALARL 143
Cdd:PRK09700 88 ELsvideltvlenLYIGRHL-TKKVCGV--NIIDWREMRVRAAM-----MLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491074653 144 WLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK 204
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
13-202 |
1.59e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 58.91 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAayqqDLLFIGHQPGIkaVL--- 89
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKV----KLSDIRKKVGL--VFqyp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 90 -------TPFENLQFYQAVRGAAEQQA---IWRALEQVGLV--GYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:PRK13637 93 eyqlfeeTIEKDIAFGPINLGLSEEEIenrVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491074653 158 TAIDKQGVAELISLFEQ-HAQRGGMVLLTTH--QDLAGVSQTV-----GKIRL 202
Cdd:PRK13637 173 AGLDPKGRDEILNKIKElHKEYNMTIILVSHsmEDVAKLADRIivmnkGKCEL 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-197 |
1.65e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 3 EAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEV-CwrgrNTLRDRAAYQQdllfigh 81
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhC----GTKLEVAYFDQ------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 82 qpgIKAVLTP----FENLqfyqavrgAAEQQAIWRALEQVGLVGY-EDL---------PVAQLSAGQQRRVALARLWLSA 147
Cdd:PRK11147 390 ---HRAELDPektvMDNL--------AEGKQEVMVNGRPRHVLGYlQDFlfhpkramtPVKALSGGERNRLLLARLFLKP 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491074653 148 APLWILDEPLTAIDKQGVAELISLFEQHAqrgGMVLLTTHqDLAGVSQTV 197
Cdd:PRK11147 459 SNLLILDEPTNDLDVETLELLEELLDSYQ---GTVLLVSH-DRQFVDNTV 504
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-205 |
1.75e-10 |
|
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: 59.45 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLaRPDG---GEVCWRGR----NTLRDRAA-----YQQDL----------- 76
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSplkaSNIRDTERagiviIHQELtlvpelsvaen 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 77 LFIGHQPGIKAVLTPfenlqfYQAVRGAAEQqaiwrALEQVGLVGYED-LPVAQLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:TIGR02633 99 IFLGNEITLPGGRMA------YNAMYLRAKN-----LLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491074653 156 PLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ--DLAGVSQTVGKIRLAEH 205
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKAHGVACVYISHKlnEVKAVCDTICVIRDGQH 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-184 |
1.91e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 17 FSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN----TLRDRAAY---------QQDLLFIGHQP 83
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEinalSTAQRLARglvylpedrQSSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 84 GIKAVLTPFENLQFYQavRGAAEQQAIWRALEQVGL-VGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAID 161
Cdd:PRK15439 359 AWNVCALTHNRRGFWI--KPARENAVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKC-LEASPqLLIVDEPTRGVD 435
|
170 180
....*....|....*....|...
gi 491074653 162 KQGVAELISLFEQHAQRGGMVLL 184
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLF 458
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-195 |
3.17e-10 |
|
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: 58.93 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKT----SLLRILAGLARPDGGEVCWRGRNTLR-DRAAYQ-----------QD-------L 76
Cdd:COG4172 29 VSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGlSERELRrirgnriamifQEpmtslnpL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 77 LFIGHQPGikavltpfENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVA---QLSAGQQRRV--ALArlwLSAAP-L 150
Cdd:COG4172 109 HTIGKQIA--------EVLRLHRGLSGAAARARALELLERVGIPDPERRLDAyphQLSGGQRQRVmiAMA---LANEPdL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491074653 151 WILDEPLTAIDkqgV---AELISLFEQHAQRGGM-VLLTTHqDLAGVSQ 195
Cdd:COG4172 178 LIADEPTTALD---VtvqAQILDLLKDLQRELGMaLLLITH-DLGVVRR 222
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
11-188 |
3.69e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 58.58 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRnTLRD----------RAAYQQDLLFIG 80
Cdd:TIGR00958 491 RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV-PLVQydhhylhrqvALVGQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 81 H-QPGIKAVLTPFENLQFYQAVRGAAEQQAIwRALEQ-----VGLVGyedlpvAQLSAGQQRRVALARLWLSAAPLWILD 154
Cdd:TIGR00958 570 SvRENIAYGLTDTPDEEIMAAAKAANAHDFI-MEFPNgydteVGEKG------SQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190
....*....|....*....|....*....|....*
gi 491074653 155 EPLTAIDkqgvAELISLFEQHAQRGGM-VLLTTHQ 188
Cdd:TIGR00958 643 EATSALD----AECEQLLQESRSRASRtVLLIAHR 673
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-161 |
4.43e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILfSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGlARPDGgevcwrgrntlrdraaYQQDLLFIGHQPG------- 84
Cdd:PRK10938 272 DRPIL-HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQG----------------YSNDLTLFGRRRGsgetiwd 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 85 IK------------------AVLTP-----FENLQFYQAVRGAAEQQAI-WraLEQVGLVGY-EDLPVAQLSAGQQRRVA 139
Cdd:PRK10938 334 IKkhigyvssslhldyrvstSVRNVilsgfFDSIGIYQAVSDRQQKLAQqW--LDILGIDKRtADAPFHSLSWGQQRLAL 411
|
170 180
....*....|....*....|..
gi 491074653 140 LARLWLSAAPLWILDEPLTAID 161
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-190 |
5.63e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.49 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRDRAAYQQDLLFIGHQPGIKavLTPFEN--- 94
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlHFGDYSYRSQRIRMIFQDPSTS--LNPRQRisq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 95 -----LQFYQAVRGAAEQQAIWRALEQVGL----VGYedLPVAqLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGV 165
Cdd:PRK15112 109 ildfpLRLNTDLEPEQREKQIIETLRQVGLlpdhASY--YPHM-LAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180
....*....|....*....|....*
gi 491074653 166 AELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHL 210
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-174 |
6.51e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 6.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 3 EAKSLSCVRDERILFS------ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRDRAAYQQ 74
Cdd:PRK15439 7 TAPPLLCARSISKQYSgvevlkGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPcaRLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 75 DLLFIGHQPGIKAVLTPFENLQFYQAvRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILD 154
Cdd:PRK15439 87 GIYLVPQEPLLFPNLSVKENILFGLP-KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180
....*....|....*....|
gi 491074653 155 EPLTAIDKqgvAELISLFEQ 174
Cdd:PRK15439 166 EPTASLTP---AETERLFSR 182
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
18-188 |
6.58e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 57.50 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRD---RAAYQQ--------DLLfighqpg 84
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltALSEkelRKARRQigmifqhfNLL------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 85 ikAVLTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDL----PvAQLSAGQQRRVALARLwLSAAPLWIL-DEPLTA 159
Cdd:PRK11153 95 --SSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKadryP-AQLSGGQKQRVAIARA-LASNPKVLLcDEATSA 170
|
170 180 190
....*....|....*....|....*....|
gi 491074653 160 IDKQGVAELISLFEQHAQRGGM-VLLTTHQ 188
Cdd:PRK11153 171 LDPATTRSILELLKDINRELGLtIVLITHE 200
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-169 |
1.14e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.12 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWR----------GRNTLRDRAAYQQDLLFigHQPGIKAVL 89
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkPGPDGRGRAKRYIGILH--QEYDLYPHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 90 TPFENLQfyQAVR-GAAEQQAIWRALEQVGLVGYED---------LPvAQLSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:TIGR03269 381 TVLDNLT--EAIGlELPDELARMKAVITLKMVGFDEekaeeildkYP-DELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170
....*....|...
gi 491074653 160 ID---KQGVAELI 169
Cdd:TIGR03269 458 MDpitKVDVTHSI 470
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-187 |
1.90e-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: 56.88 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAY------QQDLLFiGHQpg 84
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWiqndslRENILF-GKA-- 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 85 ikavLTPfenlQFYQAVRGAAeqqAIWRALE--------QVGLVGyedlpvAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:TIGR00957 725 ----LNE----KYYQQVLEAC---ALLPDLEilpsgdrtEIGEKG------VNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190
....*....|....*....|....*....|....*.
gi 491074653 157 LTAIDKQgVAELIslFEQHAQRGGMV-----LLTTH 187
Cdd:TIGR00957 788 LSAVDAH-VGKHI--FEHVIGPEGVLknktrILVTH 820
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-190 |
1.91e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 55.87 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRG-RNTLRDRAAYQQDLLFIGHQPGIKAVLTPFEN-LQF 97
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGeLLTAENVWNLRRKIGMVFQNPDNQFVGATVEDdVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 98 YQAVRGAAEQQAIWR---ALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQ 174
Cdd:PRK13642 106 GMENQGIPREEMIKRvdeALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHE 185
|
170
....*....|....*.
gi 491074653 175 HAQRGGMVLLTTHQDL 190
Cdd:PRK13642 186 IKEKYQLTVLSITHDL 201
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-188 |
2.07e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.01 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDER-----ILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcWRGRNTLRDRAAYQQD 75
Cdd:PRK13631 21 ILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI-QVGDIYIGDKKNNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 76 LLFiGHQPGIKAvltpFENL--------QF--YQAVR--------------GAAEQQAIWRA---LEQVGLvGYEDLPVA 128
Cdd:PRK13631 100 ITN-PYSKKIKN----FKELrrrvsmvfQFpeYQLFKdtiekdimfgpvalGVKKSEAKKLAkfyLNKMGL-DDSYLERS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491074653 129 --QLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:PRK13631 174 pfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-188 |
2.58e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 17 FSELSFSVQPGDIIQVEGPNGAGKTSLLRILAG-LARPDGGEVCWRGRntlrdrAAYQQDLLFIGHQPGIKAVL--TPFE 93
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS------VAYVPQVSWIFNATVRENILfgSDFE 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 94 NLQFYQAVRGAAEQQAI----WRALEQVGLVGyedlpvAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELI 169
Cdd:PLN03232 707 SERYWRAIDVTALQHDLdllpGRDLTEIGERG------VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
170
....*....|....*....
gi 491074653 170 SLFEQHAQRGGMVLLTTHQ 188
Cdd:PLN03232 781 DSCMKDELKGKTRVLVTNQ 799
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
12-188 |
2.78e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGlaRPDGGEVCW-------RGRN-TLRDRAAY--QQDLlfigH 81
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGgdrlvngRPLDsSFQRSIGYvqQQDL----H 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 82 QPgikaVLTPFENLQFYQAVRGAAE---------QQAIWRALEQ-------VGLVGyedlpvAQLSAGQQRRVALArLWL 145
Cdd:TIGR00956 848 LP----TSTVRESLRFSAYLRQPKSvsksekmeyVEEVIKLLEMesyadavVGVPG------EGLNVEQRKRLTIG-VEL 916
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491074653 146 SAAP--LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:TIGR00956 917 VAKPklLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-185 |
3.36e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 55.91 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 15 ILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLarpdggevcWRGRNTLRDRAAyQQDLLFIGHQPGI------KAV 88
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL---------WPVYGGRLTKPA-KGKLFYVPQRPYMtlgtlrDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 89 LTPFENLQFYQavRGAAEQQAIwRALEQVGL-------VGYE------DLpvaqLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:TIGR00954 536 IYPDSSEDMKR--RGLSDKDLE-QILDNVQLthilereGGWSavqdwmDV----LSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|..
gi 491074653 156 PLTAI--DKQGvaeliSLFeQHAQRGGMVLLT 185
Cdd:TIGR00954 609 CTSAVsvDVEG-----YMY-RLCREFGITLFS 634
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-179 |
3.52e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSC---VRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGlARPdG---GEVCWRGR----NTLRDRA 70
Cdd:PRK13549 259 ILEVRNLTAwdpVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYP-GrweGEIFIDGKpvkiRNPQQAI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 71 AYQqdllfIGHQP------GIKAVLTPFENL------QFYQAVR--GAAEQQAIWRALEQVGL-VGYEDLPVAQLSAGQQ 135
Cdd:PRK13549 337 AQG-----IAMVPedrkrdGIVPVMGVGKNItlaaldRFTGGSRidDAAELKTILESIQRLKVkTASPELAIARLSGGNQ 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491074653 136 RRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRG 179
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQG 455
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-161 |
4.06e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.90 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLR-ILAGLARPDGGEVcwrgrnTLRDRAAYQQDLLFIGHQPGIKAVL-- 89
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASV------VIRGTVAYVPQVSWIFNATVRDNILfg 702
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491074653 90 TPFENLQFYQAVRGAAEQQAI----WRALEQVGLVGyedlpvAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PLN03130 703 SPFDPERYERAIDVTALQHDLdllpGGDLTEIGERG------VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-191 |
4.20e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.93 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRDRAAY---QQDL 76
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgQLRDLYALseaERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 77 LF-----IGHQ-------PGIKAVLTPFENL-----QFYQAVRGAAEQqaiWraLEQV--GLVGYEDLPvAQLSAGQQRR 137
Cdd:PRK11701 86 LLrtewgFVHQhprdglrMQVSAGGNIGERLmavgaRHYGDIRATAGD---W--LERVeiDAARIDDLP-TTFSGGMQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491074653 138 VALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGM-VLLTTHqDLA 191
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLaVVIVTH-DLA 213
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-161 |
4.46e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 54.70 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLR-DRAAYQQDLLFI 79
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 80 GHQPGIKAVLTPFENLQF--YQAVRG---AAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILD 154
Cdd:COG4604 81 RQENHINSRLTVRELVAFgrFPYSKGrltAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
....*..
gi 491074653 155 EPLTAID 161
Cdd:COG4604 161 EPLNNLD 167
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
12-163 |
5.05e-09 |
|
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: 54.41 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRG-------RNTLRDRAAY--QQDLLFIGHQ 82
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladPAWLRRQVGVvlQENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 83 PGIKAVLTPFENLQFYQAVRGAAEQQAIWRALEQvglvGYEDLPVAQ---LSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:cd03252 93 RDNIALADPGMSMERVIEAAKLAGAHDFISELPE----GYDTIVGEQgagLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
....
gi 491074653 160 IDKQ 163
Cdd:cd03252 169 LDYE 172
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-193 |
7.34e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 54.33 E-value: 7.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLR----DRAAYQQDLLFIGHQPgiKAVLTP----- 91
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmkddEWRAVRSDIQMIFQDP--LASLNPrmtig 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 92 ---FENLQFYQAVRGAAEQQAIWRA-LEQVGLvgyedLPVA------QLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PRK15079 119 eiiAEPLRTYHPKLSRQEVKDRVKAmMLKVGL-----LPNLinryphEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190
....*....|....*....|....*....|..
gi 491074653 162 KQGVAELISLFEQHAQRGGMVLLTTHQDLAGV 193
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVV 225
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-161 |
7.42e-09 |
|
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: 53.77 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDraaYQQDLL--FIGHQPGiKAVL 89
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD-IRE---VTLDSLrrAIGVVPQ-DTVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 90 ---TPFENLQF------YQAVRGAAEQQAIWRALEQV-----GLVGYEDLpvaQLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:cd03253 87 fndTIGYNIRYgrpdatDEEVIEAAKAAQIHDKIMRFpdgydTIVGERGL---KLSGGEKQRVAIARAILKNPPILLLDE 163
|
....*.
gi 491074653 156 PLTAID 161
Cdd:cd03253 164 ATSALD 169
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-161 |
9.38e-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: 54.53 E-value: 9.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDG----GEVCWRGRNTLRDRAAY----QQDLLFIGhqp 83
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGeiqiDGVSWNSVTLQTWRKAFgvipQKVFIFSG--- 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 84 GIKAVLTPFENLQfyqavrgaaeQQAIWRALEQVGLVGY-EDLPVAQ----------LSAGQQRRVALARLWLSAAPLWI 152
Cdd:TIGR01271 1307 TFRKNLDPYEQWS----------DEEIWKVAEEVGLKSViEQFPDKLdfvlvdggyvLSNGHKQLMCLARSILSKAKILL 1376
|
....*....
gi 491074653 153 LDEPLTAID 161
Cdd:TIGR01271 1377 LDEPSAHLD 1385
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-161 |
9.58e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.58 E-value: 9.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRIL-------AGLARPDGGEVCWRGRNTLRDRAA--YQQDLLF---IGhqpgika 87
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILIDGTDIRTVTRASLRRNIAvvFQDAGLFnrsIE------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 88 vltpfENLQ----------FYQAVRGAAEQQAIWRALE----QVGLVGyedlpvAQLSAGQQRRVALARLWLSAAPLWIL 153
Cdd:PRK13657 427 -----DNIRvgrpdatdeeMRAAAERAQAHDFIERKPDgydtVVGERG------RQLSGGERQRLAIARALLKDPPILIL 495
|
....*...
gi 491074653 154 DEPLTAID 161
Cdd:PRK13657 496 DEATSALD 503
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
13-187 |
1.09e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.55 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT--------LRDRAAyqqdLLFigHQPG 84
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsdeenlwdIRNKAG----MVF--QNPD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 85 IKAVLTPFE-NLQFYQAVRGAAEQQAIWR---ALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAI 160
Cdd:PRK13633 96 NQIVATIVEeDVAFGPENLGIPPEEIRERvdeSLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180
....*....|....*....|....*...
gi 491074653 161 DKQGVAELISLFEQHAQRGGM-VLLTTH 187
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGItIILITH 203
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-175 |
1.69e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 53.57 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR-------NTLRDRAAY-QQDllfighq 82
Cdd:PRK10790 351 RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsslshSVLRQGVAMvQQD------- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 83 PGIKAVlTPFENLQFYqavRGAAEQQaIWRALEQVGLVGY-EDLPVA----------QLSAGQQRRVALARLWLSAAPLW 151
Cdd:PRK10790 424 PVVLAD-TFLANVTLG---RDISEEQ-VWQALETVQLAELaRSLPDGlytplgeqgnNLSVGQKQLLALARVLVQTPQIL 498
|
170 180
....*....|....*....|....*..
gi 491074653 152 ILDEPLTAID---KQGVAELISLFEQH 175
Cdd:PRK10790 499 ILDEATANIDsgtEQAIQQALAAVREH 525
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-200 |
2.54e-08 |
|
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: 51.88 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDG---GEVCWRGRNTLRDRAAYQQDLLFIG----HQP 83
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGEIIYVSeedvHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 84 gikaVLTPFENLQF------YQAVRGaaeqqaiwraleqvglvgyedlpvaqLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:cd03233 97 ----TLTVRETLDFalrckgNEFVRG--------------------------ISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491074653 158 TAIDKQGVAELISLFEQHAQRGGMVLltthqdLAGVSQTVGKI 200
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADVLKTTT------FVSLYQASDEI 183
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-161 |
2.64e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.95 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 34 GPNGAGKTSLLRILAGLARPDGGEVCWRGRnTLRDRaayQQDLLFIGHQPGIKAV-----LTPF----ENLQFYQAVRGA 104
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGR-VLFDA---EKGICLPPEKRRIGYVfqdarLFPHykvrGNLRYGMAKSMV 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491074653 105 AEQQAIwraleqVGLVGYEDL----PvAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PRK11144 107 AQFDKI------VALLGIEPLldryP-GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-161 |
2.76e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 22 FSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRG------------RN---TLRDRAA----YQQDLLFIGHQ 82
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdppRNvegTVYDFVAegieEQAEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 83 PGIKAVLTPFE-NLQFYQAVRGAAEQQAIWR-------ALEQVGLVGyeDLPVAQLSAGQQRRVALARLWLSAAPLWILD 154
Cdd:PRK11147 104 ISHLVETDPSEkNLNELAKLQEQLDHHNLWQlenrineVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLD 181
|
....*..
gi 491074653 155 EPLTAID 161
Cdd:PRK11147 182 EPTNHLD 188
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-190 |
2.91e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.30 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcWRGRNTLRDRAAYQqdllfIGH 81
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHYASKE-----VAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 82 QPGIKA--VLTPFENLQFYQAVRGAAEQQ------------AIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSA 147
Cdd:PRK10253 82 RIGLLAqnATTPGDITVQELVARGRYPHQplftrwrkedeeAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491074653 148 APLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDL 204
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-202 |
4.45e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 51.91 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLS-CVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLrDRAAYQQDLLFI 79
Cdd:PRK13644 1 MIRLENVSySYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG-DFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 80 G---HQPGIKAV-LTPFENLQF---YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWI 152
Cdd:PRK13644 80 GivfQNPETQFVgRTVEEDLAFgpeNLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491074653 153 LDEPLTAID-KQGVAELISLFEQHaQRGGMVLLTTH--QDLAGVSQTV----GKIRL 202
Cdd:PRK13644 160 FDEVTSMLDpDSGIAVLERIKKLH-EKGKTIVYITHnlEELHDADRIIvmdrGKIVL 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-190 |
5.42e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.01 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTS----LLRILAGlarpdGGEVCWRGR--NTLRDRAayqqdLLFIGHQpgI 85
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQplHNLNRRQ-----LLPVRHR--I 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 86 KAV-------LTP--------FENLQFYQAVRGAAEQ-QAIWRALEQVGL--VGYEDLPvAQLSAGQQRRVALARLWLSA 147
Cdd:PRK15134 365 QVVfqdpnssLNPrlnvlqiiEEGLRVHQPTLSAAQReQQVIAVMEEVGLdpETRHRYP-AEFSGGQRQRIAIARALILK 443
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491074653 148 APLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDL 486
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-187 |
6.22e-08 |
|
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: 50.99 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLS-CVRDERILfSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLA--RPDGGEVCWRGRNTL------RDRAAy 72
Cdd:cd03217 1 LEIKDLHvSVGGKEIL-KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITdlppeeRARLG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 73 qqdlLFIGHQ-----PGIKavltpfeNLQFYQAVrgaaeqqaiwraleQVGlvgyedlpvaqLSAGQQRRVALARLWLSA 147
Cdd:cd03217 79 ----IFLAFQyppeiPGVK-------NADFLRYV--------------NEG-----------FSGGEKKRNEILQLLLLE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491074653 148 APLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-161 |
6.76e-08 |
|
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: 51.40 E-value: 6.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQdllfighqPGikavlTPFENLQF- 97
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIM--------PG-----TIKENIIFg 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491074653 98 -------YQAVRGAAE-QQAIWRALEQvglvgyEDLPVAQ----LSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:cd03291 122 vsydeyrYKSVVKACQlEEDITKFPEK------DNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-161 |
7.40e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 51.57 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRD-----RAAYQQDLLFIGHQPGIKAVLTPFENL 95
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaelREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491074653 96 QFYQAVRGAA---EQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PRK10070 128 AFGMELAGINaeeRREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-191 |
8.65e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.83 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 23 SVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVC----WRG-----RNT-LRDraaYQQDLLfighQPGIKAVLTPF 92
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdWDEildefRGSeLQN---YFTKLL----EGDVKVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 93 ENLQFYQAVRGAA--------EQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID-KQ 163
Cdd:cd03236 95 YVDLIPKAVKGKVgellkkkdERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDiKQ 174
|
170 180 190
....*....|....*....|....*....|
gi 491074653 164 --GVAELIslfEQHAQRGGMVLLTTHqDLA 191
Cdd:cd03236 175 rlNAARLI---RELAEDDNYVLVVEH-DLA 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-191 |
1.28e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 24 VQPGDIIQVEGPNGAGKTSLLRILAGLARPD----GGEVCW-------RGrNTLRDraaYQQDLlfigHQPGIKAVLTPF 92
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNlgdyEEEPSWdevlkrfRG-TELQN---YFKKL----YNGEIKVVHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 93 ENLQFYQAVRG-------AAEQQAIWRAL-EQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID-KQ 163
Cdd:PRK13409 168 YVDLIPKVFKGkvrellkKVDERGKLDEVvERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDiRQ 247
|
170 180 190
....*....|....*....|....*....|
gi 491074653 164 --GVAELIslfeQHAQRGGMVLLTTHqDLA 191
Cdd:PRK13409 248 rlNVARLI----RELAEGKYVLVVEH-DLA 272
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
17-156 |
1.30e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.94 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 17 FSELSFSVQPGDI-----IQVEGPNGAGKTSLLRILAGLARPDGGEVcwrgrnTLRDRAAYQ------------QDLLFi 79
Cdd:COG1245 351 YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV------DEDLKISYKpqyispdydgtvEEFLR- 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491074653 80 ghqpgiKAVLTPFENLQFYQAVrgaAEQQAIWRALEQvglvgyedlPVAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:COG1245 424 ------SANTDDFGSSYYKTEI---IKPLGLEKLLDK---------NVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-174 |
1.80e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT--------LRDRAAY-----QQDLLFIGHQPGIKA 87
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtrspqdgLANGIVYisedrKRDGLVLGMSVKENM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 88 VLTPFENL-QFYQAVRGAAEQQAIWRALEQVGL-VGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID---K 162
Cdd:PRK10762 352 SLTALRYFsRAGGSLKHADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDvgaK 431
|
170
....*....|..
gi 491074653 163 QGVAELISLFEQ 174
Cdd:PRK10762 432 KEIYQLINQFKA 443
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-193 |
2.11e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRDRA--AYQQDLLFIGHQPgiKAVLTP---- 91
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQriDTLSPGKlqALRRDIQFIFQDP--YASLDPrqtv 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 92 ----FENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVA-QLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVA 166
Cdd:PRK10261 421 gdsiMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPhEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
|
170 180
....*....|....*....|....*..
gi 491074653 167 ELISLFEQHAQRGGMVLLTTHQDLAGV 193
Cdd:PRK10261 501 QIINLLLDLQRDFGIAYLFISHDMAVV 527
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-161 |
2.38e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.77 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRIL--AGLARPD---GGEVCWRGRNTLRDRAAYQQD 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 76 LLFIG---HQPGiKAVLTPFENLQFYQAVRGAAEQQAIWRALEQvGLVG----------YEDLPVAqLSAGQQRRVALAR 142
Cdd:PRK14239 85 RKEIGmvfQQPN-PFPMSIYENVVYGLRLKGIKDKQVLDEAVEK-SLKGasiwdevkdrLHDSALG-LSGGQQQRVCIAR 161
|
170
....*....|....*....
gi 491074653 143 LWLSAAPLWILDEPLTAID 161
Cdd:PRK14239 162 VLATSPKIILLDEPTSALD 180
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
11-163 |
2.67e-07 |
|
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: 49.46 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT-------LRDRAAY--QQDLLFIGh 81
Cdd:cd03249 13 RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrdlnlrwLRSQIGLvsQEPVLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 82 qpgikavlTPFENLQFYQAVRGAAEQQAIWRALE--------------QVGLVGyedlpvAQLSAGQQRRVALARLWLSA 147
Cdd:cd03249 92 --------TIAENIRYGKPDATDEEVEEAAKKANihdfimslpdgydtLVGERG------SQLSGGQKQRIAIARALLRN 157
|
170
....*....|....*.
gi 491074653 148 APLWILDEPLTAIDKQ 163
Cdd:cd03249 158 PKILLLDEATSALDAE 173
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-183 |
2.73e-07 |
|
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: 48.72 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 24 VQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWrgrntlrdraayqqdllfighqPGIKAVLTPfenlqfyqavrg 103
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW----------------------DGITPVYKP------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 104 aaeqQAIwraleqvglvgyedlpvaQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQ---GVAELISLFEQHAQRGG 180
Cdd:cd03222 68 ----QYI------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlNAARAIRRLSEEGKKTA 125
|
...
gi 491074653 181 MVL 183
Cdd:cd03222 126 LVV 128
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-190 |
3.28e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.26 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSL-SCVRDERILfSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGlaRPD----GGEVCWRGRNTL----RDRA- 70
Cdd:CHL00131 7 ILEIKNLhASVNENEIL-KGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILdlepEERAh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 71 -----AYQ----------QDLLFIGHQPGIKAV-LTPFENLQFYQAVRgaaeqqaiwralEQVGLVGYEDLPVAQ----- 129
Cdd:CHL00131 84 lgiflAFQypieipgvsnADFLRLAYNSKRKFQgLPELDPLEFLEIIN------------EKLKLVGMDPSFLSRnvneg 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491074653 130 LSAGQQRRVALARLWLSAAPLWILDEPLTAID---KQGVAELISLFEQHAQrgGMVLLTTHQDL 190
Cdd:CHL00131 152 FSGGEKKRNEILQMALLDSELAILDETDSGLDidaLKIIAEGINKLMTSEN--SIILITHYQRL 213
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-161 |
3.73e-07 |
|
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: 49.91 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGrntlrdRAAYQQDLLFIghQPGikavlTPFENLQF- 97
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------RISFSPQTSWI--MPG-----TIKDNIIFg 510
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491074653 98 -------YQAVRGAAEQQaiwralEQVGLVGYEDLPV-----AQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:TIGR01271 511 lsydeyrYTSVIKACQLE------EDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-190 |
4.28e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.02 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 14 RILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVC--------WRGRNTLRDRAAYQQ----------- 74
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILldaqplesWSSKAFARKVAYLPQqlpaaegmtvr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 75 DLLFIGHQPGIKAvLTPFenlqfyqavrGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILD 154
Cdd:PRK10575 104 ELVAIGRYPWHGA-LGRF----------GAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 491074653 155 EPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDI 208
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-161 |
4.48e-07 |
|
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: 49.56 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 9 CVR---DERILFSELSFSVQPGDIIQVEGPNGAGKTS----LLRIL---AGLARPDGGEVCWRGRNTLRDRAAY--QQDL 76
Cdd:TIGR00957 1291 CLRyreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINesaEGEIIIDGLNIAKIGLHDLRFKITIipQDPV 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 77 LFIGhqpGIKAVLTPFenlqfyqavrGAAEQQAIWRALEQVGLVGY-EDLPVA----------QLSAGQQRRVALARLWL 145
Cdd:TIGR00957 1371 LFSG---SLRMNLDPF----------SQYSDEEVWWALELAHLKTFvSALPDKldhecaeggeNLSVGQRQLVCLARALL 1437
|
170
....*....|....*.
gi 491074653 146 SAAPLWILDEPLTAID 161
Cdd:TIGR00957 1438 RKTKILVLDEATAAVD 1453
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-195 |
4.54e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.32 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 13 ERILFSELSFSVQPGDIIQVEGPNGAGKT----SLLRIL--------AGLARPDGGEVCWRGRNTLRDRAAYQQDLLFig 80
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypSGDIRFHGESLLHASEQTLRGVRGNKIAMIF-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 81 HQPGIKavLTPFENL--QFYQ------AVRGAAEQQAIWRALEQVGLVG----YEDLPvAQLSAGQQRRVALARLWLSAA 148
Cdd:PRK15134 99 QEPMVS--LNPLHTLekQLYEvlslhrGMRREAARGEILNCLDRVGIRQaakrLTDYP-HQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491074653 149 PLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDLAGVSQ 195
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRK 222
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
20-161 |
4.73e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.07 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTL--RDRaayqqdllfighqpGIKAV------- 88
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvNELepADR--------------DIAMVfqnyaly 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491074653 89 --LTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDL----PvAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PRK11650 89 phMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLldrkP-RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
11-155 |
5.95e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.20 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 11 RDERILFSELSFSVQP-------GDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRDRAAYQQdlLFighq 82
Cdd:PRK10522 326 RNVTFAYQDNGFSVGPinltikrGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPvTAEQPEDYRK--LF---- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 83 pgiKAVLT---PFENLQFYQAVRGAAEQQAIWraLEQVGL---VGYEDLPVA--QLSAGQQRRVALARLWLSAAPLWILD 154
Cdd:PRK10522 400 ---SAVFTdfhLFDQLLGPEGKPANPALVEKW--LERLKMahkLELEDGRISnlKLSKGQKKRLALLLALAEERDILLLD 474
|
.
gi 491074653 155 E 155
Cdd:PRK10522 475 E 475
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
20-187 |
6.09e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLlRILAGLARPDGGEVCWRGRNTLRDRAAYQQDllfIG-HQP---GIKAVLTPFENL 95
Cdd:NF000106 32 VDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRT---IG*HRPvr*GRRESFSGRENL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 96 QFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLF 172
Cdd:NF000106 108 YMIGR*LDLSRKDARARAdelLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV 187
|
170
....*....|....*
gi 491074653 173 EQHAQRGGMVLLTTH 187
Cdd:NF000106 188 RSMVRDGATVLLTTQ 202
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
34-161 |
6.63e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 48.87 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 34 GPNGAGKTSLLRILAGLARPDGGEvcwrgrntlrdraayqqdlLFIGHQ------P---GIKAV---------LTPFENL 95
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEDITSGD-------------------LFIGEKrmndvpPaerGVGMVfqsyalyphLSVAENM 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491074653 96 QFYQAVRGAAEQQaIWRALEQVGlvgyEDLPVAQL--------SAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PRK11000 97 SFGLKLAGAKKEE-INQRVNQVA----EVLQLAHLldrkpkalSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-184 |
7.37e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 48.34 E-value: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAA--YQQDLLF 78
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 79 IGHQPGIKAVLTPFENLqfyqAVRG-AAEQQAIWRALEQVglvgYEDLP---------VAQLSAGQQRRVALARLWLSAA 148
Cdd:PRK11614 85 VPEGRRVFSRMTVEENL----AMGGfFAERDQFQERIKWV----YELFPrlherriqrAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 491074653 149 PLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLL 184
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFL 192
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
15-188 |
9.11e-07 |
|
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: 46.97 E-value: 9.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 15 ILFSELSFSVqpgdiiqVEGPNGAGKTSLLRilaglarpdggEVCWrgrntlrdraayqqdlLFIGHQPgikavltpfen 94
Cdd:cd03227 16 VTFGEGSLTI-------ITGPNGSGKSTILD-----------AIGL----------------ALGGAQS----------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 95 lqfyQAVRGAAEQQAIWRALEQVGLVgyedLPVAQLSAGQQRRVALA---RLWLSA-APLWILDEPLTAIDKQGVAELIS 170
Cdd:cd03227 51 ----ATRRRSGVKAGCIVAAVSAELI----FTRLQLSGGEKELSALAlilALASLKpRPLYILDEIDRGLDPRDGQALAE 122
|
170
....*....|....*...
gi 491074653 171 LFEQHAQRGGMVLLTTHQ 188
Cdd:cd03227 123 AILEHLVKGAQVIVITHL 140
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-187 |
1.30e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.70 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCW------RGRNTLRDRAAYQQDLLFIGHQPGIKAVLTPFE- 93
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKKIKEVKRLRKEIGLVFQFPEYQLFQETIEk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 94 NLQFYQAVRGAAEQQAIWRALEQVGLVG----YEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELI 169
Cdd:PRK13645 111 DIAFGPVNLGENKQEAYKKVPELLKLVQlpedYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFI 190
|
170
....*....|....*....
gi 491074653 170 SLFEQ-HAQRGGMVLLTTH 187
Cdd:PRK13645 191 NLFERlNKEYKKRIIMVTH 209
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-179 |
1.38e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVLTPFEN------ 94
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNNTDMLSPGEDdtgrtt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 95 ---LQFYQAVRGAAEQQAiwralEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISL 171
Cdd:PRK10938 103 aeiIQDEVKDPARCEQLA-----QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAEL 177
|
....*...
gi 491074653 172 FEQHAQRG 179
Cdd:PRK10938 178 LASLHQSG 185
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
17-156 |
2.74e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 17 FSELSFSVQPGDI-----IQVEGPNGAGKTSLLRILAGLARPDGGEVCWrgrnTLrdRAAYQ------------QDLLfi 79
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP----EL--KISYKpqyikpdydgtvEDLL-- 421
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491074653 80 ghqpgiKAVLTPFENLQFYQAVrgaAEQQAIWRALEQvglvgyedlPVAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:PRK13409 422 ------RSITDDLGSSYYKSEI---IKPLQLERLLDK---------NVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-182 |
3.54e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.92 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRDRAAYQQDLLFIGHQP-GIKAVLTPFENL 95
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEvTFNGPKSSQEAGIGIIHQElNLIPQLTIAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 96 ----QFYQAVrGAAEQQAIWRA----LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKqgvAE 167
Cdd:PRK10762 101 flgrEFVNRF-GRIDWKKMYAEadklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTD---TE 176
|
170
....*....|....*....
gi 491074653 168 LISLF----EQHAQRGGMV 182
Cdd:PRK10762 177 TESLFrvirELKSQGRGIV 195
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-172 |
3.64e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 46.50 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLlfighQPGIKAVL-TPFENLQFYQ 99
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLL-----RQKIQIVFqNPYGSLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 100 AVR-------------GAAEQQAiwRALEQVGLVG-----YEDLPvAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PRK11308 110 KVGqileepllintslSAAERRE--KALAMMAKVGlrpehYDRYP-HMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170
....*....|.
gi 491074653 162 KQGVAELISLF 172
Cdd:PRK11308 187 VSVQAQVLNLM 197
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-163 |
3.80e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 46.63 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR-------NTLRDRAAY--QQDLLFIGHQPGIKAV 88
Cdd:PRK10789 332 ENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIpltklqlDSWRSRLAVvsQTPFLFSDTVANNIAL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 89 LTP-FENLQFYQAVRGAAEQQAIWRALE----QVGLVGyedlpvAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQ 163
Cdd:PRK10789 412 GRPdATQQEIEHVARLASVHDDILRLPQgydtEVGERG------VMLSGGQKQRISIARALLLNAEILILDDALSAVDGR 485
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-191 |
4.27e-06 |
|
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: 46.70 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 25 QPGDIIQVEGPNGAGKTSLLRILAGLARPDGG----EVCW-----RGRNT-LRDraaYQQDLLfighQPGIKAVLTPfen 94
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGdydeEPSWdevlkRFRGTeLQD---YFKKLA----NGEIKVAHKP--- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 95 lqfyQAV--------------------RGAAEQQAiwralEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILD 154
Cdd:COG1245 167 ----QYVdlipkvfkgtvrellekvdeRGKLDELA-----EKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491074653 155 EPLTAID-KQ--GVAELISLFeqhAQRGGMVLLTTHqDLA 191
Cdd:COG1245 238 EPSSYLDiYQrlNVARLIREL---AEEGKYVLVVEH-DLA 273
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-168 |
5.24e-06 |
|
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: 45.48 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT-------LRDRAAY--QQDLLFIGhqpGIKAVLT 90
Cdd:cd03369 27 VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIstipledLRSSLTIipQDPTLFSG---TIRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 91 PFE---NLQFYQAVRgaaeqqaiwraLEQVGLvgyedlpvaQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAE 167
Cdd:cd03369 104 PFDeysDEEIYGALR-----------VSEGGL---------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
.
gi 491074653 168 L 168
Cdd:cd03369 164 I 164
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-187 |
7.07e-06 |
|
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: 44.91 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 34 GPNGAGKTSLLR----ILAGLARPDGgevcwRGRNTLRDRAA-----YQQDLLFIgHQPGIKavltpfenlqfYQAVRGA 104
Cdd:cd03240 29 GQNGAGKTTIIEalkyALTGELPPNS-----KGGAHDPKLIRegevrAQVKLAFE-NANGKK-----------YTITRSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 105 AeqqaiwrALEQVGLVGYED------LPVAQLSAGQQR------RVALARLWLSAAPLWILDEPLTAIDKQGVAE-LISL 171
Cdd:cd03240 92 A-------ILENVIFCHQGEsnwpllDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEsLAEI 164
|
170
....*....|....*..
gi 491074653 172 FE-QHAQRGGMVLLTTH 187
Cdd:cd03240 165 IEeRKSQKNFQLIVITH 181
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-193 |
7.35e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.67 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRD-RAAYQQDLLFIGH---QPGIKAVLTPFEN- 94
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPiDIRSpRDAIRAGIMLCPEdrkAEGIIPVHSVADNi 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 95 --------LQFYQAVRGAAEQQaiwRALEQVGLVGYE----DLPVAQLSAGQQRRVALARlWLSAA-PLWILDEPLTAID 161
Cdd:PRK11288 353 nisarrhhLRAGCLINNRWEAE---NADRFIRSLNIKtpsrEQLIMNLSGGNQQKAILGR-WLSEDmKVILLDEPTRGID 428
|
170 180 190
....*....|....*....|....*....|..
gi 491074653 162 KQGVAELISLFEQHAQRGGMVLLTThQDLAGV 193
Cdd:PRK11288 429 VGAKHEIYNVIYELAAQGVAVLFVS-SDLPEV 459
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-200 |
7.86e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.50 E-value: 7.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKT-SLLRILaglarpdgGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAV---------- 88
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIM--------GLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVgaevamifqd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 89 ----LTP-----FENLQFYQAVRGAAEQQAIWRALEQVGLVGYED----LPV--AQLSAGQQRRVALARLWLSAAPLWIL 153
Cdd:PRK11022 98 pmtsLNPcytvgFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpasrLDVypHQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491074653 154 DEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDLAGVSQTVGKI 200
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKI 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
12-187 |
9.55e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 44.98 E-value: 9.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGrNTLRdraayQQDLLFIGHQPGIKavltp 91
Cdd:PRK13632 20 SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG-ITIS-----KENLKEIRKKIGII----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 92 FENL--QFYqavrGAAEQQAIWRALE------------------QVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-L 150
Cdd:PRK13632 89 FQNPdnQFI----GATVEDDIAFGLEnkkvppkkmkdiiddlakKVGMEDYLDKEPQNLSGGQKQRVAIASV-LALNPeI 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 491074653 151 WILDEPLTAIDKQGVAELISLFEQ-HAQRGGMVLLTTH 187
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDlRKTRKKTLISITH 201
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-187 |
1.09e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.27 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLrdraayqqdllfIGHQPGIKAVLTPFENLQF 97
Cdd:PRK13545 41 NNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL------------IAISSGLNGQLTGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 98 YQAVRGAAEQQA---IWRALEQVGLVGYEDLPVAQLSAGQQRRVALArLWLSAAP-LWILDEPLTAIDKQGVAELISLFE 173
Cdd:PRK13545 109 KGLMMGLTKEKIkeiIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFA-ISVHINPdILVIDEALSVGDQTFTKKCLDKMN 187
|
170
....*....|....
gi 491074653 174 QHAQRGGMVLLTTH 187
Cdd:PRK13545 188 EFKEQGKTIFFISH 201
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-187 |
1.10e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.99 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 17 FSELSFSVQPGDIIQVeGPNGAGKTSLLRILAGLARPDGG---------------------EVCWRG--RNTLRDRAAYQ 73
Cdd:COG3593 14 IKDLSIELSDDLTVLV-GENNSGKSSILEALRLLLGPSSSrkfdeedfylgddpdlpeieiELTFGSllSRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 74 QDLLFIGH----QPGIKAVLTPFENL---QFYQAVRGA-------AEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVA 139
Cdd:COG3593 93 DKEELEEAleelNEELKEALKALNELlseYLKELLDGLdlelelsLDELEDLLKSLSLRIEDGKELPLDRLGSGFQRLIL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491074653 140 LA-RLWLSAA------PLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:COG3593 173 LAlLSALAELkrapanPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-188 |
1.23e-05 |
|
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: 44.85 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDG----GEVCWRGRNTLRDRAAY----QQDLLFIGhqpgikavlTP 91
Cdd:cd03289 23 ISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGdiqiDGVSWNSVPLQKWRKAFgvipQKVFIFSG---------TF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 92 FENLQFYqavrGAAEQQAIWRALEQVGLV-------GYEDLPVAQ----LSAGQQRRVALARLWLSAAPLWILDEPLTAI 160
Cdd:cd03289 94 RKNLDPY----GKWSDEEIWKVAEEVGLKsvieqfpGQLDFVLVDggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180
....*....|....*....|....*...
gi 491074653 161 DKQgVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:cd03289 170 DPI-TYQVIRKTLKQAFADCTVILSEHR 196
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-70 |
2.52e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.63 E-value: 2.52e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGlaRPD----GGEVCWRGRNTL----RDRA 70
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG--REDyevtGGTVEFKGKDLLelspEDRA 76
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-186 |
3.82e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.62 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYqqdllfIGHQPGIKAVLTPFENLQFY 98
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKD-ISPRSPL------DAVKKGMAYITESRRDNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 99 QAVrGAAEQQAIWRALEQVGLVGY-----------------EDLP---------VAQLSAGQQRRVALARlWLSAAP-LW 151
Cdd:PRK09700 354 PNF-SIAQNMAISRSLKDGGYKGAmglfhevdeqrtaenqrELLAlkchsvnqnITELSGGNQQKVLISK-WLCCCPeVI 431
|
170 180 190
....*....|....*....|....*....|....*
gi 491074653 152 ILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTT 186
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS 466
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
121-190 |
6.00e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.76 E-value: 6.00e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074653 121 GYEDLPVAQLSAGQQRRVALARLWLSAAP---LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:pfam13304 228 GGGELPAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
9-207 |
6.49e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 42.38 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 9 CVRDERILFSELSFSVQPGDIIQVEGPNGAGKT----SLLRILAGLARPDGGEVCWRGR----NTLRDRAAYQqdllfIG 80
Cdd:PRK10418 11 ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKpvapCALRGRKIAT-----IM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 81 HQPgiKAVLTPFENLQFY-----QAVRGAAEQQAIWRALEQVGLVGYEDLPVA---QLSAGQQRRVALARLWLSAAPLWI 152
Cdd:PRK10418 86 QNP--RSAFNPLHTMHTHaretcLALGKPADDATLTAALEAVGLENAARVLKLypfEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491074653 153 LDEPLTAIDKQGVAELISLFEQ-HAQRGGMVLLTTHqDLAGVSqtvgkiRLAEHDA 207
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESiVQKRALGMLLVTH-DMGVVA------RLADDVA 212
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-159 |
9.69e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLaRPDG---------GEVCwrgrnTLRDRAAYQQDLLFIGHQpgiKAV 88
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyegeilfdGEVC-----RFKDIRDSEALGIVIIHQ---ELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 89 LTPF----ENLqFY---QAVRGAAE-QQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPl 157
Cdd:NF040905 89 LIPYlsiaENI-FLgneRAKRGVIDwNETNRRArelLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP- 166
|
..
gi 491074653 158 TA 159
Cdd:NF040905 167 TA 168
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-185 |
1.67e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 41.37 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 29 IIQVEGPNGAGKTSLLRILAGL------ARPDGgEVCWRGRNTlrdraaYQQDLLFIGHQPGIKAVL---TPFENLQFY- 98
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFNRLlelneeARVEG-EVRLFGRNI------YSPDVDPIEVRREVGMVFqypNPFPHLTIYd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 99 -------------------QAVRGAAEQQAIWRALEQvglvGYEDLPvAQLSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:PRK14267 105 nvaigvklnglvkskkeldERVEWALKKAALWDEVKD----RLNDYP-SNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180
....*....|....*....|....*.
gi 491074653 160 IDKQGVAELISLFEQHAQRGGMVLLT 185
Cdd:PRK14267 180 IDPVGTAKIEELLFELKKEYTIVLVT 205
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-188 |
2.10e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.69 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 14 RILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcWRGRNTlrdraAYqqdllfIGHQPGIKAVlTPFE 93
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSI-----AY------VPQQAWIMNA-TVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 94 NLQFYQAVRGAAEQQAIwR-------------ALE-QVGLVGyedlpvAQLSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:PTZ00243 740 NILFFDEEDAARLADAV-RvsqleadlaqlggGLEtEIGEKG------VNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190
....*....|....*....|....*....|.
gi 491074653 160 IDKQgVAELI--SLFEQHAqRGGMVLLTTHQ 188
Cdd:PTZ00243 813 LDAH-VGERVveECFLGAL-AGKTRVLATHQ 841
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-185 |
2.31e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 40.85 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 14 RILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLA-RPDG----GEVCWRGRNTL--RDRAAYQQDLLFIGHQP--- 83
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdKVSGyrysGDVLLGGRSIFnyRDVLEFRRRVGMLFQRPnpf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 84 ----------GIKA-VLTPFEnlQFYQAVRGAAEQQAIWRALEQvglvGYEDLPVaQLSAGQQRRVALARLWLSAAPLWI 152
Cdd:PRK14271 114 pmsimdnvlaGVRAhKLVPRK--EFRGVAQARLTEVGLWDAVKD----RLSDSPF-RLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190
....*....|....*....|....*....|...
gi 491074653 153 LDEPLTAIDKQGVAELISLFEQHAQRGGMVLLT 185
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADRLTVIIVT 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-191 |
2.52e-04 |
|
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: 41.21 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLArPDGGEVCWRGRN--TLRD------RAAYQ---QDllfighqpgikav 88
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDldGLSRralrplRRRMQvvfQD------------- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 89 ltPF--------------ENLQFYQAVRGAAEQQA-IWRALEQVGLvgyedLPVA------QLSAGQQRRVALAR-LWLS 146
Cdd:COG4172 371 --PFgslsprmtvgqiiaEGLRVHGPGLSAAERRArVAEALEEVGL-----DPAArhryphEFSGGQRQRIAIARaLILE 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491074653 147 aaP-LWILDEPLTAIDKQGVAELISLFEQHAQRGGMV-LLTTHqDLA 191
Cdd:COG4172 444 --PkLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAyLFISH-DLA 487
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-161 |
3.07e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEV----CWRGRNTLRD-RAAY----QQDLLFIGhqpGIKAVLT 90
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIlidgCDISKFGLMDlRKVLgiipQAPVLFSG---TVRFNLD 1334
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491074653 91 PF---ENLQFYQAVRGAAEQQAIWRalEQVGLvgyeDLPVAQ----LSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PLN03130 1335 PFnehNDADLWESLERAHLKDVIRR--NSLGL----DAEVSEagenFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-187 |
3.54e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.99 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEV-----CWRGRN----TLRDRAAYQQ------DLLFIGHQP 83
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRSrqviELSEQSAAQMrhvrgaDMAMIFQEP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 84 giKAVLTPF--------ENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVA---QLSAGQQRRVALArLWLSAAP-LW 151
Cdd:PRK10261 114 --MTSLNPVftvgeqiaESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRyphQLSGGMRQRVMIA-MALSCRPaVL 190
|
170 180 190
....*....|....*....|....*....|....*....
gi 491074653 152 ILDEPLTAID---KQGVAELISLFEQHAQRGgmVLLTTH 187
Cdd:PRK10261 191 IADEPTTALDvtiQAQILQLIKVLQKEMSMG--VIFITH 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-194 |
3.57e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.54 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGL------ARPDgGEVCWRGRN---------TL 66
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgFRVE-GKVTFHGKNlyapdvdpvEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 67 RDRAAyqqdLLFIGHQPGIKAVltpFENLQF------YQA-----VRGAAEQQAIW----RALEQVGLvgyedlpvaQLS 131
Cdd:PRK14243 90 RRRIG----MVFQKPNPFPKSI---YDNIAYgaringYKGdmdelVERSLRQAALWdevkDKLKQSGL---------SLS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 132 AGQQRRVALARLwLSAAPLWIL-DEPLTAID---KQGVAELI-SLFEQHAqrggmVLLTTH--QDLAGVS 194
Cdd:PRK14243 154 GGQQQRLCIARA-IAVQPEVILmDEPCSALDpisTLRIEELMhELKEQYT-----IIIVTHnmQQAARVS 217
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-173 |
4.21e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.54 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLfig 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFL--- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 81 hqpgiKAVLTPFENLqfyqaVRgAAEQQAIWRALEQVGLVGYE----DLPVAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:PRK10636 389 -----RADESPLQHL-----AR-LAPQELEQKLRDYLGGFGFQgdkvTEETRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
|
170 180
....*....|....*....|
gi 491074653 157 LTAID---KQGVAELISLFE 173
Cdd:PRK10636 458 TNHLDldmRQALTEALIDFE 477
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
128-161 |
4.30e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 40.39 E-value: 4.30e-04
10 20 30
....*....|....*....|....*....|....
gi 491074653 128 AQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-188 |
4.45e-04 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 40.01 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 17 FSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQD-----LLFIGHQPGI-KAVL- 89
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSrnrysVAYAAQKPWLlNATVe 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 90 ------TPFeNLQFYQAVRGAAEQQAIWRAL-----EQVGLVGYedlpvaQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:cd03290 97 enitfgSPF-NKQRYKAVTDACSLQPDIDLLpfgdqTEIGERGI------NLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 491074653 159 AID--------KQGVAELIslfeQHAQRggMVLLTTHQ 188
Cdd:cd03290 170 ALDihlsdhlmQEGILKFL----QDDKR--TLVLVTHK 201
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-161 |
5.42e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.34 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRIL-------AGLARPDGGEVCWRGRNTLRDRAAY--QQDLLFIGhqpGIKAVLT 90
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALfriveleKGRIMIDDCDVAKFGLTDLRRVLSIipQSPVLFSG---TVRFNID 1331
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491074653 91 PFE---NLQFYQAVRGAAEQQAIWRalEQVGLvgyeDLPVAQ----LSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PLN03232 1332 PFSehnDADLWEALERAHIKDVIDR--NPFGL----DAEVSEggenFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-170 |
7.04e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.09 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 24 VQPGDIIQVEGPNGAGKTSLLRILA----GLARPDGGEVCWRGRNTLRDRAAYQQDLLFIG----HQPgikaVLTPFENL 95
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAetdvHFP----HLTVGETL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 96 QFYQAVR-------GAAEQQAIWR----ALEQVGL-------VGyEDLpVAQLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:TIGR00956 160 DFAARCKtpqnrpdGVSREEYAKHiadvYMATYGLshtrntkVG-NDF-VRGVSGGERKRVSIAEASLGGAKIQCWDNAT 237
|
170
....*....|...
gi 491074653 158 TAIDKQGVAELIS 170
Cdd:TIGR00956 238 RGLDSATALEFIR 250
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-188 |
7.58e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 23 SVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRDRAAYQQDLLFIgHQPgIKAVL--TPFENLQF- 97
Cdd:PRK10982 20 KVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFKSSKEALENGISMV-HQE-LNLVLqrSVMDNMWLg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 98 -YQAVRGAAEQQAIWRALEQVglvgYEDL--------PVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAEL 168
Cdd:PRK10982 98 rYPTKGMFVDQDKMYRDTKAI----FDELdididpraKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHL 173
|
170 180
....*....|....*....|
gi 491074653 169 ISLFEQHAQRGGMVLLTTHQ 188
Cdd:PRK10982 174 FTIIRKLKERGCGIVYISHK 193
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
89-187 |
9.05e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 89 LTPFENLQFYQAVrgaaeqQAIWRALE---QVGLvGYEDL--PVAQLSAGQQRRVALARlWLSA----APLWILDEPLTA 159
Cdd:TIGR00630 791 MTVEEAYEFFEAV------PSISRKLQtlcDVGL-GYIRLgqPATTLSGGEAQRIKLAK-ELSKrstgRTLYILDEPTTG 862
|
90 100
....*....|....*....|....*...
gi 491074653 160 IDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:TIGR00630 863 LHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-187 |
1.30e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.74 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 26 PGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcwrgrntlrdraayqqdllfighqpgikavltpfenlqfyqaVRGAA 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV------------------------------------------IYIDG 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 106 EqqAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHA------QRG 179
Cdd:smart00382 39 E--DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllksEKN 116
|
....*...
gi 491074653 180 GMVLLTTH 187
Cdd:smart00382 117 LTVILTTN 124
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-97 |
1.37e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.64 E-value: 1.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491074653 19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGrntlrdraayqqDLLFIGHQPGIKAVLTPFENLQF 97
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------------EVSVIAISAGLSGQLTGIENIEF 108
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-200 |
1.53e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 38.63 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDggevcWRgrnTLRDRAAYQQ-DLL---------FIGHQPGI---- 85
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDN-----WR---VTADRMRFDDiDLLrlsprerrkLVGHNVSMifqe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 86 -KAVLTPFENL--QFYQAV-----RGAAEQQAIWR---ALEQVGLVGYED-------LPVaQLSAGQQRRVALARLWLSA 147
Cdd:PRK15093 98 pQSCLDPSERVgrQLMQNIpgwtyKGRWWQRFGWRkrrAIELLHRVGIKDhkdamrsFPY-ELTEGECQKVMIAIALANQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491074653 148 APLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDLAGVSQTVGKI 200
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
126-187 |
2.10e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.66 E-value: 2.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491074653 126 PVAQLSAGQQRRVALARLWLSAAP---LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-64 |
3.04e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 38.08 E-value: 3.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491074653 2 LEAKSLScVRDER--ILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN 64
Cdd:COG3845 258 LEVENLS-VRDDRgvPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGED 321
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
9-161 |
3.27e-03 |
|
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: 37.58 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 9 CVRDERIL---FSELSFSVQPGDIIQVEGPNGAGKTSL-------LRILAGLARPDGGEVCWRGRNTLRDRAA--YQQDL 76
Cdd:cd03288 26 CVRYENNLkpvLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIVIDGIDISKLPLHTLRSRLSiiLQDPI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 77 LFIGhqpGIKAVLTPfenlqfyqavRGAAEQQAIWRALEQV-------GLVGYEDLPVAQ----LSAGQQRRVALARLWL 145
Cdd:cd03288 106 LFSG---SIRFNLDP----------ECKCTDDRLWEALEIAqlknmvkSLPGGLDAVVTEggenFSVGQRQLFCLARAFV 172
|
170
....*....|....*.
gi 491074653 146 SAAPLWILDEPLTAID 161
Cdd:cd03288 173 RKSSILIMDEATASID 188
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-175 |
3.49e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 37.84 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGrntlRDRAAY-------------QQDLLFIGhqpGIK 86
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG----REIGAYglrelrrqfsmipQDPVLFDG---TVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 87 AVLTPFenLQfyqavrgaAEQQAIWRALEQVGL---VGYE----DLPV----AQLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:PTZ00243 1402 QNVDPF--LE--------ASSAEVWAALELVGLrerVASEsegiDSRVleggSNYSVGQRQLMCMARALLKKGSGFILMD 1471
|
170 180
....*....|....*....|....*
gi 491074653 156 PLT-----AIDKQGVAELISLFEQH 175
Cdd:PTZ00243 1472 EATanidpALDRQIQATVMSAFSAY 1496
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-189 |
4.75e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 36.53 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 20 LSFSVQPGDIIQVEGPNGAGKTSLLriLAGLARpdggEVCWRGRNTLrdRAAYQQDLLFIGhqpgikavltpfeNLQFyq 99
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYA----SGKARLISFL--PKFSRNKLIFID-------------QLQF-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 100 avrgaaeqqaiwraLEQVGLvGYEDL--PVAQLSAGQQRRVALAR-LWLSAAP-LWILDEPLTAIDKQGVAELISLFEQH 175
Cdd:cd03238 71 --------------LIDVGL-GYLTLgqKLSTLSGGELQRVKLASeLFSEPPGtLFILDEPSTGLHQQDINQLLEVIKGL 135
|
170
....*....|....
gi 491074653 176 AQRGGMVLLTTHQD 189
Cdd:cd03238 136 IDLGNTVILIEHNL 149
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
127-189 |
4.85e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 4.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491074653 127 VAQLSAGQQRRVALARlWLSA---APLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQD 189
Cdd:PRK00635 474 LATLSGGEQERTALAK-HLGAeliGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDE 538
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
19-48 |
6.49e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 36.51 E-value: 6.49e-03
10 20 30
....*....|....*....|....*....|
gi 491074653 19 ELSFSVQPGDIIQVeGPNGAGKTSLLRILA 48
Cdd:COG3950 18 EIDFDNPPRLTVLV-GENGSGKTTLLEAIA 46
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
129-200 |
7.35e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 36.68 E-value: 7.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074653 129 QLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQ-HAQRGGMVLLTTHqDLAGVSQTVGKI 200
Cdd:PRK13646 145 QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlQTDENKTIILVSH-DMNEVARYADEV 216
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
27-60 |
8.08e-03 |
|
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange. While prokaryotes have a single RecA protein, eukaryotes have multiple RecA homologs such as Rad51, DMC1 and Rad55/57. Archaea have the RecA-like homologs RadA and RadB.
Pssm-ID: 410881 [Multi-domain] Cd Length: 185 Bit Score: 35.79 E-value: 8.08e-03
10 20 30
....*....|....*....|....*....|....
gi 491074653 27 GDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCW 60
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVW 34
|
|
| Dck |
COG1428 |
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism]; |
29-48 |
8.63e-03 |
|
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
Pssm-ID: 441037 [Multi-domain] Cd Length: 205 Bit Score: 35.92 E-value: 8.63e-03
|
|